data_7ZXF
# 
_entry.id   7ZXF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.359 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7ZXF         pdb_00007zxf 10.2210/pdb7zxf/pdb 
WWPDB D_1292123146 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7ZXF 
_pdbx_database_status.recvd_initial_deposition_date   2022-05-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ko, K.T.'       1 ? 
'Lennartz, F.L.' 2 ? 
'Higgins, M.K.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ko, K.T.'       1 ? 
primary 'Lennartz, F.L.' 2 ? 
primary 'Higgins, M.K.'  3 ? 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7ZXF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     156.880 
_cell.length_a_esd                 ? 
_cell.length_b                     156.880 
_cell.length_b_esd                 ? 
_cell.length_c                     148.761 
_cell.length_c_esd                 ? 
_cell.volume                       3661206.717 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         7ZXF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            'P 4abw 2nw' 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer  man 'Gametocyte surface protein P45/48' 51545.887 1 ? ? ? ? 
2 polymer  man '85RF45.1 heavy chain' 49338.469 1 ? ? ? ? 
3 polymer  man '85RF45.1 light chain' 23638.053 1 ? ? ? ? 
4 polymer  man '10D8 heavy chain' 51485.203 1 ? ? ? ? 
5 polymer  man '10D8 light chain' 26537.549 1 ? ? ? ? 
6 branched man 
;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
748.682   2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Pfs48/45 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MMLYISAKKAQVAFILYIVLVLRIISGNNDFCKPSSLNSEISGFIGYKCNFSNEGVHNLKPDMRERRSIFCTIHSYFIYD
KIRLIIPKKSSSPEFKILPEKCFQKVYTDYENRVETDISELGLIEYEIEENDTNPNYNERTITISPFSPKDIEFFCFCDN
TEKVISSIEGRSAMVHVRVLKYPHNILFTNLTNDLFTYLPKTYNESNFVSNVLEVELNDGELFVLACELINKKCFQEGKE
KALYKSNKIIYHKNLTIFKAPFYVTSKDVNTECTCKFKNNNYKIVLKPKYEKKVIHGCNFSSNVSSKHTFTDSLDISLVD
DSAHISCNVHLSEPKYNHLVGLNCPGDIIPDCFFQVYQPESEELEPSNIVYLDSQINIGDIEYYEDAEGDDKIKLFGIVG
SIPKTTSFTCICKKDKKSAYMTVTIDSAYYGFLAKTFIFLIVAILLYI
;
;MMLYISAKKAQVAFILYIVLVLRIISGNNDFCKPSSLNSEISGFIGYKCNFSNEGVHNLKPDMRERRSIFCTIHSYFIYD
KIRLIIPKKSSSPEFKILPEKCFQKVYTDYENRVETDISELGLIEYEIEENDTNPNYNERTITISPFSPKDIEFFCFCDN
TEKVISSIEGRSAMVHVRVLKYPHNILFTNLTNDLFTYLPKTYNESNFVSNVLEVELNDGELFVLACELINKKCFQEGKE
KALYKSNKIIYHKNLTIFKAPFYVTSKDVNTECTCKFKNNNYKIVLKPKYEKKVIHGCNFSSNVSSKHTFTDSLDISLVD
DSAHISCNVHLSEPKYNHLVGLNCPGDIIPDCFFQVYQPESEELEPSNIVYLDSQINIGDIEYYEDAEGDDKIKLFGIVG
SIPKTTSFTCICKKDKKSAYMTVTIDSAYYGFLAKTFIFLIVAILLYI
;
A ? 
2 'polypeptide(L)' no no 
;EVQLVESGGGLLQPGRSLKLSCVASGFTFNNYWMSWIRQAPGKGLEWIASISNIGGTIYYPDSVKGRFTISRDSAQNTLY
LQMNSLRSEDTATYYCTRDLRMSDYFDYWGQGVMVTVSSAETTAPSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTW
NSGALSSGVHTFPAVLQSGLYTLTSSVTVPSSTWPSQTVTCNVAHPASSTKVDKKIVPRNCGGDCKPCICTGSEVSSVFI
FPPKPKDVLTITLTPKVTCVVVDISQDDPEVHFSWFVDDVEVHTAQTRPPEEQFNSTFRSVSELPILHQDWLNGRTFRCK
VTSAAFPSPIEKTISKPEGRTQVPHVYTMSPTKEEMTQNEVSITCMVKGFYPPDIYVEWQMNGQPQENYKNTPPTMDTDG
SYFLYSKLNVKKEKWQQGNTFTCSVLHEGLHNHHTEKSLSHSPGK
;
;EVQLVESGGGLLQPGRSLKLSCVASGFTFNNYWMSWIRQAPGKGLEWIASISNIGGTIYYPDSVKGRFTISRDSAQNTLY
LQMNSLRSEDTATYYCTRDLRMSDYFDYWGQGVMVTVSSAETTAPSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTW
NSGALSSGVHTFPAVLQSGLYTLTSSVTVPSSTWPSQTVTCNVAHPASSTKVDKKIVPRNCGGDCKPCICTGSEVSSVFI
FPPKPKDVLTITLTPKVTCVVVDISQDDPEVHFSWFVDDVEVHTAQTRPPEEQFNSTFRSVSELPILHQDWLNGRTFRCK
VTSAAFPSPIEKTISKPEGRTQVPHVYTMSPTKEEMTQNEVSITCMVKGFYPPDIYVEWQMNGQPQENYKNTPPTMDTDG
SYFLYSKLNVKKEKWQQGNTFTCSVLHEGLHNHHTEKSLSHSPGK
;
B ? 
3 'polypeptide(L)' no no 
;QFVLSQPNSVSTNLGSTVKLSCKRSTGNIGSNYVSWYQHHEGRSPTTMIYRDDQRPDGVPDRFSGSIDRSSNSALLTIDN
VQTEDEAAYFCHSYSTGMYIFGGGTKLTVLGQPKSTPTLTMFPPSPEELQENKATLVCLISNFSPSGVTVAWKANGTPIT
QGVDTSNPTKEDNKYMASSFLHLTSDQWRSHNSFTCQVTHEGNTVEKTVSPTECVA
;
;QFVLSQPNSVSTNLGSTVKLSCKRSTGNIGSNYVSWYQHHEGRSPTTMIYRDDQRPDGVPDRFSGSIDRSSNSALLTIDN
VQTEDEAAYFCHSYSTGMYIFGGGTKLTVLGQPKSTPTLTMFPPSPEELQENKATLVCLISNFSPSGVTVAWKANGTPIT
QGVDTSNPTKEDNKYMASSFLHLTSDQWRSHNSFTCQVTHEGNTVEKTVSPTECVA
;
C ? 
4 'polypeptide(L)' no no 
;MNFGLSLIFLVLVLKGVQCEVMLVESGGDLVKPGGSLKVSCAASGFTFSNYAMSWVRQTPEKRLEWVATISSGASYTHYP
DSVKGRFTISRDNAKNTLYLQMSSLRSEDTAMYYCGRQVNRHDRALDAMDYWGQGTSVTVSPAKTTPPSVYPLAPGSAAQ
TNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIV
PRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVVVDISKDDPEVQFSWFVDDVEVHTAQTQPREEQFNSTFR
SVSELPIMHQDWLNGKEFKCRVNSAAFPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEW
QWNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLHNHHTEKSLSHSPGK
;
;MNFGLSLIFLVLVLKGVQCEVMLVESGGDLVKPGGSLKVSCAASGFTFSNYAMSWVRQTPEKRLEWVATISSGASYTHYP
DSVKGRFTISRDNAKNTLYLQMSSLRSEDTAMYYCGRQVNRHDRALDAMDYWGQGTSVTVSPAKTTPPSVYPLAPGSAAQ
TNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIV
PRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVVVDISKDDPEVQFSWFVDDVEVHTAQTQPREEQFNSTFR
SVSELPIMHQDWLNGKEFKCRVNSAAFPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEW
QWNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLHNHHTEKSLSHSPGK
;
D ? 
5 'polypeptide(L)' no no 
;MDSQAQVLMLLLLWVSGTCGDIVMSQSPSSLAVSVGEKVTMSCKSSQSLFYSSNQKNYLAWYQQKPGQSPKLLIYWASTR
ESGVPDRFTGSGSGTDFTLTISSVKAEDLAVYYCQQYYSYPPTFGGGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVC
FLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
;
;MDSQAQVLMLLLLWVSGTCGDIVMSQSPSSLAVSVGEKVTMSCKSSQSLFYSSNQKNYLAWYQQKPGQSPKLLIYWASTR
ESGVPDRFTGSGSGTDFTLTISSVKAEDLAVYYCQQYYSYPPTFGGGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVC
FLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
;
E ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   LEU n 
1 4   TYR n 
1 5   ILE n 
1 6   SER n 
1 7   ALA n 
1 8   LYS n 
1 9   LYS n 
1 10  ALA n 
1 11  GLN n 
1 12  VAL n 
1 13  ALA n 
1 14  PHE n 
1 15  ILE n 
1 16  LEU n 
1 17  TYR n 
1 18  ILE n 
1 19  VAL n 
1 20  LEU n 
1 21  VAL n 
1 22  LEU n 
1 23  ARG n 
1 24  ILE n 
1 25  ILE n 
1 26  SER n 
1 27  GLY n 
1 28  ASN n 
1 29  ASN n 
1 30  ASP n 
1 31  PHE n 
1 32  CYS n 
1 33  LYS n 
1 34  PRO n 
1 35  SER n 
1 36  SER n 
1 37  LEU n 
1 38  ASN n 
1 39  SER n 
1 40  GLU n 
1 41  ILE n 
1 42  SER n 
1 43  GLY n 
1 44  PHE n 
1 45  ILE n 
1 46  GLY n 
1 47  TYR n 
1 48  LYS n 
1 49  CYS n 
1 50  ASN n 
1 51  PHE n 
1 52  SER n 
1 53  ASN n 
1 54  GLU n 
1 55  GLY n 
1 56  VAL n 
1 57  HIS n 
1 58  ASN n 
1 59  LEU n 
1 60  LYS n 
1 61  PRO n 
1 62  ASP n 
1 63  MET n 
1 64  ARG n 
1 65  GLU n 
1 66  ARG n 
1 67  ARG n 
1 68  SER n 
1 69  ILE n 
1 70  PHE n 
1 71  CYS n 
1 72  THR n 
1 73  ILE n 
1 74  HIS n 
1 75  SER n 
1 76  TYR n 
1 77  PHE n 
1 78  ILE n 
1 79  TYR n 
1 80  ASP n 
1 81  LYS n 
1 82  ILE n 
1 83  ARG n 
1 84  LEU n 
1 85  ILE n 
1 86  ILE n 
1 87  PRO n 
1 88  LYS n 
1 89  LYS n 
1 90  SER n 
1 91  SER n 
1 92  SER n 
1 93  PRO n 
1 94  GLU n 
1 95  PHE n 
1 96  LYS n 
1 97  ILE n 
1 98  LEU n 
1 99  PRO n 
1 100 GLU n 
1 101 LYS n 
1 102 CYS n 
1 103 PHE n 
1 104 GLN n 
1 105 LYS n 
1 106 VAL n 
1 107 TYR n 
1 108 THR n 
1 109 ASP n 
1 110 TYR n 
1 111 GLU n 
1 112 ASN n 
1 113 ARG n 
1 114 VAL n 
1 115 GLU n 
1 116 THR n 
1 117 ASP n 
1 118 ILE n 
1 119 SER n 
1 120 GLU n 
1 121 LEU n 
1 122 GLY n 
1 123 LEU n 
1 124 ILE n 
1 125 GLU n 
1 126 TYR n 
1 127 GLU n 
1 128 ILE n 
1 129 GLU n 
1 130 GLU n 
1 131 ASN n 
1 132 ASP n 
1 133 THR n 
1 134 ASN n 
1 135 PRO n 
1 136 ASN n 
1 137 TYR n 
1 138 ASN n 
1 139 GLU n 
1 140 ARG n 
1 141 THR n 
1 142 ILE n 
1 143 THR n 
1 144 ILE n 
1 145 SER n 
1 146 PRO n 
1 147 PHE n 
1 148 SER n 
1 149 PRO n 
1 150 LYS n 
1 151 ASP n 
1 152 ILE n 
1 153 GLU n 
1 154 PHE n 
1 155 PHE n 
1 156 CYS n 
1 157 PHE n 
1 158 CYS n 
1 159 ASP n 
1 160 ASN n 
1 161 THR n 
1 162 GLU n 
1 163 LYS n 
1 164 VAL n 
1 165 ILE n 
1 166 SER n 
1 167 SER n 
1 168 ILE n 
1 169 GLU n 
1 170 GLY n 
1 171 ARG n 
1 172 SER n 
1 173 ALA n 
1 174 MET n 
1 175 VAL n 
1 176 HIS n 
1 177 VAL n 
1 178 ARG n 
1 179 VAL n 
1 180 LEU n 
1 181 LYS n 
1 182 TYR n 
1 183 PRO n 
1 184 HIS n 
1 185 ASN n 
1 186 ILE n 
1 187 LEU n 
1 188 PHE n 
1 189 THR n 
1 190 ASN n 
1 191 LEU n 
1 192 THR n 
1 193 ASN n 
1 194 ASP n 
1 195 LEU n 
1 196 PHE n 
1 197 THR n 
1 198 TYR n 
1 199 LEU n 
1 200 PRO n 
1 201 LYS n 
1 202 THR n 
1 203 TYR n 
1 204 ASN n 
1 205 GLU n 
1 206 SER n 
1 207 ASN n 
1 208 PHE n 
1 209 VAL n 
1 210 SER n 
1 211 ASN n 
1 212 VAL n 
1 213 LEU n 
1 214 GLU n 
1 215 VAL n 
1 216 GLU n 
1 217 LEU n 
1 218 ASN n 
1 219 ASP n 
1 220 GLY n 
1 221 GLU n 
1 222 LEU n 
1 223 PHE n 
1 224 VAL n 
1 225 LEU n 
1 226 ALA n 
1 227 CYS n 
1 228 GLU n 
1 229 LEU n 
1 230 ILE n 
1 231 ASN n 
1 232 LYS n 
1 233 LYS n 
1 234 CYS n 
1 235 PHE n 
1 236 GLN n 
1 237 GLU n 
1 238 GLY n 
1 239 LYS n 
1 240 GLU n 
1 241 LYS n 
1 242 ALA n 
1 243 LEU n 
1 244 TYR n 
1 245 LYS n 
1 246 SER n 
1 247 ASN n 
1 248 LYS n 
1 249 ILE n 
1 250 ILE n 
1 251 TYR n 
1 252 HIS n 
1 253 LYS n 
1 254 ASN n 
1 255 LEU n 
1 256 THR n 
1 257 ILE n 
1 258 PHE n 
1 259 LYS n 
1 260 ALA n 
1 261 PRO n 
1 262 PHE n 
1 263 TYR n 
1 264 VAL n 
1 265 THR n 
1 266 SER n 
1 267 LYS n 
1 268 ASP n 
1 269 VAL n 
1 270 ASN n 
1 271 THR n 
1 272 GLU n 
1 273 CYS n 
1 274 THR n 
1 275 CYS n 
1 276 LYS n 
1 277 PHE n 
1 278 LYS n 
1 279 ASN n 
1 280 ASN n 
1 281 ASN n 
1 282 TYR n 
1 283 LYS n 
1 284 ILE n 
1 285 VAL n 
1 286 LEU n 
1 287 LYS n 
1 288 PRO n 
1 289 LYS n 
1 290 TYR n 
1 291 GLU n 
1 292 LYS n 
1 293 LYS n 
1 294 VAL n 
1 295 ILE n 
1 296 HIS n 
1 297 GLY n 
1 298 CYS n 
1 299 ASN n 
1 300 PHE n 
1 301 SER n 
1 302 SER n 
1 303 ASN n 
1 304 VAL n 
1 305 SER n 
1 306 SER n 
1 307 LYS n 
1 308 HIS n 
1 309 THR n 
1 310 PHE n 
1 311 THR n 
1 312 ASP n 
1 313 SER n 
1 314 LEU n 
1 315 ASP n 
1 316 ILE n 
1 317 SER n 
1 318 LEU n 
1 319 VAL n 
1 320 ASP n 
1 321 ASP n 
1 322 SER n 
1 323 ALA n 
1 324 HIS n 
1 325 ILE n 
1 326 SER n 
1 327 CYS n 
1 328 ASN n 
1 329 VAL n 
1 330 HIS n 
1 331 LEU n 
1 332 SER n 
1 333 GLU n 
1 334 PRO n 
1 335 LYS n 
1 336 TYR n 
1 337 ASN n 
1 338 HIS n 
1 339 LEU n 
1 340 VAL n 
1 341 GLY n 
1 342 LEU n 
1 343 ASN n 
1 344 CYS n 
1 345 PRO n 
1 346 GLY n 
1 347 ASP n 
1 348 ILE n 
1 349 ILE n 
1 350 PRO n 
1 351 ASP n 
1 352 CYS n 
1 353 PHE n 
1 354 PHE n 
1 355 GLN n 
1 356 VAL n 
1 357 TYR n 
1 358 GLN n 
1 359 PRO n 
1 360 GLU n 
1 361 SER n 
1 362 GLU n 
1 363 GLU n 
1 364 LEU n 
1 365 GLU n 
1 366 PRO n 
1 367 SER n 
1 368 ASN n 
1 369 ILE n 
1 370 VAL n 
1 371 TYR n 
1 372 LEU n 
1 373 ASP n 
1 374 SER n 
1 375 GLN n 
1 376 ILE n 
1 377 ASN n 
1 378 ILE n 
1 379 GLY n 
1 380 ASP n 
1 381 ILE n 
1 382 GLU n 
1 383 TYR n 
1 384 TYR n 
1 385 GLU n 
1 386 ASP n 
1 387 ALA n 
1 388 GLU n 
1 389 GLY n 
1 390 ASP n 
1 391 ASP n 
1 392 LYS n 
1 393 ILE n 
1 394 LYS n 
1 395 LEU n 
1 396 PHE n 
1 397 GLY n 
1 398 ILE n 
1 399 VAL n 
1 400 GLY n 
1 401 SER n 
1 402 ILE n 
1 403 PRO n 
1 404 LYS n 
1 405 THR n 
1 406 THR n 
1 407 SER n 
1 408 PHE n 
1 409 THR n 
1 410 CYS n 
1 411 ILE n 
1 412 CYS n 
1 413 LYS n 
1 414 LYS n 
1 415 ASP n 
1 416 LYS n 
1 417 LYS n 
1 418 SER n 
1 419 ALA n 
1 420 TYR n 
1 421 MET n 
1 422 THR n 
1 423 VAL n 
1 424 THR n 
1 425 ILE n 
1 426 ASP n 
1 427 SER n 
1 428 ALA n 
1 429 TYR n 
1 430 TYR n 
1 431 GLY n 
1 432 PHE n 
1 433 LEU n 
1 434 ALA n 
1 435 LYS n 
1 436 THR n 
1 437 PHE n 
1 438 ILE n 
1 439 PHE n 
1 440 LEU n 
1 441 ILE n 
1 442 VAL n 
1 443 ALA n 
1 444 ILE n 
1 445 LEU n 
1 446 LEU n 
1 447 TYR n 
1 448 ILE n 
2 1   GLU n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  LEU n 
2 13  GLN n 
2 14  PRO n 
2 15  GLY n 
2 16  ARG n 
2 17  SER n 
2 18  LEU n 
2 19  LYS n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  VAL n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  PHE n 
2 28  THR n 
2 29  PHE n 
2 30  ASN n 
2 31  ASN n 
2 32  TYR n 
2 33  TRP n 
2 34  MET n 
2 35  SER n 
2 36  TRP n 
2 37  ILE n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  ILE n 
2 49  ALA n 
2 50  SER n 
2 51  ILE n 
2 52  SER n 
2 53  ASN n 
2 54  ILE n 
2 55  GLY n 
2 56  GLY n 
2 57  THR n 
2 58  ILE n 
2 59  TYR n 
2 60  TYR n 
2 61  PRO n 
2 62  ASP n 
2 63  SER n 
2 64  VAL n 
2 65  LYS n 
2 66  GLY n 
2 67  ARG n 
2 68  PHE n 
2 69  THR n 
2 70  ILE n 
2 71  SER n 
2 72  ARG n 
2 73  ASP n 
2 74  SER n 
2 75  ALA n 
2 76  GLN n 
2 77  ASN n 
2 78  THR n 
2 79  LEU n 
2 80  TYR n 
2 81  LEU n 
2 82  GLN n 
2 83  MET n 
2 84  ASN n 
2 85  SER n 
2 86  LEU n 
2 87  ARG n 
2 88  SER n 
2 89  GLU n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  THR n 
2 94  TYR n 
2 95  TYR n 
2 96  CYS n 
2 97  THR n 
2 98  ARG n 
2 99  ASP n 
2 100 LEU n 
2 101 ARG n 
2 102 MET n 
2 103 SER n 
2 104 ASP n 
2 105 TYR n 
2 106 PHE n 
2 107 ASP n 
2 108 TYR n 
2 109 TRP n 
2 110 GLY n 
2 111 GLN n 
2 112 GLY n 
2 113 VAL n 
2 114 MET n 
2 115 VAL n 
2 116 THR n 
2 117 VAL n 
2 118 SER n 
2 119 SER n 
2 120 ALA n 
2 121 GLU n 
2 122 THR n 
2 123 THR n 
2 124 ALA n 
2 125 PRO n 
2 126 SER n 
2 127 VAL n 
2 128 TYR n 
2 129 PRO n 
2 130 LEU n 
2 131 ALA n 
2 132 PRO n 
2 133 GLY n 
2 134 THR n 
2 135 ALA n 
2 136 LEU n 
2 137 LYS n 
2 138 SER n 
2 139 ASN n 
2 140 SER n 
2 141 MET n 
2 142 VAL n 
2 143 THR n 
2 144 LEU n 
2 145 GLY n 
2 146 CYS n 
2 147 LEU n 
2 148 VAL n 
2 149 LYS n 
2 150 GLY n 
2 151 TYR n 
2 152 PHE n 
2 153 PRO n 
2 154 GLU n 
2 155 PRO n 
2 156 VAL n 
2 157 THR n 
2 158 VAL n 
2 159 THR n 
2 160 TRP n 
2 161 ASN n 
2 162 SER n 
2 163 GLY n 
2 164 ALA n 
2 165 LEU n 
2 166 SER n 
2 167 SER n 
2 168 GLY n 
2 169 VAL n 
2 170 HIS n 
2 171 THR n 
2 172 PHE n 
2 173 PRO n 
2 174 ALA n 
2 175 VAL n 
2 176 LEU n 
2 177 GLN n 
2 178 SER n 
2 179 GLY n 
2 180 LEU n 
2 181 TYR n 
2 182 THR n 
2 183 LEU n 
2 184 THR n 
2 185 SER n 
2 186 SER n 
2 187 VAL n 
2 188 THR n 
2 189 VAL n 
2 190 PRO n 
2 191 SER n 
2 192 SER n 
2 193 THR n 
2 194 TRP n 
2 195 PRO n 
2 196 SER n 
2 197 GLN n 
2 198 THR n 
2 199 VAL n 
2 200 THR n 
2 201 CYS n 
2 202 ASN n 
2 203 VAL n 
2 204 ALA n 
2 205 HIS n 
2 206 PRO n 
2 207 ALA n 
2 208 SER n 
2 209 SER n 
2 210 THR n 
2 211 LYS n 
2 212 VAL n 
2 213 ASP n 
2 214 LYS n 
2 215 LYS n 
2 216 ILE n 
2 217 VAL n 
2 218 PRO n 
2 219 ARG n 
2 220 ASN n 
2 221 CYS n 
2 222 GLY n 
2 223 GLY n 
2 224 ASP n 
2 225 CYS n 
2 226 LYS n 
2 227 PRO n 
2 228 CYS n 
2 229 ILE n 
2 230 CYS n 
2 231 THR n 
2 232 GLY n 
2 233 SER n 
2 234 GLU n 
2 235 VAL n 
2 236 SER n 
2 237 SER n 
2 238 VAL n 
2 239 PHE n 
2 240 ILE n 
2 241 PHE n 
2 242 PRO n 
2 243 PRO n 
2 244 LYS n 
2 245 PRO n 
2 246 LYS n 
2 247 ASP n 
2 248 VAL n 
2 249 LEU n 
2 250 THR n 
2 251 ILE n 
2 252 THR n 
2 253 LEU n 
2 254 THR n 
2 255 PRO n 
2 256 LYS n 
2 257 VAL n 
2 258 THR n 
2 259 CYS n 
2 260 VAL n 
2 261 VAL n 
2 262 VAL n 
2 263 ASP n 
2 264 ILE n 
2 265 SER n 
2 266 GLN n 
2 267 ASP n 
2 268 ASP n 
2 269 PRO n 
2 270 GLU n 
2 271 VAL n 
2 272 HIS n 
2 273 PHE n 
2 274 SER n 
2 275 TRP n 
2 276 PHE n 
2 277 VAL n 
2 278 ASP n 
2 279 ASP n 
2 280 VAL n 
2 281 GLU n 
2 282 VAL n 
2 283 HIS n 
2 284 THR n 
2 285 ALA n 
2 286 GLN n 
2 287 THR n 
2 288 ARG n 
2 289 PRO n 
2 290 PRO n 
2 291 GLU n 
2 292 GLU n 
2 293 GLN n 
2 294 PHE n 
2 295 ASN n 
2 296 SER n 
2 297 THR n 
2 298 PHE n 
2 299 ARG n 
2 300 SER n 
2 301 VAL n 
2 302 SER n 
2 303 GLU n 
2 304 LEU n 
2 305 PRO n 
2 306 ILE n 
2 307 LEU n 
2 308 HIS n 
2 309 GLN n 
2 310 ASP n 
2 311 TRP n 
2 312 LEU n 
2 313 ASN n 
2 314 GLY n 
2 315 ARG n 
2 316 THR n 
2 317 PHE n 
2 318 ARG n 
2 319 CYS n 
2 320 LYS n 
2 321 VAL n 
2 322 THR n 
2 323 SER n 
2 324 ALA n 
2 325 ALA n 
2 326 PHE n 
2 327 PRO n 
2 328 SER n 
2 329 PRO n 
2 330 ILE n 
2 331 GLU n 
2 332 LYS n 
2 333 THR n 
2 334 ILE n 
2 335 SER n 
2 336 LYS n 
2 337 PRO n 
2 338 GLU n 
2 339 GLY n 
2 340 ARG n 
2 341 THR n 
2 342 GLN n 
2 343 VAL n 
2 344 PRO n 
2 345 HIS n 
2 346 VAL n 
2 347 TYR n 
2 348 THR n 
2 349 MET n 
2 350 SER n 
2 351 PRO n 
2 352 THR n 
2 353 LYS n 
2 354 GLU n 
2 355 GLU n 
2 356 MET n 
2 357 THR n 
2 358 GLN n 
2 359 ASN n 
2 360 GLU n 
2 361 VAL n 
2 362 SER n 
2 363 ILE n 
2 364 THR n 
2 365 CYS n 
2 366 MET n 
2 367 VAL n 
2 368 LYS n 
2 369 GLY n 
2 370 PHE n 
2 371 TYR n 
2 372 PRO n 
2 373 PRO n 
2 374 ASP n 
2 375 ILE n 
2 376 TYR n 
2 377 VAL n 
2 378 GLU n 
2 379 TRP n 
2 380 GLN n 
2 381 MET n 
2 382 ASN n 
2 383 GLY n 
2 384 GLN n 
2 385 PRO n 
2 386 GLN n 
2 387 GLU n 
2 388 ASN n 
2 389 TYR n 
2 390 LYS n 
2 391 ASN n 
2 392 THR n 
2 393 PRO n 
2 394 PRO n 
2 395 THR n 
2 396 MET n 
2 397 ASP n 
2 398 THR n 
2 399 ASP n 
2 400 GLY n 
2 401 SER n 
2 402 TYR n 
2 403 PHE n 
2 404 LEU n 
2 405 TYR n 
2 406 SER n 
2 407 LYS n 
2 408 LEU n 
2 409 ASN n 
2 410 VAL n 
2 411 LYS n 
2 412 LYS n 
2 413 GLU n 
2 414 LYS n 
2 415 TRP n 
2 416 GLN n 
2 417 GLN n 
2 418 GLY n 
2 419 ASN n 
2 420 THR n 
2 421 PHE n 
2 422 THR n 
2 423 CYS n 
2 424 SER n 
2 425 VAL n 
2 426 LEU n 
2 427 HIS n 
2 428 GLU n 
2 429 GLY n 
2 430 LEU n 
2 431 HIS n 
2 432 ASN n 
2 433 HIS n 
2 434 HIS n 
2 435 THR n 
2 436 GLU n 
2 437 LYS n 
2 438 SER n 
2 439 LEU n 
2 440 SER n 
2 441 HIS n 
2 442 SER n 
2 443 PRO n 
2 444 GLY n 
2 445 LYS n 
3 1   GLN n 
3 2   PHE n 
3 3   VAL n 
3 4   LEU n 
3 5   SER n 
3 6   GLN n 
3 7   PRO n 
3 8   ASN n 
3 9   SER n 
3 10  VAL n 
3 11  SER n 
3 12  THR n 
3 13  ASN n 
3 14  LEU n 
3 15  GLY n 
3 16  SER n 
3 17  THR n 
3 18  VAL n 
3 19  LYS n 
3 20  LEU n 
3 21  SER n 
3 22  CYS n 
3 23  LYS n 
3 24  ARG n 
3 25  SER n 
3 26  THR n 
3 27  GLY n 
3 28  ASN n 
3 29  ILE n 
3 30  GLY n 
3 31  SER n 
3 32  ASN n 
3 33  TYR n 
3 34  VAL n 
3 35  SER n 
3 36  TRP n 
3 37  TYR n 
3 38  GLN n 
3 39  HIS n 
3 40  HIS n 
3 41  GLU n 
3 42  GLY n 
3 43  ARG n 
3 44  SER n 
3 45  PRO n 
3 46  THR n 
3 47  THR n 
3 48  MET n 
3 49  ILE n 
3 50  TYR n 
3 51  ARG n 
3 52  ASP n 
3 53  ASP n 
3 54  GLN n 
3 55  ARG n 
3 56  PRO n 
3 57  ASP n 
3 58  GLY n 
3 59  VAL n 
3 60  PRO n 
3 61  ASP n 
3 62  ARG n 
3 63  PHE n 
3 64  SER n 
3 65  GLY n 
3 66  SER n 
3 67  ILE n 
3 68  ASP n 
3 69  ARG n 
3 70  SER n 
3 71  SER n 
3 72  ASN n 
3 73  SER n 
3 74  ALA n 
3 75  LEU n 
3 76  LEU n 
3 77  THR n 
3 78  ILE n 
3 79  ASP n 
3 80  ASN n 
3 81  VAL n 
3 82  GLN n 
3 83  THR n 
3 84  GLU n 
3 85  ASP n 
3 86  GLU n 
3 87  ALA n 
3 88  ALA n 
3 89  TYR n 
3 90  PHE n 
3 91  CYS n 
3 92  HIS n 
3 93  SER n 
3 94  TYR n 
3 95  SER n 
3 96  THR n 
3 97  GLY n 
3 98  MET n 
3 99  TYR n 
3 100 ILE n 
3 101 PHE n 
3 102 GLY n 
3 103 GLY n 
3 104 GLY n 
3 105 THR n 
3 106 LYS n 
3 107 LEU n 
3 108 THR n 
3 109 VAL n 
3 110 LEU n 
3 111 GLY n 
3 112 GLN n 
3 113 PRO n 
3 114 LYS n 
3 115 SER n 
3 116 THR n 
3 117 PRO n 
3 118 THR n 
3 119 LEU n 
3 120 THR n 
3 121 MET n 
3 122 PHE n 
3 123 PRO n 
3 124 PRO n 
3 125 SER n 
3 126 PRO n 
3 127 GLU n 
3 128 GLU n 
3 129 LEU n 
3 130 GLN n 
3 131 GLU n 
3 132 ASN n 
3 133 LYS n 
3 134 ALA n 
3 135 THR n 
3 136 LEU n 
3 137 VAL n 
3 138 CYS n 
3 139 LEU n 
3 140 ILE n 
3 141 SER n 
3 142 ASN n 
3 143 PHE n 
3 144 SER n 
3 145 PRO n 
3 146 SER n 
3 147 GLY n 
3 148 VAL n 
3 149 THR n 
3 150 VAL n 
3 151 ALA n 
3 152 TRP n 
3 153 LYS n 
3 154 ALA n 
3 155 ASN n 
3 156 GLY n 
3 157 THR n 
3 158 PRO n 
3 159 ILE n 
3 160 THR n 
3 161 GLN n 
3 162 GLY n 
3 163 VAL n 
3 164 ASP n 
3 165 THR n 
3 166 SER n 
3 167 ASN n 
3 168 PRO n 
3 169 THR n 
3 170 LYS n 
3 171 GLU n 
3 172 ASP n 
3 173 ASN n 
3 174 LYS n 
3 175 TYR n 
3 176 MET n 
3 177 ALA n 
3 178 SER n 
3 179 SER n 
3 180 PHE n 
3 181 LEU n 
3 182 HIS n 
3 183 LEU n 
3 184 THR n 
3 185 SER n 
3 186 ASP n 
3 187 GLN n 
3 188 TRP n 
3 189 ARG n 
3 190 SER n 
3 191 HIS n 
3 192 ASN n 
3 193 SER n 
3 194 PHE n 
3 195 THR n 
3 196 CYS n 
3 197 GLN n 
3 198 VAL n 
3 199 THR n 
3 200 HIS n 
3 201 GLU n 
3 202 GLY n 
3 203 ASN n 
3 204 THR n 
3 205 VAL n 
3 206 GLU n 
3 207 LYS n 
3 208 THR n 
3 209 VAL n 
3 210 SER n 
3 211 PRO n 
3 212 THR n 
3 213 GLU n 
3 214 CYS n 
3 215 VAL n 
3 216 ALA n 
4 1   MET n 
4 2   ASN n 
4 3   PHE n 
4 4   GLY n 
4 5   LEU n 
4 6   SER n 
4 7   LEU n 
4 8   ILE n 
4 9   PHE n 
4 10  LEU n 
4 11  VAL n 
4 12  LEU n 
4 13  VAL n 
4 14  LEU n 
4 15  LYS n 
4 16  GLY n 
4 17  VAL n 
4 18  GLN n 
4 19  CYS n 
4 20  GLU n 
4 21  VAL n 
4 22  MET n 
4 23  LEU n 
4 24  VAL n 
4 25  GLU n 
4 26  SER n 
4 27  GLY n 
4 28  GLY n 
4 29  ASP n 
4 30  LEU n 
4 31  VAL n 
4 32  LYS n 
4 33  PRO n 
4 34  GLY n 
4 35  GLY n 
4 36  SER n 
4 37  LEU n 
4 38  LYS n 
4 39  VAL n 
4 40  SER n 
4 41  CYS n 
4 42  ALA n 
4 43  ALA n 
4 44  SER n 
4 45  GLY n 
4 46  PHE n 
4 47  THR n 
4 48  PHE n 
4 49  SER n 
4 50  ASN n 
4 51  TYR n 
4 52  ALA n 
4 53  MET n 
4 54  SER n 
4 55  TRP n 
4 56  VAL n 
4 57  ARG n 
4 58  GLN n 
4 59  THR n 
4 60  PRO n 
4 61  GLU n 
4 62  LYS n 
4 63  ARG n 
4 64  LEU n 
4 65  GLU n 
4 66  TRP n 
4 67  VAL n 
4 68  ALA n 
4 69  THR n 
4 70  ILE n 
4 71  SER n 
4 72  SER n 
4 73  GLY n 
4 74  ALA n 
4 75  SER n 
4 76  TYR n 
4 77  THR n 
4 78  HIS n 
4 79  TYR n 
4 80  PRO n 
4 81  ASP n 
4 82  SER n 
4 83  VAL n 
4 84  LYS n 
4 85  GLY n 
4 86  ARG n 
4 87  PHE n 
4 88  THR n 
4 89  ILE n 
4 90  SER n 
4 91  ARG n 
4 92  ASP n 
4 93  ASN n 
4 94  ALA n 
4 95  LYS n 
4 96  ASN n 
4 97  THR n 
4 98  LEU n 
4 99  TYR n 
4 100 LEU n 
4 101 GLN n 
4 102 MET n 
4 103 SER n 
4 104 SER n 
4 105 LEU n 
4 106 ARG n 
4 107 SER n 
4 108 GLU n 
4 109 ASP n 
4 110 THR n 
4 111 ALA n 
4 112 MET n 
4 113 TYR n 
4 114 TYR n 
4 115 CYS n 
4 116 GLY n 
4 117 ARG n 
4 118 GLN n 
4 119 VAL n 
4 120 ASN n 
4 121 ARG n 
4 122 HIS n 
4 123 ASP n 
4 124 ARG n 
4 125 ALA n 
4 126 LEU n 
4 127 ASP n 
4 128 ALA n 
4 129 MET n 
4 130 ASP n 
4 131 TYR n 
4 132 TRP n 
4 133 GLY n 
4 134 GLN n 
4 135 GLY n 
4 136 THR n 
4 137 SER n 
4 138 VAL n 
4 139 THR n 
4 140 VAL n 
4 141 SER n 
4 142 PRO n 
4 143 ALA n 
4 144 LYS n 
4 145 THR n 
4 146 THR n 
4 147 PRO n 
4 148 PRO n 
4 149 SER n 
4 150 VAL n 
4 151 TYR n 
4 152 PRO n 
4 153 LEU n 
4 154 ALA n 
4 155 PRO n 
4 156 GLY n 
4 157 SER n 
4 158 ALA n 
4 159 ALA n 
4 160 GLN n 
4 161 THR n 
4 162 ASN n 
4 163 SER n 
4 164 MET n 
4 165 VAL n 
4 166 THR n 
4 167 LEU n 
4 168 GLY n 
4 169 CYS n 
4 170 LEU n 
4 171 VAL n 
4 172 LYS n 
4 173 GLY n 
4 174 TYR n 
4 175 PHE n 
4 176 PRO n 
4 177 GLU n 
4 178 PRO n 
4 179 VAL n 
4 180 THR n 
4 181 VAL n 
4 182 THR n 
4 183 TRP n 
4 184 ASN n 
4 185 SER n 
4 186 GLY n 
4 187 SER n 
4 188 LEU n 
4 189 SER n 
4 190 SER n 
4 191 GLY n 
4 192 VAL n 
4 193 HIS n 
4 194 THR n 
4 195 PHE n 
4 196 PRO n 
4 197 ALA n 
4 198 VAL n 
4 199 LEU n 
4 200 GLN n 
4 201 SER n 
4 202 ASP n 
4 203 LEU n 
4 204 TYR n 
4 205 THR n 
4 206 LEU n 
4 207 SER n 
4 208 SER n 
4 209 SER n 
4 210 VAL n 
4 211 THR n 
4 212 VAL n 
4 213 PRO n 
4 214 SER n 
4 215 SER n 
4 216 THR n 
4 217 TRP n 
4 218 PRO n 
4 219 SER n 
4 220 GLU n 
4 221 THR n 
4 222 VAL n 
4 223 THR n 
4 224 CYS n 
4 225 ASN n 
4 226 VAL n 
4 227 ALA n 
4 228 HIS n 
4 229 PRO n 
4 230 ALA n 
4 231 SER n 
4 232 SER n 
4 233 THR n 
4 234 LYS n 
4 235 VAL n 
4 236 ASP n 
4 237 LYS n 
4 238 LYS n 
4 239 ILE n 
4 240 VAL n 
4 241 PRO n 
4 242 ARG n 
4 243 ASP n 
4 244 CYS n 
4 245 GLY n 
4 246 CYS n 
4 247 LYS n 
4 248 PRO n 
4 249 CYS n 
4 250 ILE n 
4 251 CYS n 
4 252 THR n 
4 253 VAL n 
4 254 PRO n 
4 255 GLU n 
4 256 VAL n 
4 257 SER n 
4 258 SER n 
4 259 VAL n 
4 260 PHE n 
4 261 ILE n 
4 262 PHE n 
4 263 PRO n 
4 264 PRO n 
4 265 LYS n 
4 266 PRO n 
4 267 LYS n 
4 268 ASP n 
4 269 VAL n 
4 270 LEU n 
4 271 THR n 
4 272 ILE n 
4 273 THR n 
4 274 LEU n 
4 275 THR n 
4 276 PRO n 
4 277 LYS n 
4 278 VAL n 
4 279 THR n 
4 280 CYS n 
4 281 VAL n 
4 282 VAL n 
4 283 VAL n 
4 284 ASP n 
4 285 ILE n 
4 286 SER n 
4 287 LYS n 
4 288 ASP n 
4 289 ASP n 
4 290 PRO n 
4 291 GLU n 
4 292 VAL n 
4 293 GLN n 
4 294 PHE n 
4 295 SER n 
4 296 TRP n 
4 297 PHE n 
4 298 VAL n 
4 299 ASP n 
4 300 ASP n 
4 301 VAL n 
4 302 GLU n 
4 303 VAL n 
4 304 HIS n 
4 305 THR n 
4 306 ALA n 
4 307 GLN n 
4 308 THR n 
4 309 GLN n 
4 310 PRO n 
4 311 ARG n 
4 312 GLU n 
4 313 GLU n 
4 314 GLN n 
4 315 PHE n 
4 316 ASN n 
4 317 SER n 
4 318 THR n 
4 319 PHE n 
4 320 ARG n 
4 321 SER n 
4 322 VAL n 
4 323 SER n 
4 324 GLU n 
4 325 LEU n 
4 326 PRO n 
4 327 ILE n 
4 328 MET n 
4 329 HIS n 
4 330 GLN n 
4 331 ASP n 
4 332 TRP n 
4 333 LEU n 
4 334 ASN n 
4 335 GLY n 
4 336 LYS n 
4 337 GLU n 
4 338 PHE n 
4 339 LYS n 
4 340 CYS n 
4 341 ARG n 
4 342 VAL n 
4 343 ASN n 
4 344 SER n 
4 345 ALA n 
4 346 ALA n 
4 347 PHE n 
4 348 PRO n 
4 349 ALA n 
4 350 PRO n 
4 351 ILE n 
4 352 GLU n 
4 353 LYS n 
4 354 THR n 
4 355 ILE n 
4 356 SER n 
4 357 LYS n 
4 358 THR n 
4 359 LYS n 
4 360 GLY n 
4 361 ARG n 
4 362 PRO n 
4 363 LYS n 
4 364 ALA n 
4 365 PRO n 
4 366 GLN n 
4 367 VAL n 
4 368 TYR n 
4 369 THR n 
4 370 ILE n 
4 371 PRO n 
4 372 PRO n 
4 373 PRO n 
4 374 LYS n 
4 375 GLU n 
4 376 GLN n 
4 377 MET n 
4 378 ALA n 
4 379 LYS n 
4 380 ASP n 
4 381 LYS n 
4 382 VAL n 
4 383 SER n 
4 384 LEU n 
4 385 THR n 
4 386 CYS n 
4 387 MET n 
4 388 ILE n 
4 389 THR n 
4 390 ASP n 
4 391 PHE n 
4 392 PHE n 
4 393 PRO n 
4 394 GLU n 
4 395 ASP n 
4 396 ILE n 
4 397 THR n 
4 398 VAL n 
4 399 GLU n 
4 400 TRP n 
4 401 GLN n 
4 402 TRP n 
4 403 ASN n 
4 404 GLY n 
4 405 GLN n 
4 406 PRO n 
4 407 ALA n 
4 408 GLU n 
4 409 ASN n 
4 410 TYR n 
4 411 LYS n 
4 412 ASN n 
4 413 THR n 
4 414 GLN n 
4 415 PRO n 
4 416 ILE n 
4 417 MET n 
4 418 ASP n 
4 419 THR n 
4 420 ASP n 
4 421 GLY n 
4 422 SER n 
4 423 TYR n 
4 424 PHE n 
4 425 VAL n 
4 426 TYR n 
4 427 SER n 
4 428 LYS n 
4 429 LEU n 
4 430 ASN n 
4 431 VAL n 
4 432 GLN n 
4 433 LYS n 
4 434 SER n 
4 435 ASN n 
4 436 TRP n 
4 437 GLU n 
4 438 ALA n 
4 439 GLY n 
4 440 ASN n 
4 441 THR n 
4 442 PHE n 
4 443 THR n 
4 444 CYS n 
4 445 SER n 
4 446 VAL n 
4 447 LEU n 
4 448 HIS n 
4 449 GLU n 
4 450 GLY n 
4 451 LEU n 
4 452 HIS n 
4 453 ASN n 
4 454 HIS n 
4 455 HIS n 
4 456 THR n 
4 457 GLU n 
4 458 LYS n 
4 459 SER n 
4 460 LEU n 
4 461 SER n 
4 462 HIS n 
4 463 SER n 
4 464 PRO n 
4 465 GLY n 
4 466 LYS n 
5 1   MET n 
5 2   ASP n 
5 3   SER n 
5 4   GLN n 
5 5   ALA n 
5 6   GLN n 
5 7   VAL n 
5 8   LEU n 
5 9   MET n 
5 10  LEU n 
5 11  LEU n 
5 12  LEU n 
5 13  LEU n 
5 14  TRP n 
5 15  VAL n 
5 16  SER n 
5 17  GLY n 
5 18  THR n 
5 19  CYS n 
5 20  GLY n 
5 21  ASP n 
5 22  ILE n 
5 23  VAL n 
5 24  MET n 
5 25  SER n 
5 26  GLN n 
5 27  SER n 
5 28  PRO n 
5 29  SER n 
5 30  SER n 
5 31  LEU n 
5 32  ALA n 
5 33  VAL n 
5 34  SER n 
5 35  VAL n 
5 36  GLY n 
5 37  GLU n 
5 38  LYS n 
5 39  VAL n 
5 40  THR n 
5 41  MET n 
5 42  SER n 
5 43  CYS n 
5 44  LYS n 
5 45  SER n 
5 46  SER n 
5 47  GLN n 
5 48  SER n 
5 49  LEU n 
5 50  PHE n 
5 51  TYR n 
5 52  SER n 
5 53  SER n 
5 54  ASN n 
5 55  GLN n 
5 56  LYS n 
5 57  ASN n 
5 58  TYR n 
5 59  LEU n 
5 60  ALA n 
5 61  TRP n 
5 62  TYR n 
5 63  GLN n 
5 64  GLN n 
5 65  LYS n 
5 66  PRO n 
5 67  GLY n 
5 68  GLN n 
5 69  SER n 
5 70  PRO n 
5 71  LYS n 
5 72  LEU n 
5 73  LEU n 
5 74  ILE n 
5 75  TYR n 
5 76  TRP n 
5 77  ALA n 
5 78  SER n 
5 79  THR n 
5 80  ARG n 
5 81  GLU n 
5 82  SER n 
5 83  GLY n 
5 84  VAL n 
5 85  PRO n 
5 86  ASP n 
5 87  ARG n 
5 88  PHE n 
5 89  THR n 
5 90  GLY n 
5 91  SER n 
5 92  GLY n 
5 93  SER n 
5 94  GLY n 
5 95  THR n 
5 96  ASP n 
5 97  PHE n 
5 98  THR n 
5 99  LEU n 
5 100 THR n 
5 101 ILE n 
5 102 SER n 
5 103 SER n 
5 104 VAL n 
5 105 LYS n 
5 106 ALA n 
5 107 GLU n 
5 108 ASP n 
5 109 LEU n 
5 110 ALA n 
5 111 VAL n 
5 112 TYR n 
5 113 TYR n 
5 114 CYS n 
5 115 GLN n 
5 116 GLN n 
5 117 TYR n 
5 118 TYR n 
5 119 SER n 
5 120 TYR n 
5 121 PRO n 
5 122 PRO n 
5 123 THR n 
5 124 PHE n 
5 125 GLY n 
5 126 GLY n 
5 127 GLY n 
5 128 THR n 
5 129 LYS n 
5 130 LEU n 
5 131 GLU n 
5 132 ILE n 
5 133 LYS n 
5 134 ARG n 
5 135 ALA n 
5 136 ASP n 
5 137 ALA n 
5 138 ALA n 
5 139 PRO n 
5 140 THR n 
5 141 VAL n 
5 142 SER n 
5 143 ILE n 
5 144 PHE n 
5 145 PRO n 
5 146 PRO n 
5 147 SER n 
5 148 SER n 
5 149 GLU n 
5 150 GLN n 
5 151 LEU n 
5 152 THR n 
5 153 SER n 
5 154 GLY n 
5 155 GLY n 
5 156 ALA n 
5 157 SER n 
5 158 VAL n 
5 159 VAL n 
5 160 CYS n 
5 161 PHE n 
5 162 LEU n 
5 163 ASN n 
5 164 ASN n 
5 165 PHE n 
5 166 TYR n 
5 167 PRO n 
5 168 LYS n 
5 169 ASP n 
5 170 ILE n 
5 171 ASN n 
5 172 VAL n 
5 173 LYS n 
5 174 TRP n 
5 175 LYS n 
5 176 ILE n 
5 177 ASP n 
5 178 GLY n 
5 179 SER n 
5 180 GLU n 
5 181 ARG n 
5 182 GLN n 
5 183 ASN n 
5 184 GLY n 
5 185 VAL n 
5 186 LEU n 
5 187 ASN n 
5 188 SER n 
5 189 TRP n 
5 190 THR n 
5 191 ASP n 
5 192 GLN n 
5 193 ASP n 
5 194 SER n 
5 195 LYS n 
5 196 ASP n 
5 197 SER n 
5 198 THR n 
5 199 TYR n 
5 200 SER n 
5 201 MET n 
5 202 SER n 
5 203 SER n 
5 204 THR n 
5 205 LEU n 
5 206 THR n 
5 207 LEU n 
5 208 THR n 
5 209 LYS n 
5 210 ASP n 
5 211 GLU n 
5 212 TYR n 
5 213 GLU n 
5 214 ARG n 
5 215 HIS n 
5 216 ASN n 
5 217 SER n 
5 218 TYR n 
5 219 THR n 
5 220 CYS n 
5 221 GLU n 
5 222 ALA n 
5 223 THR n 
5 224 HIS n 
5 225 LYS n 
5 226 THR n 
5 227 SER n 
5 228 THR n 
5 229 SER n 
5 230 PRO n 
5 231 ILE n 
5 232 VAL n 
5 233 LYS n 
5 234 SER n 
5 235 PHE n 
5 236 ASN n 
5 237 ARG n 
5 238 ASN n 
5 239 GLU n 
5 240 CYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 448 'malaria parasite P. falciparum' ? 'PF45/48, PFS45-48, PFS45/48, PF13_0247, PF3D7_1346700' 
? ? ? ? ? ? 'Plasmodium falciparum' 5833  ? ? ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 445 ?                                ? ?                                                       
? ? ? ? ? ? 'Rattus norvegicus'     10116 ? ? ? ? ? ? ? ? 'Rattus norvegicus' 10116 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 216 ?                                ? ?                                                       
? ? ? ? ? ? 'Rattus norvegicus'     10116 ? ? ? ? ? ? ? ? 'Rattus norvegicus' 10116 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 466 ?                                ? ?                                                       
? ? ? ? ? ? 'Mus musculus'          10090 ? ? ? ? ? ? ? ? 'Mus musculus'      10090 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5 1 sample 'Biological sequence' 1 240 ?                                ? ?                                                       
? ? ? ? ? ? 'Mus musculus'          10090 ? ? ? ? ? ? ? ? 'Mus musculus'      10090 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP P4548_PLAF7 Q8I6T1 ? 1 
;MMLYISAKKAQVAFILYIVLVLRIISGNNDFCKPSSLNSEISGFIGYKCNFSNEGVHNLKPDMRERRSIFCTIHSYFIYD
KIRLIIPKKSSSPEFKILPEKCFQKVYTDYENRVETDISELGLIEYEIEENDTNPNYNERTITISPFSPKDIEFFCFCDN
TEKVISSIEGRSAMVHVRVLKYPHNILFTNLTNDLFTYLPKTYNESNFVSNVLEVELNDGELFVLACELINKKCFQEGKE
KALYKSNKIIYHKNLTIFKAPFYVTSKDVNTECTCKFKNNNYKIVLKPKYEKKVIHGCNFSSNVSSKHTFTDSLDISLVD
DSAHISCNVHLSEPKYNHLVGLNCPGDIIPDCFFQVYQPESEELEPSNIVYLDSQINIGDIEYYEDAEGDDKIKLFGIVG
SIPKTTSFTCICKKDKKSAYMTVTIDSAYYGFLAKTFIFLIVAILLYI
;
1 
2 PDB 7ZXF        7ZXF   ? 2 ? 1 
3 PDB 7ZXF        7ZXF   ? 3 ? 1 
4 PDB 7ZXF        7ZXF   ? 4 ? 1 
5 PDB 7ZXF        7ZXF   ? 5 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7ZXF A 1 ? 448 ? Q8I6T1 1   ? 448 ? -1  448 
2 2 7ZXF B 1 ? 445 ? 7ZXF   1   ? 445 ? 1   445 
3 3 7ZXF C 1 ? 216 ? 7ZXF   1   ? 216 ? 1   216 
4 4 7ZXF D 1 ? 466 ? 7ZXF   -18 ? 447 ? -18 447 
5 5 7ZXF E 1 ? 240 ? 7ZXF   -19 ? 220 ? -19 220 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'           y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'           y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      
180.156 
CYS 'L-peptide linking'           y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'           y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'             y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'           y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking'           y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose                    'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6' 
180.156 
MET 'L-peptide linking'           y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'           y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   7ZXF 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.63 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.20 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Lithium sulfate, 0.1M HEPES pH 7.0 and 20 % w/v Polyvinylpyrrolidone' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-12-18 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99998 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99998 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          189.87 
_reflns.entry_id                                       7ZXF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.72 
_reflns.d_resolution_low                               108 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     456518 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           94.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                26.8 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
_reflns.pdbx_CC_split_method                           ? 
# 
_reflns_shell.d_res_high                                    3.72 
_reflns_shell.d_res_low                                     4.06 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             56247 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.875 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.377 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               216.24 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7ZXF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.72 
_refine.ls_d_res_low                             70.16 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     16937 
_refine.ls_number_reflns_R_free                  869 
_refine.ls_number_reflns_R_work                  16068 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    84.60 
_refine.ls_percent_reflns_R_free                 5.13 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2817 
_refine.ls_R_factor_R_free                       0.2976 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2809 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      6H5N 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 39.7104 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.5504 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.72 
_refine_hist.d_res_low                        70.16 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               9384 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        9284 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         100 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0028  ? 9606  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5996  ? 13061 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0610  ? 1498  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0047  ? 1645  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.6041 ? 3486  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 3.72 3.96  . . 65  919  30.22  . . . 0.4436 . 0.3899 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.96 4.26  . . 113 2487 79.10  . . . 0.3815 . 0.3761 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.26 4.69  . . 143 3025 96.56  . . . 0.3210 . 0.3151 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.69 5.37  . . 163 3147 100.00 . . . 0.3222 . 0.2994 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.37 6.76  . . 213 3150 99.97  . . . 0.3155 . 0.3228 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 6.76 70.16 . . 172 3340 99.69  . . . 0.2684 . 0.2441 . . . . . . . . . . . 
# 
_struct.entry_id                                   7ZXF 
_struct.title                                      'Pfs48/45 bound to monoclonal antibodies 10D8 and 85RF45.1' 
_struct.pdbx_structure_determination_methodology   ? 
_struct.pdbx_model_details                         ? 
_struct.pdbx_formula_weight                        ? 
_struct.pdbx_formula_weight_method                 ? 
_struct.pdbx_model_type_details                    ? 
_struct.pdbx_CASP_flag                             N 
# 
_struct_keywords.entry_id        7ZXF 
_struct_keywords.text            'Pfs48/45, malaria, transmission-blocking, Plasmodium falciparum, gamete, antibody, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 204 ? PHE A 208 ? ASN A 204 PHE A 208 5 ? 5 
HELX_P HELX_P2  AA2 LEU A 372 ? ASN A 377 ? LEU A 372 ASN A 377 1 ? 6 
HELX_P HELX_P3  AA3 THR B 28  ? TYR B 32  ? THR B 28  TYR B 32  5 ? 5 
HELX_P HELX_P4  AA4 PRO B 61  ? LYS B 65  ? PRO B 61  LYS B 65  5 ? 5 
HELX_P HELX_P5  AA5 ARG B 87  ? THR B 91  ? ARG B 87  THR B 91  5 ? 5 
HELX_P HELX_P6  AA6 ASN C 28  ? ASN C 32  ? ASN C 28  ASN C 32  5 ? 5 
HELX_P HELX_P7  AA7 GLN C 82  ? GLU C 86  ? GLN C 82  GLU C 86  5 ? 5 
HELX_P HELX_P8  AA8 SER C 125 ? GLU C 131 ? SER C 125 GLU C 131 1 ? 7 
HELX_P HELX_P9  AA9 THR C 184 ? HIS C 191 ? THR C 184 HIS C 191 1 ? 8 
HELX_P HELX_P10 AB1 THR D 47  ? TYR D 51  ? THR D 28  TYR D 32  5 ? 5 
HELX_P HELX_P11 AB2 ARG D 106 ? THR D 110 ? ARG D 87  THR D 91  5 ? 5 
HELX_P HELX_P12 AB3 SER E 147 ? GLY E 154 ? SER E 127 GLY E 134 1 ? 8 
HELX_P HELX_P13 AB4 LYS E 209 ? GLU E 213 ? LYS E 189 GLU E 193 1 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 49  SG  ? ? ? 1_555 A CYS 71  SG ? ? A CYS 47  A CYS 73  1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf2  disulf ?    ? A CYS 102 SG  ? ? ? 1_555 A CYS 156 SG ? ? A CYS 104 A CYS 158 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf3  disulf ?    ? A CYS 227 SG  ? ? ? 1_555 A CYS 275 SG ? ? A CYS 227 A CYS 275 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf4  disulf ?    ? A CYS 234 SG  ? ? ? 1_555 A CYS 273 SG ? ? A CYS 234 A CYS 273 1_555 ? ? ? ? ? ? ? 2.041 ? ?               
disulf5  disulf ?    ? A CYS 298 SG  ? ? ? 1_555 A CYS 327 SG ? ? A CYS 298 A CYS 327 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf6  disulf ?    ? A CYS 344 SG  ? ? ? 1_555 A CYS 412 SG ? ? A CYS 344 A CYS 412 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf7  disulf ?    ? A CYS 352 SG  ? ? ? 1_555 A CYS 410 SG ? ? A CYS 352 A CYS 410 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf8  disulf ?    ? B CYS 22  SG  ? ? ? 1_555 B CYS 96  SG ? ? B CYS 22  B CYS 96  1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf9  disulf ?    ? B CYS 146 SG  ? ? ? 1_555 B CYS 201 SG ? ? B CYS 146 B CYS 201 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf10 disulf ?    ? C CYS 22  SG  ? ? ? 1_555 C CYS 91  SG ? ? C CYS 22  C CYS 91  1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf11 disulf ?    ? C CYS 138 SG  ? ? ? 1_555 C CYS 196 SG ? ? C CYS 138 C CYS 196 1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf12 disulf ?    ? D CYS 41  SG  ? ? ? 1_555 D CYS 115 SG ? ? D CYS 22  D CYS 96  1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf13 disulf ?    ? D CYS 169 SG  ? ? ? 1_555 D CYS 224 SG ? ? D CYS 150 D CYS 205 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf14 disulf ?    ? E CYS 43  SG  ? ? ? 1_555 E CYS 114 SG ? ? E CYS 23  E CYS 94  1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf15 disulf ?    ? E CYS 160 SG  ? ? ? 1_555 E CYS 220 SG ? ? E CYS 140 E CYS 200 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
covale1  covale one  ? A ASN 190 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 190 G NAG 1   1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale2  covale one  ? A ASN 204 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 204 F NAG 1   1_555 ? ? ? ? ? ? ? 1.447 ? N-Glycosylation 
covale3  covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? F NAG 1   F NAG 2   1_555 ? ? ? ? ? ? ? 1.449 ? ?               
covale4  covale both ? F NAG .   O4  ? ? ? 1_555 F BMA .   C1 ? ? F NAG 2   F BMA 3   1_555 ? ? ? ? ? ? ? 1.476 ? ?               
covale5  covale both ? F BMA .   O3  ? ? ? 1_555 F MAN .   C1 ? ? F BMA 3   F MAN 4   1_555 ? ? ? ? ? ? ? 1.445 ? ?               
covale6  covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.449 ? ?               
covale7  covale both ? G NAG .   O4  ? ? ? 1_555 G BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.429 ? ?               
covale8  covale both ? G BMA .   O3  ? ? ? 1_555 G MAN .   C1 ? ? G BMA 3   G MAN 4   1_555 ? ? ? ? ? ? ? 1.445 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  LEU 98  A . ? LEU 100 A PRO 99  A ? PRO 101 A 1 0.96  
2  ILE 349 A . ? ILE 349 A PRO 350 A ? PRO 350 A 1 -4.41 
3  CYS 352 A . ? CYS 352 A PHE 353 A ? PHE 353 A 1 4.70  
4  GLN 358 A . ? GLN 358 A PRO 359 A ? PRO 359 A 1 -1.05 
5  PHE 152 B . ? PHE 152 B PRO 153 B ? PRO 153 B 1 1.46  
6  GLU 154 B . ? GLU 154 B PRO 155 B ? PRO 155 B 1 -5.42 
7  TRP 194 B . ? TRP 194 B PRO 195 B ? PRO 195 B 1 3.52  
8  SER 144 C . ? SER 144 C PRO 145 C ? PRO 145 C 1 -1.69 
9  PHE 175 D . ? PHE 156 D PRO 176 D ? PRO 157 D 1 -0.37 
10 GLU 177 D . ? GLU 158 D PRO 178 D ? PRO 159 D 1 1.47  
11 TRP 217 D . ? TRP 198 D PRO 218 D ? PRO 199 D 1 3.19  
12 SER 27  E . ? SER 7   E PRO 28  E ? PRO 8   E 1 -0.19 
13 TYR 120 E . ? TYR 100 E PRO 121 E ? PRO 101 E 1 -1.80 
14 TYR 166 E . ? TYR 146 E PRO 167 E ? PRO 147 E 1 2.59  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 5 ? 
AA7 ? 3 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 6 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 3 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 5 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 4 ? 
AC4 ? 4 ? 
AC5 ? 4 ? 
AC6 ? 2 ? 
AC7 ? 5 ? 
AC8 ? 5 ? 
AC9 ? 4 ? 
AD1 ? 3 ? 
AD2 ? 4 ? 
AD3 ? 2 ? 
AD4 ? 4 ? 
AD5 ? 4 ? 
AD6 ? 4 ? 
AD7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB2 5 6 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC6 1 2 ? parallel      
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC7 4 5 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC8 4 5 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD3 1 2 ? parallel      
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
AD7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 48  ? ASN A 50  ? LYS A 46  ASN A 48  
AA1 2 ASP A 80  ? ILE A 85  ? ASP A 82  ILE A 87  
AA1 3 GLU A 139 ? ILE A 144 ? GLU A 141 ILE A 146 
AA1 4 TYR A 126 ? ASN A 131 ? TYR A 128 ASN A 133 
AA2 1 ILE A 73  ? SER A 75  ? ILE A 75  SER A 77  
AA2 2 VAL A 175 ? VAL A 179 ? VAL A 175 VAL A 179 
AA2 3 ILE A 152 ? CYS A 156 ? ILE A 154 CYS A 158 
AA3 1 LYS A 105 ? VAL A 106 ? LYS A 107 VAL A 108 
AA3 2 THR A 116 ? ASP A 117 ? THR A 118 ASP A 119 
AA4 1 ILE A 186 ? ASN A 190 ? ILE A 186 ASN A 190 
AA4 2 LEU A 222 ? ALA A 226 ? LEU A 222 ALA A 226 
AA4 3 LEU A 255 ? LYS A 259 ? LEU A 255 LYS A 259 
AA4 4 LYS A 248 ? HIS A 252 ? LYS A 248 HIS A 252 
AA5 1 VAL A 212 ? LEU A 217 ? VAL A 212 LEU A 217 
AA5 2 ASN A 280 ? PRO A 288 ? ASN A 280 PRO A 288 
AA5 3 THR A 271 ? PHE A 277 ? THR A 271 PHE A 277 
AA5 4 GLU A 228 ? CYS A 234 ? GLU A 228 CYS A 234 
AA6 1 PHE A 310 ? SER A 313 ? PHE A 310 SER A 313 
AA6 2 ILE A 295 ? ASN A 299 ? ILE A 295 ASN A 299 
AA6 3 ASN A 337 ? CYS A 344 ? ASN A 337 CYS A 344 
AA6 4 LYS A 392 ? VAL A 399 ? LYS A 392 VAL A 399 
AA6 5 GLU A 382 ? ASP A 386 ? GLU A 382 ASP A 386 
AA7 1 SER A 326 ? CYS A 327 ? SER A 326 CYS A 327 
AA7 2 LYS A 417 ? ILE A 425 ? LYS A 417 ILE A 425 
AA7 3 HIS A 330 ? LEU A 331 ? HIS A 330 LEU A 331 
AA8 1 SER A 326 ? CYS A 327 ? SER A 326 CYS A 327 
AA8 2 LYS A 417 ? ILE A 425 ? LYS A 417 ILE A 425 
AA8 3 THR A 406 ? LYS A 414 ? THR A 406 LYS A 414 
AA8 4 ASP A 347 ? ILE A 349 ? ASP A 347 ILE A 349 
AA9 1 GLN A 355 ? TYR A 357 ? GLN A 355 TYR A 357 
AA9 2 ILE A 369 ? TYR A 371 ? ILE A 369 TYR A 371 
AB1 1 VAL B 5   ? SER B 7   ? VAL B 5   SER B 7   
AB1 2 LEU B 18  ? VAL B 23  ? LEU B 18  VAL B 23  
AB1 3 THR B 78  ? MET B 83  ? THR B 78  MET B 83  
AB1 4 PHE B 68  ? ASP B 73  ? PHE B 68  ASP B 73  
AB2 1 LEU B 11  ? LEU B 12  ? LEU B 11  LEU B 12  
AB2 2 VAL B 113 ? VAL B 117 ? VAL B 113 VAL B 117 
AB2 3 ALA B 92  ? LEU B 100 ? ALA B 92  LEU B 100 
AB2 4 TRP B 33  ? GLN B 39  ? TRP B 33  GLN B 39  
AB2 5 LEU B 45  ? ILE B 51  ? LEU B 45  ILE B 51  
AB2 6 ILE B 58  ? TYR B 59  ? ILE B 58  TYR B 59  
AB3 1 LEU B 11  ? LEU B 12  ? LEU B 11  LEU B 12  
AB3 2 VAL B 113 ? VAL B 117 ? VAL B 113 VAL B 117 
AB3 3 ALA B 92  ? LEU B 100 ? ALA B 92  LEU B 100 
AB3 4 TYR B 105 ? TRP B 109 ? TYR B 105 TRP B 109 
AB4 1 SER B 126 ? VAL B 127 ? SER B 126 VAL B 127 
AB4 2 LEU B 144 ? TYR B 151 ? LEU B 144 TYR B 151 
AB4 3 TYR B 181 ? VAL B 187 ? TYR B 181 VAL B 187 
AB4 4 VAL B 169 ? THR B 171 ? VAL B 169 THR B 171 
AB5 1 SER B 126 ? VAL B 127 ? SER B 126 VAL B 127 
AB5 2 LEU B 144 ? TYR B 151 ? LEU B 144 TYR B 151 
AB5 3 TYR B 181 ? VAL B 187 ? TYR B 181 VAL B 187 
AB5 4 VAL B 175 ? LEU B 176 ? VAL B 175 LEU B 176 
AB6 1 THR B 157 ? TRP B 160 ? THR B 157 TRP B 160 
AB6 2 THR B 200 ? HIS B 205 ? THR B 200 HIS B 205 
AB6 3 THR B 210 ? LYS B 215 ? THR B 210 LYS B 215 
AB7 1 LEU C 4   ? SER C 5   ? LEU C 4   SER C 5   
AB7 2 VAL C 18  ? ARG C 24  ? VAL C 18  ARG C 24  
AB7 3 SER C 73  ? ILE C 78  ? SER C 73  ILE C 78  
AB7 4 PHE C 63  ? SER C 64  ? PHE C 63  SER C 64  
AB8 1 LEU C 4   ? SER C 5   ? LEU C 4   SER C 5   
AB8 2 VAL C 18  ? ARG C 24  ? VAL C 18  ARG C 24  
AB8 3 SER C 73  ? ILE C 78  ? SER C 73  ILE C 78  
AB8 4 ILE C 67  ? ASP C 68  ? ILE C 67  ASP C 68  
AB9 1 SER C 9   ? THR C 12  ? SER C 9   THR C 12  
AB9 2 THR C 105 ? VAL C 109 ? THR C 105 VAL C 109 
AB9 3 ALA C 88  ? SER C 95  ? ALA C 88  SER C 95  
AB9 4 VAL C 34  ? HIS C 39  ? VAL C 34  HIS C 39  
AB9 5 THR C 46  ? ILE C 49  ? THR C 46  ILE C 49  
AC1 1 SER C 9   ? THR C 12  ? SER C 9   THR C 12  
AC1 2 THR C 105 ? VAL C 109 ? THR C 105 VAL C 109 
AC1 3 ALA C 88  ? SER C 95  ? ALA C 88  SER C 95  
AC1 4 MET C 98  ? PHE C 101 ? MET C 98  PHE C 101 
AC2 1 THR C 118 ? PHE C 122 ? THR C 118 PHE C 122 
AC2 2 ALA C 134 ? PHE C 143 ? ALA C 134 PHE C 143 
AC2 3 TYR C 175 ? LEU C 183 ? TYR C 175 LEU C 183 
AC2 4 VAL C 163 ? THR C 165 ? VAL C 163 THR C 165 
AC3 1 THR C 118 ? PHE C 122 ? THR C 118 PHE C 122 
AC3 2 ALA C 134 ? PHE C 143 ? ALA C 134 PHE C 143 
AC3 3 TYR C 175 ? LEU C 183 ? TYR C 175 LEU C 183 
AC3 4 THR C 169 ? LYS C 170 ? THR C 169 LYS C 170 
AC4 1 THR C 157 ? PRO C 158 ? THR C 157 PRO C 158 
AC4 2 VAL C 148 ? ALA C 154 ? VAL C 148 ALA C 154 
AC4 3 PHE C 194 ? HIS C 200 ? PHE C 194 HIS C 200 
AC4 4 ASN C 203 ? VAL C 209 ? ASN C 203 VAL C 209 
AC5 1 MET D 22  ? SER D 26  ? MET D 3   SER D 7   
AC5 2 LEU D 37  ? SER D 44  ? LEU D 18  SER D 25  
AC5 3 THR D 97  ? MET D 102 ? THR D 78  MET D 83  
AC5 4 PHE D 87  ? ASP D 92  ? PHE D 68  ASP D 73  
AC6 1 LEU D 30  ? VAL D 31  ? LEU D 11  VAL D 12  
AC6 2 THR D 139 ? VAL D 140 ? THR D 120 VAL D 121 
AC7 1 THR D 77  ? HIS D 78  ? THR D 58  HIS D 59  
AC7 2 LEU D 64  ? ILE D 70  ? LEU D 45  ILE D 51  
AC7 3 MET D 53  ? GLN D 58  ? MET D 34  GLN D 39  
AC7 4 MET D 112 ? GLN D 118 ? MET D 93  GLN D 99  
AC7 5 MET D 129 ? TYR D 131 ? MET D 110 TYR D 112 
AC8 1 THR D 77  ? HIS D 78  ? THR D 58  HIS D 59  
AC8 2 LEU D 64  ? ILE D 70  ? LEU D 45  ILE D 51  
AC8 3 MET D 53  ? GLN D 58  ? MET D 34  GLN D 39  
AC8 4 MET D 112 ? GLN D 118 ? MET D 93  GLN D 99  
AC8 5 THR D 136 ? SER D 137 ? THR D 117 SER D 118 
AC9 1 SER D 149 ? LEU D 153 ? SER D 130 LEU D 134 
AC9 2 THR D 166 ? TYR D 174 ? THR D 147 TYR D 155 
AC9 3 TYR D 204 ? THR D 211 ? TYR D 185 THR D 192 
AC9 4 VAL D 192 ? LEU D 199 ? VAL D 173 LEU D 180 
AD1 1 THR D 180 ? TRP D 183 ? THR D 161 TRP D 164 
AD1 2 THR D 223 ? HIS D 228 ? THR D 204 HIS D 209 
AD1 3 THR D 233 ? LYS D 238 ? THR D 214 LYS D 219 
AD2 1 MET E 24  ? SER E 27  ? MET E 4   SER E 7   
AD2 2 VAL E 39  ? SER E 45  ? VAL E 19  SER E 25  
AD2 3 ASP E 96  ? ILE E 101 ? ASP E 76  ILE E 81  
AD2 4 SER E 91  ? SER E 93  ? SER E 71  SER E 73  
AD3 1 ALA E 32  ? VAL E 33  ? ALA E 12  VAL E 13  
AD3 2 GLU E 131 ? ILE E 132 ? GLU E 111 ILE E 112 
AD4 1 THR E 79  ? ARG E 80  ? THR E 59  ARG E 60  
AD4 2 PRO E 70  ? TYR E 75  ? PRO E 50  TYR E 55  
AD4 3 LEU E 59  ? GLN E 64  ? LEU E 39  GLN E 44  
AD4 4 VAL E 111 ? GLN E 116 ? VAL E 91  GLN E 96  
AD5 1 ILE E 143 ? PHE E 144 ? ILE E 123 PHE E 124 
AD5 2 GLY E 155 ? CYS E 160 ? GLY E 135 CYS E 140 
AD5 3 TYR E 199 ? THR E 208 ? TYR E 179 THR E 188 
AD5 4 LEU E 162 ? PHE E 165 ? LEU E 142 PHE E 145 
AD6 1 ILE E 143 ? PHE E 144 ? ILE E 123 PHE E 124 
AD6 2 GLY E 155 ? CYS E 160 ? GLY E 135 CYS E 140 
AD6 3 TYR E 199 ? THR E 208 ? TYR E 179 THR E 188 
AD6 4 VAL E 185 ? TRP E 189 ? VAL E 165 TRP E 169 
AD7 1 SER E 179 ? GLU E 180 ? SER E 159 GLU E 160 
AD7 2 ASN E 171 ? ILE E 176 ? ASN E 151 ILE E 156 
AD7 3 SER E 217 ? THR E 223 ? SER E 197 THR E 203 
AD7 4 ILE E 231 ? ASN E 236 ? ILE E 211 ASN E 216 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N CYS A 49  ? N CYS A 47  O ARG A 83  ? O ARG A 85  
AA1 2 3 N ILE A 82  ? N ILE A 84  O ILE A 142 ? O ILE A 144 
AA1 3 4 O THR A 143 ? O THR A 145 N GLU A 127 ? N GLU A 129 
AA2 1 2 N ILE A 73  ? N ILE A 75  O ARG A 178 ? O ARG A 178 
AA2 2 3 O VAL A 177 ? O VAL A 177 N PHE A 154 ? N PHE A 156 
AA3 1 2 N VAL A 106 ? N VAL A 108 O THR A 116 ? O THR A 118 
AA4 1 2 N LEU A 187 ? N LEU A 187 O VAL A 224 ? O VAL A 224 
AA4 2 3 N PHE A 223 ? N PHE A 223 O PHE A 258 ? O PHE A 258 
AA4 3 4 O LEU A 255 ? O LEU A 255 N HIS A 252 ? N HIS A 252 
AA5 1 2 N LEU A 213 ? N LEU A 213 O VAL A 285 ? O VAL A 285 
AA5 2 3 O TYR A 282 ? O TYR A 282 N CYS A 275 ? N CYS A 275 
AA5 3 4 O LYS A 276 ? O LYS A 276 N GLU A 228 ? N GLU A 228 
AA6 1 2 N THR A 311 ? N THR A 311 O ILE A 295 ? O ILE A 295 
AA6 2 3 N HIS A 296 ? N HIS A 296 O LEU A 339 ? O LEU A 339 
AA6 3 4 N VAL A 340 ? N VAL A 340 O PHE A 396 ? O PHE A 396 
AA6 4 5 O ILE A 393 ? O ILE A 393 N ASP A 386 ? N ASP A 386 
AA7 1 2 N CYS A 327 ? N CYS A 327 O TYR A 420 ? O TYR A 420 
AA7 2 3 O THR A 424 ? O THR A 424 N LEU A 331 ? N LEU A 331 
AA8 1 2 N CYS A 327 ? N CYS A 327 O TYR A 420 ? O TYR A 420 
AA8 2 3 O ALA A 419 ? O ALA A 419 N CYS A 412 ? N CYS A 412 
AA8 3 4 O LYS A 413 ? O LYS A 413 N ASP A 347 ? N ASP A 347 
AA9 1 2 N VAL A 356 ? N VAL A 356 O VAL A 370 ? O VAL A 370 
AB1 1 2 N VAL B 5   ? N VAL B 5   O VAL B 23  ? O VAL B 23  
AB1 2 3 N LEU B 18  ? N LEU B 18  O MET B 83  ? O MET B 83  
AB1 3 4 O TYR B 80  ? O TYR B 80  N SER B 71  ? N SER B 71  
AB2 1 2 N LEU B 12  ? N LEU B 12  O THR B 116 ? O THR B 116 
AB2 2 3 O VAL B 113 ? O VAL B 113 N TYR B 94  ? N TYR B 94  
AB2 3 4 O TYR B 95  ? O TYR B 95  N ILE B 37  ? N ILE B 37  
AB2 4 5 N MET B 34  ? N MET B 34  O ILE B 51  ? O ILE B 51  
AB2 5 6 N SER B 50  ? N SER B 50  O TYR B 59  ? O TYR B 59  
AB3 1 2 N LEU B 12  ? N LEU B 12  O THR B 116 ? O THR B 116 
AB3 2 3 O VAL B 113 ? O VAL B 113 N TYR B 94  ? N TYR B 94  
AB3 3 4 N LEU B 100 ? N LEU B 100 O TYR B 105 ? O TYR B 105 
AB4 1 2 N SER B 126 ? N SER B 126 O LYS B 149 ? O LYS B 149 
AB4 2 3 N VAL B 148 ? N VAL B 148 O LEU B 183 ? O LEU B 183 
AB4 3 4 O SER B 186 ? O SER B 186 N HIS B 170 ? N HIS B 170 
AB5 1 2 N SER B 126 ? N SER B 126 O LYS B 149 ? O LYS B 149 
AB5 2 3 N VAL B 148 ? N VAL B 148 O LEU B 183 ? O LEU B 183 
AB5 3 4 N THR B 182 ? N THR B 182 O VAL B 175 ? O VAL B 175 
AB6 1 2 N THR B 159 ? N THR B 159 O ASN B 202 ? O ASN B 202 
AB6 2 3 N CYS B 201 ? N CYS B 201 O LYS B 214 ? O LYS B 214 
AB7 1 2 N SER C 5   ? N SER C 5   O LYS C 23  ? O LYS C 23  
AB7 2 3 N VAL C 18  ? N VAL C 18  O ILE C 78  ? O ILE C 78  
AB7 3 4 O THR C 77  ? O THR C 77  N SER C 64  ? N SER C 64  
AB8 1 2 N SER C 5   ? N SER C 5   O LYS C 23  ? O LYS C 23  
AB8 2 3 N VAL C 18  ? N VAL C 18  O ILE C 78  ? O ILE C 78  
AB8 3 4 O SER C 73  ? O SER C 73  N ASP C 68  ? N ASP C 68  
AB9 1 2 N THR C 12  ? N THR C 12  O THR C 108 ? O THR C 108 
AB9 2 3 O THR C 105 ? O THR C 105 N TYR C 89  ? N TYR C 89  
AB9 3 4 O ALA C 88  ? O ALA C 88  N HIS C 39  ? N HIS C 39  
AB9 4 5 N GLN C 38  ? N GLN C 38  O THR C 46  ? O THR C 46  
AC1 1 2 N THR C 12  ? N THR C 12  O THR C 108 ? O THR C 108 
AC1 2 3 O THR C 105 ? O THR C 105 N TYR C 89  ? N TYR C 89  
AC1 3 4 N SER C 93  ? N SER C 93  O ILE C 100 ? O ILE C 100 
AC2 1 2 N THR C 120 ? N THR C 120 O LEU C 139 ? O LEU C 139 
AC2 2 3 N ALA C 134 ? N ALA C 134 O LEU C 183 ? O LEU C 183 
AC2 3 4 O PHE C 180 ? O PHE C 180 N ASP C 164 ? N ASP C 164 
AC3 1 2 N THR C 120 ? N THR C 120 O LEU C 139 ? O LEU C 139 
AC3 2 3 N ALA C 134 ? N ALA C 134 O LEU C 183 ? O LEU C 183 
AC3 3 4 O MET C 176 ? O MET C 176 N THR C 169 ? N THR C 169 
AC4 1 2 O THR C 157 ? O THR C 157 N ALA C 154 ? N ALA C 154 
AC4 2 3 N THR C 149 ? N THR C 149 O THR C 199 ? O THR C 199 
AC4 3 4 N HIS C 200 ? N HIS C 200 O ASN C 203 ? O ASN C 203 
AC5 1 2 N VAL D 24  ? N VAL D 5   O ALA D 42  ? O ALA D 23  
AC5 2 3 N LEU D 37  ? N LEU D 18  O MET D 102 ? O MET D 83  
AC5 3 4 O GLN D 101 ? O GLN D 82  N THR D 88  ? N THR D 69  
AC6 1 2 N VAL D 31  ? N VAL D 12  O THR D 139 ? O THR D 120 
AC7 1 2 O HIS D 78  ? O HIS D 59  N THR D 69  ? N THR D 50  
AC7 2 3 O ALA D 68  ? O ALA D 49  N TRP D 55  ? N TRP D 36  
AC7 3 4 N VAL D 56  ? N VAL D 37  O TYR D 114 ? O TYR D 95  
AC7 4 5 N ARG D 117 ? N ARG D 98  O TYR D 131 ? O TYR D 112 
AC8 1 2 O HIS D 78  ? O HIS D 59  N THR D 69  ? N THR D 50  
AC8 2 3 O ALA D 68  ? O ALA D 49  N TRP D 55  ? N TRP D 36  
AC8 3 4 N VAL D 56  ? N VAL D 37  O TYR D 114 ? O TYR D 95  
AC8 4 5 N TYR D 113 ? N TYR D 94  O THR D 136 ? O THR D 117 
AC9 1 2 N TYR D 151 ? N TYR D 132 O LEU D 170 ? O LEU D 151 
AC9 2 3 N LEU D 167 ? N LEU D 148 O VAL D 210 ? O VAL D 191 
AC9 3 4 O SER D 209 ? O SER D 190 N HIS D 193 ? N HIS D 174 
AD1 1 2 N THR D 182 ? N THR D 163 O ASN D 225 ? O ASN D 206 
AD1 2 3 N VAL D 226 ? N VAL D 207 O VAL D 235 ? O VAL D 216 
AD2 1 2 N SER E 25  ? N SER E 5   O LYS E 44  ? O LYS E 24  
AD2 2 3 N CYS E 43  ? N CYS E 23  O PHE E 97  ? O PHE E 77  
AD2 3 4 O THR E 98  ? O THR E 78  N SER E 91  ? N SER E 71  
AD3 1 2 N VAL E 33  ? N VAL E 13  O GLU E 131 ? O GLU E 111 
AD4 1 2 O THR E 79  ? O THR E 59  N TYR E 75  ? N TYR E 55  
AD4 2 3 O LYS E 71  ? O LYS E 51  N GLN E 63  ? N GLN E 43  
AD4 3 4 N ALA E 60  ? N ALA E 40  O GLN E 115 ? O GLN E 95  
AD5 1 2 N PHE E 144 ? N PHE E 124 O VAL E 159 ? O VAL E 139 
AD5 2 3 N VAL E 158 ? N VAL E 138 O LEU E 205 ? O LEU E 185 
AD5 3 4 O MET E 201 ? O MET E 181 N LEU E 162 ? N LEU E 142 
AD6 1 2 N PHE E 144 ? N PHE E 124 O VAL E 159 ? O VAL E 139 
AD6 2 3 N VAL E 158 ? N VAL E 138 O LEU E 205 ? O LEU E 185 
AD6 3 4 O SER E 202 ? O SER E 182 N SER E 188 ? N SER E 168 
AD7 1 2 O SER E 179 ? O SER E 159 N ILE E 176 ? N ILE E 156 
AD7 2 3 N LYS E 173 ? N LYS E 153 O GLU E 221 ? O GLU E 201 
AD7 3 4 N TYR E 218 ? N TYR E 198 O PHE E 235 ? O PHE E 215 
# 
_atom_sites.entry_id                    7ZXF 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.006374 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006374 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006722 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 5.96793  ? ? ? 14.89577 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 6.96715  ? ? ? 11.43723 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527  ? ? ? 9.05267  ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 15.91112 ? ? ? 10.84690 ? ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ILE A 1 45  ? 40.15638  -4.59612  12.04255  1.000 234.70423 ? 43  ILE A N   1 
ATOM   2    C CA  . ILE A 1 45  ? 40.41108  -4.76968  10.61868  1.000 235.72145 ? 43  ILE A CA  1 
ATOM   3    C C   . ILE A 1 45  ? 40.00969  -3.51619  9.84968   1.000 232.28783 ? 43  ILE A C   1 
ATOM   4    O O   . ILE A 1 45  ? 39.37931  -2.61222  10.39937  1.000 229.58884 ? 43  ILE A O   1 
ATOM   5    C CB  . ILE A 1 45  ? 39.66977  -5.99588  10.06385  1.000 231.92202 ? 43  ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 45  ? 38.15775  -5.78384  10.16246  1.000 224.39444 ? 43  ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 45  ? 40.09387  -7.25684  10.80363  1.000 237.55639 ? 43  ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 45  ? 37.35427  -6.65829  9.22614   1.000 221.33098 ? 43  ILE A CD1 1 
ATOM   9    N N   . GLY A 1 46  ? 40.37422  -3.47418  8.57371   1.000 246.80902 ? 44  GLY A N   1 
ATOM   10   C CA  . GLY A 1 46  ? 40.02813  -2.35737  7.72599   1.000 247.37155 ? 44  GLY A CA  1 
ATOM   11   C C   . GLY A 1 46  ? 40.20492  -2.70770  6.26527   1.000 248.72508 ? 44  GLY A C   1 
ATOM   12   O O   . GLY A 1 46  ? 40.45665  -3.86049  5.90807   1.000 248.57206 ? 44  GLY A O   1 
ATOM   13   N N   . TYR A 1 47  ? 40.06980  -1.68825  5.42103   1.000 263.65598 ? 45  TYR A N   1 
ATOM   14   C CA  . TYR A 1 47  ? 40.19451  -1.87711  3.98308   1.000 265.60283 ? 45  TYR A CA  1 
ATOM   15   C C   . TYR A 1 47  ? 41.62936  -2.23678  3.61017   1.000 268.83569 ? 45  TYR A C   1 
ATOM   16   O O   . TYR A 1 47  ? 42.58592  -1.85846  4.29130   1.000 269.04771 ? 45  TYR A O   1 
ATOM   17   C CB  . TYR A 1 47  ? 39.76094  -0.61257  3.24114   1.000 233.92727 ? 45  TYR A CB  1 
ATOM   18   C CG  . TYR A 1 47  ? 38.43131  -0.05265  3.70079   1.000 223.15771 ? 45  TYR A CG  1 
ATOM   19   C CD1 . TYR A 1 47  ? 37.23598  -0.52255  3.17157   1.000 219.47749 ? 45  TYR A CD1 1 
ATOM   20   C CD2 . TYR A 1 47  ? 38.37264  0.95008   4.66120   1.000 221.02500 ? 45  TYR A CD2 1 
ATOM   21   C CE1 . TYR A 1 47  ? 36.01967  -0.01158  3.58832   1.000 213.98163 ? 45  TYR A CE1 1 
ATOM   22   C CE2 . TYR A 1 47  ? 37.16173  1.46552   5.08476   1.000 215.50063 ? 45  TYR A CE2 1 
ATOM   23   C CZ  . TYR A 1 47  ? 35.98939  0.98225   4.54430   1.000 212.01349 ? 45  TYR A CZ  1 
ATOM   24   O OH  . TYR A 1 47  ? 34.78293  1.49444   4.96236   1.000 206.82663 ? 45  TYR A OH  1 
ATOM   25   N N   . LYS A 1 48  ? 41.77343  -2.97413  2.50979   1.000 286.64775 ? 46  LYS A N   1 
ATOM   26   C CA  . LYS A 1 48  ? 43.07962  -3.44847  2.07633   1.000 289.24371 ? 46  LYS A CA  1 
ATOM   27   C C   . LYS A 1 48  ? 43.07815  -3.63047  0.56435   1.000 291.80374 ? 46  LYS A C   1 
ATOM   28   O O   . LYS A 1 48  ? 42.04417  -3.93107  -0.03831  1.000 290.97150 ? 46  LYS A O   1 
ATOM   29   C CB  . LYS A 1 48  ? 43.45623  -4.76444  2.77622   1.000 212.86931 ? 46  LYS A CB  1 
ATOM   30   C CG  . LYS A 1 48  ? 44.88432  -5.22762  2.51369   1.000 214.94537 ? 46  LYS A CG  1 
ATOM   31   C CD  . LYS A 1 48  ? 45.27729  -6.40806  3.38662   1.000 214.57058 ? 46  LYS A CD  1 
ATOM   32   C CE  . LYS A 1 48  ? 44.65797  -7.70003  2.88307   1.000 215.32376 ? 46  LYS A CE  1 
ATOM   33   N NZ  . LYS A 1 48  ? 45.25791  -8.89023  3.54855   1.000 215.76276 ? 46  LYS A NZ  1 
ATOM   34   N N   . CYS A 1 49  ? 44.24839  -3.42935  -0.04241  1.000 271.58190 ? 47  CYS A N   1 
ATOM   35   C CA  . CYS A 1 49  ? 44.45183  -3.69496  -1.46182  1.000 274.63863 ? 47  CYS A CA  1 
ATOM   36   C C   . CYS A 1 49  ? 45.87513  -4.20073  -1.65954  1.000 276.35420 ? 47  CYS A C   1 
ATOM   37   O O   . CYS A 1 49  ? 46.82564  -3.60978  -1.13767  1.000 278.14310 ? 47  CYS A O   1 
ATOM   38   C CB  . CYS A 1 49  ? 44.17710  -2.44396  -2.30867  1.000 278.16699 ? 47  CYS A CB  1 
ATOM   39   S SG  . CYS A 1 49  ? 42.41904  -2.20317  -2.67747  1.000 277.45508 ? 47  CYS A SG  1 
ATOM   40   N N   . ASN A 1 50  ? 46.01100  -5.30073  -2.39952  1.000 272.60284 ? 48  ASN A N   1 
ATOM   41   C CA  . ASN A 1 50  ? 47.24719  -6.07043  -2.47559  1.000 273.85416 ? 48  ASN A CA  1 
ATOM   42   C C   . ASN A 1 50  ? 47.76692  -6.07437  -3.90697  1.000 277.13844 ? 48  ASN A C   1 
ATOM   43   O O   . ASN A 1 50  ? 47.00149  -6.31299  -4.84726  1.000 276.56254 ? 48  ASN A O   1 
ATOM   44   C CB  . ASN A 1 50  ? 47.00749  -7.50396  -1.98901  1.000 270.51703 ? 48  ASN A CB  1 
ATOM   45   C CG  . ASN A 1 50  ? 48.26214  -8.16332  -1.45938  1.000 271.55647 ? 48  ASN A CG  1 
ATOM   46   O OD1 . ASN A 1 50  ? 49.31081  -8.14245  -2.10206  1.000 274.20428 ? 48  ASN A OD1 1 
ATOM   47   N ND2 . ASN A 1 50  ? 48.15918  -8.75678  -0.27593  1.000 269.61317 ? 48  ASN A ND2 1 
ATOM   48   N N   . PHE A 1 51  ? 49.07057  -5.82248  -4.06958  1.000 273.42399 ? 49  PHE A N   1 
ATOM   49   C CA  . PHE A 1 51  ? 49.68948  -5.74141  -5.38937  1.000 276.88815 ? 49  PHE A CA  1 
ATOM   50   C C   . PHE A 1 51  ? 51.00921  -6.50384  -5.44681  1.000 278.19429 ? 49  PHE A C   1 
ATOM   51   O O   . PHE A 1 51  ? 51.92237  -6.11419  -6.17953  1.000 281.85646 ? 49  PHE A O   1 
ATOM   52   C CB  . PHE A 1 51  ? 49.91044  -4.28644  -5.80186  1.000 280.58838 ? 49  PHE A CB  1 
ATOM   53   C CG  . PHE A 1 51  ? 48.66878  -3.45002  -5.75940  1.000 279.76797 ? 49  PHE A CG  1 
ATOM   54   C CD1 . PHE A 1 51  ? 47.73870  -3.51686  -6.78227  1.000 279.70999 ? 49  PHE A CD1 1 
ATOM   55   C CD2 . PHE A 1 51  ? 48.43295  -2.59258  -4.69857  1.000 278.22231 ? 49  PHE A CD2 1 
ATOM   56   C CE1 . PHE A 1 51  ? 46.59444  -2.74687  -6.74665  1.000 279.02728 ? 49  PHE A CE1 1 
ATOM   57   C CE2 . PHE A 1 51  ? 47.29079  -1.81963  -4.65734  1.000 276.80366 ? 49  PHE A CE2 1 
ATOM   58   C CZ  . PHE A 1 51  ? 46.36973  -1.89891  -5.68247  1.000 278.35752 ? 49  PHE A CZ  1 
ATOM   59   N N   . SER A 1 52  ? 51.13105  -7.59076  -4.68652  1.000 280.24498 ? 50  SER A N   1 
ATOM   60   C CA  . SER A 1 52  ? 52.34736  -8.39430  -4.72543  1.000 281.51171 ? 50  SER A CA  1 
ATOM   61   C C   . SER A 1 52  ? 52.01589  -9.87902  -4.65545  1.000 278.72759 ? 50  SER A C   1 
ATOM   62   O O   . SER A 1 52  ? 52.60508  -10.68814 -5.37954  1.000 279.91324 ? 50  SER A O   1 
ATOM   63   C CB  . SER A 1 52  ? 53.29039  -8.00544  -3.58455  1.000 282.26043 ? 50  SER A CB  1 
ATOM   64   O OG  . SER A 1 52  ? 52.74813  -8.36679  -2.32688  1.000 278.83957 ? 50  SER A OG  1 
ATOM   65   N N   . ASN A 1 53  ? 51.07741  -10.24421 -3.78812  1.000 282.01380 ? 51  ASN A N   1 
ATOM   66   C CA  . ASN A 1 53  ? 50.66405  -11.63540 -3.64994  1.000 279.47070 ? 51  ASN A CA  1 
ATOM   67   C C   . ASN A 1 53  ? 49.82943  -12.07634 -4.84637  1.000 278.77263 ? 51  ASN A C   1 
ATOM   68   O O   . ASN A 1 53  ? 50.20220  -13.00141 -5.56687  1.000 279.29444 ? 51  ASN A O   1 
ATOM   69   C CB  . ASN A 1 53  ? 49.87312  -11.83892 -2.35678  1.000 276.32793 ? 51  ASN A CB  1 
ATOM   70   C CG  . ASN A 1 53  ? 50.68016  -11.50144 -1.12117  1.000 277.00230 ? 51  ASN A CG  1 
ATOM   71   O OD1 . ASN A 1 53  ? 51.91020  -11.47241 -1.15680  1.000 279.65420 ? 51  ASN A OD1 1 
ATOM   72   N ND2 . ASN A 1 53  ? 49.98978  -11.24876 -0.01601  1.000 274.70071 ? 51  ASN A ND2 1 
ATOM   73   N N   . ILE A 1 69  ? 43.75247  -4.41813  -12.84025 1.000 281.79868 ? 71  ILE A N   1 
ATOM   74   C CA  . ILE A 1 69  ? 42.73571  -4.41193  -11.79705 1.000 278.76625 ? 71  ILE A CA  1 
ATOM   75   C C   . ILE A 1 69  ? 42.65393  -3.01615  -11.18654 1.000 280.47823 ? 71  ILE A C   1 
ATOM   76   O O   . ILE A 1 69  ? 43.56545  -2.20473  -11.35390 1.000 283.95504 ? 71  ILE A O   1 
ATOM   77   C CB  . ILE A 1 69  ? 43.03078  -5.47550  -10.72636 1.000 275.95481 ? 71  ILE A CB  1 
ATOM   78   C CG1 . ILE A 1 69  ? 43.70311  -6.69251  -11.36214 1.000 275.40037 ? 71  ILE A CG1 1 
ATOM   79   C CG2 . ILE A 1 69  ? 41.74869  -5.90612  -10.02812 1.000 271.93725 ? 71  ILE A CG2 1 
ATOM   80   C CD1 . ILE A 1 69  ? 44.12486  -7.74890  -10.36385 1.000 273.11182 ? 71  ILE A CD1 1 
ATOM   81   N N   . PHE A 1 70  ? 41.56066  -2.73524  -10.48098 1.000 275.73446 ? 72  PHE A N   1 
ATOM   82   C CA  . PHE A 1 70  ? 41.32721  -1.42208  -9.89834  1.000 276.97737 ? 72  PHE A CA  1 
ATOM   83   C C   . PHE A 1 70  ? 40.84424  -1.56542  -8.46215  1.000 274.06906 ? 72  PHE A C   1 
ATOM   84   O O   . PHE A 1 70  ? 39.98718  -2.40231  -8.16254  1.000 270.26449 ? 72  PHE A O   1 
ATOM   85   C CB  . PHE A 1 70  ? 40.31361  -0.62375  -10.72930 1.000 276.97921 ? 72  PHE A CB  1 
ATOM   86   C CG  . PHE A 1 70  ? 40.73188  -0.42510  -12.15906 1.000 279.31806 ? 72  PHE A CG  1 
ATOM   87   C CD1 . PHE A 1 70  ? 41.54088  0.64058   -12.51640 1.000 282.94417 ? 72  PHE A CD1 1 
ATOM   88   C CD2 . PHE A 1 70  ? 40.32688  -1.31152  -13.14338 1.000 277.62499 ? 72  PHE A CD2 1 
ATOM   89   C CE1 . PHE A 1 70  ? 41.93383  0.82275   -13.82996 1.000 284.72865 ? 72  PHE A CE1 1 
ATOM   90   C CE2 . PHE A 1 70  ? 40.71645  -1.13514  -14.45950 1.000 279.44754 ? 72  PHE A CE2 1 
ATOM   91   C CZ  . PHE A 1 70  ? 41.52095  -0.06617  -14.80274 1.000 282.98703 ? 72  PHE A CZ  1 
ATOM   92   N N   . CYS A 1 71  ? 41.40684  -0.73820  -7.57919  1.000 275.12984 ? 73  CYS A N   1 
ATOM   93   C CA  . CYS A 1 71  ? 41.10689  -0.76473  -6.14707  1.000 272.18587 ? 73  CYS A CA  1 
ATOM   94   C C   . CYS A 1 71  ? 40.16185  0.39650   -5.83900  1.000 272.01139 ? 73  CYS A C   1 
ATOM   95   O O   . CYS A 1 71  ? 40.56521  1.46544   -5.38089  1.000 273.01270 ? 73  CYS A O   1 
ATOM   96   C CB  . CYS A 1 71  ? 42.40683  -0.69638  -5.34012  1.000 273.56125 ? 73  CYS A CB  1 
ATOM   97   S SG  . CYS A 1 71  ? 42.26536  -0.37766  -3.55819  1.000 266.75621 ? 73  CYS A SG  1 
ATOM   98   N N   . THR A 1 72  ? 38.87616  0.17401   -6.11219  1.000 268.01464 ? 74  THR A N   1 
ATOM   99   C CA  . THR A 1 72  ? 37.85929  1.20374   -5.92891  1.000 267.58150 ? 74  THR A CA  1 
ATOM   100  C C   . THR A 1 72  ? 37.37370  1.21912   -4.48390  1.000 264.23933 ? 74  THR A C   1 
ATOM   101  O O   . THR A 1 72  ? 37.01112  0.17591   -3.93126  1.000 260.19695 ? 74  THR A O   1 
ATOM   102  C CB  . THR A 1 72  ? 36.68444  0.96613   -6.88027  1.000 264.41270 ? 74  THR A CB  1 
ATOM   103  O OG1 . THR A 1 72  ? 37.08355  1.27175   -8.22266  1.000 269.32937 ? 74  THR A OG1 1 
ATOM   104  C CG2 . THR A 1 72  ? 35.48928  1.83150   -6.49728  1.000 260.95109 ? 74  THR A CG2 1 
ATOM   105  N N   . ILE A 1 73  ? 37.36181  2.40306   -3.87462  1.000 263.14252 ? 75  ILE A N   1 
ATOM   106  C CA  . ILE A 1 73  ? 36.97789  2.54264   -2.47337  1.000 259.15026 ? 75  ILE A CA  1 
ATOM   107  C C   . ILE A 1 73  ? 36.38188  3.92764   -2.25664  1.000 258.12475 ? 75  ILE A C   1 
ATOM   108  O O   . ILE A 1 73  ? 36.90478  4.93054   -2.75206  1.000 259.29853 ? 75  ILE A O   1 
ATOM   109  C CB  . ILE A 1 73  ? 38.18095  2.28929   -1.53703  1.000 248.99545 ? 75  ILE A CB  1 
ATOM   110  C CG1 . ILE A 1 73  ? 37.80457  2.56957   -0.08024  1.000 230.92390 ? 75  ILE A CG1 1 
ATOM   111  C CG2 . ILE A 1 73  ? 39.38446  3.11889   -1.96500  1.000 259.28060 ? 75  ILE A CG2 1 
ATOM   112  C CD1 . ILE A 1 73  ? 38.91232  2.26763   0.90303   1.000 231.45037 ? 75  ILE A CD1 1 
ATOM   113  N N   . HIS A 1 74  ? 35.27471  3.97217   -1.51489  1.000 262.90344 ? 76  HIS A N   1 
ATOM   114  C CA  . HIS A 1 74  ? 34.64050  5.22668   -1.12730  1.000 260.72097 ? 76  HIS A CA  1 
ATOM   115  C C   . HIS A 1 74  ? 33.68017  4.94554   0.01807   1.000 255.71717 ? 76  HIS A C   1 
ATOM   116  O O   . HIS A 1 74  ? 32.82257  4.06438   -0.09670  1.000 253.91272 ? 76  HIS A O   1 
ATOM   117  C CB  . HIS A 1 74  ? 33.90020  5.86901   -2.30681  1.000 236.78150 ? 76  HIS A CB  1 
ATOM   118  C CG  . HIS A 1 74  ? 32.82064  5.01113   -2.88794  1.000 234.32886 ? 76  HIS A CG  1 
ATOM   119  N ND1 . HIS A 1 74  ? 33.08361  3.94833   -3.72487  1.000 249.17224 ? 76  HIS A ND1 1 
ATOM   120  C CD2 . HIS A 1 74  ? 31.47406  5.06248   -2.75646  1.000 227.41177 ? 76  HIS A CD2 1 
ATOM   121  C CE1 . HIS A 1 74  ? 31.94572  3.38002   -4.08175  1.000 248.70178 ? 76  HIS A CE1 1 
ATOM   122  N NE2 . HIS A 1 74  ? 30.95392  4.03697   -3.50783  1.000 230.75697 ? 76  HIS A NE2 1 
ATOM   123  N N   . SER A 1 75  ? 33.82796  5.68641   1.11381   1.000 245.52883 ? 77  SER A N   1 
ATOM   124  C CA  . SER A 1 75  ? 32.99749  5.49356   2.29729   1.000 237.11961 ? 77  SER A CA  1 
ATOM   125  C C   . SER A 1 75  ? 33.29370  6.61052   3.28772   1.000 236.29407 ? 77  SER A C   1 
ATOM   126  O O   . SER A 1 75  ? 34.23459  7.38971   3.11410   1.000 242.04379 ? 77  SER A O   1 
ATOM   127  C CB  . SER A 1 75  ? 33.24389  4.12671   2.94416   1.000 234.46005 ? 77  SER A CB  1 
ATOM   128  O OG  . SER A 1 75  ? 32.52339  3.99807   4.15700   1.000 229.72936 ? 77  SER A OG  1 
ATOM   129  N N   . TYR A 1 76  ? 32.47076  6.67852   4.33160   1.000 254.99187 ? 78  TYR A N   1 
ATOM   130  C CA  . TYR A 1 76  ? 32.74808  7.52628   5.48330   1.000 253.77853 ? 78  TYR A CA  1 
ATOM   131  C C   . TYR A 1 76  ? 33.65344  6.74805   6.43182   1.000 253.60856 ? 78  TYR A C   1 
ATOM   132  O O   . TYR A 1 76  ? 33.26337  5.69690   6.95145   1.000 251.41760 ? 78  TYR A O   1 
ATOM   133  C CB  . TYR A 1 76  ? 31.45382  7.96730   6.17177   1.000 204.67484 ? 78  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 76  ? 30.58693  6.84714   6.70928   1.000 199.17168 ? 78  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 76  ? 29.77270  6.10317   5.86439   1.000 197.19508 ? 78  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 76  ? 30.56698  6.55045   8.06689   1.000 196.43955 ? 78  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 76  ? 28.97710  5.08566   6.35295   1.000 192.27914 ? 78  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 76  ? 29.77520  5.53485   8.56447   1.000 191.83303 ? 78  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 76  ? 28.98124  4.80709   7.70367   1.000 189.56035 ? 78  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 76  ? 28.19002  3.79508   8.19604   1.000 185.19807 ? 78  TYR A OH  1 
ATOM   141  N N   . PHE A 1 77  ? 34.86884  7.24659   6.63397   1.000 247.81742 ? 79  PHE A N   1 
ATOM   142  C CA  . PHE A 1 77  ? 35.91915  6.49394   7.31064   1.000 248.82243 ? 79  PHE A CA  1 
ATOM   143  C C   . PHE A 1 77  ? 35.98508  6.91273   8.77537   1.000 247.97481 ? 79  PHE A C   1 
ATOM   144  O O   . PHE A 1 77  ? 36.33846  8.05409   9.08942   1.000 249.63017 ? 79  PHE A O   1 
ATOM   145  C CB  . PHE A 1 77  ? 37.25766  6.69995   6.60632   1.000 211.45303 ? 79  PHE A CB  1 
ATOM   146  C CG  . PHE A 1 77  ? 37.24011  6.30102   5.15705   1.000 215.66673 ? 79  PHE A CG  1 
ATOM   147  C CD1 . PHE A 1 77  ? 37.06401  4.97617   4.79383   1.000 212.51564 ? 79  PHE A CD1 1 
ATOM   148  C CD2 . PHE A 1 77  ? 37.39417  7.24781   4.15892   1.000 228.46672 ? 79  PHE A CD2 1 
ATOM   149  C CE1 . PHE A 1 77  ? 37.04261  4.60319   3.46257   1.000 216.80120 ? 79  PHE A CE1 1 
ATOM   150  C CE2 . PHE A 1 77  ? 37.37473  6.88008   2.82564   1.000 235.04412 ? 79  PHE A CE2 1 
ATOM   151  C CZ  . PHE A 1 77  ? 37.19888  5.55691   2.47771   1.000 227.96437 ? 79  PHE A CZ  1 
ATOM   152  N N   . ILE A 1 78  ? 35.64904  5.98092   9.66715   1.000 241.39326 ? 80  ILE A N   1 
ATOM   153  C CA  . ILE A 1 78  ? 35.66360  6.22525   11.10481  1.000 241.33849 ? 80  ILE A CA  1 
ATOM   154  C C   . ILE A 1 78  ? 36.95924  5.67525   11.68727  1.000 244.43987 ? 80  ILE A C   1 
ATOM   155  O O   . ILE A 1 78  ? 36.97885  4.57765   12.25657  1.000 244.10202 ? 80  ILE A O   1 
ATOM   156  C CB  . ILE A 1 78  ? 34.43603  5.59438   11.78938  1.000 191.08306 ? 80  ILE A CB  1 
ATOM   157  C CG1 . ILE A 1 78  ? 33.15566  5.94360   11.02650  1.000 187.41072 ? 80  ILE A CG1 1 
ATOM   158  C CG2 . ILE A 1 78  ? 34.33065  6.05448   13.23624  1.000 191.79186 ? 80  ILE A CG2 1 
ATOM   159  C CD1 . ILE A 1 78  ? 32.88178  7.42846   10.93021  1.000 189.05274 ? 80  ILE A CD1 1 
ATOM   160  N N   . TYR A 1 79  ? 38.04743  6.43494   11.54312  1.000 243.44664 ? 81  TYR A N   1 
ATOM   161  C CA  . TYR A 1 79  ? 39.37060  6.03058   12.02575  1.000 244.86495 ? 81  TYR A CA  1 
ATOM   162  C C   . TYR A 1 79  ? 39.75433  4.64624   11.50805  1.000 244.70891 ? 81  TYR A C   1 
ATOM   163  O O   . TYR A 1 79  ? 40.30051  3.81387   12.23526  1.000 245.24285 ? 81  TYR A O   1 
ATOM   164  C CB  . TYR A 1 79  ? 39.44434  6.08508   13.55335  1.000 204.76718 ? 81  TYR A CB  1 
ATOM   165  C CG  . TYR A 1 79  ? 39.67299  7.47626   14.10240  1.000 208.50608 ? 81  TYR A CG  1 
ATOM   166  C CD1 . TYR A 1 79  ? 40.85131  8.16129   13.83573  1.000 231.52216 ? 81  TYR A CD1 1 
ATOM   167  C CD2 . TYR A 1 79  ? 38.71784  8.10048   14.89413  1.000 206.25991 ? 81  TYR A CD2 1 
ATOM   168  C CE1 . TYR A 1 79  ? 41.06974  9.43120   14.33502  1.000 244.60233 ? 81  TYR A CE1 1 
ATOM   169  C CE2 . TYR A 1 79  ? 38.92747  9.37245   15.39835  1.000 218.84000 ? 81  TYR A CE2 1 
ATOM   170  C CZ  . TYR A 1 79  ? 40.10506  10.03233  15.11495  1.000 242.29878 ? 81  TYR A CZ  1 
ATOM   171  O OH  . TYR A 1 79  ? 40.32041  11.29664  15.61384  1.000 249.55358 ? 81  TYR A OH  1 
ATOM   172  N N   . ASP A 1 80  ? 39.46273  4.39891   10.23607  1.000 260.16111 ? 82  ASP A N   1 
ATOM   173  C CA  . ASP A 1 80  ? 39.81021  3.14108   9.59580   1.000 260.52898 ? 82  ASP A CA  1 
ATOM   174  C C   . ASP A 1 80  ? 41.17332  3.25063   8.92047   1.000 261.93837 ? 82  ASP A C   1 
ATOM   175  O O   . ASP A 1 80  ? 41.65951  4.34253   8.61755   1.000 262.47461 ? 82  ASP A O   1 
ATOM   176  C CB  . ASP A 1 80  ? 38.74274  2.74071   8.57712   1.000 218.35858 ? 82  ASP A CB  1 
ATOM   177  C CG  . ASP A 1 80  ? 37.37082  2.58361   9.20393   1.000 212.42913 ? 82  ASP A CG  1 
ATOM   178  O OD1 . ASP A 1 80  ? 37.30007  2.28215   10.41460  1.000 210.64453 ? 82  ASP A OD1 1 
ATOM   179  O OD2 . ASP A 1 80  ? 36.36390  2.76297   8.48671   1.000 210.05734 ? 82  ASP A OD2 1 
ATOM   180  N N   . LYS A 1 81  ? 41.78842  2.09517   8.68354   1.000 253.18618 ? 83  LYS A N   1 
ATOM   181  C CA  . LYS A 1 81  ? 43.14614  2.01701   8.15474   1.000 254.72454 ? 83  LYS A CA  1 
ATOM   182  C C   . LYS A 1 81  ? 43.10103  1.39473   6.76338   1.000 255.98238 ? 83  LYS A C   1 
ATOM   183  O O   . LYS A 1 81  ? 42.82272  0.19934   6.61994   1.000 256.22121 ? 83  LYS A O   1 
ATOM   184  C CB  . LYS A 1 81  ? 44.04351  1.21171   9.09256   1.000 255.22861 ? 83  LYS A CB  1 
ATOM   185  C CG  . LYS A 1 81  ? 45.52775  1.37468   8.81902   1.000 256.74198 ? 83  LYS A CG  1 
ATOM   186  C CD  . LYS A 1 81  ? 46.17082  0.05530   8.43319   1.000 258.05717 ? 83  LYS A CD  1 
ATOM   187  C CE  . LYS A 1 81  ? 46.24498  -0.90258  9.60842   1.000 257.97891 ? 83  LYS A CE  1 
ATOM   188  N NZ  . LYS A 1 81  ? 46.90393  -2.18279  9.22325   1.000 259.47959 ? 83  LYS A NZ  1 
ATOM   189  N N   . ILE A 1 82  ? 43.37700  2.20463   5.74511   1.000 250.58290 ? 84  ILE A N   1 
ATOM   190  C CA  . ILE A 1 82  ? 43.41781  1.72858   4.36570   1.000 252.62006 ? 84  ILE A CA  1 
ATOM   191  C C   . ILE A 1 82  ? 44.78489  1.10790   4.10717   1.000 254.40145 ? 84  ILE A C   1 
ATOM   192  O O   . ILE A 1 82  ? 45.81215  1.78560   4.20493   1.000 254.94651 ? 84  ILE A O   1 
ATOM   193  C CB  . ILE A 1 82  ? 43.13429  2.86922   3.37839   1.000 253.68352 ? 84  ILE A CB  1 
ATOM   194  C CG1 . ILE A 1 82  ? 41.73563  3.44377   3.61122   1.000 252.13308 ? 84  ILE A CG1 1 
ATOM   195  C CG2 . ILE A 1 82  ? 43.28926  2.38494   1.94441   1.000 256.57126 ? 84  ILE A CG2 1 
ATOM   196  C CD1 . ILE A 1 82  ? 41.39738  4.60746   2.70478   1.000 246.77460 ? 84  ILE A CD1 1 
ATOM   197  N N   . ARG A 1 83  ? 44.80025  -0.17757  3.76724   1.000 255.97512 ? 85  ARG A N   1 
ATOM   198  C CA  . ARG A 1 83  ? 46.03692  -0.92963  3.59729   1.000 257.73879 ? 85  ARG A CA  1 
ATOM   199  C C   . ARG A 1 83  ? 46.37732  -1.06451  2.11728   1.000 260.72203 ? 85  ARG A C   1 
ATOM   200  O O   . ARG A 1 83  ? 45.51315  -1.40941  1.30460   1.000 261.63671 ? 85  ARG A O   1 
ATOM   201  C CB  . ARG A 1 83  ? 45.91712  -2.31544  4.23434   1.000 257.26429 ? 85  ARG A CB  1 
ATOM   202  C CG  . ARG A 1 83  ? 45.60417  -2.31667  5.72599   1.000 254.97047 ? 85  ARG A CG  1 
ATOM   203  C CD  . ARG A 1 83  ? 44.68036  -3.47727  6.07795   1.000 254.25470 ? 85  ARG A CD  1 
ATOM   204  N NE  . ARG A 1 83  ? 44.75010  -3.86290  7.48296   1.000 253.18729 ? 85  ARG A NE  1 
ATOM   205  C CZ  . ARG A 1 83  ? 44.04909  -3.29756  8.45645   1.000 251.42206 ? 85  ARG A CZ  1 
ATOM   206  N NH1 . ARG A 1 83  ? 43.24109  -2.27654  8.22414   1.000 248.55772 ? 85  ARG A NH1 1 
ATOM   207  N NH2 . ARG A 1 83  ? 44.16619  -3.76556  9.69600   1.000 251.19576 ? 85  ARG A NH2 1 
ATOM   208  N N   . LEU A 1 84  ? 47.63549  -0.78853  1.77419   1.000 257.68539 ? 86  LEU A N   1 
ATOM   209  C CA  . LEU A 1 84  ? 48.16678  -1.01541  0.43702   1.000 261.05170 ? 86  LEU A CA  1 
ATOM   210  C C   . LEU A 1 84  ? 49.45494  -1.81690  0.54867   1.000 262.50152 ? 86  LEU A C   1 
ATOM   211  O O   . LEU A 1 84  ? 50.15626  -1.74437  1.55880   1.000 261.18413 ? 86  LEU A O   1 
ATOM   212  C CB  . LEU A 1 84  ? 48.43597  0.29953   -0.31099  1.000 262.42320 ? 86  LEU A CB  1 
ATOM   213  C CG  . LEU A 1 84  ? 47.27920  0.93473   -1.08740  1.000 262.91745 ? 86  LEU A CG  1 
ATOM   214  C CD1 . LEU A 1 84  ? 46.23533  1.52429   -0.15228  1.000 259.56111 ? 86  LEU A CD1 1 
ATOM   215  C CD2 . LEU A 1 84  ? 47.80145  1.99338   -2.04706  1.000 265.28778 ? 86  LEU A CD2 1 
ATOM   216  N N   . ILE A 1 85  ? 49.76292  -2.58481  -0.49544  1.000 261.51701 ? 87  ILE A N   1 
ATOM   217  C CA  . ILE A 1 85  ? 50.89872  -3.50288  -0.48958  1.000 263.16618 ? 87  ILE A CA  1 
ATOM   218  C C   . ILE A 1 85  ? 51.69446  -3.30422  -1.77363  1.000 266.86904 ? 87  ILE A C   1 
ATOM   219  O O   . ILE A 1 85  ? 51.14868  -3.45140  -2.87371  1.000 268.91285 ? 87  ILE A O   1 
ATOM   220  C CB  . ILE A 1 85  ? 50.45100  -4.96960  -0.35894  1.000 263.06110 ? 87  ILE A CB  1 
ATOM   221  C CG1 . ILE A 1 85  ? 49.54970  -5.15937  0.86467   1.000 259.72641 ? 87  ILE A CG1 1 
ATOM   222  C CG2 . ILE A 1 85  ? 51.65622  -5.89029  -0.27414  1.000 264.73451 ? 87  ILE A CG2 1 
ATOM   223  C CD1 . ILE A 1 85  ? 50.24876  -4.92936  2.18680   1.000 257.98580 ? 87  ILE A CD1 1 
ATOM   224  N N   . ILE A 1 86  ? 52.97850  -2.98062  -1.63577  1.000 255.32823 ? 88  ILE A N   1 
ATOM   225  C CA  . ILE A 1 86  ? 53.87682  -2.87025  -2.78381  1.000 259.07452 ? 88  ILE A CA  1 
ATOM   226  C C   . ILE A 1 86  ? 55.20008  -3.56646  -2.48165  1.000 260.29507 ? 88  ILE A C   1 
ATOM   227  O O   . ILE A 1 86  ? 55.93820  -3.16174  -1.58235  1.000 258.95097 ? 88  ILE A O   1 
ATOM   228  C CB  . ILE A 1 86  ? 54.11276  -1.39926  -3.18359  1.000 259.67916 ? 88  ILE A CB  1 
ATOM   229  C CG1 . ILE A 1 86  ? 52.88187  -0.83255  -3.89228  1.000 259.88888 ? 88  ILE A CG1 1 
ATOM   230  C CG2 . ILE A 1 86  ? 55.33616  -1.27642  -4.08382  1.000 263.35932 ? 88  ILE A CG2 1 
ATOM   231  C CD1 . ILE A 1 86  ? 52.59039  -1.49036  -5.22475  1.000 263.39214 ? 88  ILE A CD1 1 
ATOM   232  N N   . ILE A 1 97  ? 54.34399  3.38162   -8.24981  1.000 251.43560 ? 99  ILE A N   1 
ATOM   233  C CA  . ILE A 1 97  ? 53.42511  4.17197   -7.44100  1.000 247.79189 ? 99  ILE A CA  1 
ATOM   234  C C   . ILE A 1 97  ? 53.64152  5.66237   -7.69492  1.000 247.32217 ? 99  ILE A C   1 
ATOM   235  O O   . ILE A 1 97  ? 54.71562  6.20535   -7.43475  1.000 247.31916 ? 99  ILE A O   1 
ATOM   236  C CB  . ILE A 1 97  ? 53.57022  3.83199   -5.94556  1.000 244.45430 ? 99  ILE A CB  1 
ATOM   237  C CG1 . ILE A 1 97  ? 55.04637  3.77316   -5.54615  1.000 245.00653 ? 99  ILE A CG1 1 
ATOM   238  C CG2 . ILE A 1 97  ? 52.87866  2.51311   -5.63155  1.000 243.88282 ? 99  ILE A CG2 1 
ATOM   239  C CD1 . ILE A 1 97  ? 55.26958  3.55133   -4.06838  1.000 241.51019 ? 99  ILE A CD1 1 
ATOM   240  N N   . LEU A 1 98  ? 52.60998  6.31683   -8.21662  1.000 254.41585 ? 100 LEU A N   1 
ATOM   241  C CA  . LEU A 1 98  ? 52.65810  7.72302   -8.58105  1.000 254.10335 ? 100 LEU A CA  1 
ATOM   242  C C   . LEU A 1 98  ? 51.35274  8.37824   -8.15747  1.000 251.46313 ? 100 LEU A C   1 
ATOM   243  O O   . LEU A 1 98  ? 50.31511  7.70782   -8.09577  1.000 250.91255 ? 100 LEU A O   1 
ATOM   244  C CB  . LEU A 1 98  ? 52.87224  7.90914   -10.09399 1.000 257.43603 ? 100 LEU A CB  1 
ATOM   245  C CG  . LEU A 1 98  ? 54.08649  7.23751   -10.74698 1.000 260.60816 ? 100 LEU A CG  1 
ATOM   246  C CD1 . LEU A 1 98  ? 53.77530  5.80442   -11.16367 1.000 262.42587 ? 100 LEU A CD1 1 
ATOM   247  C CD2 . LEU A 1 98  ? 54.57530  8.04576   -11.93804 1.000 262.78533 ? 100 LEU A CD2 1 
ATOM   248  N N   . PRO A 1 99  ? 51.36583  9.68972   -7.86479  1.000 250.23320 ? 101 PRO A N   1 
ATOM   249  C CA  . PRO A 1 99  ? 52.49016  10.63414  -7.90988  1.000 250.67725 ? 101 PRO A CA  1 
ATOM   250  C C   . PRO A 1 99  ? 53.42151  10.57602  -6.69788  1.000 248.74725 ? 101 PRO A C   1 
ATOM   251  O O   . PRO A 1 99  ? 52.94424  10.47412  -5.56657  1.000 245.87002 ? 101 PRO A O   1 
ATOM   252  C CB  . PRO A 1 99  ? 51.79385  12.00050  -7.96454  1.000 249.56163 ? 101 PRO A CB  1 
ATOM   253  C CG  . PRO A 1 99  ? 50.34562  11.71515  -8.24989  1.000 249.25535 ? 101 PRO A CG  1 
ATOM   254  C CD  . PRO A 1 99  ? 50.09361  10.38867  -7.63163  1.000 248.32274 ? 101 PRO A CD  1 
ATOM   255  N N   . GLU A 1 100 ? 54.73064  10.66577  -6.95482  1.000 251.80551 ? 102 GLU A N   1 
ATOM   256  C CA  . GLU A 1 100 ? 55.77082  10.67969  -5.92828  1.000 250.35603 ? 102 GLU A CA  1 
ATOM   257  C C   . GLU A 1 100 ? 55.52821  9.63287   -4.84754  1.000 248.36054 ? 102 GLU A C   1 
ATOM   258  O O   . GLU A 1 100 ? 55.39886  8.44105   -5.14546  1.000 249.79529 ? 102 GLU A O   1 
ATOM   259  C CB  . GLU A 1 100 ? 55.88232  12.06796  -5.29046  1.000 248.20415 ? 102 GLU A CB  1 
ATOM   260  C CG  . GLU A 1 100 ? 56.28925  13.17983  -6.24347  1.000 250.04828 ? 102 GLU A CG  1 
ATOM   261  C CD  . GLU A 1 100 ? 55.10083  13.90420  -6.84295  1.000 250.17171 ? 102 GLU A CD  1 
ATOM   262  O OE1 . GLU A 1 100 ? 54.38769  14.60768  -6.09597  1.000 247.79508 ? 102 GLU A OE1 1 
ATOM   263  O OE2 . GLU A 1 100 ? 54.87917  13.76631  -8.06297  1.000 252.79913 ? 102 GLU A OE2 1 
ATOM   264  N N   . LYS A 1 101 ? 55.47111  10.07118  -3.59132  1.000 247.45374 ? 103 LYS A N   1 
ATOM   265  C CA  . LYS A 1 101 ? 55.14334  9.20913   -2.46074  1.000 245.15761 ? 103 LYS A CA  1 
ATOM   266  C C   . LYS A 1 101 ? 53.70953  9.50988   -2.04594  1.000 242.83425 ? 103 LYS A C   1 
ATOM   267  O O   . LYS A 1 101 ? 53.41368  10.61272  -1.57500  1.000 241.13775 ? 103 LYS A O   1 
ATOM   268  C CB  . LYS A 1 101 ? 56.10245  9.43713   -1.29578  1.000 243.45281 ? 103 LYS A CB  1 
ATOM   269  C CG  . LYS A 1 101 ? 57.56208  9.16982   -1.60967  1.000 245.61691 ? 103 LYS A CG  1 
ATOM   270  C CD  . LYS A 1 101 ? 58.41811  9.40302   -0.37629  1.000 243.83054 ? 103 LYS A CD  1 
ATOM   271  C CE  . LYS A 1 101 ? 59.88459  9.12731   -0.64668  1.000 245.97600 ? 103 LYS A CE  1 
ATOM   272  N NZ  . LYS A 1 101 ? 60.71107  9.33047   0.57437   1.000 244.43290 ? 103 LYS A NZ  1 
ATOM   273  N N   . CYS A 1 102 ? 52.82302  8.53190   -2.21411  1.000 250.31803 ? 104 CYS A N   1 
ATOM   274  C CA  . CYS A 1 102 ? 51.42001  8.76242   -1.91809  1.000 248.37271 ? 104 CYS A CA  1 
ATOM   275  C C   . CYS A 1 102 ? 51.20669  8.95031   -0.41707  1.000 245.00555 ? 104 CYS A C   1 
ATOM   276  O O   . CYS A 1 102 ? 52.10782  8.75174   0.40502   1.000 244.24732 ? 104 CYS A O   1 
ATOM   277  C CB  . CYS A 1 102 ? 50.55722  7.61144   -2.42903  1.000 249.36102 ? 104 CYS A CB  1 
ATOM   278  S SG  . CYS A 1 102 ? 48.79021  7.98961   -2.42317  1.000 247.70748 ? 104 CYS A SG  1 
ATOM   279  N N   . PHE A 1 103 ? 49.98079  9.35735   -0.07786  1.000 244.58100 ? 105 PHE A N   1 
ATOM   280  C CA  . PHE A 1 103 ? 49.54151  9.66383   1.28233   1.000 241.69252 ? 105 PHE A CA  1 
ATOM   281  C C   . PHE A 1 103 ? 50.18271  10.95340  1.78636   1.000 241.29968 ? 105 PHE A C   1 
ATOM   282  O O   . PHE A 1 103 ? 49.75774  11.50612  2.80472   1.000 239.55868 ? 105 PHE A O   1 
ATOM   283  C CB  . PHE A 1 103 ? 49.81031  8.48868   2.23157   1.000 240.47764 ? 105 PHE A CB  1 
ATOM   284  C CG  . PHE A 1 103 ? 48.96807  7.26924   1.93876   1.000 240.51467 ? 105 PHE A CG  1 
ATOM   285  C CD1 . PHE A 1 103 ? 47.88418  7.35029   1.07836   1.000 241.20511 ? 105 PHE A CD1 1 
ATOM   286  C CD2 . PHE A 1 103 ? 49.25497  6.04703   2.52677   1.000 240.05857 ? 105 PHE A CD2 1 
ATOM   287  C CE1 . PHE A 1 103 ? 47.10834  6.23904   0.80149   1.000 241.44105 ? 105 PHE A CE1 1 
ATOM   288  C CE2 . PHE A 1 103 ? 48.47960  4.92912   2.25166   1.000 240.19324 ? 105 PHE A CE2 1 
ATOM   289  C CZ  . PHE A 1 103 ? 47.40618  5.02735   1.38901   1.000 240.87972 ? 105 PHE A CZ  1 
ATOM   290  N N   . GLN A 1 104 ? 51.18373  11.45838  1.07530   1.000 237.30613 ? 106 GLN A N   1 
ATOM   291  C CA  . GLN A 1 104 ? 51.54770  12.85706  1.18817   1.000 237.45367 ? 106 GLN A CA  1 
ATOM   292  C C   . GLN A 1 104 ? 51.51457  13.56487  -0.15568  1.000 239.62659 ? 106 GLN A C   1 
ATOM   293  O O   . GLN A 1 104 ? 51.36480  14.78980  -0.18759  1.000 239.73838 ? 106 GLN A O   1 
ATOM   294  C CB  . GLN A 1 104 ? 52.93247  13.01593  1.84102   1.000 237.77463 ? 106 GLN A CB  1 
ATOM   295  C CG  . GLN A 1 104 ? 53.23338  14.45935  2.22842   1.000 238.33999 ? 106 GLN A CG  1 
ATOM   296  C CD  . GLN A 1 104 ? 54.63249  14.66719  2.79950   1.000 239.68585 ? 106 GLN A CD  1 
ATOM   297  O OE1 . GLN A 1 104 ? 55.31627  13.70927  3.15849   1.000 239.66948 ? 106 GLN A OE1 1 
ATOM   298  N NE2 . GLN A 1 104 ? 55.06178  15.92909  2.88450   1.000 241.02683 ? 106 GLN A NE2 1 
ATOM   299  N N   . LYS A 1 105 ? 51.61458  12.82495  -1.25669  1.000 242.13557 ? 107 LYS A N   1 
ATOM   300  C CA  . LYS A 1 105 ? 51.38984  13.33702  -2.59986  1.000 244.43439 ? 107 LYS A CA  1 
ATOM   301  C C   . LYS A 1 105 ? 50.14467  12.67344  -3.16906  1.000 244.82264 ? 107 LYS A C   1 
ATOM   302  O O   . LYS A 1 105 ? 49.87833  11.49793  -2.89970  1.000 244.29190 ? 107 LYS A O   1 
ATOM   303  C CB  . LYS A 1 105 ? 52.60124  13.07346  -3.49520  1.000 247.08870 ? 107 LYS A CB  1 
ATOM   304  C CG  . LYS A 1 105 ? 53.90076  13.58856  -2.90647  1.000 246.77641 ? 107 LYS A CG  1 
ATOM   305  C CD  . LYS A 1 105 ? 53.95727  15.10691  -2.90013  1.000 246.72567 ? 107 LYS A CD  1 
ATOM   306  C CE  . LYS A 1 105 ? 55.33502  15.59859  -2.48158  1.000 246.90923 ? 107 LYS A CE  1 
ATOM   307  N NZ  . LYS A 1 105 ? 56.39466  15.10190  -3.40327  1.000 249.37445 ? 107 LYS A NZ  1 
ATOM   308  N N   . VAL A 1 106 ? 49.37062  13.43364  -3.93699  1.000 244.23440 ? 108 VAL A N   1 
ATOM   309  C CA  . VAL A 1 106 ? 48.02575  13.01259  -4.31076  1.000 244.27622 ? 108 VAL A CA  1 
ATOM   310  C C   . VAL A 1 106 ? 47.72410  13.41977  -5.74975  1.000 247.12301 ? 108 VAL A C   1 
ATOM   311  O O   . VAL A 1 106 ? 48.14610  14.48365  -6.21569  1.000 248.30923 ? 108 VAL A O   1 
ATOM   312  C CB  . VAL A 1 106 ? 46.98806  13.58456  -3.31967  1.000 241.68733 ? 108 VAL A CB  1 
ATOM   313  C CG1 . VAL A 1 106 ? 45.67754  13.89911  -4.00555  1.000 242.48919 ? 108 VAL A CG1 1 
ATOM   314  C CG2 . VAL A 1 106 ? 46.79110  12.62294  -2.15530  1.000 239.25075 ? 108 VAL A CG2 1 
ATOM   315  N N   . TYR A 1 107 ? 46.98552  12.55547  -6.44547  1.000 250.91584 ? 109 TYR A N   1 
ATOM   316  C CA  . TYR A 1 107 ? 46.60251  12.73939  -7.84542  1.000 253.71852 ? 109 TYR A CA  1 
ATOM   317  C C   . TYR A 1 107 ? 45.20107  13.35213  -7.90694  1.000 253.07312 ? 109 TYR A C   1 
ATOM   318  O O   . TYR A 1 107 ? 44.22739  12.72590  -8.32732  1.000 253.50286 ? 109 TYR A O   1 
ATOM   319  C CB  . TYR A 1 107 ? 46.67942  11.39173  -8.56382  1.000 255.58068 ? 109 TYR A CB  1 
ATOM   320  C CG  . TYR A 1 107 ? 46.50670  11.35925  -10.06176 1.000 258.59378 ? 109 TYR A CG  1 
ATOM   321  C CD1 . TYR A 1 107 ? 47.20944  12.21946  -10.88936 1.000 260.42264 ? 109 TYR A CD1 1 
ATOM   322  C CD2 . TYR A 1 107 ? 45.68656  10.40607  -10.65088 1.000 259.51269 ? 109 TYR A CD2 1 
ATOM   323  C CE1 . TYR A 1 107 ? 47.06336  12.15950  -12.26182 1.000 262.77707 ? 109 TYR A CE1 1 
ATOM   324  C CE2 . TYR A 1 107 ? 45.53548  10.33652  -12.01640 1.000 261.92001 ? 109 TYR A CE2 1 
ATOM   325  C CZ  . TYR A 1 107 ? 46.22702  11.21441  -12.82012 1.000 263.43148 ? 109 TYR A CZ  1 
ATOM   326  O OH  . TYR A 1 107 ? 46.07415  11.14681  -14.18567 1.000 265.46903 ? 109 TYR A OH  1 
ATOM   327  N N   . THR A 1 108 ? 45.11257  14.60655  -7.44795  1.000 242.21606 ? 110 THR A N   1 
ATOM   328  C CA  . THR A 1 108 ? 43.83518  15.31131  -7.34690  1.000 241.88932 ? 110 THR A CA  1 
ATOM   329  C C   . THR A 1 108 ? 43.15511  15.45253  -8.70247  1.000 244.13041 ? 110 THR A C   1 
ATOM   330  O O   . THR A 1 108 ? 42.14968  14.78666  -8.96929  1.000 243.22997 ? 110 THR A O   1 
ATOM   331  C CB  . THR A 1 108 ? 44.01616  16.70105  -6.72415  1.000 242.57594 ? 110 THR A CB  1 
ATOM   332  O OG1 . THR A 1 108 ? 45.30203  17.22649  -7.07090  1.000 244.71130 ? 110 THR A OG1 1 
ATOM   333  C CG2 . THR A 1 108 ? 43.87011  16.64974  -5.20926  1.000 239.86189 ? 110 THR A CG2 1 
ATOM   334  N N   . ASP A 1 109 ? 43.68124  16.32606  -9.55720  1.000 253.45139 ? 111 ASP A N   1 
ATOM   335  C CA  . ASP A 1 109 ? 43.14089  16.50424  -10.90347 1.000 255.09576 ? 111 ASP A CA  1 
ATOM   336  C C   . ASP A 1 109 ? 43.73967  15.41982  -11.78874 1.000 256.97556 ? 111 ASP A C   1 
ATOM   337  O O   . ASP A 1 109 ? 44.89316  15.51273  -12.21456 1.000 258.30477 ? 111 ASP A O   1 
ATOM   338  C CB  . ASP A 1 109 ? 43.44872  17.90034  -11.43163 1.000 255.83632 ? 111 ASP A CB  1 
ATOM   339  C CG  . ASP A 1 109 ? 42.53711  18.30693  -12.57434 1.000 256.96191 ? 111 ASP A CG  1 
ATOM   340  O OD1 . ASP A 1 109 ? 42.19949  17.44227  -13.41011 1.000 257.99013 ? 111 ASP A OD1 1 
ATOM   341  O OD2 . ASP A 1 109 ? 42.15258  19.49416  -12.63216 1.000 256.88545 ? 111 ASP A OD2 1 
ATOM   342  N N   . TYR A 1 110 ? 42.95042  14.37738  -12.06003 1.000 258.67858 ? 112 TYR A N   1 
ATOM   343  C CA  . TYR A 1 110 ? 43.46229  13.23160  -12.80437 1.000 260.35477 ? 112 TYR A CA  1 
ATOM   344  C C   . TYR A 1 110 ? 43.79164  13.60354  -14.24497 1.000 262.49688 ? 112 TYR A C   1 
ATOM   345  O O   . TYR A 1 110 ? 44.76342  13.09504  -14.81620 1.000 264.13390 ? 112 TYR A O   1 
ATOM   346  C CB  . TYR A 1 110 ? 42.44741  12.08832  -12.76778 1.000 259.89257 ? 112 TYR A CB  1 
ATOM   347  C CG  . TYR A 1 110 ? 41.31961  12.25293  -13.76020 1.000 260.46814 ? 112 TYR A CG  1 
ATOM   348  C CD1 . TYR A 1 110 ? 40.31411  13.18726  -13.54948 1.000 259.25642 ? 112 TYR A CD1 1 
ATOM   349  C CD2 . TYR A 1 110 ? 41.26793  11.48352  -14.91497 1.000 262.21981 ? 112 TYR A CD2 1 
ATOM   350  C CE1 . TYR A 1 110 ? 39.28583  13.34786  -14.45844 1.000 259.77030 ? 112 TYR A CE1 1 
ATOM   351  C CE2 . TYR A 1 110 ? 40.24404  11.63599  -15.82893 1.000 262.62856 ? 112 TYR A CE2 1 
ATOM   352  C CZ  . TYR A 1 110 ? 39.25533  12.56881  -15.59585 1.000 261.41340 ? 112 TYR A CZ  1 
ATOM   353  O OH  . TYR A 1 110 ? 38.23337  12.72252  -16.50436 1.000 261.86106 ? 112 TYR A OH  1 
ATOM   354  N N   . GLU A 1 111 ? 42.99843  14.49103  -14.84766 1.000 260.39861 ? 113 GLU A N   1 
ATOM   355  C CA  . GLU A 1 111 ? 43.18857  14.81244  -16.25780 1.000 262.32667 ? 113 GLU A CA  1 
ATOM   356  C C   . GLU A 1 111 ? 44.40065  15.71386  -16.45506 1.000 263.24358 ? 113 GLU A C   1 
ATOM   357  O O   . GLU A 1 111 ? 45.22323  15.47972  -17.34818 1.000 265.09905 ? 113 GLU A O   1 
ATOM   358  C CB  . GLU A 1 111 ? 41.92548  15.46488  -16.81905 1.000 262.09475 ? 113 GLU A CB  1 
ATOM   359  C CG  . GLU A 1 111 ? 41.78325  15.35802  -18.32929 1.000 263.99347 ? 113 GLU A CG  1 
ATOM   360  C CD  . GLU A 1 111 ? 41.64793  13.92251  -18.80715 1.000 264.74828 ? 113 GLU A CD  1 
ATOM   361  O OE1 . GLU A 1 111 ? 42.68267  13.24025  -18.96560 1.000 265.78893 ? 113 GLU A OE1 1 
ATOM   362  O OE2 . GLU A 1 111 ? 40.50240  13.47375  -19.02069 1.000 264.35087 ? 113 GLU A OE2 1 
ATOM   363  N N   . ASN A 1 112 ? 44.52945  16.75115  -15.62595 1.000 265.58651 ? 114 ASN A N   1 
ATOM   364  C CA  . ASN A 1 112 ? 45.69867  17.61875  -15.67860 1.000 266.32448 ? 114 ASN A CA  1 
ATOM   365  C C   . ASN A 1 112 ? 46.94871  16.95406  -15.11708 1.000 266.53299 ? 114 ASN A C   1 
ATOM   366  O O   . ASN A 1 112 ? 48.03719  17.52721  -15.23855 1.000 267.35567 ? 114 ASN A O   1 
ATOM   367  C CB  . ASN A 1 112 ? 45.41359  18.92026  -14.92667 1.000 264.95753 ? 114 ASN A CB  1 
ATOM   368  C CG  . ASN A 1 112 ? 44.40291  19.79647  -15.64193 1.000 265.32664 ? 114 ASN A CG  1 
ATOM   369  O OD1 . ASN A 1 112 ? 43.27289  19.37946  -15.89717 1.000 264.95550 ? 114 ASN A OD1 1 
ATOM   370  N ND2 . ASN A 1 112 ? 44.80410  21.02140  -15.96336 1.000 266.16392 ? 114 ASN A ND2 1 
ATOM   371  N N   . ARG A 1 113 ? 46.81528  15.76838  -14.52305 1.000 260.91457 ? 115 ARG A N   1 
ATOM   372  C CA  . ARG A 1 113 ? 47.92258  15.01049  -13.94024 1.000 261.15636 ? 115 ARG A CA  1 
ATOM   373  C C   . ARG A 1 113 ? 48.77138  15.89818  -13.02577 1.000 260.24227 ? 115 ARG A C   1 
ATOM   374  O O   . ARG A 1 113 ? 49.92899  16.21501  -13.29971 1.000 261.45575 ? 115 ARG A O   1 
ATOM   375  C CB  . ARG A 1 113 ? 48.77304  14.35682  -15.03564 1.000 263.59224 ? 115 ARG A CB  1 
ATOM   376  C CG  . ARG A 1 113 ? 49.74391  13.30674  -14.50684 1.000 264.03387 ? 115 ARG A CG  1 
ATOM   377  C CD  . ARG A 1 113 ? 50.44879  12.55436  -15.62611 1.000 266.55310 ? 115 ARG A CD  1 
ATOM   378  N NE  . ARG A 1 113 ? 51.44655  11.62786  -15.10255 1.000 267.13635 ? 115 ARG A NE  1 
ATOM   379  C CZ  . ARG A 1 113 ? 52.13088  10.76333  -15.83946 1.000 269.39884 ? 115 ARG A CZ  1 
ATOM   380  N NH1 . ARG A 1 113 ? 51.94443  10.66842  -17.14567 1.000 271.18414 ? 115 ARG A NH1 1 
ATOM   381  N NH2 . ARG A 1 113 ? 53.02338  9.97226   -15.25028 1.000 269.86223 ? 115 ARG A NH2 1 
ATOM   382  N N   . VAL A 1 114 ? 48.14781  16.29538  -11.92201 1.000 257.45005 ? 116 VAL A N   1 
ATOM   383  C CA  . VAL A 1 114 ? 48.77594  17.17284  -10.94803 1.000 256.21874 ? 116 VAL A CA  1 
ATOM   384  C C   . VAL A 1 114 ? 49.12967  16.36383  -9.70263  1.000 254.64114 ? 116 VAL A C   1 
ATOM   385  O O   . VAL A 1 114 ? 48.73705  15.20598  -9.54870  1.000 253.97034 ? 116 VAL A O   1 
ATOM   386  C CB  . VAL A 1 114 ? 47.88403  18.37833  -10.59656 1.000 254.73230 ? 116 VAL A CB  1 
ATOM   387  C CG1 . VAL A 1 114 ? 47.44894  19.09778  -11.86332 1.000 256.28024 ? 116 VAL A CG1 1 
ATOM   388  C CG2 . VAL A 1 114 ? 46.68182  17.92538  -9.79932  1.000 252.78193 ? 116 VAL A CG2 1 
ATOM   389  N N   . GLU A 1 115 ? 49.88762  16.99860  -8.79837  1.000 252.81182 ? 117 GLU A N   1 
ATOM   390  C CA  . GLU A 1 115 ? 50.45078  16.34092  -7.61495  1.000 250.48092 ? 117 GLU A CA  1 
ATOM   391  C C   . GLU A 1 115 ? 50.21310  17.24136  -6.40036  1.000 247.88255 ? 117 GLU A C   1 
ATOM   392  O O   . GLU A 1 115 ? 51.12966  17.89687  -5.90181  1.000 247.45388 ? 117 GLU A O   1 
ATOM   393  C CB  . GLU A 1 115 ? 51.93734  16.03940  -7.81412  1.000 251.71070 ? 117 GLU A CB  1 
ATOM   394  C CG  . GLU A 1 115 ? 52.26304  15.21418  -9.05692  1.000 254.66850 ? 117 GLU A CG  1 
ATOM   395  C CD  . GLU A 1 115 ? 52.33766  16.03984  -10.32775 1.000 257.42095 ? 117 GLU A CD  1 
ATOM   396  O OE1 . GLU A 1 115 ? 52.24844  17.28176  -10.23751 1.000 257.25483 ? 117 GLU A OE1 1 
ATOM   397  O OE2 . GLU A 1 115 ? 52.48567  15.44503  -11.41717 1.000 259.72208 ? 117 GLU A OE2 1 
ATOM   398  N N   . THR A 1 116 ? 48.97309  17.27008  -5.92066  1.000 249.19225 ? 118 THR A N   1 
ATOM   399  C CA  . THR A 1 116 ? 48.63615  18.06045  -4.74375  1.000 246.93482 ? 118 THR A CA  1 
ATOM   400  C C   . THR A 1 116 ? 49.02758  17.30295  -3.48149  1.000 244.48900 ? 118 THR A C   1 
ATOM   401  O O   . THR A 1 116 ? 48.70770  16.12094  -3.33465  1.000 243.68827 ? 118 THR A O   1 
ATOM   402  C CB  . THR A 1 116 ? 47.14214  18.38332  -4.72418  1.000 246.34541 ? 118 THR A CB  1 
ATOM   403  O OG1 . THR A 1 116 ? 46.78636  19.07157  -5.93018  1.000 248.66131 ? 118 THR A OG1 1 
ATOM   404  C CG2 . THR A 1 116 ? 46.80163  19.26009  -3.52913  1.000 244.47239 ? 118 THR A CG2 1 
ATOM   405  N N   . ASP A 1 117 ? 49.71777  17.98146  -2.57034  1.000 245.98089 ? 119 ASP A N   1 
ATOM   406  C CA  . ASP A 1 117 ? 50.11937  17.33498  -1.33233  1.000 243.83729 ? 119 ASP A CA  1 
ATOM   407  C C   . ASP A 1 117 ? 48.91025  17.10804  -0.42971  1.000 241.70927 ? 119 ASP A C   1 
ATOM   408  O O   . ASP A 1 117 ? 47.89389  17.80418  -0.51769  1.000 241.75704 ? 119 ASP A O   1 
ATOM   409  C CB  . ASP A 1 117 ? 51.17352  18.16683  -0.60175  1.000 243.73192 ? 119 ASP A CB  1 
ATOM   410  C CG  . ASP A 1 117 ? 52.50324  18.19524  -1.33050  1.000 245.54574 ? 119 ASP A CG  1 
ATOM   411  O OD1 . ASP A 1 117 ? 52.52503  17.89067  -2.53995  1.000 247.37193 ? 119 ASP A OD1 1 
ATOM   412  O OD2 . ASP A 1 117 ? 53.52747  18.51283  -0.68891  1.000 245.35074 ? 119 ASP A OD2 1 
ATOM   413  N N   . ILE A 1 118 ? 49.03127  16.11069  0.45202   1.000 240.56541 ? 120 ILE A N   1 
ATOM   414  C CA  . ILE A 1 118 ? 47.95774  15.81408  1.39464   1.000 238.56435 ? 120 ILE A CA  1 
ATOM   415  C C   . ILE A 1 118 ? 47.78602  16.89873  2.44699   1.000 237.90579 ? 120 ILE A C   1 
ATOM   416  O O   . ILE A 1 118 ? 46.75740  16.92804  3.13425   1.000 236.68426 ? 120 ILE A O   1 
ATOM   417  C CB  . ILE A 1 118 ? 48.17879  14.45607  2.09453   1.000 237.10663 ? 120 ILE A CB  1 
ATOM   418  C CG1 . ILE A 1 118 ? 46.83083  13.87920  2.54107   1.000 235.47889 ? 120 ILE A CG1 1 
ATOM   419  C CG2 . ILE A 1 118 ? 49.12034  14.61029  3.28191   1.000 236.36008 ? 120 ILE A CG2 1 
ATOM   420  C CD1 . ILE A 1 118 ? 46.92068  12.64175  3.39735   1.000 233.96558 ? 120 ILE A CD1 1 
ATOM   421  N N   . SER A 1 119 ? 48.76215  17.79905  2.58545   1.000 242.53614 ? 121 SER A N   1 
ATOM   422  C CA  . SER A 1 119 ? 48.64104  18.88196  3.55688   1.000 242.61235 ? 121 SER A CA  1 
ATOM   423  C C   . SER A 1 119 ? 47.61713  19.91875  3.11029   1.000 243.50774 ? 121 SER A C   1 
ATOM   424  O O   . SER A 1 119 ? 46.87163  20.45893  3.93593   1.000 243.19039 ? 121 SER A O   1 
ATOM   425  C CB  . SER A 1 119 ? 50.00347  19.53867  3.78285   1.000 243.84695 ? 121 SER A CB  1 
ATOM   426  O OG  . SER A 1 119 ? 50.57913  19.96171  2.55807   1.000 245.48149 ? 121 SER A OG  1 
ATOM   427  N N   . GLU A 1 120 ? 47.56609  20.21081  1.81221   1.000 242.34445 ? 122 GLU A N   1 
ATOM   428  C CA  . GLU A 1 120 ? 46.65933  21.22770  1.27879   1.000 243.51589 ? 122 GLU A CA  1 
ATOM   429  C C   . GLU A 1 120 ? 45.34301  20.58772  0.82899   1.000 242.79257 ? 122 GLU A C   1 
ATOM   430  O O   . GLU A 1 120 ? 44.90431  20.71398  -0.31388  1.000 244.09979 ? 122 GLU A O   1 
ATOM   431  C CB  . GLU A 1 120 ? 47.33420  21.98416  0.13926   1.000 245.77161 ? 122 GLU A CB  1 
ATOM   432  C CG  . GLU A 1 120 ? 46.63216  23.27094  -0.26921  1.000 247.27659 ? 122 GLU A CG  1 
ATOM   433  C CD  . GLU A 1 120 ? 46.22701  23.27352  -1.73058  1.000 248.72639 ? 122 GLU A CD  1 
ATOM   434  O OE1 . GLU A 1 120 ? 46.68801  22.38607  -2.47916  1.000 249.03321 ? 122 GLU A OE1 1 
ATOM   435  O OE2 . GLU A 1 120 ? 45.44515  24.16180  -2.12999  1.000 249.76670 ? 122 GLU A OE2 1 
ATOM   436  N N   . LEU A 1 121 ? 44.71018  19.88377  1.76508   1.000 238.36898 ? 123 LEU A N   1 
ATOM   437  C CA  . LEU A 1 121 ? 43.44789  19.20255  1.51807   1.000 237.48478 ? 123 LEU A CA  1 
ATOM   438  C C   . LEU A 1 121 ? 42.47361  19.51595  2.64828   1.000 236.23928 ? 123 LEU A C   1 
ATOM   439  O O   . LEU A 1 121 ? 42.83599  20.11529  3.66403   1.000 236.16101 ? 123 LEU A O   1 
ATOM   440  C CB  . LEU A 1 121 ? 43.65435  17.68831  1.36711   1.000 236.41750 ? 123 LEU A CB  1 
ATOM   441  C CG  . LEU A 1 121 ? 44.50813  17.26739  0.16509   1.000 238.06075 ? 123 LEU A CG  1 
ATOM   442  C CD1 . LEU A 1 121 ? 44.66637  15.75908  0.10027   1.000 237.30729 ? 123 LEU A CD1 1 
ATOM   443  C CD2 . LEU A 1 121 ? 43.91223  17.79247  -1.13225  1.000 240.12452 ? 123 LEU A CD2 1 
ATOM   444  N N   . GLY A 1 122 ? 41.22166  19.10063  2.46319   1.000 236.46059 ? 124 GLY A N   1 
ATOM   445  C CA  . GLY A 1 122 ? 40.13134  19.48967  3.33305   1.000 235.64180 ? 124 GLY A CA  1 
ATOM   446  C C   . GLY A 1 122 ? 39.87640  18.63178  4.55186   1.000 233.55341 ? 124 GLY A C   1 
ATOM   447  O O   . GLY A 1 122 ? 38.96398  18.93987  5.32460   1.000 232.25433 ? 124 GLY A O   1 
ATOM   448  N N   . LEU A 1 123 ? 40.64403  17.56648  4.75977   1.000 231.39928 ? 125 LEU A N   1 
ATOM   449  C CA  . LEU A 1 123 ? 40.43764  16.70126  5.91280   1.000 229.59061 ? 125 LEU A CA  1 
ATOM   450  C C   . LEU A 1 123 ? 41.02366  17.33650  7.16827   1.000 229.94351 ? 125 LEU A C   1 
ATOM   451  O O   . LEU A 1 123 ? 42.06373  17.99935  7.11914   1.000 231.23481 ? 125 LEU A O   1 
ATOM   452  C CB  . LEU A 1 123 ? 41.06995  15.33169  5.66576   1.000 228.71846 ? 125 LEU A CB  1 
ATOM   453  C CG  . LEU A 1 123 ? 40.97755  14.28472  6.77679   1.000 227.00318 ? 125 LEU A CG  1 
ATOM   454  C CD1 . LEU A 1 123 ? 39.53363  13.94883  7.09250   1.000 225.82903 ? 125 LEU A CD1 1 
ATOM   455  C CD2 . LEU A 1 123 ? 41.73009  13.03769  6.37345   1.000 226.65118 ? 125 LEU A CD2 1 
ATOM   456  N N   . ILE A 1 124 ? 40.34758  17.13091  8.29863   1.000 230.06374 ? 126 ILE A N   1 
ATOM   457  C CA  . ILE A 1 124 ? 40.78462  17.73884  9.55365   1.000 231.03844 ? 126 ILE A CA  1 
ATOM   458  C C   . ILE A 1 124 ? 41.96167  16.97347  10.14747  1.000 230.89368 ? 126 ILE A C   1 
ATOM   459  O O   . ILE A 1 124 ? 43.04608  17.53106  10.35169  1.000 232.31483 ? 126 ILE A O   1 
ATOM   460  C CB  . ILE A 1 124 ? 39.61273  17.83056  10.54923  1.000 230.73567 ? 126 ILE A CB  1 
ATOM   461  C CG1 . ILE A 1 124 ? 38.68096  18.98374  10.17247  1.000 230.36216 ? 126 ILE A CG1 1 
ATOM   462  C CG2 . ILE A 1 124 ? 40.12642  18.00674  11.97135  1.000 231.95330 ? 126 ILE A CG2 1 
ATOM   463  C CD1 . ILE A 1 124 ? 37.63108  19.29028  11.21953  1.000 229.06225 ? 126 ILE A CD1 1 
ATOM   464  N N   . GLU A 1 125 ? 41.76799  15.68814  10.43656  1.000 230.95172 ? 127 GLU A N   1 
ATOM   465  C CA  . GLU A 1 125 ? 42.77559  14.88338  11.11491  1.000 231.01056 ? 127 GLU A CA  1 
ATOM   466  C C   . GLU A 1 125 ? 43.05993  13.62930  10.30395  1.000 229.65568 ? 127 GLU A C   1 
ATOM   467  O O   . GLU A 1 125 ? 42.13766  12.87762  9.97223   1.000 228.31737 ? 127 GLU A O   1 
ATOM   468  C CB  . GLU A 1 125 ? 42.31990  14.51189  12.53157  1.000 231.18879 ? 127 GLU A CB  1 
ATOM   469  C CG  . GLU A 1 125 ? 43.23018  13.52775  13.24928  1.000 231.50616 ? 127 GLU A CG  1 
ATOM   470  C CD  . GLU A 1 125 ? 42.80132  13.27901  14.68338  1.000 232.56108 ? 127 GLU A CD  1 
ATOM   471  O OE1 . GLU A 1 125 ? 42.23760  14.20434  15.30485  1.000 233.93930 ? 127 GLU A OE1 1 
ATOM   472  O OE2 . GLU A 1 125 ? 43.02324  12.15793  15.18799  1.000 232.34638 ? 127 GLU A OE2 1 
ATOM   473  N N   . TYR A 1 126 ? 44.33448  13.40749  9.98816   1.000 230.55876 ? 128 TYR A N   1 
ATOM   474  C CA  . TYR A 1 126 ? 44.75562  12.21886  9.26325   1.000 229.83846 ? 128 TYR A CA  1 
ATOM   475  C C   . TYR A 1 126 ? 46.05702  11.70162  9.85758   1.000 230.48995 ? 128 TYR A C   1 
ATOM   476  O O   . TYR A 1 126 ? 46.75044  12.40354  10.59743  1.000 231.71046 ? 128 TYR A O   1 
ATOM   477  C CB  . TYR A 1 126 ? 44.92756  12.49435  7.76118   1.000 230.38923 ? 128 TYR A CB  1 
ATOM   478  C CG  . TYR A 1 126 ? 46.09066  13.39573  7.40457   1.000 231.89146 ? 128 TYR A CG  1 
ATOM   479  C CD1 . TYR A 1 126 ? 45.97111  14.77817  7.46773   1.000 232.86092 ? 128 TYR A CD1 1 
ATOM   480  C CD2 . TYR A 1 126 ? 47.30213  12.86279  6.98372   1.000 232.53831 ? 128 TYR A CD2 1 
ATOM   481  C CE1 . TYR A 1 126 ? 47.03081  15.60378  7.13476   1.000 234.33118 ? 128 TYR A CE1 1 
ATOM   482  C CE2 . TYR A 1 126 ? 48.36607  13.67920  6.64963   1.000 233.92066 ? 128 TYR A CE2 1 
ATOM   483  C CZ  . TYR A 1 126 ? 48.22536  15.04831  6.72599   1.000 234.76576 ? 128 TYR A CZ  1 
ATOM   484  O OH  . TYR A 1 126 ? 49.28382  15.86251  6.39254   1.000 236.23038 ? 128 TYR A OH  1 
ATOM   485  N N   . GLU A 1 127 ? 46.37903  10.45402  9.52333   1.000 239.62249 ? 129 GLU A N   1 
ATOM   486  C CA  . GLU A 1 127 ? 47.61438  9.82588   9.98466   1.000 240.36308 ? 129 GLU A CA  1 
ATOM   487  C C   . GLU A 1 127 ? 48.10042  8.90225   8.87824   1.000 240.48001 ? 129 GLU A C   1 
ATOM   488  O O   . GLU A 1 127 ? 47.45513  7.89149   8.58773   1.000 239.78345 ? 129 GLU A O   1 
ATOM   489  C CB  . GLU A 1 127 ? 47.39327  9.06194   11.28892  1.000 240.19815 ? 129 GLU A CB  1 
ATOM   490  C CG  . GLU A 1 127 ? 48.65871  8.46726   11.89534  1.000 241.38855 ? 129 GLU A CG  1 
ATOM   491  C CD  . GLU A 1 127 ? 48.97280  7.07902   11.36810  1.000 241.06054 ? 129 GLU A CD  1 
ATOM   492  O OE1 . GLU A 1 127 ? 48.02643  6.28903   11.16547  1.000 239.99745 ? 129 GLU A OE1 1 
ATOM   493  O OE2 . GLU A 1 127 ? 50.16639  6.78007   11.15261  1.000 242.06991 ? 129 GLU A OE2 1 
ATOM   494  N N   . ILE A 1 128 ? 49.22805  9.24637   8.26733   1.000 238.46054 ? 130 ILE A N   1 
ATOM   495  C CA  . ILE A 1 128 ? 49.79179  8.48128   7.16189   1.000 239.30082 ? 130 ILE A CA  1 
ATOM   496  C C   . ILE A 1 128 ? 50.97259  7.67195   7.67618   1.000 240.03868 ? 130 ILE A C   1 
ATOM   497  O O   . ILE A 1 128 ? 51.79321  8.16989   8.45858   1.000 240.52729 ? 130 ILE A O   1 
ATOM   498  C CB  . ILE A 1 128 ? 50.19640  9.41136   6.00252   1.000 240.53429 ? 130 ILE A CB  1 
ATOM   499  C CG1 . ILE A 1 128 ? 51.21594  10.45190  6.47514   1.000 241.23755 ? 130 ILE A CG1 1 
ATOM   500  C CG2 . ILE A 1 128 ? 48.96504  10.10072  5.45239   1.000 240.11982 ? 130 ILE A CG2 1 
ATOM   501  C CD1 . ILE A 1 128 ? 51.51504  11.54736  5.47086   1.000 242.44290 ? 130 ILE A CD1 1 
ATOM   502  N N   . GLU A 1 129 ? 51.05395  6.41415   7.24911   1.000 246.22940 ? 131 GLU A N   1 
ATOM   503  C CA  . GLU A 1 129 ? 52.03324  5.47956   7.78152   1.000 247.01701 ? 131 GLU A CA  1 
ATOM   504  C C   . GLU A 1 129 ? 52.73716  4.75057   6.64647   1.000 248.69924 ? 131 GLU A C   1 
ATOM   505  O O   . GLU A 1 129 ? 52.10900  4.36663   5.65512   1.000 249.11224 ? 131 GLU A O   1 
ATOM   506  C CB  . GLU A 1 129 ? 51.36768  4.47258   8.72967   1.000 246.10078 ? 131 GLU A CB  1 
ATOM   507  C CG  . GLU A 1 129 ? 52.33030  3.74622   9.65383   1.000 247.02620 ? 131 GLU A CG  1 
ATOM   508  C CD  . GLU A 1 129 ? 52.72915  2.38064   9.13324   1.000 248.03595 ? 131 GLU A CD  1 
ATOM   509  O OE1 . GLU A 1 129 ? 52.12081  1.91609   8.14598   1.000 248.00474 ? 131 GLU A OE1 1 
ATOM   510  O OE2 . GLU A 1 129 ? 53.65002  1.77018   9.71605   1.000 249.14858 ? 131 GLU A OE2 1 
ATOM   511  N N   . GLU A 1 130 ? 54.04769  4.57093   6.80216   1.000 250.44117 ? 132 GLU A N   1 
ATOM   512  C CA  . GLU A 1 130 ? 54.87996  3.84364   5.85146   1.000 252.49353 ? 132 GLU A CA  1 
ATOM   513  C C   . GLU A 1 130 ? 55.63447  2.76455   6.61167   1.000 253.13750 ? 132 GLU A C   1 
ATOM   514  O O   . GLU A 1 130 ? 56.41579  3.07357   7.51744   1.000 253.19219 ? 132 GLU A O   1 
ATOM   515  C CB  . GLU A 1 130 ? 55.85346  4.78422   5.13390   1.000 253.92104 ? 132 GLU A CB  1 
ATOM   516  C CG  . GLU A 1 130 ? 57.10960  4.11987   4.57246   1.000 256.30955 ? 132 GLU A CG  1 
ATOM   517  C CD  . GLU A 1 130 ? 56.83669  3.24406   3.36384   1.000 258.17706 ? 132 GLU A CD  1 
ATOM   518  O OE1 . GLU A 1 130 ? 56.26540  2.14667   3.53296   1.000 257.90947 ? 132 GLU A OE1 1 
ATOM   519  O OE2 . GLU A 1 130 ? 57.19542  3.65615   2.24046   1.000 260.17090 ? 132 GLU A OE2 1 
ATOM   520  N N   . ASN A 1 131 ? 55.39820  1.50628   6.25152   1.000 255.87108 ? 133 ASN A N   1 
ATOM   521  C CA  . ASN A 1 131 ? 56.02879  0.37038   6.90776   1.000 256.69602 ? 133 ASN A CA  1 
ATOM   522  C C   . ASN A 1 131 ? 56.97386  -0.31688  5.93266   1.000 259.25593 ? 133 ASN A C   1 
ATOM   523  O O   . ASN A 1 131 ? 56.56293  -0.72093  4.83930   1.000 260.30972 ? 133 ASN A O   1 
ATOM   524  C CB  . ASN A 1 131 ? 54.98335  -0.61834  7.42753   1.000 255.60197 ? 133 ASN A CB  1 
ATOM   525  C CG  . ASN A 1 131 ? 55.60608  -1.81371  8.11954   1.000 256.65520 ? 133 ASN A CG  1 
ATOM   526  O OD1 . ASN A 1 131 ? 55.86668  -1.78295  9.32202   1.000 256.30780 ? 133 ASN A OD1 1 
ATOM   527  N ND2 . ASN A 1 131 ? 55.84469  -2.87829  7.36223   1.000 258.27298 ? 133 ASN A ND2 1 
ATOM   528  N N   . ASP A 1 132 ? 58.23834  -0.44219  6.33365   1.000 289.18453 ? 134 ASP A N   1 
ATOM   529  C CA  . ASP A 1 132 ? 59.23811  -1.18662  5.58401   1.000 291.82259 ? 134 ASP A CA  1 
ATOM   530  C C   . ASP A 1 132 ? 59.78363  -2.36348  6.37874   1.000 292.61554 ? 134 ASP A C   1 
ATOM   531  O O   . ASP A 1 132 ? 60.61323  -3.11806  5.85678   1.000 294.93340 ? 134 ASP A O   1 
ATOM   532  C CB  . ASP A 1 132 ? 60.39173  -0.26104  5.16704   1.000 215.10085 ? 134 ASP A CB  1 
ATOM   533  C CG  . ASP A 1 132 ? 61.24252  -0.84814  4.05528   1.000 218.14422 ? 134 ASP A CG  1 
ATOM   534  O OD1 . ASP A 1 132 ? 60.82462  -1.86687  3.46168   1.000 219.23118 ? 134 ASP A OD1 1 
ATOM   535  O OD2 . ASP A 1 132 ? 62.32883  -0.29092  3.78080   1.000 219.57819 ? 134 ASP A OD2 1 
ATOM   536  N N   . THR A 1 133 ? 59.33071  -2.54353  7.62331   1.000 264.86011 ? 135 THR A N   1 
ATOM   537  C CA  . THR A 1 133 ? 59.85631  -3.60271  8.47793   1.000 265.82337 ? 135 THR A CA  1 
ATOM   538  C C   . THR A 1 133 ? 59.62950  -4.98180  7.87535   1.000 267.10631 ? 135 THR A C   1 
ATOM   539  O O   . THR A 1 133 ? 60.44816  -5.88691  8.07378   1.000 268.93203 ? 135 THR A O   1 
ATOM   540  C CB  . THR A 1 133 ? 59.21073  -3.52303  9.86174   1.000 264.19657 ? 135 THR A CB  1 
ATOM   541  O OG1 . THR A 1 133 ? 57.85087  -3.96804  9.78033   1.000 262.82820 ? 135 THR A OG1 1 
ATOM   542  C CG2 . THR A 1 133 ? 59.23014  -2.09052  10.37001  1.000 262.96621 ? 135 THR A CG2 1 
ATOM   543  N N   . ASN A 1 134 ? 58.53745  -5.16068  7.14353   1.000 271.85630 ? 136 ASN A N   1 
ATOM   544  C CA  . ASN A 1 134 ? 58.26179  -6.44751  6.51878   1.000 273.17236 ? 136 ASN A CA  1 
ATOM   545  C C   . ASN A 1 134 ? 59.28946  -6.72179  5.42567   1.000 276.02324 ? 136 ASN A C   1 
ATOM   546  O O   . ASN A 1 134 ? 59.57068  -5.83608  4.60946   1.000 276.59789 ? 136 ASN A O   1 
ATOM   547  C CB  . ASN A 1 134 ? 56.85032  -6.46677  5.93967   1.000 271.80999 ? 136 ASN A CB  1 
ATOM   548  C CG  . ASN A 1 134 ? 56.46411  -7.82507  5.39729   1.000 273.06143 ? 136 ASN A CG  1 
ATOM   549  O OD1 . ASN A 1 134 ? 56.67404  -8.12016  4.22136   1.000 275.02697 ? 136 ASN A OD1 1 
ATOM   550  N ND2 . ASN A 1 134 ? 55.89567  -8.66283  6.25496   1.000 272.16212 ? 136 ASN A ND2 1 
ATOM   551  N N   . PRO A 1 135 ? 59.87329  -7.91992  5.37666   1.000 264.94708 ? 137 PRO A N   1 
ATOM   552  C CA  . PRO A 1 135 ? 60.91711  -8.21110  4.38805   1.000 267.93849 ? 137 PRO A CA  1 
ATOM   553  C C   . PRO A 1 135 ? 60.40405  -8.54814  2.99675   1.000 269.35811 ? 137 PRO A C   1 
ATOM   554  O O   . PRO A 1 135 ? 61.21001  -8.91598  2.13774   1.000 272.20622 ? 137 PRO A O   1 
ATOM   555  C CB  . PRO A 1 135 ? 61.62930  -9.42273  5.00772   1.000 269.46442 ? 137 PRO A CB  1 
ATOM   556  C CG  . PRO A 1 135 ? 60.55416  -10.12564 5.75604   1.000 267.73936 ? 137 PRO A CG  1 
ATOM   557  C CD  . PRO A 1 135 ? 59.64965  -9.04833  6.29808   1.000 264.76590 ? 137 PRO A CD  1 
ATOM   558  N N   . ASN A 1 136 ? 59.10300  -8.43913  2.74433   1.000 275.19009 ? 138 ASN A N   1 
ATOM   559  C CA  . ASN A 1 136 ? 58.54606  -8.75638  1.43762   1.000 276.55282 ? 138 ASN A CA  1 
ATOM   560  C C   . ASN A 1 136 ? 57.87318  -7.58211  0.74605   1.000 275.99682 ? 138 ASN A C   1 
ATOM   561  O O   . ASN A 1 136 ? 57.88562  -7.52952  -0.48549  1.000 278.27773 ? 138 ASN A O   1 
ATOM   562  C CB  . ASN A 1 136 ? 57.53163  -9.90578  1.54763   1.000 273.53307 ? 138 ASN A CB  1 
ATOM   563  C CG  . ASN A 1 136 ? 58.19546  -11.25216 1.75180   1.000 273.73654 ? 138 ASN A CG  1 
ATOM   564  O OD1 . ASN A 1 136 ? 59.35205  -11.45082 1.37959   1.000 276.22600 ? 138 ASN A OD1 1 
ATOM   565  N ND2 . ASN A 1 136 ? 57.46122  -12.18964 2.33872   1.000 271.25025 ? 138 ASN A ND2 1 
ATOM   566  N N   . TYR A 1 137 ? 57.28894  -6.64317  1.48851   1.000 273.10231 ? 139 TYR A N   1 
ATOM   567  C CA  . TYR A 1 137 ? 56.56722  -5.54084  0.87149   1.000 272.40708 ? 139 TYR A CA  1 
ATOM   568  C C   . TYR A 1 137 ? 56.81282  -4.24294  1.62745   1.000 270.45160 ? 139 TYR A C   1 
ATOM   569  O O   . TYR A 1 137 ? 57.05358  -4.24071  2.83755   1.000 268.73108 ? 139 TYR A O   1 
ATOM   570  C CB  . TYR A 1 137 ? 55.05790  -5.82267  0.79736   1.000 270.71418 ? 139 TYR A CB  1 
ATOM   571  C CG  . TYR A 1 137 ? 54.43936  -6.37680  2.06525   1.000 268.07380 ? 139 TYR A CG  1 
ATOM   572  C CD1 . TYR A 1 137 ? 54.19144  -5.55892  3.16113   1.000 265.42121 ? 139 TYR A CD1 1 
ATOM   573  C CD2 . TYR A 1 137 ? 54.07664  -7.71467  2.15317   1.000 268.45478 ? 139 TYR A CD2 1 
ATOM   574  C CE1 . TYR A 1 137 ? 53.61797  -6.06341  4.31474   1.000 263.43776 ? 139 TYR A CE1 1 
ATOM   575  C CE2 . TYR A 1 137 ? 53.50187  -8.22698  3.30056   1.000 265.82917 ? 139 TYR A CE2 1 
ATOM   576  C CZ  . TYR A 1 137 ? 53.27466  -7.39793  4.37774   1.000 263.96904 ? 139 TYR A CZ  1 
ATOM   577  O OH  . TYR A 1 137 ? 52.70254  -7.90687  5.52110   1.000 262.31895 ? 139 TYR A OH  1 
ATOM   578  N N   . ASN A 1 138 ? 56.75078  -3.13621  0.88657   1.000 259.42143 ? 140 ASN A N   1 
ATOM   579  C CA  . ASN A 1 138 ? 56.79675  -1.78351  1.44286   1.000 257.52887 ? 140 ASN A CA  1 
ATOM   580  C C   . ASN A 1 138 ? 55.36660  -1.25393  1.43424   1.000 255.42773 ? 140 ASN A C   1 
ATOM   581  O O   . ASN A 1 138 ? 54.93417  -0.59181  0.49012   1.000 256.37984 ? 140 ASN A O   1 
ATOM   582  C CB  . ASN A 1 138 ? 57.73366  -0.88877  0.63806   1.000 259.70816 ? 140 ASN A CB  1 
ATOM   583  C CG  . ASN A 1 138 ? 59.19199  -1.08928  0.99950   1.000 260.99264 ? 140 ASN A CG  1 
ATOM   584  O OD1 . ASN A 1 138 ? 59.87670  -0.14859  1.40274   1.000 260.47542 ? 140 ASN A OD1 1 
ATOM   585  N ND2 . ASN A 1 138 ? 59.67400  -2.31900  0.86296   1.000 262.71720 ? 140 ASN A ND2 1 
ATOM   586  N N   . GLU A 1 139 ? 54.62723  -1.55224  2.49744   1.000 259.62993 ? 141 GLU A N   1 
ATOM   587  C CA  . GLU A 1 139 ? 53.20854  -1.23676  2.53582   1.000 257.68383 ? 141 GLU A CA  1 
ATOM   588  C C   . GLU A 1 139 ? 52.97594  0.20465   2.97538   1.000 255.81773 ? 141 GLU A C   1 
ATOM   589  O O   . GLU A 1 139 ? 53.77170  0.79164   3.71394   1.000 255.20196 ? 141 GLU A O   1 
ATOM   590  C CB  . GLU A 1 139 ? 52.47139  -2.19919  3.46858   1.000 255.88520 ? 141 GLU A CB  1 
ATOM   591  C CG  . GLU A 1 139 ? 52.82156  -2.07002  4.93562   1.000 254.15704 ? 141 GLU A CG  1 
ATOM   592  C CD  . GLU A 1 139 ? 51.94042  -2.93890  5.81201   1.000 252.62176 ? 141 GLU A CD  1 
ATOM   593  O OE1 . GLU A 1 139 ? 50.85662  -3.34972  5.34417   1.000 252.15521 ? 141 GLU A OE1 1 
ATOM   594  O OE2 . GLU A 1 139 ? 52.33190  -3.21458  6.96530   1.000 252.12812 ? 141 GLU A OE2 1 
ATOM   595  N N   . ARG A 1 140 ? 51.86689  0.77305   2.50537   1.000 249.93460 ? 142 ARG A N   1 
ATOM   596  C CA  . ARG A 1 140 ? 51.48977  2.14791   2.80428   1.000 248.29902 ? 142 ARG A CA  1 
ATOM   597  C C   . ARG A 1 140 ? 50.07013  2.15772   3.35030   1.000 245.94687 ? 142 ARG A C   1 
ATOM   598  O O   . ARG A 1 140 ? 49.17397  1.54283   2.76299   1.000 246.30080 ? 142 ARG A O   1 
ATOM   599  C CB  . ARG A 1 140 ? 51.58803  3.02982   1.55432   1.000 250.23330 ? 142 ARG A CB  1 
ATOM   600  C CG  . ARG A 1 140 ? 52.19952  4.39911   1.79607   1.000 249.71300 ? 142 ARG A CG  1 
ATOM   601  C CD  . ARG A 1 140 ? 53.68285  4.29780   2.10315   1.000 250.73587 ? 142 ARG A CD  1 
ATOM   602  N NE  . ARG A 1 140 ? 54.28092  5.60557   2.34384   1.000 250.30016 ? 142 ARG A NE  1 
ATOM   603  C CZ  . ARG A 1 140 ? 54.83025  6.36417   1.40516   1.000 252.14336 ? 142 ARG A CZ  1 
ATOM   604  N NH1 . ARG A 1 140 ? 54.87046  5.97867   0.14023   1.000 254.83436 ? 142 ARG A NH1 1 
ATOM   605  N NH2 . ARG A 1 140 ? 55.35302  7.53915   1.74433   1.000 251.54011 ? 142 ARG A NH2 1 
ATOM   606  N N   . THR A 1 141 ? 49.86759  2.84871   4.47206   1.000 244.39164 ? 143 THR A N   1 
ATOM   607  C CA  . THR A 1 141 ? 48.56980  2.89086   5.13225   1.000 242.21687 ? 143 THR A CA  1 
ATOM   608  C C   . THR A 1 141 ? 48.26924  4.31283   5.58840   1.000 240.95963 ? 143 THR A C   1 
ATOM   609  O O   . THR A 1 141 ? 49.15676  5.16683   5.65345   1.000 241.51632 ? 143 THR A O   1 
ATOM   610  C CB  . THR A 1 141 ? 48.50897  1.92989   6.32856   1.000 241.15319 ? 143 THR A CB  1 
ATOM   611  O OG1 . THR A 1 141 ? 49.59410  2.20485   7.22241   1.000 241.35426 ? 143 THR A OG1 1 
ATOM   612  C CG2 . THR A 1 141 ? 48.59661  0.48354   5.86131   1.000 242.35313 ? 143 THR A CG2 1 
ATOM   613  N N   . ILE A 1 142 ? 46.99950  4.55847   5.90596   1.000 239.71627 ? 144 ILE A N   1 
ATOM   614  C CA  . ILE A 1 142 ? 46.55406  5.88482   6.32387   1.000 238.73251 ? 144 ILE A CA  1 
ATOM   615  C C   . ILE A 1 142 ? 45.28196  5.73301   7.14774   1.000 236.96837 ? 144 ILE A C   1 
ATOM   616  O O   . ILE A 1 142 ? 44.39978  4.93592   6.81618   1.000 236.54507 ? 144 ILE A O   1 
ATOM   617  C CB  . ILE A 1 142 ? 46.34338  6.81712   5.10543   1.000 239.77806 ? 144 ILE A CB  1 
ATOM   618  C CG1 . ILE A 1 142 ? 45.80068  8.17907   5.54815   1.000 238.94104 ? 144 ILE A CG1 1 
ATOM   619  C CG2 . ILE A 1 142 ? 45.41987  6.17128   4.08311   1.000 240.42900 ? 144 ILE A CG2 1 
ATOM   620  C CD1 . ILE A 1 142 ? 45.59012  9.15348   4.40694   1.000 240.16171 ? 144 ILE A CD1 1 
ATOM   621  N N   . THR A 1 143 ? 45.19902  6.50315   8.23039   1.000 240.52020 ? 145 THR A N   1 
ATOM   622  C CA  . THR A 1 143 ? 44.02806  6.54206   9.09685   1.000 239.22147 ? 145 THR A CA  1 
ATOM   623  C C   . THR A 1 143 ? 43.27804  7.84633   8.86256   1.000 238.99241 ? 145 THR A C   1 
ATOM   624  O O   . THR A 1 143 ? 43.88965  8.91942   8.82189   1.000 239.82286 ? 145 THR A O   1 
ATOM   625  C CB  . THR A 1 143 ? 44.42702  6.41610   10.56954  1.000 239.37830 ? 145 THR A CB  1 
ATOM   626  O OG1 . THR A 1 143 ? 45.16458  5.20332   10.76395  1.000 239.87914 ? 145 THR A OG1 1 
ATOM   627  C CG2 . THR A 1 143 ? 43.19247  6.39854   11.45871  1.000 238.47654 ? 145 THR A CG2 1 
ATOM   628  N N   . ILE A 1 144 ? 41.95958  7.75162   8.71080   1.000 232.42635 ? 146 ILE A N   1 
ATOM   629  C CA  . ILE A 1 144 ? 41.11226  8.89292   8.38079   1.000 232.38900 ? 146 ILE A CA  1 
ATOM   630  C C   . ILE A 1 144 ? 40.15446  9.12593   9.54028   1.000 231.49096 ? 146 ILE A C   1 
ATOM   631  O O   . ILE A 1 144 ? 39.27694  8.29403   9.80431   1.000 230.44685 ? 146 ILE A O   1 
ATOM   632  C CB  . ILE A 1 144 ? 40.33544  8.67181   7.07642   1.000 232.57366 ? 146 ILE A CB  1 
ATOM   633  C CG1 . ILE A 1 144 ? 41.29616  8.40233   5.91695   1.000 234.12799 ? 146 ILE A CG1 1 
ATOM   634  C CG2 . ILE A 1 144 ? 39.44552  9.87124   6.77780   1.000 232.80188 ? 146 ILE A CG2 1 
ATOM   635  C CD1 . ILE A 1 144 ? 42.18862  9.56763   5.58460   1.000 235.39503 ? 146 ILE A CD1 1 
ATOM   636  N N   . SER A 1 145 ? 40.30623  10.25752  10.22147  1.000 225.26932 ? 147 SER A N   1 
ATOM   637  C CA  . SER A 1 145 ? 39.35225  10.62521  11.25137  1.000 225.03455 ? 147 SER A CA  1 
ATOM   638  C C   . SER A 1 145 ? 38.00867  10.96631  10.61359  1.000 223.87501 ? 147 SER A C   1 
ATOM   639  O O   . SER A 1 145 ? 37.96288  11.50961  9.50511   1.000 224.11615 ? 147 SER A O   1 
ATOM   640  C CB  . SER A 1 145 ? 39.85337  11.82130  12.05623  1.000 226.63232 ? 147 SER A CB  1 
ATOM   641  O OG  . SER A 1 145 ? 39.73133  13.02343  11.31297  1.000 227.31049 ? 147 SER A OG  1 
ATOM   642  N N   . PRO A 1 146 ? 36.89913  10.65964  11.29083  1.000 218.50164 ? 148 PRO A N   1 
ATOM   643  C CA  . PRO A 1 146 ? 35.58401  11.05894  10.76095  1.000 215.74914 ? 148 PRO A CA  1 
ATOM   644  C C   . PRO A 1 146 ? 35.41955  12.56115  10.61912  1.000 216.59423 ? 148 PRO A C   1 
ATOM   645  O O   . PRO A 1 146 ? 34.49141  13.00731  9.93287   1.000 215.28224 ? 148 PRO A O   1 
ATOM   646  C CB  . PRO A 1 146 ? 34.60102  10.48085  11.79112  1.000 213.26924 ? 148 PRO A CB  1 
ATOM   647  C CG  . PRO A 1 146 ? 35.41991  10.25597  13.02643  1.000 215.56185 ? 148 PRO A CG  1 
ATOM   648  C CD  . PRO A 1 146 ? 36.78920  9.90305   12.54950  1.000 218.25533 ? 148 PRO A CD  1 
ATOM   649  N N   . PHE A 1 147 ? 36.29277  13.35260  11.23784  1.000 218.35665 ? 149 PHE A N   1 
ATOM   650  C CA  . PHE A 1 147 ? 36.24114  14.80934  11.13600  1.000 219.57470 ? 149 PHE A CA  1 
ATOM   651  C C   . PHE A 1 147 ? 36.66445  15.22134  9.73267   1.000 220.77230 ? 149 PHE A C   1 
ATOM   652  O O   . PHE A 1 147 ? 37.85581  15.30309  9.42745   1.000 223.17460 ? 149 PHE A O   1 
ATOM   653  C CB  . PHE A 1 147 ? 37.14179  15.45335  12.18440  1.000 221.11630 ? 149 PHE A CB  1 
ATOM   654  C CG  . PHE A 1 147 ? 36.80853  15.06904  13.59833  1.000 220.58047 ? 149 PHE A CG  1 
ATOM   655  C CD1 . PHE A 1 147 ? 35.52962  14.66334  13.94364  1.000 213.82719 ? 149 PHE A CD1 1 
ATOM   656  C CD2 . PHE A 1 147 ? 37.77913  15.11695  14.58469  1.000 225.62671 ? 149 PHE A CD2 1 
ATOM   657  C CE1 . PHE A 1 147 ? 35.22757  14.30802  15.24485  1.000 212.60748 ? 149 PHE A CE1 1 
ATOM   658  C CE2 . PHE A 1 147 ? 37.48221  14.76481  15.88631  1.000 226.44147 ? 149 PHE A CE2 1 
ATOM   659  C CZ  . PHE A 1 147 ? 36.20544  14.36083  16.21752  1.000 219.64606 ? 149 PHE A CZ  1 
ATOM   660  N N   . SER A 1 148 ? 35.68781  15.48636  8.87109   1.000 223.01777 ? 150 SER A N   1 
ATOM   661  C CA  . SER A 1 148 ? 35.97161  15.94360  7.51738   1.000 224.65920 ? 150 SER A CA  1 
ATOM   662  C C   . SER A 1 148 ? 34.89626  16.92451  7.06744   1.000 224.11630 ? 150 SER A C   1 
ATOM   663  O O   . SER A 1 148 ? 33.75733  16.51873  6.80793   1.000 222.12806 ? 150 SER A O   1 
ATOM   664  C CB  . SER A 1 148 ? 36.05556  14.76154  6.55040   1.000 223.19752 ? 150 SER A CB  1 
ATOM   665  O OG  . SER A 1 148 ? 36.41602  15.19593  5.25056   1.000 226.14703 ? 150 SER A OG  1 
ATOM   666  N N   . PRO A 1 149 ? 35.21175  18.21956  6.96742   1.000 222.27684 ? 151 PRO A N   1 
ATOM   667  C CA  . PRO A 1 149 ? 34.19693  19.19868  6.55286   1.000 222.07941 ? 151 PRO A CA  1 
ATOM   668  C C   . PRO A 1 149 ? 33.94617  19.24792  5.05391   1.000 223.01150 ? 151 PRO A C   1 
ATOM   669  O O   . PRO A 1 149 ? 32.98549  19.90565  4.63035   1.000 222.78055 ? 151 PRO A O   1 
ATOM   670  C CB  . PRO A 1 149 ? 34.77815  20.52680  7.05279   1.000 224.21420 ? 151 PRO A CB  1 
ATOM   671  C CG  . PRO A 1 149 ? 36.25155  20.31554  7.00762   1.000 226.25034 ? 151 PRO A CG  1 
ATOM   672  C CD  . PRO A 1 149 ? 36.48244  18.86279  7.34387   1.000 224.78920 ? 151 PRO A CD  1 
ATOM   673  N N   . LYS A 1 150 ? 34.77024  18.59057  4.24115   1.000 230.86533 ? 152 LYS A N   1 
ATOM   674  C CA  . LYS A 1 150 ? 34.58094  18.55608  2.79920   1.000 232.33013 ? 152 LYS A CA  1 
ATOM   675  C C   . LYS A 1 150 ? 34.64600  17.11688  2.30939   1.000 232.00615 ? 152 LYS A C   1 
ATOM   676  O O   . LYS A 1 150 ? 35.12205  16.21937  3.00923   1.000 231.07957 ? 152 LYS A O   1 
ATOM   677  C CB  . LYS A 1 150 ? 35.63526  19.39148  2.05946   1.000 235.34969 ? 152 LYS A CB  1 
ATOM   678  C CG  . LYS A 1 150 ? 35.77681  20.82446  2.53674   1.000 236.00127 ? 152 LYS A CG  1 
ATOM   679  C CD  . LYS A 1 150 ? 36.81108  21.55227  1.69426   1.000 239.03767 ? 152 LYS A CD  1 
ATOM   680  C CE  . LYS A 1 150 ? 37.54620  22.60971  2.49653   1.000 239.66944 ? 152 LYS A CE  1 
ATOM   681  N NZ  . LYS A 1 150 ? 38.70199  23.16019  1.73617   1.000 242.58693 ? 152 LYS A NZ  1 
ATOM   682  N N   . ASP A 1 151 ? 34.16550  16.90925  1.08561   1.000 237.97766 ? 153 ASP A N   1 
ATOM   683  C CA  . ASP A 1 151 ? 34.23385  15.60486  0.43038   1.000 238.52005 ? 153 ASP A CA  1 
ATOM   684  C C   . ASP A 1 151 ? 35.50005  15.58415  -0.41750  1.000 241.78028 ? 153 ASP A C   1 
ATOM   685  O O   . ASP A 1 151 ? 35.51652  16.07724  -1.54799  1.000 244.25706 ? 153 ASP A O   1 
ATOM   686  C CB  . ASP A 1 151 ? 32.98235  15.35172  -0.40184  1.000 238.59217 ? 153 ASP A CB  1 
ATOM   687  C CG  . ASP A 1 151 ? 32.59956  13.88560  -0.44597  1.000 236.52016 ? 153 ASP A CG  1 
ATOM   688  O OD1 . ASP A 1 151 ? 33.44741  13.05603  -0.83702  1.000 238.38246 ? 153 ASP A OD1 1 
ATOM   689  O OD2 . ASP A 1 151 ? 31.45212  13.56182  -0.07356  1.000 229.62381 ? 153 ASP A OD2 1 
ATOM   690  N N   . ILE A 1 152 ? 36.56283  15.01412  0.13442   1.000 239.05465 ? 154 ILE A N   1 
ATOM   691  C CA  . ILE A 1 152 ? 37.89005  15.04536  -0.46853  1.000 242.05045 ? 154 ILE A CA  1 
ATOM   692  C C   . ILE A 1 152 ? 38.07266  13.82086  -1.35532  1.000 243.71067 ? 154 ILE A C   1 
ATOM   693  O O   . ILE A 1 152 ? 37.64965  12.71215  -1.00659  1.000 242.02182 ? 154 ILE A O   1 
ATOM   694  C CB  . ILE A 1 152 ? 38.96921  15.12186  0.62936   1.000 241.20021 ? 154 ILE A CB  1 
ATOM   695  C CG1 . ILE A 1 152 ? 40.37118  14.93527  0.05059   1.000 242.44883 ? 154 ILE A CG1 1 
ATOM   696  C CG2 . ILE A 1 152 ? 38.69365  14.10262  1.72397   1.000 238.81428 ? 154 ILE A CG2 1 
ATOM   697  C CD1 . ILE A 1 152 ? 41.43575  14.82028  1.11406   1.000 241.04049 ? 154 ILE A CD1 1 
ATOM   698  N N   . GLU A 1 153 ? 38.69754  14.02252  -2.51592  1.000 244.10807 ? 155 GLU A N   1 
ATOM   699  C CA  . GLU A 1 153 ? 38.91826  12.96230  -3.49646  1.000 245.87036 ? 155 GLU A CA  1 
ATOM   700  C C   . GLU A 1 153 ? 40.39111  12.96351  -3.88609  1.000 247.22709 ? 155 GLU A C   1 
ATOM   701  O O   . GLU A 1 153 ? 40.85654  13.89097  -4.55660  1.000 249.06059 ? 155 GLU A O   1 
ATOM   702  C CB  . GLU A 1 153 ? 38.02543  13.15795  -4.72314  1.000 248.22956 ? 155 GLU A CB  1 
ATOM   703  C CG  . GLU A 1 153 ? 36.53973  13.23248  -4.40059  1.000 246.25756 ? 155 GLU A CG  1 
ATOM   704  C CD  . GLU A 1 153 ? 35.67474  13.35522  -5.63946  1.000 248.12232 ? 155 GLU A CD  1 
ATOM   705  O OE1 . GLU A 1 153 ? 36.16483  13.88459  -6.65894  1.000 250.94849 ? 155 GLU A OE1 1 
ATOM   706  O OE2 . GLU A 1 153 ? 34.50518  12.91779  -5.59448  1.000 246.70031 ? 155 GLU A OE2 1 
ATOM   707  N N   . PHE A 1 154 ? 41.12174  11.92542  -3.47683  1.000 247.15402 ? 156 PHE A N   1 
ATOM   708  C CA  . PHE A 1 154 ? 42.56320  11.85304  -3.68593  1.000 248.23894 ? 156 PHE A CA  1 
ATOM   709  C C   . PHE A 1 154 ? 42.92799  10.52029  -4.32817  1.000 249.90950 ? 156 PHE A C   1 
ATOM   710  O O   . PHE A 1 154 ? 42.53146  9.45959   -3.83637  1.000 248.80201 ? 156 PHE A O   1 
ATOM   711  C CB  . PHE A 1 154 ? 43.31563  12.05367  -2.36066  1.000 245.83099 ? 156 PHE A CB  1 
ATOM   712  C CG  . PHE A 1 154 ? 43.22778  10.89104  -1.41419  1.000 243.80088 ? 156 PHE A CG  1 
ATOM   713  C CD1 . PHE A 1 154 ? 42.11812  10.71871  -0.60497  1.000 241.59834 ? 156 PHE A CD1 1 
ATOM   714  C CD2 . PHE A 1 154 ? 44.26949  9.98214   -1.31786  1.000 244.21052 ? 156 PHE A CD2 1 
ATOM   715  C CE1 . PHE A 1 154 ? 42.04238  9.65265   0.27118   1.000 239.77618 ? 156 PHE A CE1 1 
ATOM   716  C CE2 . PHE A 1 154 ? 44.19883  8.91445   -0.44554  1.000 242.47339 ? 156 PHE A CE2 1 
ATOM   717  C CZ  . PHE A 1 154 ? 43.08496  8.75040   0.35161   1.000 240.20626 ? 156 PHE A CZ  1 
ATOM   718  N N   . PHE A 1 155 ? 43.67507  10.57384  -5.43034  1.000 251.47735 ? 157 PHE A N   1 
ATOM   719  C CA  . PHE A 1 155 ? 43.98392  9.39056   -6.22191  1.000 253.73130 ? 157 PHE A CA  1 
ATOM   720  C C   . PHE A 1 155 ? 45.47938  9.09188   -6.17680  1.000 254.68094 ? 157 PHE A C   1 
ATOM   721  O O   . PHE A 1 155 ? 46.29780  9.96254   -5.87218  1.000 254.18267 ? 157 PHE A O   1 
ATOM   722  C CB  . PHE A 1 155 ? 43.53718  9.55504   -7.68737  1.000 256.61825 ? 157 PHE A CB  1 
ATOM   723  C CG  . PHE A 1 155 ? 42.03745  9.54123   -7.89003  1.000 256.19000 ? 157 PHE A CG  1 
ATOM   724  C CD1 . PHE A 1 155 ? 41.16312  9.63372   -6.81835  1.000 253.38813 ? 157 PHE A CD1 1 
ATOM   725  C CD2 . PHE A 1 155 ? 41.50618  9.42567   -9.16497  1.000 258.53890 ? 157 PHE A CD2 1 
ATOM   726  C CE1 . PHE A 1 155 ? 39.79399  9.62256   -7.01188  1.000 253.13592 ? 157 PHE A CE1 1 
ATOM   727  C CE2 . PHE A 1 155 ? 40.13608  9.40956   -9.36524  1.000 258.15645 ? 157 PHE A CE2 1 
ATOM   728  C CZ  . PHE A 1 155 ? 39.27993  9.50811   -8.28662  1.000 255.56569 ? 157 PHE A CZ  1 
ATOM   729  N N   . CYS A 1 156 ? 45.82151  7.83879   -6.49582  1.000 258.29507 ? 158 CYS A N   1 
ATOM   730  C CA  . CYS A 1 156 ? 47.19803  7.34574   -6.53691  1.000 259.69922 ? 158 CYS A CA  1 
ATOM   731  C C   . CYS A 1 156 ? 47.25290  6.00340   -7.25815  1.000 262.26260 ? 158 CYS A C   1 
ATOM   732  O O   . CYS A 1 156 ? 46.66077  5.03023   -6.78675  1.000 261.34829 ? 158 CYS A O   1 
ATOM   733  C CB  . CYS A 1 156 ? 47.77110  7.17402   -5.12700  1.000 256.92665 ? 158 CYS A CB  1 
ATOM   734  S SG  . CYS A 1 156 ? 48.42705  8.64422   -4.30934  1.000 254.70054 ? 158 CYS A SG  1 
ATOM   735  N N   . PHE A 1 157 ? 47.96991  5.91275   -8.37191  1.000 256.45323 ? 159 PHE A N   1 
ATOM   736  C CA  . PHE A 1 157 ? 47.97869  4.68628   -9.16249  1.000 259.07672 ? 159 PHE A CA  1 
ATOM   737  C C   . PHE A 1 157 ? 49.37333  4.06421   -9.17494  1.000 260.93360 ? 159 PHE A C   1 
ATOM   738  O O   . PHE A 1 157 ? 50.33204  4.60665   -8.61971  1.000 260.22988 ? 159 PHE A O   1 
ATOM   739  C CB  . PHE A 1 157 ? 47.48819  4.95388   -10.58819 1.000 261.27026 ? 159 PHE A CB  1 
ATOM   740  C CG  . PHE A 1 157 ? 48.54236  5.50520   -11.50269 1.000 263.55869 ? 159 PHE A CG  1 
ATOM   741  C CD1 . PHE A 1 157 ? 49.05647  6.77521   -11.30498 1.000 262.76185 ? 159 PHE A CD1 1 
ATOM   742  C CD2 . PHE A 1 157 ? 49.00774  4.75741   -12.57209 1.000 266.42455 ? 159 PHE A CD2 1 
ATOM   743  C CE1 . PHE A 1 157 ? 50.02328  7.28539   -12.14944 1.000 264.85171 ? 159 PHE A CE1 1 
ATOM   744  C CE2 . PHE A 1 157 ? 49.97406  5.26238   -13.42116 1.000 268.42723 ? 159 PHE A CE2 1 
ATOM   745  C CZ  . PHE A 1 157 ? 50.48244  6.52832   -13.20922 1.000 267.67128 ? 159 PHE A CZ  1 
ATOM   746  N N   . CYS A 1 158 ? 49.46977  2.90420   -9.81956  1.000 257.24747 ? 160 CYS A N   1 
ATOM   747  C CA  . CYS A 1 158 ? 50.73144  2.18379   -9.94833  1.000 259.43140 ? 160 CYS A CA  1 
ATOM   748  C C   . CYS A 1 158 ? 50.80084  1.44505   -11.28235 1.000 262.73864 ? 160 CYS A C   1 
ATOM   749  O O   . CYS A 1 158 ? 49.89725  0.68390   -11.63096 1.000 262.94441 ? 160 CYS A O   1 
ATOM   750  C CB  . CYS A 1 158 ? 50.91050  1.19844   -8.79131  1.000 257.80628 ? 160 CYS A CB  1 
ATOM   751  S SG  . CYS A 1 158 ? 52.46144  0.26647   -8.83504  1.000 260.16057 ? 160 CYS A SG  1 
ATOM   752  N N   . MET A 1 174 ? 45.72819  0.78664   -10.32510 1.000 269.60683 ? 174 MET A N   1 
ATOM   753  C CA  . MET A 1 174 ? 45.15265  2.08631   -9.99551  1.000 268.26916 ? 174 MET A CA  1 
ATOM   754  C C   . MET A 1 174 ? 44.38763  2.03004   -8.67547  1.000 264.93275 ? 174 MET A C   1 
ATOM   755  O O   . MET A 1 174 ? 43.59417  1.11697   -8.44573  1.000 264.29120 ? 174 MET A O   1 
ATOM   756  C CB  . MET A 1 174 ? 44.23610  2.56714   -11.12374 1.000 269.11187 ? 174 MET A CB  1 
ATOM   757  C CG  . MET A 1 174 ? 43.21638  3.61410   -10.69726 1.000 266.74139 ? 174 MET A CG  1 
ATOM   758  S SD  . MET A 1 174 ? 43.94769  5.10544   -9.99135  1.000 265.15804 ? 174 MET A SD  1 
ATOM   759  C CE  . MET A 1 174 ? 44.19606  6.09703   -11.46138 1.000 267.38252 ? 174 MET A CE  1 
ATOM   760  N N   . VAL A 1 175 ? 44.63631  3.01213   -7.80845  1.000 268.33016 ? 175 VAL A N   1 
ATOM   761  C CA  . VAL A 1 175 ? 44.04299  3.06535   -6.47080  1.000 264.70169 ? 175 VAL A CA  1 
ATOM   762  C C   . VAL A 1 175 ? 43.48111  4.47394   -6.28936  1.000 263.00471 ? 175 VAL A C   1 
ATOM   763  O O   . VAL A 1 175 ? 44.19290  5.39618   -5.88092  1.000 262.04676 ? 175 VAL A O   1 
ATOM   764  C CB  . VAL A 1 175 ? 45.04879  2.72880   -5.36384  1.000 262.96755 ? 175 VAL A CB  1 
ATOM   765  C CG1 . VAL A 1 175 ? 44.33275  2.53019   -4.03676  1.000 259.11269 ? 175 VAL A CG1 1 
ATOM   766  C CG2 . VAL A 1 175 ? 45.87274  1.50594   -5.72973  1.000 265.23206 ? 175 VAL A CG2 1 
ATOM   767  N N   . HIS A 1 176 ? 42.19578  4.64847   -6.57656  1.000 264.92106 ? 176 HIS A N   1 
ATOM   768  C CA  . HIS A 1 176 ? 41.52696  5.92570   -6.37354  1.000 263.31165 ? 176 HIS A CA  1 
ATOM   769  C C   . HIS A 1 176 ? 40.68366  5.87146   -5.10501  1.000 259.87938 ? 176 HIS A C   1 
ATOM   770  O O   . HIS A 1 176 ? 39.99115  4.88188   -4.84977  1.000 259.26574 ? 176 HIS A O   1 
ATOM   771  C CB  . HIS A 1 176 ? 40.65701  6.28658   -7.57941  1.000 265.19462 ? 176 HIS A CB  1 
ATOM   772  C CG  . HIS A 1 176 ? 39.51799  5.34494   -7.81173  1.000 265.39826 ? 176 HIS A CG  1 
ATOM   773  N ND1 . HIS A 1 176 ? 38.34697  5.39956   -7.08700  1.000 263.12826 ? 176 HIS A ND1 1 
ATOM   774  C CD2 . HIS A 1 176 ? 39.36989  4.32566   -8.69021  1.000 267.57096 ? 176 HIS A CD2 1 
ATOM   775  C CE1 . HIS A 1 176 ? 37.52694  4.45391   -7.50856  1.000 263.93893 ? 176 HIS A CE1 1 
ATOM   776  N NE2 . HIS A 1 176 ? 38.12354  3.78799   -8.48073  1.000 266.58979 ? 176 HIS A NE2 1 
ATOM   777  N N   . VAL A 1 177 ? 40.75815  6.93291   -4.30259  1.000 254.11931 ? 177 VAL A N   1 
ATOM   778  C CA  . VAL A 1 177 ? 40.08477  6.99619   -3.00877  1.000 250.70550 ? 177 VAL A CA  1 
ATOM   779  C C   . VAL A 1 177 ? 39.38761  8.34515   -2.89034  1.000 249.79354 ? 177 VAL A C   1 
ATOM   780  O O   . VAL A 1 177 ? 40.04276  9.39129   -2.94682  1.000 250.06489 ? 177 VAL A O   1 
ATOM   781  C CB  . VAL A 1 177 ? 41.06165  6.80125   -1.83334  1.000 248.56355 ? 177 VAL A CB  1 
ATOM   782  C CG1 . VAL A 1 177 ? 40.29491  6.60706   -0.53007  1.000 245.26000 ? 177 VAL A CG1 1 
ATOM   783  C CG2 . VAL A 1 177 ? 42.00919  5.63559   -2.08613  1.000 250.04309 ? 177 VAL A CG2 1 
ATOM   784  N N   . ARG A 1 178 ? 38.06897  8.32668   -2.71363  1.000 249.25503 ? 178 ARG A N   1 
ATOM   785  C CA  . ARG A 1 178 ? 37.30877  9.53262   -2.40032  1.000 248.19723 ? 178 ARG A CA  1 
ATOM   786  C C   . ARG A 1 178 ? 36.71128  9.36550   -1.00674  1.000 244.29197 ? 178 ARG A C   1 
ATOM   787  O O   . ARG A 1 178 ? 35.84933  8.50674   -0.78899  1.000 242.37925 ? 178 ARG A O   1 
ATOM   788  C CB  . ARG A 1 178 ? 36.23205  9.81428   -3.45078  1.000 249.51910 ? 178 ARG A CB  1 
ATOM   789  C CG  . ARG A 1 178 ? 35.32999  8.64818   -3.80740  1.000 250.44058 ? 178 ARG A CG  1 
ATOM   790  C CD  . ARG A 1 178 ? 34.19383  9.09834   -4.71373  1.000 251.10000 ? 178 ARG A CD  1 
ATOM   791  N NE  . ARG A 1 178 ? 33.16922  8.07238   -4.86660  1.000 247.23562 ? 178 ARG A NE  1 
ATOM   792  C CZ  . ARG A 1 178 ? 32.10008  8.19164   -5.64205  1.000 238.16170 ? 178 ARG A CZ  1 
ATOM   793  N NH1 . ARG A 1 178 ? 31.88675  9.28040   -6.36300  1.000 243.97074 ? 178 ARG A NH1 1 
ATOM   794  N NH2 . ARG A 1 178 ? 31.22342  7.19302   -5.69654  1.000 227.75721 ? 178 ARG A NH2 1 
ATOM   795  N N   . VAL A 1 179 ? 37.18833  10.17127  -0.06293  1.000 241.39516 ? 179 VAL A N   1 
ATOM   796  C CA  . VAL A 1 179 ? 36.71233  10.11223  1.31496   1.000 237.59251 ? 179 VAL A CA  1 
ATOM   797  C C   . VAL A 1 179 ? 35.39102  10.86445  1.40622   1.000 235.47712 ? 179 VAL A C   1 
ATOM   798  O O   . VAL A 1 179 ? 35.33560  12.07458  1.16438   1.000 236.31282 ? 179 VAL A O   1 
ATOM   799  C CB  . VAL A 1 179 ? 37.74932  10.69579  2.28524   1.000 237.52641 ? 179 VAL A CB  1 
ATOM   800  C CG1 . VAL A 1 179 ? 37.19545  10.73091  3.70133   1.000 234.11132 ? 179 VAL A CG1 1 
ATOM   801  C CG2 . VAL A 1 179 ? 39.04620  9.89805   2.22930   1.000 238.23843 ? 179 VAL A CG2 1 
ATOM   802  N N   . LEU A 1 180 ? 34.32444  10.14831  1.74839   1.000 241.50729 ? 180 LEU A N   1 
ATOM   803  C CA  . LEU A 1 180 ? 33.01728  10.76762  1.88994   1.000 239.46443 ? 180 LEU A CA  1 
ATOM   804  C C   . LEU A 1 180 ? 32.87747  11.42180  3.26250   1.000 236.76755 ? 180 LEU A C   1 
ATOM   805  O O   . LEU A 1 180 ? 33.60132  11.10392  4.21038   1.000 235.95501 ? 180 LEU A O   1 
ATOM   806  C CB  . LEU A 1 180 ? 31.90349  9.73926   1.68481   1.000 237.33963 ? 180 LEU A CB  1 
ATOM   807  C CG  . LEU A 1 180 ? 31.40476  9.50322   0.25596   1.000 240.58601 ? 180 LEU A CG  1 
ATOM   808  C CD1 . LEU A 1 180 ? 32.48973  8.90801   -0.62847  1.000 244.19802 ? 180 LEU A CD1 1 
ATOM   809  C CD2 . LEU A 1 180 ? 30.17599  8.61023   0.26697   1.000 236.58949 ? 180 LEU A CD2 1 
ATOM   810  N N   . LYS A 1 181 ? 31.92721  12.34976  3.35640   1.000 255.86218 ? 181 LYS A N   1 
ATOM   811  C CA  . LYS A 1 181 ? 31.64352  13.05036  4.60071   1.000 253.76167 ? 181 LYS A CA  1 
ATOM   812  C C   . LYS A 1 181 ? 30.52306  12.34729  5.35583   1.000 250.30028 ? 181 LYS A C   1 
ATOM   813  O O   . LYS A 1 181 ? 29.56675  11.85138  4.75367   1.000 249.51657 ? 181 LYS A O   1 
ATOM   814  C CB  . LYS A 1 181 ? 31.25771  14.50576  4.32898   1.000 186.20657 ? 181 LYS A CB  1 
ATOM   815  C CG  . LYS A 1 181 ? 31.09897  15.35311  5.58361   1.000 185.59271 ? 181 LYS A CG  1 
ATOM   816  C CD  . LYS A 1 181 ? 30.75668  16.79558  5.24188   1.000 187.38089 ? 181 LYS A CD  1 
ATOM   817  C CE  . LYS A 1 181 ? 30.80719  17.68770  6.47649   1.000 187.33768 ? 181 LYS A CE  1 
ATOM   818  N NZ  . LYS A 1 181 ? 29.89268  17.20623  7.55267   1.000 185.78218 ? 181 LYS A NZ  1 
ATOM   819  N N   . TYR A 1 182 ? 30.64860  12.31020  6.67673   1.000 213.77497 ? 182 TYR A N   1 
ATOM   820  C CA  . TYR A 1 182 ? 29.65430  11.65647  7.51804   1.000 210.50634 ? 182 TYR A CA  1 
ATOM   821  C C   . TYR A 1 182 ? 28.40350  12.52448  7.60886   1.000 209.41746 ? 182 TYR A C   1 
ATOM   822  O O   . TYR A 1 182 ? 28.48337  13.65588  8.10096   1.000 210.39058 ? 182 TYR A O   1 
ATOM   823  C CB  . TYR A 1 182 ? 30.22940  11.40435  8.90592   1.000 209.89020 ? 182 TYR A CB  1 
ATOM   824  C CG  . TYR A 1 182 ? 29.41805  10.45668  9.75725   1.000 206.82722 ? 182 TYR A CG  1 
ATOM   825  C CD1 . TYR A 1 182 ? 28.60954  9.48730   9.18006   1.000 204.85713 ? 182 TYR A CD1 1 
ATOM   826  C CD2 . TYR A 1 182 ? 29.45803  10.53514  11.14053  1.000 206.38857 ? 182 TYR A CD2 1 
ATOM   827  C CE1 . TYR A 1 182 ? 27.86399  8.62245   9.95665   1.000 201.97506 ? 182 TYR A CE1 1 
ATOM   828  C CE2 . TYR A 1 182 ? 28.71736  9.67549   11.92377  1.000 203.94085 ? 182 TYR A CE2 1 
ATOM   829  C CZ  . TYR A 1 182 ? 27.92247  8.72090   11.32859  1.000 201.51717 ? 182 TYR A CZ  1 
ATOM   830  O OH  . TYR A 1 182 ? 27.18286  7.86239   12.10870  1.000 199.07600 ? 182 TYR A OH  1 
ATOM   831  N N   . PRO A 1 183 ? 27.24100  12.04601  7.15226   1.000 210.88851 ? 183 PRO A N   1 
ATOM   832  C CA  . PRO A 1 183 ? 26.04378  12.90409  7.15439   1.000 210.26429 ? 183 PRO A CA  1 
ATOM   833  C C   . PRO A 1 183 ? 25.47673  13.18491  8.53662   1.000 208.09860 ? 183 PRO A C   1 
ATOM   834  O O   . PRO A 1 183 ? 24.67921  14.12059  8.67537   1.000 208.23586 ? 183 PRO A O   1 
ATOM   835  C CB  . PRO A 1 183 ? 25.04473  12.11098  6.30054   1.000 209.33158 ? 183 PRO A CB  1 
ATOM   836  C CG  . PRO A 1 183 ? 25.48870  10.69031  6.43330   1.000 207.87474 ? 183 PRO A CG  1 
ATOM   837  C CD  . PRO A 1 183 ? 26.98783  10.74882  6.50096   1.000 209.94118 ? 183 PRO A CD  1 
ATOM   838  N N   . HIS A 1 184 ? 25.85418  12.42211  9.55570   1.000 209.16141 ? 184 HIS A N   1 
ATOM   839  C CA  . HIS A 1 184 ? 25.23743  12.54276  10.86763  1.000 207.56262 ? 184 HIS A CA  1 
ATOM   840  C C   . HIS A 1 184 ? 25.92716  13.60978  11.71284  1.000 209.75398 ? 184 HIS A C   1 
ATOM   841  O O   . HIS A 1 184 ? 27.07670  13.98681  11.47351  1.000 212.13491 ? 184 HIS A O   1 
ATOM   842  C CB  . HIS A 1 184 ? 25.27180  11.20122  11.59815  1.000 205.51494 ? 184 HIS A CB  1 
ATOM   843  C CG  . HIS A 1 184 ? 24.49824  10.12006  10.91152  1.000 203.26936 ? 184 HIS A CG  1 
ATOM   844  N ND1 . HIS A 1 184 ? 24.67167  8.78358   11.19958  1.000 202.00273 ? 184 HIS A ND1 1 
ATOM   845  C CD2 . HIS A 1 184 ? 23.54038  10.17787  9.95631   1.000 202.67433 ? 184 HIS A CD2 1 
ATOM   846  C CE1 . HIS A 1 184 ? 23.85777  8.06420   10.44781  1.000 198.06106 ? 184 HIS A CE1 1 
ATOM   847  N NE2 . HIS A 1 184 ? 23.16037  8.88609   9.68443   1.000 198.47460 ? 184 HIS A NE2 1 
ATOM   848  N N   . ASN A 1 185 ? 25.19861  14.09479  12.71541  1.000 208.95313 ? 185 ASN A N   1 
ATOM   849  C CA  . ASN A 1 185 ? 25.76389  15.03365  13.67205  1.000 211.27326 ? 185 ASN A CA  1 
ATOM   850  C C   . ASN A 1 185 ? 26.76395  14.32490  14.57866  1.000 212.23894 ? 185 ASN A C   1 
ATOM   851  O O   . ASN A 1 185 ? 26.66123  13.12243  14.83573  1.000 210.32706 ? 185 ASN A O   1 
ATOM   852  C CB  . ASN A 1 185 ? 24.65861  15.67293  14.51424  1.000 175.70280 ? 185 ASN A CB  1 
ATOM   853  C CG  . ASN A 1 185 ? 23.65102  16.43786  13.67664  1.000 177.24340 ? 185 ASN A CG  1 
ATOM   854  O OD1 . ASN A 1 185 ? 23.71100  16.42776  12.44726  1.000 176.60419 ? 185 ASN A OD1 1 
ATOM   855  N ND2 . ASN A 1 185 ? 22.71111  17.10030  14.34232  1.000 180.51339 ? 185 ASN A ND2 1 
ATOM   856  N N   . ILE A 1 186 ? 27.74015  15.08447  15.06745  1.000 189.10811 ? 186 ILE A N   1 
ATOM   857  C CA  . ILE A 1 186 ? 28.79080  14.56095  15.93165  1.000 191.00335 ? 186 ILE A CA  1 
ATOM   858  C C   . ILE A 1 186 ? 28.77209  15.33749  17.23990  1.000 193.31912 ? 186 ILE A C   1 
ATOM   859  O O   . ILE A 1 186 ? 28.80499  16.57362  17.23560  1.000 194.91483 ? 186 ILE A O   1 
ATOM   860  C CB  . ILE A 1 186 ? 30.17363  14.64337  15.26018  1.000 193.28531 ? 186 ILE A CB  1 
ATOM   861  C CG1 . ILE A 1 186 ? 30.21793  13.73473  14.03017  1.000 191.26070 ? 186 ILE A CG1 1 
ATOM   862  C CG2 . ILE A 1 186 ? 31.26981  14.26707  16.24423  1.000 196.08716 ? 186 ILE A CG2 1 
ATOM   863  C CD1 . ILE A 1 186 ? 31.56784  13.68708  13.35513  1.000 193.39642 ? 186 ILE A CD1 1 
ATOM   864  N N   . LEU A 1 187 ? 28.72006  14.61164  18.35381  1.000 187.35584 ? 187 LEU A N   1 
ATOM   865  C CA  . LEU A 1 187 ? 28.67058  15.19588  19.69195  1.000 190.01422 ? 187 LEU A CA  1 
ATOM   866  C C   . LEU A 1 187 ? 29.96457  14.82756  20.41225  1.000 194.20950 ? 187 LEU A C   1 
ATOM   867  O O   . LEU A 1 187 ? 30.12168  13.69880  20.88593  1.000 194.46691 ? 187 LEU A O   1 
ATOM   868  C CB  . LEU A 1 187 ? 27.44400  14.69917  20.45158  1.000 188.15227 ? 187 LEU A CB  1 
ATOM   869  C CG  . LEU A 1 187 ? 26.13992  14.65467  19.64968  1.000 183.97338 ? 187 LEU A CG  1 
ATOM   870  C CD1 . LEU A 1 187 ? 25.01952  14.03440  20.47089  1.000 182.29032 ? 187 LEU A CD1 1 
ATOM   871  C CD2 . LEU A 1 187 ? 25.74858  16.04300  19.16269  1.000 184.10006 ? 187 LEU A CD2 1 
ATOM   872  N N   . PHE A 1 188 ? 30.88709  15.78228  20.49476  1.000 196.11314 ? 188 PHE A N   1 
ATOM   873  C CA  . PHE A 1 188 ? 32.19545  15.56683  21.10082  1.000 199.99113 ? 188 PHE A CA  1 
ATOM   874  C C   . PHE A 1 188 ? 32.16254  16.03607  22.55084  1.000 203.30032 ? 188 PHE A C   1 
ATOM   875  O O   . PHE A 1 188 ? 31.88146  17.20883  22.82172  1.000 204.13830 ? 188 PHE A O   1 
ATOM   876  C CB  . PHE A 1 188 ? 33.27953  16.30820  20.31931  1.000 201.73874 ? 188 PHE A CB  1 
ATOM   877  C CG  . PHE A 1 188 ? 34.67814  15.98080  20.75726  1.000 205.61419 ? 188 PHE A CG  1 
ATOM   878  C CD1 . PHE A 1 188 ? 34.97734  14.74758  21.31360  1.000 206.67785 ? 188 PHE A CD1 1 
ATOM   879  C CD2 . PHE A 1 188 ? 35.69340  16.91187  20.61879  1.000 208.51336 ? 188 PHE A CD2 1 
ATOM   880  C CE1 . PHE A 1 188 ? 36.26455  14.44760  21.71727  1.000 210.70764 ? 188 PHE A CE1 1 
ATOM   881  C CE2 . PHE A 1 188 ? 36.98141  16.61853  21.02158  1.000 212.26614 ? 188 PHE A CE2 1 
ATOM   882  C CZ  . PHE A 1 188 ? 37.26708  15.38481  21.57120  1.000 213.43588 ? 188 PHE A CZ  1 
ATOM   883  N N   . THR A 1 189 ? 32.45341  15.12365  23.47457  1.000 196.10530 ? 189 THR A N   1 
ATOM   884  C CA  . THR A 1 189 ? 32.48378  15.41166  24.90868  1.000 199.62410 ? 189 THR A CA  1 
ATOM   885  C C   . THR A 1 189 ? 33.93553  15.29946  25.37053  1.000 204.43404 ? 189 THR A C   1 
ATOM   886  O O   . THR A 1 189 ? 34.37355  14.25547  25.85651  1.000 206.46398 ? 189 THR A O   1 
ATOM   887  C CB  . THR A 1 189 ? 31.57294  14.46225  25.68462  1.000 198.69923 ? 189 THR A CB  1 
ATOM   888  O OG1 . THR A 1 189 ? 30.25243  14.50923  25.13119  1.000 194.09417 ? 189 THR A OG1 1 
ATOM   889  C CG2 . THR A 1 189 ? 31.51212  14.86254  27.15333  1.000 201.95257 ? 189 THR A CG2 1 
ATOM   890  N N   . ASN A 1 190 ? 34.68015  16.39028  25.22495  1.000 215.96509 ? 190 ASN A N   1 
ATOM   891  C CA  . ASN A 1 190 ? 36.11164  16.39524  25.50436  1.000 220.34425 ? 190 ASN A CA  1 
ATOM   892  C C   . ASN A 1 190 ? 36.32606  16.66473  26.98797  1.000 224.21815 ? 190 ASN A C   1 
ATOM   893  O O   . ASN A 1 190 ? 36.06923  17.76975  27.47730  1.000 224.54229 ? 190 ASN A O   1 
ATOM   894  C CB  . ASN A 1 190 ? 36.80495  17.41214  24.60341  1.000 220.78554 ? 190 ASN A CB  1 
ATOM   895  C CG  . ASN A 1 190 ? 37.98825  18.11339  25.25442  1.000 225.00809 ? 190 ASN A CG  1 
ATOM   896  O OD1 . ASN A 1 190 ? 38.91312  17.51625  25.80455  1.000 228.43855 ? 190 ASN A OD1 1 
ATOM   897  N ND2 . ASN A 1 190 ? 37.93062  19.42243  25.16316  1.000 224.76761 ? 190 ASN A ND2 1 
ATOM   898  N N   . LEU A 1 191 ? 36.77383  15.63379  27.70041  1.000 220.13755 ? 191 LEU A N   1 
ATOM   899  C CA  . LEU A 1 191 ? 37.04093  15.70535  29.12897  1.000 223.88220 ? 191 LEU A CA  1 
ATOM   900  C C   . LEU A 1 191 ? 38.49567  15.34162  29.38836  1.000 228.40599 ? 191 LEU A C   1 
ATOM   901  O O   . LEU A 1 191 ? 38.79011  14.52211  30.26337  1.000 230.82098 ? 191 LEU A O   1 
ATOM   902  C CB  . LEU A 1 191 ? 36.10743  14.76681  29.89703  1.000 223.00346 ? 191 LEU A CB  1 
ATOM   903  C CG  . LEU A 1 191 ? 34.60519  14.97145  29.69557  1.000 218.47447 ? 191 LEU A CG  1 
ATOM   904  C CD1 . LEU A 1 191 ? 33.81647  13.82429  30.31058  1.000 217.68878 ? 191 LEU A CD1 1 
ATOM   905  C CD2 . LEU A 1 191 ? 34.17098  16.29871  30.28882  1.000 218.48502 ? 191 LEU A CD2 1 
ATOM   906  N N   . THR A 1 192 ? 39.40914  15.92944  28.61888  1.000 237.77638 ? 192 THR A N   1 
ATOM   907  C CA  . THR A 1 192 ? 40.82806  15.63267  28.73865  1.000 240.14780 ? 192 THR A CA  1 
ATOM   908  C C   . THR A 1 192 ? 41.61722  16.93401  28.70496  1.000 241.82772 ? 192 THR A C   1 
ATOM   909  O O   . THR A 1 192 ? 41.09828  17.99625  28.34962  1.000 240.72432 ? 192 THR A O   1 
ATOM   910  C CB  . THR A 1 192 ? 41.30729  14.68378  27.63049  1.000 238.13616 ? 192 THR A CB  1 
ATOM   911  O OG1 . THR A 1 192 ? 42.68775  14.35989  27.83825  1.000 240.76053 ? 192 THR A OG1 1 
ATOM   912  C CG2 . THR A 1 192 ? 41.14826  15.33135  26.26655  1.000 234.78393 ? 192 THR A CG2 1 
ATOM   913  N N   . ASN A 1 193 ? 42.89527  16.83374  29.07769  1.000 250.17232 ? 193 ASN A N   1 
ATOM   914  C CA  . ASN A 1 193 ? 43.74887  18.01510  29.14853  1.000 252.20485 ? 193 ASN A CA  1 
ATOM   915  C C   . ASN A 1 193 ? 44.03155  18.58781  27.76539  1.000 250.10539 ? 193 ASN A C   1 
ATOM   916  O O   . ASN A 1 193 ? 44.13566  19.80968  27.60467  1.000 250.58424 ? 193 ASN A O   1 
ATOM   917  C CB  . ASN A 1 193 ? 45.05845  17.66971  29.85548  1.000 255.42881 ? 193 ASN A CB  1 
ATOM   918  C CG  . ASN A 1 193 ? 45.74113  16.45791  29.25131  1.000 254.67488 ? 193 ASN A CG  1 
ATOM   919  O OD1 . ASN A 1 193 ? 45.14150  15.38931  29.13170  1.000 253.12306 ? 193 ASN A OD1 1 
ATOM   920  N ND2 . ASN A 1 193 ? 46.99612  16.62335  28.85049  1.000 255.86388 ? 193 ASN A ND2 1 
ATOM   921  N N   . ASP A 1 194 ? 44.16419  17.72553  26.75988  1.000 251.28244 ? 194 ASP A N   1 
ATOM   922  C CA  . ASP A 1 194 ? 44.53597  18.17500  25.42401  1.000 248.92921 ? 194 ASP A CA  1 
ATOM   923  C C   . ASP A 1 194 ? 43.46136  19.08233  24.83962  1.000 246.37830 ? 194 ASP A C   1 
ATOM   924  O O   . ASP A 1 194 ? 42.31581  18.66281  24.64657  1.000 243.83089 ? 194 ASP A O   1 
ATOM   925  C CB  . ASP A 1 194 ? 44.77263  16.97198  24.51270  1.000 246.15004 ? 194 ASP A CB  1 
ATOM   926  C CG  . ASP A 1 194 ? 46.01766  16.19359  24.88649  1.000 248.77345 ? 194 ASP A CG  1 
ATOM   927  O OD1 . ASP A 1 194 ? 46.92598  16.78737  25.50473  1.000 252.38436 ? 194 ASP A OD1 1 
ATOM   928  O OD2 . ASP A 1 194 ? 46.09033  14.99040  24.55810  1.000 247.07280 ? 194 ASP A OD2 1 
ATOM   929  N N   . LEU A 1 195 ? 43.83720  20.32813  24.56202  1.000 246.26325 ? 195 LEU A N   1 
ATOM   930  C CA  . LEU A 1 195 ? 42.93685  21.30151  23.94920  1.000 244.34830 ? 195 LEU A CA  1 
ATOM   931  C C   . LEU A 1 195 ? 42.64932  20.86729  22.51862  1.000 240.19493 ? 195 LEU A C   1 
ATOM   932  O O   . LEU A 1 195 ? 43.46931  21.06099  21.61885  1.000 239.45364 ? 195 LEU A O   1 
ATOM   933  C CB  . LEU A 1 195 ? 43.55580  22.69375  23.98883  1.000 246.70805 ? 195 LEU A CB  1 
ATOM   934  C CG  . LEU A 1 195 ? 43.93766  23.24181  25.36459  1.000 250.73045 ? 195 LEU A CG  1 
ATOM   935  C CD1 . LEU A 1 195 ? 44.55638  24.62282  25.22756  1.000 252.64487 ? 195 LEU A CD1 1 
ATOM   936  C CD2 . LEU A 1 195 ? 42.73187  23.27888  26.29096  1.000 250.75204 ? 195 LEU A CD2 1 
ATOM   937  N N   . PHE A 1 196 ? 41.47595  20.27322  22.30144  1.000 241.65634 ? 196 PHE A N   1 
ATOM   938  C CA  . PHE A 1 196 ? 41.10524  19.74606  20.98866  1.000 237.63244 ? 196 PHE A CA  1 
ATOM   939  C C   . PHE A 1 196 ? 40.39352  20.84243  20.20192  1.000 236.45905 ? 196 PHE A C   1 
ATOM   940  O O   . PHE A 1 196 ? 39.16480  20.92497  20.14200  1.000 233.91196 ? 196 PHE A O   1 
ATOM   941  C CB  . PHE A 1 196 ? 40.25336  18.49391  21.14237  1.000 235.50763 ? 196 PHE A CB  1 
ATOM   942  C CG  . PHE A 1 196 ? 41.03602  17.28780  21.57553  1.000 236.26244 ? 196 PHE A CG  1 
ATOM   943  C CD1 . PHE A 1 196 ? 42.37037  17.15686  21.22749  1.000 237.02834 ? 196 PHE A CD1 1 
ATOM   944  C CD2 . PHE A 1 196 ? 40.44600  16.29066  22.33304  1.000 236.42714 ? 196 PHE A CD2 1 
ATOM   945  C CE1 . PHE A 1 196 ? 43.09958  16.05169  21.61844  1.000 237.92448 ? 196 PHE A CE1 1 
ATOM   946  C CE2 . PHE A 1 196 ? 41.17111  15.18102  22.72795  1.000 237.54020 ? 196 PHE A CE2 1 
ATOM   947  C CZ  . PHE A 1 196 ? 42.50058  15.06340  22.37221  1.000 238.31504 ? 196 PHE A CZ  1 
ATOM   948  N N   . THR A 1 197 ? 41.20098  21.69708  19.57920  1.000 237.25471 ? 197 THR A N   1 
ATOM   949  C CA  . THR A 1 197 ? 40.71332  22.85298  18.84229  1.000 236.94820 ? 197 THR A CA  1 
ATOM   950  C C   . THR A 1 197 ? 40.37396  22.53667  17.39089  1.000 233.56635 ? 197 THR A C   1 
ATOM   951  O O   . THR A 1 197 ? 40.09203  23.46159  16.62218  1.000 233.12149 ? 197 THR A O   1 
ATOM   952  C CB  . THR A 1 197 ? 41.74837  23.98052  18.88751  1.000 239.81605 ? 197 THR A CB  1 
ATOM   953  O OG1 . THR A 1 197 ? 42.92225  23.58006  18.16965  1.000 239.22124 ? 197 THR A OG1 1 
ATOM   954  C CG2 . THR A 1 197 ? 42.12832  24.29880  20.32521  1.000 243.35228 ? 197 THR A CG2 1 
ATOM   955  N N   . TYR A 1 198 ? 40.39726  21.26128  16.99357  1.000 238.35901 ? 198 TYR A N   1 
ATOM   956  C CA  . TYR A 1 198 ? 40.08345  20.93437  15.60533  1.000 235.58667 ? 198 TYR A CA  1 
ATOM   957  C C   . TYR A 1 198 ? 38.60059  21.13623  15.30891  1.000 232.58150 ? 198 TYR A C   1 
ATOM   958  O O   . TYR A 1 198 ? 38.24211  21.68222  14.25921  1.000 231.53633 ? 198 TYR A O   1 
ATOM   959  C CB  . TYR A 1 198 ? 40.52148  19.50507  15.27191  1.000 233.42001 ? 198 TYR A CB  1 
ATOM   960  C CG  . TYR A 1 198 ? 40.34611  18.47908  16.37272  1.000 233.41702 ? 198 TYR A CG  1 
ATOM   961  C CD1 . TYR A 1 198 ? 39.08354  18.05332  16.76363  1.000 232.19384 ? 198 TYR A CD1 1 
ATOM   962  C CD2 . TYR A 1 198 ? 41.44957  17.90525  16.99171  1.000 234.67458 ? 198 TYR A CD2 1 
ATOM   963  C CE1 . TYR A 1 198 ? 38.92244  17.11090  17.75960  1.000 232.55300 ? 198 TYR A CE1 1 
ATOM   964  C CE2 . TYR A 1 198 ? 41.29833  16.95665  17.98538  1.000 235.16323 ? 198 TYR A CE2 1 
ATOM   965  C CZ  . TYR A 1 198 ? 40.03178  16.56248  18.36400  1.000 234.14991 ? 198 TYR A CZ  1 
ATOM   966  O OH  . TYR A 1 198 ? 39.87146  15.61923  19.35263  1.000 234.95520 ? 198 TYR A OH  1 
ATOM   967  N N   . LEU A 1 199 ? 37.72562  20.71322  16.22014  1.000 234.42806 ? 199 LEU A N   1 
ATOM   968  C CA  . LEU A 1 199 ? 36.29679  20.96021  16.09945  1.000 231.69859 ? 199 LEU A CA  1 
ATOM   969  C C   . LEU A 1 199 ? 35.89714  22.04331  17.08691  1.000 233.46582 ? 199 LEU A C   1 
ATOM   970  O O   . LEU A 1 199 ? 36.12328  21.88016  18.29576  1.000 235.23539 ? 199 LEU A O   1 
ATOM   971  C CB  . LEU A 1 199 ? 35.49283  19.68719  16.35015  1.000 228.47689 ? 199 LEU A CB  1 
ATOM   972  C CG  . LEU A 1 199 ? 35.31264  18.74024  15.16153  1.000 225.36731 ? 199 LEU A CG  1 
ATOM   973  C CD1 . LEU A 1 199 ? 34.26660  17.68176  15.47493  1.000 221.60155 ? 199 LEU A CD1 1 
ATOM   974  C CD2 . LEU A 1 199 ? 34.93599  19.50813  13.90420  1.000 224.51015 ? 199 LEU A CD2 1 
ATOM   975  N N   . PRO A 1 200 ? 35.31490  23.15320  16.62572  1.000 227.97547 ? 200 PRO A N   1 
ATOM   976  C CA  . PRO A 1 200 ? 34.97176  24.25412  17.53855  1.000 229.87613 ? 200 PRO A CA  1 
ATOM   977  C C   . PRO A 1 200 ? 34.01641  23.85719  18.65626  1.000 228.64710 ? 200 PRO A C   1 
ATOM   978  O O   . PRO A 1 200 ? 34.38102  23.92296  19.83348  1.000 231.15907 ? 200 PRO A O   1 
ATOM   979  C CB  . PRO A 1 200 ? 34.33908  25.29141  16.60140  1.000 229.12145 ? 200 PRO A CB  1 
ATOM   980  C CG  . PRO A 1 200 ? 34.96338  25.01442  15.27005  1.000 228.71277 ? 200 PRO A CG  1 
ATOM   981  C CD  . PRO A 1 200 ? 35.12136  23.52200  15.21289  1.000 226.66143 ? 200 PRO A CD  1 
ATOM   982  N N   . LYS A 1 201 ? 32.79983  23.44261  18.31200  1.000 226.97961 ? 201 LYS A N   1 
ATOM   983  C CA  . LYS A 1 201 ? 31.80095  23.13537  19.32909  1.000 225.71360 ? 201 LYS A CA  1 
ATOM   984  C C   . LYS A 1 201 ? 32.16198  21.85794  20.07928  1.000 225.93982 ? 201 LYS A C   1 
ATOM   985  O O   . LYS A 1 201 ? 32.52302  20.84719  19.46865  1.000 224.46893 ? 201 LYS A O   1 
ATOM   986  C CB  . LYS A 1 201 ? 30.42079  22.99914  18.69027  1.000 221.98496 ? 201 LYS A CB  1 
ATOM   987  C CG  . LYS A 1 201 ? 29.81467  24.31291  18.22914  1.000 222.27207 ? 201 LYS A CG  1 
ATOM   988  C CD  . LYS A 1 201 ? 28.32238  24.16600  17.98396  1.000 219.21187 ? 201 LYS A CD  1 
ATOM   989  C CE  . LYS A 1 201 ? 27.65743  25.51948  17.81101  1.000 220.12435 ? 201 LYS A CE  1 
ATOM   990  N NZ  . LYS A 1 201 ? 26.17535  25.40259  17.85792  1.000 217.60317 ? 201 LYS A NZ  1 
ATOM   991  N N   . THR A 1 202 ? 32.05562  21.90243  21.40793  1.000 217.53530 ? 202 THR A N   1 
ATOM   992  C CA  . THR A 1 202 ? 32.36021  20.74581  22.23962  1.000 218.19781 ? 202 THR A CA  1 
ATOM   993  C C   . THR A 1 202 ? 31.60809  20.85281  23.55924  1.000 218.68490 ? 202 THR A C   1 
ATOM   994  O O   . THR A 1 202 ? 31.10204  21.91597  23.93064  1.000 219.23733 ? 202 THR A O   1 
ATOM   995  C CB  . THR A 1 202 ? 33.86660  20.60748  22.49821  1.000 221.97355 ? 202 THR A CB  1 
ATOM   996  O OG1 . THR A 1 202 ? 34.12653  19.36588  23.16765  1.000 222.48387 ? 202 THR A OG1 1 
ATOM   997  C CG2 . THR A 1 202 ? 34.36226  21.75296  23.36017  1.000 225.98915 ? 202 THR A CG2 1 
ATOM   998  N N   . TYR A 1 203 ? 31.53367  19.72247  24.25769  1.000 215.82825 ? 203 TYR A N   1 
ATOM   999  C CA  . TYR A 1 203 ? 30.85162  19.60583  25.54003  1.000 216.22853 ? 203 TYR A CA  1 
ATOM   1000 C C   . TYR A 1 203 ? 31.84692  19.17236  26.60840  1.000 220.31830 ? 203 TYR A C   1 
ATOM   1001 O O   . TYR A 1 203 ? 32.71595  18.33453  26.34897  1.000 221.31336 ? 203 TYR A O   1 
ATOM   1002 C CB  . TYR A 1 203 ? 29.70559  18.58800  25.46776  1.000 212.00114 ? 203 TYR A CB  1 
ATOM   1003 C CG  . TYR A 1 203 ? 28.63997  18.90683  24.43894  1.000 208.98996 ? 203 TYR A CG  1 
ATOM   1004 C CD1 . TYR A 1 203 ? 27.49038  19.60080  24.79500  1.000 207.33275 ? 203 TYR A CD1 1 
ATOM   1005 C CD2 . TYR A 1 203 ? 28.77671  18.50416  23.11377  1.000 207.72862 ? 203 TYR A CD2 1 
ATOM   1006 C CE1 . TYR A 1 203 ? 26.51226  19.89400  23.85934  1.000 204.85561 ? 203 TYR A CE1 1 
ATOM   1007 C CE2 . TYR A 1 203 ? 27.80129  18.79554  22.17124  1.000 204.79800 ? 203 TYR A CE2 1 
ATOM   1008 C CZ  . TYR A 1 203 ? 26.67366  19.48927  22.55282  1.000 203.56926 ? 203 TYR A CZ  1 
ATOM   1009 O OH  . TYR A 1 203 ? 25.69966  19.78346  21.62969  1.000 201.41669 ? 203 TYR A OH  1 
ATOM   1010 N N   . ASN A 1 204 ? 31.71901  19.72609  27.81426  1.000 213.08821 ? 204 ASN A N   1 
ATOM   1011 C CA  . ASN A 1 204 ? 32.62931  19.35846  28.89674  1.000 217.23587 ? 204 ASN A CA  1 
ATOM   1012 C C   . ASN A 1 204 ? 31.83512  19.27505  30.19821  1.000 217.63770 ? 204 ASN A C   1 
ATOM   1013 O O   . ASN A 1 204 ? 30.60078  19.22798  30.19340  1.000 214.46944 ? 204 ASN A O   1 
ATOM   1014 C CB  . ASN A 1 204 ? 33.84448  20.30685  28.93914  1.000 220.94985 ? 204 ASN A CB  1 
ATOM   1015 C CG  . ASN A 1 204 ? 33.55580  21.67692  29.54801  1.000 221.94590 ? 204 ASN A CG  1 
ATOM   1016 O OD1 . ASN A 1 204 ? 32.65192  21.84924  30.36224  1.000 221.23859 ? 204 ASN A OD1 1 
ATOM   1017 N ND2 . ASN A 1 204 ? 34.35230  22.66798  29.14825  1.000 223.64987 ? 204 ASN A ND2 1 
ATOM   1018 N N   . GLU A 1 205 ? 32.55903  19.25707  31.32051  1.000 219.16606 ? 205 GLU A N   1 
ATOM   1019 C CA  . GLU A 1 205 ? 31.97662  18.83676  32.59197  1.000 219.50758 ? 205 GLU A CA  1 
ATOM   1020 C C   . GLU A 1 205 ? 30.93066  19.80534  33.12424  1.000 217.89221 ? 205 GLU A C   1 
ATOM   1021 O O   . GLU A 1 205 ? 30.10172  19.40908  33.95202  1.000 216.82970 ? 205 GLU A O   1 
ATOM   1022 C CB  . GLU A 1 205 ? 33.07402  18.65290  33.64084  1.000 223.62785 ? 205 GLU A CB  1 
ATOM   1023 C CG  . GLU A 1 205 ? 34.12336  19.74933  33.64194  1.000 226.42071 ? 205 GLU A CG  1 
ATOM   1024 C CD  . GLU A 1 205 ? 35.34819  19.37707  32.83016  1.000 228.41990 ? 205 GLU A CD  1 
ATOM   1025 O OE1 . GLU A 1 205 ? 36.24717  18.70583  33.37974  1.000 231.30006 ? 205 GLU A OE1 1 
ATOM   1026 O OE2 . GLU A 1 205 ? 35.40705  19.74640  31.64009  1.000 227.06766 ? 205 GLU A OE2 1 
ATOM   1027 N N   . SER A 1 206 ? 30.95092  21.06274  32.68435  1.000 223.99527 ? 206 SER A N   1 
ATOM   1028 C CA  . SER A 1 206 ? 29.96141  22.01462  33.17200  1.000 222.79229 ? 206 SER A CA  1 
ATOM   1029 C C   . SER A 1 206 ? 28.54753  21.60428  32.78230  1.000 218.78715 ? 206 SER A C   1 
ATOM   1030 O O   . SER A 1 206 ? 27.59001  21.91289  33.50249  1.000 218.01871 ? 206 SER A O   1 
ATOM   1031 C CB  . SER A 1 206 ? 30.27256  23.41133  32.64531  1.000 223.74068 ? 206 SER A CB  1 
ATOM   1032 O OG  . SER A 1 206 ? 29.28055  24.32371  33.07140  1.000 226.90019 ? 206 SER A OG  1 
ATOM   1033 N N   . ASN A 1 207 ? 28.39769  20.90009  31.65878  1.000 215.03788 ? 207 ASN A N   1 
ATOM   1034 C CA  . ASN A 1 207 ? 27.09167  20.42413  31.22074  1.000 211.08122 ? 207 ASN A CA  1 
ATOM   1035 C C   . ASN A 1 207 ? 26.56776  19.26968  32.06462  1.000 210.76748 ? 207 ASN A C   1 
ATOM   1036 O O   . ASN A 1 207 ? 25.38526  18.93019  31.94890  1.000 207.97547 ? 207 ASN A O   1 
ATOM   1037 C CB  . ASN A 1 207 ? 27.16072  20.00496  29.75311  1.000 208.38025 ? 207 ASN A CB  1 
ATOM   1038 C CG  . ASN A 1 207 ? 27.78741  21.06780  28.88053  1.000 209.37493 ? 207 ASN A CG  1 
ATOM   1039 O OD1 . ASN A 1 207 ? 29.01038  21.20905  28.82886  1.000 212.24418 ? 207 ASN A OD1 1 
ATOM   1040 N ND2 . ASN A 1 207 ? 26.95135  21.83396  28.19854  1.000 206.97172 ? 207 ASN A ND2 1 
ATOM   1041 N N   . PHE A 1 208 ? 27.40432  18.66664  32.90507  1.000 206.49491 ? 208 PHE A N   1 
ATOM   1042 C CA  . PHE A 1 208 ? 26.94647  17.59016  33.76842  1.000 206.73520 ? 208 PHE A CA  1 
ATOM   1043 C C   . PHE A 1 208 ? 26.02984  18.13165  34.86307  1.000 206.54262 ? 208 PHE A C   1 
ATOM   1044 O O   . PHE A 1 208 ? 26.09323  19.30429  35.24515  1.000 208.06393 ? 208 PHE A O   1 
ATOM   1045 C CB  . PHE A 1 208 ? 28.13778  16.85884  34.38684  1.000 210.54946 ? 208 PHE A CB  1 
ATOM   1046 C CG  . PHE A 1 208 ? 28.62712  15.69871  33.57002  1.000 210.39152 ? 208 PHE A CG  1 
ATOM   1047 C CD1 . PHE A 1 208 ? 29.24912  15.90194  32.34972  1.000 209.81845 ? 208 PHE A CD1 1 
ATOM   1048 C CD2 . PHE A 1 208 ? 28.46746  14.40211  34.02742  1.000 210.97548 ? 208 PHE A CD2 1 
ATOM   1049 C CE1 . PHE A 1 208 ? 29.69879  14.83168  31.59901  1.000 209.61871 ? 208 PHE A CE1 1 
ATOM   1050 C CE2 . PHE A 1 208 ? 28.91291  13.32990  33.28276  1.000 211.06417 ? 208 PHE A CE2 1 
ATOM   1051 C CZ  . PHE A 1 208 ? 29.53077  13.54392  32.06800  1.000 210.30539 ? 208 PHE A CZ  1 
ATOM   1052 N N   . VAL A 1 209 ? 25.16039  17.25523  35.36135  1.000 211.96196 ? 209 VAL A N   1 
ATOM   1053 C CA  . VAL A 1 209 ? 24.17593  17.59285  36.38693  1.000 211.45639 ? 209 VAL A CA  1 
ATOM   1054 C C   . VAL A 1 209 ? 24.41172  16.63739  37.54938  1.000 213.51708 ? 209 VAL A C   1 
ATOM   1055 O O   . VAL A 1 209 ? 23.94432  15.49325  37.52356  1.000 212.45662 ? 209 VAL A O   1 
ATOM   1056 C CB  . VAL A 1 209 ? 22.73596  17.49231  35.87020  1.000 207.47742 ? 209 VAL A CB  1 
ATOM   1057 C CG1 . VAL A 1 209 ? 21.74331  17.89249  36.95765  1.000 206.86634 ? 209 VAL A CG1 1 
ATOM   1058 C CG2 . VAL A 1 209 ? 22.55586  18.36075  34.63274  1.000 205.20658 ? 209 VAL A CG2 1 
ATOM   1059 N N   . SER A 1 210 ? 25.13249  17.10280  38.57138  1.000 214.13616 ? 210 SER A N   1 
ATOM   1060 C CA  . SER A 1 210 ? 25.51308  16.27299  39.71613  1.000 216.35756 ? 210 SER A CA  1 
ATOM   1061 C C   . SER A 1 210 ? 26.26569  15.02834  39.24740  1.000 217.43520 ? 210 SER A C   1 
ATOM   1062 O O   . SER A 1 210 ? 25.99739  13.90741  39.68526  1.000 217.44844 ? 210 SER A O   1 
ATOM   1063 C CB  . SER A 1 210 ? 24.29134  15.89619  40.55910  1.000 214.74246 ? 210 SER A CB  1 
ATOM   1064 O OG  . SER A 1 210 ? 23.47602  17.02709  40.80604  1.000 213.42301 ? 210 SER A OG  1 
ATOM   1065 N N   . ASN A 1 211 ? 27.21439  15.24452  38.33249  1.000 212.62479 ? 211 ASN A N   1 
ATOM   1066 C CA  . ASN A 1 211 ? 27.99229  14.17206  37.70810  1.000 213.80933 ? 211 ASN A CA  1 
ATOM   1067 C C   . ASN A 1 211 ? 27.08742  13.19820  36.95189  1.000 211.01290 ? 211 ASN A C   1 
ATOM   1068 O O   . ASN A 1 211 ? 27.19762  11.97837  37.08458  1.000 212.00535 ? 211 ASN A O   1 
ATOM   1069 C CB  . ASN A 1 211 ? 28.85863  13.43882  38.73801  1.000 217.18579 ? 211 ASN A CB  1 
ATOM   1070 C CG  . ASN A 1 211 ? 30.16094  14.16127  39.02691  1.000 220.59606 ? 211 ASN A CG  1 
ATOM   1071 O OD1 . ASN A 1 211 ? 30.69404  14.86811  38.17103  1.000 220.81093 ? 211 ASN A OD1 1 
ATOM   1072 N ND2 . ASN A 1 211 ? 30.68655  13.97760  40.23305  1.000 223.24853 ? 211 ASN A ND2 1 
ATOM   1073 N N   . VAL A 1 212 ? 26.18891  13.75376  36.14214  1.000 207.50609 ? 212 VAL A N   1 
ATOM   1074 C CA  . VAL A 1 212 ? 25.28990  12.96864  35.29908  1.000 204.26202 ? 212 VAL A CA  1 
ATOM   1075 C C   . VAL A 1 212 ? 25.04168  13.74723  34.01346  1.000 201.38015 ? 212 VAL A C   1 
ATOM   1076 O O   . VAL A 1 212 ? 24.77056  14.95174  34.04815  1.000 200.72231 ? 212 VAL A O   1 
ATOM   1077 C CB  . VAL A 1 212 ? 23.96548  12.64151  36.02212  1.000 202.32320 ? 212 VAL A CB  1 
ATOM   1078 C CG1 . VAL A 1 212 ? 22.80611  12.56876  35.03592  1.000 197.77159 ? 212 VAL A CG1 1 
ATOM   1079 C CG2 . VAL A 1 212 ? 24.08756  11.33178  36.78455  1.000 204.29592 ? 212 VAL A CG2 1 
ATOM   1080 N N   . LEU A 1 213 ? 25.14564  13.05943  32.87763  1.000 198.01153 ? 213 LEU A N   1 
ATOM   1081 C CA  . LEU A 1 213 ? 24.90357  13.65348  31.56858  1.000 194.85070 ? 213 LEU A CA  1 
ATOM   1082 C C   . LEU A 1 213 ? 23.92930  12.77142  30.80394  1.000 190.86073 ? 213 LEU A C   1 
ATOM   1083 O O   . LEU A 1 213 ? 24.18470  11.57735  30.61679  1.000 191.08258 ? 213 LEU A O   1 
ATOM   1084 C CB  . LEU A 1 213 ? 26.20849  13.82118  30.78540  1.000 196.53817 ? 213 LEU A CB  1 
ATOM   1085 C CG  . LEU A 1 213 ? 26.07321  14.28398  29.33318  1.000 193.30593 ? 213 LEU A CG  1 
ATOM   1086 C CD1 . LEU A 1 213 ? 25.32203  15.60409  29.24750  1.000 191.62430 ? 213 LEU A CD1 1 
ATOM   1087 C CD2 . LEU A 1 213 ? 27.44151  14.39818  28.68025  1.000 195.34628 ? 213 LEU A CD2 1 
ATOM   1088 N N   . GLU A 1 214 ? 22.82334  13.36030  30.35914  1.000 194.09709 ? 214 GLU A N   1 
ATOM   1089 C CA  . GLU A 1 214 ? 21.74566  12.64615  29.67799  1.000 189.94029 ? 214 GLU A CA  1 
ATOM   1090 C C   . GLU A 1 214 ? 21.71706  13.10185  28.21987  1.000 186.67062 ? 214 GLU A C   1 
ATOM   1091 O O   . GLU A 1 214 ? 21.09080  14.10623  27.87836  1.000 184.67654 ? 214 GLU A O   1 
ATOM   1092 C CB  . GLU A 1 214 ? 20.41470  12.89860  30.37906  1.000 188.00583 ? 214 GLU A CB  1 
ATOM   1093 C CG  . GLU A 1 214 ? 20.31843  12.25988  31.75629  1.000 190.66700 ? 214 GLU A CG  1 
ATOM   1094 C CD  . GLU A 1 214 ? 19.26636  12.91033  32.63134  1.000 189.72244 ? 214 GLU A CD  1 
ATOM   1095 O OE1 . GLU A 1 214 ? 19.54918  13.98577  33.20082  1.000 191.59736 ? 214 GLU A OE1 1 
ATOM   1096 O OE2 . GLU A 1 214 ? 18.15532  12.35100  32.74389  1.000 187.25565 ? 214 GLU A OE2 1 
ATOM   1097 N N   . VAL A 1 215 ? 22.39547  12.34743  27.35969  1.000 191.57895 ? 215 VAL A N   1 
ATOM   1098 C CA  . VAL A 1 215 ? 22.51525  12.68531  25.94567  1.000 188.59266 ? 215 VAL A CA  1 
ATOM   1099 C C   . VAL A 1 215 ? 21.40636  11.99144  25.16704  1.000 183.90220 ? 215 VAL A C   1 
ATOM   1100 O O   . VAL A 1 215 ? 21.17060  10.78945  25.33843  1.000 183.14867 ? 215 VAL A O   1 
ATOM   1101 C CB  . VAL A 1 215 ? 23.89783  12.28669  25.40134  1.000 190.66350 ? 215 VAL A CB  1 
ATOM   1102 C CG1 . VAL A 1 215 ? 23.98038  12.54961  23.90318  1.000 187.37440 ? 215 VAL A CG1 1 
ATOM   1103 C CG2 . VAL A 1 215 ? 24.99223  13.03761  26.13341  1.000 195.32828 ? 215 VAL A CG2 1 
ATOM   1104 N N   . GLU A 1 216 ? 20.72394  12.74738  24.31176  1.000 190.22731 ? 216 GLU A N   1 
ATOM   1105 C CA  . GLU A 1 216 ? 19.76982  12.19141  23.36307  1.000 185.95603 ? 216 GLU A CA  1 
ATOM   1106 C C   . GLU A 1 216 ? 20.44469  11.99899  22.01163  1.000 184.59631 ? 216 GLU A C   1 
ATOM   1107 O O   . GLU A 1 216 ? 21.29394  12.80003  21.61009  1.000 186.36593 ? 216 GLU A O   1 
ATOM   1108 C CB  . GLU A 1 216 ? 18.54720  13.09685  23.20567  1.000 184.10936 ? 216 GLU A CB  1 
ATOM   1109 C CG  . GLU A 1 216 ? 17.48315  12.90605  24.26977  1.000 183.70594 ? 216 GLU A CG  1 
ATOM   1110 C CD  . GLU A 1 216 ? 16.09094  13.20853  23.75057  1.000 180.54920 ? 216 GLU A CD  1 
ATOM   1111 O OE1 . GLU A 1 216 ? 15.91855  13.26863  22.51497  1.000 178.38374 ? 216 GLU A OE1 1 
ATOM   1112 O OE2 . GLU A 1 216 ? 15.16982  13.38552  24.57467  1.000 180.45670 ? 216 GLU A OE2 1 
ATOM   1113 N N   . LEU A 1 217 ? 20.05843  10.93639  21.31140  1.000 192.57584 ? 217 LEU A N   1 
ATOM   1114 C CA  . LEU A 1 217 ? 20.62812  10.60121  20.01433  1.000 191.22345 ? 217 LEU A CA  1 
ATOM   1115 C C   . LEU A 1 217 ? 19.51563  10.43377  18.99195  1.000 188.05791 ? 217 LEU A C   1 
ATOM   1116 O O   . LEU A 1 217 ? 18.49377  9.79947   19.27276  1.000 185.92630 ? 217 LEU A O   1 
ATOM   1117 C CB  . LEU A 1 217 ? 21.46469  9.31889   20.08679  1.000 191.78276 ? 217 LEU A CB  1 
ATOM   1118 C CG  . LEU A 1 217 ? 22.77392  9.41821   20.86938  1.000 195.97595 ? 217 LEU A CG  1 
ATOM   1119 C CD1 . LEU A 1 217 ? 23.43833  8.05596   20.97509  1.000 196.72380 ? 217 LEU A CD1 1 
ATOM   1120 C CD2 . LEU A 1 217 ? 23.71111  10.42536  20.21870  1.000 197.34914 ? 217 LEU A CD2 1 
ATOM   1121 N N   . ASN A 1 218 ? 19.72172  10.99839  17.80499  1.000 206.38356 ? 218 ASN A N   1 
ATOM   1122 C CA  . ASN A 1 218 ? 18.75334  10.87274  16.72845  1.000 203.33804 ? 218 ASN A CA  1 
ATOM   1123 C C   . ASN A 1 218 ? 18.84420  9.47636   16.11271  1.000 198.70306 ? 218 ASN A C   1 
ATOM   1124 O O   . ASN A 1 218 ? 19.56424  8.60056   16.60269  1.000 199.35533 ? 218 ASN A O   1 
ATOM   1125 C CB  . ASN A 1 218 ? 18.97543  11.96717  15.68789  1.000 205.29239 ? 218 ASN A CB  1 
ATOM   1126 C CG  . ASN A 1 218 ? 17.67866  12.48276  15.10228  1.000 203.84952 ? 218 ASN A CG  1 
ATOM   1127 O OD1 . ASN A 1 218 ? 16.69594  11.74917  15.00301  1.000 198.76079 ? 218 ASN A OD1 1 
ATOM   1128 N ND2 . ASN A 1 218 ? 17.66599  13.75352  14.71674  1.000 205.71241 ? 218 ASN A ND2 1 
ATOM   1129 N N   . ASP A 1 219 ? 18.09773  9.26820   15.02293  1.000 212.96871 ? 219 ASP A N   1 
ATOM   1130 C CA  . ASP A 1 219 ? 18.01011  7.95307   14.39104  1.000 209.80526 ? 219 ASP A CA  1 
ATOM   1131 C C   . ASP A 1 219 ? 19.39161  7.35927   14.13975  1.000 211.32995 ? 219 ASP A C   1 
ATOM   1132 O O   . ASP A 1 219 ? 19.70208  6.25486   14.59655  1.000 210.25660 ? 219 ASP A O   1 
ATOM   1133 C CB  . ASP A 1 219 ? 17.21972  8.05403   13.08444  1.000 207.88608 ? 219 ASP A CB  1 
ATOM   1134 C CG  . ASP A 1 219 ? 15.72260  8.09243   13.31148  1.000 205.26053 ? 219 ASP A CG  1 
ATOM   1135 O OD1 . ASP A 1 219 ? 15.26349  7.55159   14.33961  1.000 203.98855 ? 219 ASP A OD1 1 
ATOM   1136 O OD2 . ASP A 1 219 ? 15.00465  8.65668   12.45961  1.000 204.86886 ? 219 ASP A OD2 1 
ATOM   1137 N N   . GLY A 1 220 ? 20.23518  8.08506   13.41443  1.000 193.07450 ? 220 GLY A N   1 
ATOM   1138 C CA  . GLY A 1 220 ? 21.61927  7.69166   13.24390  1.000 195.17937 ? 220 GLY A CA  1 
ATOM   1139 C C   . GLY A 1 220 ? 22.54440  8.85584   13.52408  1.000 199.94922 ? 220 GLY A C   1 
ATOM   1140 O O   . GLY A 1 220 ? 22.37245  9.93094   12.94327  1.000 202.61257 ? 220 GLY A O   1 
ATOM   1141 N N   . GLU A 1 221 ? 23.51672  8.67034   14.41126  1.000 190.81226 ? 221 GLU A N   1 
ATOM   1142 C CA  . GLU A 1 221 ? 24.40776  9.75870   14.79788  1.000 193.87054 ? 221 GLU A CA  1 
ATOM   1143 C C   . GLU A 1 221 ? 25.69861  9.16841   15.35541  1.000 196.03859 ? 221 GLU A C   1 
ATOM   1144 O O   . GLU A 1 221 ? 25.94542  7.96148   15.25802  1.000 195.15074 ? 221 GLU A O   1 
ATOM   1145 C CB  . GLU A 1 221 ? 23.72128  10.69492  15.79756  1.000 194.47011 ? 221 GLU A CB  1 
ATOM   1146 C CG  . GLU A 1 221 ? 23.25405  12.00125  15.17919  1.000 195.24319 ? 221 GLU A CG  1 
ATOM   1147 C CD  . GLU A 1 221 ? 22.30394  12.76639  16.07403  1.000 195.08194 ? 221 GLU A CD  1 
ATOM   1148 O OE1 . GLU A 1 221 ? 22.05379  12.30722  17.20790  1.000 194.81257 ? 221 GLU A OE1 1 
ATOM   1149 O OE2 . GLU A 1 221 ? 21.80123  13.82439  15.64017  1.000 195.54820 ? 221 GLU A OE2 1 
ATOM   1150 N N   . LEU A 1 222 ? 26.52485  10.03001  15.94552  1.000 183.67628 ? 222 LEU A N   1 
ATOM   1151 C CA  . LEU A 1 222 ? 27.84810  9.63864   16.41762  1.000 186.48726 ? 222 LEU A CA  1 
ATOM   1152 C C   . LEU A 1 222 ? 28.19093  10.47089  17.64204  1.000 189.84907 ? 222 LEU A C   1 
ATOM   1153 O O   . LEU A 1 222 ? 28.22851  11.70236  17.56205  1.000 191.33601 ? 222 LEU A O   1 
ATOM   1154 C CB  . LEU A 1 222 ? 28.89534  9.83974   15.32238  1.000 187.71769 ? 222 LEU A CB  1 
ATOM   1155 C CG  . LEU A 1 222 ? 30.19959  9.05142   15.43021  1.000 189.79286 ? 222 LEU A CG  1 
ATOM   1156 C CD1 . LEU A 1 222 ? 29.95422  7.58036   15.13455  1.000 187.46870 ? 222 LEU A CD1 1 
ATOM   1157 C CD2 . LEU A 1 222 ? 31.24972  9.62543   14.49241  1.000 191.83551 ? 222 LEU A CD2 1 
ATOM   1158 N N   . PHE A 1 223 ? 28.43907  9.80418   18.76499  1.000 180.07833 ? 223 PHE A N   1 
ATOM   1159 C CA  . PHE A 1 223 ? 28.81319  10.45917  20.01102  1.000 184.38261 ? 223 PHE A CA  1 
ATOM   1160 C C   . PHE A 1 223 ? 30.28352  10.18664  20.29568  1.000 188.38742 ? 223 PHE A C   1 
ATOM   1161 O O   . PHE A 1 223 ? 30.71739  9.03076   20.27659  1.000 188.68829 ? 223 PHE A O   1 
ATOM   1162 C CB  . PHE A 1 223 ? 27.94210  9.96667   21.17036  1.000 184.63392 ? 223 PHE A CB  1 
ATOM   1163 C CG  . PHE A 1 223 ? 28.28490  10.58731  22.49572  1.000 188.94114 ? 223 PHE A CG  1 
ATOM   1164 C CD1 . PHE A 1 223 ? 27.71441  11.78883  22.88212  1.000 189.16291 ? 223 PHE A CD1 1 
ATOM   1165 C CD2 . PHE A 1 223 ? 29.17326  9.96629   23.35826  1.000 193.08494 ? 223 PHE A CD2 1 
ATOM   1166 C CE1 . PHE A 1 223 ? 28.02837  12.36095  24.10107  1.000 193.11873 ? 223 PHE A CE1 1 
ATOM   1167 C CE2 . PHE A 1 223 ? 29.49029  10.53465  24.57583  1.000 197.37086 ? 223 PHE A CE2 1 
ATOM   1168 C CZ  . PHE A 1 223 ? 28.91741  11.73152  24.94808  1.000 197.18373 ? 223 PHE A CZ  1 
ATOM   1169 N N   . VAL A 1 224 ? 31.04494  11.24752  20.55903  1.000 187.12187 ? 224 VAL A N   1 
ATOM   1170 C CA  . VAL A 1 224 ? 32.47611  11.14256  20.81684  1.000 191.21968 ? 224 VAL A CA  1 
ATOM   1171 C C   . VAL A 1 224 ? 32.77186  11.71205  22.19857  1.000 195.66900 ? 224 VAL A C   1 
ATOM   1172 O O   . VAL A 1 224 ? 32.06513  12.59618  22.69340  1.000 195.45093 ? 224 VAL A O   1 
ATOM   1173 C CB  . VAL A 1 224 ? 33.30830  11.86858  19.73276  1.000 191.38610 ? 224 VAL A CB  1 
ATOM   1174 C CG1 . VAL A 1 224 ? 34.77789  11.47190  19.81738  1.000 195.04902 ? 224 VAL A CG1 1 
ATOM   1175 C CG2 . VAL A 1 224 ? 32.75601  11.57622  18.34462  1.000 187.26334 ? 224 VAL A CG2 1 
ATOM   1176 N N   . LEU A 1 225 ? 33.82320  11.18781  22.82674  1.000 195.64487 ? 225 LEU A N   1 
ATOM   1177 C CA  . LEU A 1 225 ? 34.28240  11.67634  24.11972  1.000 197.56463 ? 225 LEU A CA  1 
ATOM   1178 C C   . LEU A 1 225 ? 35.76660  11.37075  24.24975  1.000 198.36256 ? 225 LEU A C   1 
ATOM   1179 O O   . LEU A 1 225 ? 36.28551  10.46050  23.60218  1.000 197.35783 ? 225 LEU A O   1 
ATOM   1180 C CB  . LEU A 1 225 ? 33.49132  11.04976  25.27596  1.000 197.72281 ? 225 LEU A CB  1 
ATOM   1181 C CG  . LEU A 1 225 ? 33.64029  9.53697   25.45846  1.000 196.80914 ? 225 LEU A CG  1 
ATOM   1182 C CD1 . LEU A 1 225 ? 34.60458  9.22235   26.58303  1.000 199.06610 ? 225 LEU A CD1 1 
ATOM   1183 C CD2 . LEU A 1 225 ? 32.29900  8.87002   25.70789  1.000 195.76041 ? 225 LEU A CD2 1 
ATOM   1184 N N   . ALA A 1 226 ? 36.45046  12.13753  25.10035  1.000 209.68329 ? 226 ALA A N   1 
ATOM   1185 C CA  . ALA A 1 226 ? 37.90207  12.01124  25.25652  1.000 213.63761 ? 226 ALA A CA  1 
ATOM   1186 C C   . ALA A 1 226 ? 38.24899  12.07010  26.74218  1.000 218.38966 ? 226 ALA A C   1 
ATOM   1187 O O   . ALA A 1 226 ? 38.33653  13.15691  27.32031  1.000 220.22667 ? 226 ALA A O   1 
ATOM   1188 C CB  . ALA A 1 226 ? 38.63150  13.09635  24.47276  1.000 212.93558 ? 226 ALA A CB  1 
ATOM   1189 N N   . CYS A 1 227 ? 38.45475  10.90368  27.34807  1.000 223.32558 ? 227 CYS A N   1 
ATOM   1190 C CA  . CYS A 1 227 ? 38.86009  10.78842  28.74768  1.000 227.30803 ? 227 CYS A CA  1 
ATOM   1191 C C   . CYS A 1 227 ? 39.42056  9.38365   28.95952  1.000 228.72035 ? 227 CYS A C   1 
ATOM   1192 O O   . CYS A 1 227 ? 39.64854  8.63926   28.00001  1.000 227.33090 ? 227 CYS A O   1 
ATOM   1193 C CB  . CYS A 1 227 ? 37.68848  11.09249  29.68920  1.000 227.38477 ? 227 CYS A CB  1 
ATOM   1194 S SG  . CYS A 1 227 ? 36.28482  9.98413   29.45854  1.000 224.08870 ? 227 CYS A SG  1 
ATOM   1195 N N   . GLU A 1 228 ? 39.63993  9.01459   30.22083  1.000 224.75266 ? 228 GLU A N   1 
ATOM   1196 C CA  . GLU A 1 228 ? 40.21073  7.72035   30.57747  1.000 225.74652 ? 228 GLU A CA  1 
ATOM   1197 C C   . GLU A 1 228 ? 39.26340  6.98242   31.51430  1.000 225.81987 ? 228 GLU A C   1 
ATOM   1198 O O   . GLU A 1 228 ? 38.87567  7.51527   32.55946  1.000 226.99706 ? 228 GLU A O   1 
ATOM   1199 C CB  . GLU A 1 228 ? 41.58886  7.88145   31.22915  1.000 228.08273 ? 228 GLU A CB  1 
ATOM   1200 C CG  . GLU A 1 228 ? 42.66029  8.45511   30.30492  1.000 228.13123 ? 228 GLU A CG  1 
ATOM   1201 C CD  . GLU A 1 228 ? 42.59985  9.96815   30.19584  1.000 228.59757 ? 228 GLU A CD  1 
ATOM   1202 O OE1 . GLU A 1 228 ? 41.81057  10.58779  30.94134  1.000 228.92158 ? 228 GLU A OE1 1 
ATOM   1203 O OE2 . GLU A 1 228 ? 43.34139  10.53525  29.36324  1.000 228.52546 ? 228 GLU A OE2 1 
ATOM   1204 N N   . LEU A 1 229 ? 38.91005  5.75360   31.14531  1.000 229.15034 ? 229 LEU A N   1 
ATOM   1205 C CA  . LEU A 1 229 ? 37.85808  5.00939   31.82016  1.000 228.85209 ? 229 LEU A CA  1 
ATOM   1206 C C   . LEU A 1 229 ? 38.36417  4.34590   33.09786  1.000 230.81398 ? 229 LEU A C   1 
ATOM   1207 O O   . LEU A 1 229 ? 39.55989  4.09813   33.27656  1.000 231.86577 ? 229 LEU A O   1 
ATOM   1208 C CB  . LEU A 1 229 ? 37.28370  3.94036   30.89332  1.000 226.68124 ? 229 LEU A CB  1 
ATOM   1209 C CG  . LEU A 1 229 ? 36.69875  4.42873   29.57358  1.000 224.56877 ? 229 LEU A CG  1 
ATOM   1210 C CD1 . LEU A 1 229 ? 36.42555  3.25066   28.65397  1.000 221.41483 ? 229 LEU A CD1 1 
ATOM   1211 C CD2 . LEU A 1 229 ? 35.43126  5.20865   29.84606  1.000 223.48004 ? 229 LEU A CD2 1 
ATOM   1212 N N   . ILE A 1 230 ? 37.42095  4.05181   33.98898  1.000 235.35231 ? 230 ILE A N   1 
ATOM   1213 C CA  . ILE A 1 230 ? 37.68325  3.24875   35.17761  1.000 236.84208 ? 230 ILE A CA  1 
ATOM   1214 C C   . ILE A 1 230 ? 37.39263  1.79636   34.82731  1.000 235.74066 ? 230 ILE A C   1 
ATOM   1215 O O   . ILE A 1 230 ? 36.25496  1.44791   34.49295  1.000 234.38768 ? 230 ILE A O   1 
ATOM   1216 C CB  . ILE A 1 230 ? 36.82480  3.70492   36.36590  1.000 237.65022 ? 230 ILE A CB  1 
ATOM   1217 C CG1 . ILE A 1 230 ? 36.70755  5.22807   36.39568  1.000 237.27122 ? 230 ILE A CG1 1 
ATOM   1218 C CG2 . ILE A 1 230 ? 37.41083  3.18460   37.67309  1.000 239.46353 ? 230 ILE A CG2 1 
ATOM   1219 C CD1 . ILE A 1 230 ? 35.79576  5.73845   37.48864  1.000 236.24364 ? 230 ILE A CD1 1 
ATOM   1220 N N   . ASN A 1 231 ? 38.42201  0.95354   34.88087  1.000 235.80140 ? 231 ASN A N   1 
ATOM   1221 C CA  . ASN A 1 231 ? 38.35039  -0.46330  34.52908  1.000 234.61812 ? 231 ASN A CA  1 
ATOM   1222 C C   . ASN A 1 231 ? 37.87585  -0.70181  33.09674  1.000 231.84175 ? 231 ASN A C   1 
ATOM   1223 O O   . ASN A 1 231 ? 37.67070  -1.85730  32.70346  1.000 230.34649 ? 231 ASN A O   1 
ATOM   1224 C CB  . ASN A 1 231 ? 37.46714  -1.24175  35.51252  1.000 235.35208 ? 231 ASN A CB  1 
ATOM   1225 C CG  . ASN A 1 231 ? 38.03129  -1.24523  36.91737  1.000 237.65894 ? 231 ASN A CG  1 
ATOM   1226 O OD1 . ASN A 1 231 ? 38.83647  -0.38558  37.27525  1.000 238.85188 ? 231 ASN A OD1 1 
ATOM   1227 N ND2 . ASN A 1 231 ? 37.61307  -2.21441  37.72241  1.000 238.29531 ? 231 ASN A ND2 1 
ATOM   1228 N N   . LYS A 1 232 ? 37.69129  0.36507   32.31325  1.000 233.18032 ? 232 LYS A N   1 
ATOM   1229 C CA  . LYS A 1 232 ? 37.46038  0.29826   30.86715  1.000 230.17484 ? 232 LYS A CA  1 
ATOM   1230 C C   . LYS A 1 232 ? 36.20610  -0.49770  30.50550  1.000 228.16320 ? 232 LYS A C   1 
ATOM   1231 O O   . LYS A 1 232 ? 36.15996  -1.16243  29.46808  1.000 224.95471 ? 232 LYS A O   1 
ATOM   1232 C CB  . LYS A 1 232 ? 38.68356  -0.26957  30.13717  1.000 228.44487 ? 232 LYS A CB  1 
ATOM   1233 C CG  . LYS A 1 232 ? 40.02413  0.28105   30.62838  1.000 230.60712 ? 232 LYS A CG  1 
ATOM   1234 C CD  . LYS A 1 232 ? 40.06285  1.80469   30.62321  1.000 232.00455 ? 232 LYS A CD  1 
ATOM   1235 C CE  . LYS A 1 232 ? 40.35260  2.37018   29.24240  1.000 229.34576 ? 232 LYS A CE  1 
ATOM   1236 N NZ  . LYS A 1 232 ? 41.81094  2.38887   28.94145  1.000 229.20544 ? 232 LYS A NZ  1 
ATOM   1237 N N   . LYS A 1 233 ? 35.17428  -0.43475  31.34390  1.000 232.64352 ? 233 LYS A N   1 
ATOM   1238 C CA  . LYS A 1 233 ? 33.87780  -1.04777  31.05047  1.000 228.66762 ? 233 LYS A CA  1 
ATOM   1239 C C   . LYS A 1 233 ? 32.90216  0.08571   30.73876  1.000 210.03154 ? 233 LYS A C   1 
ATOM   1240 O O   . LYS A 1 233 ? 32.34015  0.69535   31.65099  1.000 223.89270 ? 233 LYS A O   1 
ATOM   1241 C CB  . LYS A 1 233 ? 33.39791  -1.90217  32.22279  1.000 231.48854 ? 233 LYS A CB  1 
ATOM   1242 C CG  . LYS A 1 233 ? 34.46180  -2.81503  32.81441  1.000 233.37721 ? 233 LYS A CG  1 
ATOM   1243 C CD  . LYS A 1 233 ? 33.85179  -4.03832  33.47742  1.000 232.79810 ? 233 LYS A CD  1 
ATOM   1244 C CE  . LYS A 1 233 ? 34.93760  -4.94971  34.03523  1.000 234.45610 ? 233 LYS A CE  1 
ATOM   1245 N NZ  . LYS A 1 233 ? 34.40838  -6.30445  34.36460  1.000 233.41104 ? 233 LYS A NZ  1 
ATOM   1246 N N   . CYS A 1 234 ? 32.70184  0.37430   29.45057  1.000 227.12425 ? 234 CYS A N   1 
ATOM   1247 C CA  . CYS A 1 234 ? 31.92177  1.53496   29.04372  1.000 219.97674 ? 234 CYS A CA  1 
ATOM   1248 C C   . CYS A 1 234 ? 31.18276  1.28420   27.74329  1.000 205.46160 ? 234 CYS A C   1 
ATOM   1249 O O   . CYS A 1 234 ? 31.68184  0.59920   26.84598  1.000 201.92330 ? 234 CYS A O   1 
ATOM   1250 C CB  . CYS A 1 234 ? 32.82427  2.75966   28.87646  1.000 222.65796 ? 234 CYS A CB  1 
ATOM   1251 S SG  . CYS A 1 234 ? 32.31472  4.02849   27.71871  1.000 228.89736 ? 234 CYS A SG  1 
ATOM   1252 N N   . PHE A 1 235 ? 29.99322  1.87973   27.66484  1.000 220.81202 ? 235 PHE A N   1 
ATOM   1253 C CA  . PHE A 1 235 ? 29.19757  2.04797   26.45251  1.000 213.55964 ? 235 PHE A CA  1 
ATOM   1254 C C   . PHE A 1 235 ? 28.72697  0.73289   25.84655  1.000 210.45181 ? 235 PHE A C   1 
ATOM   1255 O O   . PHE A 1 235 ? 28.37288  0.68141   24.66739  1.000 204.72703 ? 235 PHE A O   1 
ATOM   1256 C CB  . PHE A 1 235 ? 29.94703  2.87499   25.40413  1.000 210.93075 ? 235 PHE A CB  1 
ATOM   1257 C CG  . PHE A 1 235 ? 29.61037  4.33755   25.43980  1.000 209.66918 ? 235 PHE A CG  1 
ATOM   1258 C CD1 . PHE A 1 235 ? 28.77181  4.84356   26.41956  1.000 210.84115 ? 235 PHE A CD1 1 
ATOM   1259 C CD2 . PHE A 1 235 ? 30.09981  5.20205   24.47626  1.000 207.18115 ? 235 PHE A CD2 1 
ATOM   1260 C CE1 . PHE A 1 235 ? 28.44152  6.18799   26.44606  1.000 209.47550 ? 235 PHE A CE1 1 
ATOM   1261 C CE2 . PHE A 1 235 ? 29.76904  6.55669   24.49982  1.000 206.32992 ? 235 PHE A CE2 1 
ATOM   1262 C CZ  . PHE A 1 235 ? 28.94052  7.04359   25.48775  1.000 207.46430 ? 235 PHE A CZ  1 
ATOM   1263 N N   . GLN A 1 236 ? 28.70349  -0.33915  26.62055  1.000 219.97750 ? 236 GLN A N   1 
ATOM   1264 C CA  . GLN A 1 236 ? 28.10531  -1.58163  26.16111  1.000 217.37241 ? 236 GLN A CA  1 
ATOM   1265 C C   . GLN A 1 236 ? 26.96877  -2.06263  27.04417  1.000 219.99279 ? 236 GLN A C   1 
ATOM   1266 O O   . GLN A 1 236 ? 26.05891  -2.73191  26.54870  1.000 216.06029 ? 236 GLN A O   1 
ATOM   1267 C CB  . GLN A 1 236 ? 29.16544  -2.68974  26.07727  1.000 220.83373 ? 236 GLN A CB  1 
ATOM   1268 C CG  . GLN A 1 236 ? 30.34425  -2.35868  25.18106  1.000 219.55074 ? 236 GLN A CG  1 
ATOM   1269 C CD  . GLN A 1 236 ? 31.65908  -2.82875  25.77279  1.000 226.06180 ? 236 GLN A CD  1 
ATOM   1270 O OE1 . GLN A 1 236 ? 32.15146  -3.91170  25.45134  1.000 226.28401 ? 236 GLN A OE1 1 
ATOM   1271 N NE2 . GLN A 1 236 ? 32.23092  -2.01584  26.65351  1.000 231.10509 ? 236 GLN A NE2 1 
ATOM   1272 N N   . GLU A 1 237 ? 26.99377  -1.73031  28.33049  1.000 208.50076 ? 237 GLU A N   1 
ATOM   1273 C CA  . GLU A 1 237 ? 26.03579  -2.22268  29.30295  1.000 216.63883 ? 237 GLU A CA  1 
ATOM   1274 C C   . GLU A 1 237 ? 24.82659  -1.29173  29.38530  1.000 211.06507 ? 237 GLU A C   1 
ATOM   1275 O O   . GLU A 1 237 ? 24.75915  -0.25008  28.72903  1.000 202.82978 ? 237 GLU A O   1 
ATOM   1276 C CB  . GLU A 1 237 ? 26.70952  -2.37578  30.66660  1.000 235.52781 ? 237 GLU A CB  1 
ATOM   1277 C CG  . GLU A 1 237 ? 27.63449  -1.21587  31.03350  1.000 238.53756 ? 237 GLU A CG  1 
ATOM   1278 C CD  . GLU A 1 237 ? 29.04560  -1.38606  30.49011  1.000 237.80329 ? 237 GLU A CD  1 
ATOM   1279 O OE1 . GLU A 1 237 ? 29.77652  -2.26544  30.99390  1.000 245.03454 ? 237 GLU A OE1 1 
ATOM   1280 O OE2 . GLU A 1 237 ? 29.41782  -0.64751  29.55254  1.000 222.95144 ? 237 GLU A OE2 1 
ATOM   1281 N N   . GLY A 1 238 ? 23.85453  -1.68474  30.20206  1.000 216.81414 ? 238 GLY A N   1 
ATOM   1282 C CA  . GLY A 1 238 ? 22.66600  -0.88454  30.42425  1.000 213.92171 ? 238 GLY A CA  1 
ATOM   1283 C C   . GLY A 1 238 ? 21.98297  -1.33289  31.69304  1.000 226.57596 ? 238 GLY A C   1 
ATOM   1284 O O   . GLY A 1 238 ? 21.99713  -2.51944  32.03503  1.000 233.31502 ? 238 GLY A O   1 
ATOM   1285 N N   . LYS A 1 239 ? 21.37945  -0.37693  32.40086  1.000 213.09601 ? 239 LYS A N   1 
ATOM   1286 C CA  . LYS A 1 239 ? 20.82453  -0.65434  33.71911  1.000 234.14597 ? 239 LYS A CA  1 
ATOM   1287 C C   . LYS A 1 239 ? 19.30625  -0.77178  33.74121  1.000 230.88437 ? 239 LYS A C   1 
ATOM   1288 O O   . LYS A 1 239 ? 18.75533  -1.23770  34.74402  1.000 232.37872 ? 239 LYS A O   1 
ATOM   1289 C CB  . LYS A 1 239 ? 21.26471  0.41770   34.72324  1.000 235.79364 ? 239 LYS A CB  1 
ATOM   1290 C CG  . LYS A 1 239 ? 21.54850  -0.15559  36.10217  1.000 239.65821 ? 239 LYS A CG  1 
ATOM   1291 C CD  . LYS A 1 239 ? 21.07248  0.76005   37.21046  1.000 240.08011 ? 239 LYS A CD  1 
ATOM   1292 C CE  . LYS A 1 239 ? 21.15688  0.05577   38.55314  1.000 242.49826 ? 239 LYS A CE  1 
ATOM   1293 N NZ  . LYS A 1 239 ? 20.56825  0.86596   39.65115  1.000 241.74412 ? 239 LYS A NZ  1 
ATOM   1294 N N   . GLU A 1 240 ? 18.61292  -0.37272  32.67460  1.000 241.14770 ? 240 GLU A N   1 
ATOM   1295 C CA  . GLU A 1 240 ? 17.17533  -0.58509  32.58119  1.000 238.18438 ? 240 GLU A CA  1 
ATOM   1296 C C   . GLU A 1 240 ? 16.82121  -2.00900  32.15849  1.000 238.61836 ? 240 GLU A C   1 
ATOM   1297 O O   . GLU A 1 240 ? 15.72261  -2.23042  31.63790  1.000 235.01783 ? 240 GLU A O   1 
ATOM   1298 C CB  . GLU A 1 240 ? 16.55189  0.42724   31.61536  1.000 226.73303 ? 240 GLU A CB  1 
ATOM   1299 C CG  . GLU A 1 240 ? 15.44464  1.25817   32.23428  1.000 230.62785 ? 240 GLU A CG  1 
ATOM   1300 C CD  . GLU A 1 240 ? 14.84602  2.24922   31.26307  1.000 225.14879 ? 240 GLU A CD  1 
ATOM   1301 O OE1 . GLU A 1 240 ? 15.53433  2.62814   30.29377  1.000 209.17247 ? 240 GLU A OE1 1 
ATOM   1302 O OE2 . GLU A 1 240 ? 13.68214  2.64822   31.46654  1.000 222.99020 ? 240 GLU A OE2 1 
ATOM   1303 N N   . LYS A 1 241 ? 17.72922  -2.96690  32.36961  1.000 239.19537 ? 241 LYS A N   1 
ATOM   1304 C CA  . LYS A 1 241 ? 17.60021  -4.34393  31.87972  1.000 240.57243 ? 241 LYS A CA  1 
ATOM   1305 C C   . LYS A 1 241 ? 17.35542  -4.39280  30.37148  1.000 214.93536 ? 241 LYS A C   1 
ATOM   1306 O O   . LYS A 1 241 ? 16.91305  -5.41362  29.83248  1.000 214.30523 ? 241 LYS A O   1 
ATOM   1307 C CB  . LYS A 1 241 ? 16.50462  -5.10941  32.63024  1.000 241.60736 ? 241 LYS A CB  1 
ATOM   1308 C CG  . LYS A 1 241 ? 16.77212  -5.26122  34.12342  1.000 245.17519 ? 241 LYS A CG  1 
ATOM   1309 C CD  . LYS A 1 241 ? 18.08606  -5.98817  34.37998  1.000 249.32145 ? 241 LYS A CD  1 
ATOM   1310 C CE  . LYS A 1 241 ? 18.28141  -6.29403  35.85883  1.000 252.20354 ? 241 LYS A CE  1 
ATOM   1311 N NZ  . LYS A 1 241 ? 18.35893  -5.06284  36.69302  1.000 252.12340 ? 241 LYS A NZ  1 
ATOM   1312 N N   . ALA A 1 242 ? 17.66016  -3.29492  29.68196  1.000 226.61997 ? 242 ALA A N   1 
ATOM   1313 C CA  . ALA A 1 242 ? 17.49937  -3.18162  28.23296  1.000 211.49124 ? 242 ALA A CA  1 
ATOM   1314 C C   . ALA A 1 242 ? 18.74289  -2.47132  27.70817  1.000 208.98852 ? 242 ALA A C   1 
ATOM   1315 O O   . ALA A 1 242 ? 18.85662  -1.24570  27.80995  1.000 207.92134 ? 242 ALA A O   1 
ATOM   1316 C CB  . ALA A 1 242 ? 16.22680  -2.42807  27.87052  1.000 204.63162 ? 242 ALA A CB  1 
ATOM   1317 N N   . LEU A 1 243 ? 19.66861  -3.24404  27.14926  1.000 213.13723 ? 243 LEU A N   1 
ATOM   1318 C CA  . LEU A 1 243 ? 20.97334  -2.71952  26.77421  1.000 212.71317 ? 243 LEU A CA  1 
ATOM   1319 C C   . LEU A 1 243 ? 20.90235  -1.98209  25.44276  1.000 204.29879 ? 243 LEU A C   1 
ATOM   1320 O O   . LEU A 1 243 ? 20.43676  -2.53023  24.43843  1.000 198.91021 ? 243 LEU A O   1 
ATOM   1321 C CB  . LEU A 1 243 ? 21.99867  -3.85136  26.70034  1.000 215.99474 ? 243 LEU A CB  1 
ATOM   1322 C CG  . LEU A 1 243 ? 22.77378  -4.17657  27.98269  1.000 221.74274 ? 243 LEU A CG  1 
ATOM   1323 C CD1 . LEU A 1 243 ? 21.84496  -4.55701  29.13224  1.000 226.67553 ? 243 LEU A CD1 1 
ATOM   1324 C CD2 . LEU A 1 243 ? 23.78712  -5.28183  27.72626  1.000 223.40437 ? 243 LEU A CD2 1 
ATOM   1325 N N   . TYR A 1 244 ? 21.36682  -0.73497  25.44381  1.000 207.02591 ? 244 TYR A N   1 
ATOM   1326 C CA  . TYR A 1 244 ? 21.48342  0.04404   24.21821  1.000 200.42310 ? 244 TYR A CA  1 
ATOM   1327 C C   . TYR A 1 244 ? 22.67331  -0.46621  23.41424  1.000 198.78382 ? 244 TYR A C   1 
ATOM   1328 O O   . TYR A 1 244 ? 23.82097  -0.36563  23.86026  1.000 202.38141 ? 244 TYR A O   1 
ATOM   1329 C CB  . TYR A 1 244 ? 21.65113  1.52287   24.56098  1.000 201.73253 ? 244 TYR A CB  1 
ATOM   1330 C CG  . TYR A 1 244 ? 21.42304  2.49723   23.42472  1.000 196.16480 ? 244 TYR A CG  1 
ATOM   1331 C CD1 . TYR A 1 244 ? 21.07178  2.06042   22.15331  1.000 190.28241 ? 244 TYR A CD1 1 
ATOM   1332 C CD2 . TYR A 1 244 ? 21.56506  3.86303   23.63096  1.000 197.56704 ? 244 TYR A CD2 1 
ATOM   1333 C CE1 . TYR A 1 244 ? 20.86721  2.95909   21.12158  1.000 186.41776 ? 244 TYR A CE1 1 
ATOM   1334 C CE2 . TYR A 1 244 ? 21.36353  4.76660   22.60858  1.000 193.70942 ? 244 TYR A CE2 1 
ATOM   1335 C CZ  . TYR A 1 244 ? 21.01498  4.31050   21.35593  1.000 188.33684 ? 244 TYR A CZ  1 
ATOM   1336 O OH  . TYR A 1 244 ? 20.81342  5.20988   20.33469  1.000 185.66468 ? 244 TYR A OH  1 
ATOM   1337 N N   . LYS A 1 245 ? 22.40390  -1.01989  22.23679  1.000 196.93879 ? 245 LYS A N   1 
ATOM   1338 C CA  . LYS A 1 245 ? 23.43212  -1.61496  21.39780  1.000 195.24912 ? 245 LYS A CA  1 
ATOM   1339 C C   . LYS A 1 245 ? 23.63064  -0.78543  20.13534  1.000 190.52793 ? 245 LYS A C   1 
ATOM   1340 O O   . LYS A 1 245 ? 22.70230  -0.13652  19.64547  1.000 187.08741 ? 245 LYS A O   1 
ATOM   1341 C CB  . LYS A 1 245 ? 23.06831  -3.05925  21.04281  1.000 193.51173 ? 245 LYS A CB  1 
ATOM   1342 C CG  . LYS A 1 245 ? 23.12623  -3.99916  22.23990  1.000 199.80670 ? 245 LYS A CG  1 
ATOM   1343 C CD  . LYS A 1 245 ? 22.03701  -5.05773  22.18865  1.000 198.50122 ? 245 LYS A CD  1 
ATOM   1344 C CE  . LYS A 1 245 ? 22.60634  -6.43291  21.87912  1.000 202.35516 ? 245 LYS A CE  1 
ATOM   1345 N NZ  . LYS A 1 245 ? 23.12242  -6.52307  20.48497  1.000 198.37822 ? 245 LYS A NZ  1 
ATOM   1346 N N   . SER A 1 246 ? 24.85405  -0.81474  19.61108  1.000 189.75577 ? 246 SER A N   1 
ATOM   1347 C CA  . SER A 1 246 ? 25.26152  0.06111   18.52481  1.000 187.10693 ? 246 SER A CA  1 
ATOM   1348 C C   . SER A 1 246 ? 25.78462  -0.74618  17.34488  1.000 184.56533 ? 246 SER A C   1 
ATOM   1349 O O   . SER A 1 246 ? 26.09463  -1.93628  17.45978  1.000 186.25526 ? 246 SER A O   1 
ATOM   1350 C CB  . SER A 1 246 ? 26.34643  1.04238   18.98171  1.000 192.27013 ? 246 SER A CB  1 
ATOM   1351 O OG  . SER A 1 246 ? 27.63712  0.49004   18.80232  1.000 195.33864 ? 246 SER A OG  1 
ATOM   1352 N N   . ASN A 1 247 ? 25.88457  -0.06625  16.19748  1.000 191.10483 ? 247 ASN A N   1 
ATOM   1353 C CA  . ASN A 1 247 ? 26.48637  -0.67952  15.01750  1.000 190.82012 ? 247 ASN A CA  1 
ATOM   1354 C C   . ASN A 1 247 ? 27.98584  -0.86227  15.18445  1.000 195.47241 ? 247 ASN A C   1 
ATOM   1355 O O   . ASN A 1 247 ? 28.55941  -1.81043  14.63425  1.000 196.30579 ? 247 ASN A O   1 
ATOM   1356 C CB  . ASN A 1 247 ? 26.20383  0.16586   13.77975  1.000 188.51750 ? 247 ASN A CB  1 
ATOM   1357 C CG  . ASN A 1 247 ? 24.72910  0.29611   13.49318  1.000 186.53863 ? 247 ASN A CG  1 
ATOM   1358 O OD1 . ASN A 1 247 ? 23.97656  -0.67032  13.62117  1.000 185.77616 ? 247 ASN A OD1 1 
ATOM   1359 N ND2 . ASN A 1 247 ? 24.30127  1.49136   13.10934  1.000 186.62086 ? 247 ASN A ND2 1 
ATOM   1360 N N   . LYS A 1 248 ? 28.63201  0.03057   15.93443  1.000 188.99762 ? 248 LYS A N   1 
ATOM   1361 C CA  . LYS A 1 248 ? 30.07724  -0.01872  16.13634  1.000 195.42015 ? 248 LYS A CA  1 
ATOM   1362 C C   . LYS A 1 248 ? 30.51516  0.83522   17.32547  1.000 201.91224 ? 248 LYS A C   1 
ATOM   1363 O O   . LYS A 1 248 ? 30.29162  2.05024   17.34126  1.000 203.24304 ? 248 LYS A O   1 
ATOM   1364 C CB  . LYS A 1 248 ? 30.80097  0.44178   14.86868  1.000 184.36996 ? 248 LYS A CB  1 
ATOM   1365 C CG  . LYS A 1 248 ? 32.30985  0.30221   14.91464  1.000 199.88885 ? 248 LYS A CG  1 
ATOM   1366 C CD  . LYS A 1 248 ? 32.92542  0.69572   13.58020  1.000 201.73331 ? 248 LYS A CD  1 
ATOM   1367 C CE  . LYS A 1 248 ? 34.43565  0.53346   13.58479  1.000 207.67105 ? 248 LYS A CE  1 
ATOM   1368 N NZ  . LYS A 1 248 ? 35.05437  0.89390   12.27785  1.000 210.76132 ? 248 LYS A NZ  1 
ATOM   1369 N N   . ILE A 1 249 ? 31.13691  0.21367   18.32279  1.000 200.83544 ? 249 ILE A N   1 
ATOM   1370 C CA  . ILE A 1 249 ? 31.74678  0.92228   19.44312  1.000 205.61643 ? 249 ILE A CA  1 
ATOM   1371 C C   . ILE A 1 249 ? 33.25146  0.89510   19.19679  1.000 208.74413 ? 249 ILE A C   1 
ATOM   1372 O O   . ILE A 1 249 ? 33.92722  -0.09771  19.48654  1.000 210.90166 ? 249 ILE A O   1 
ATOM   1373 C CB  . ILE A 1 249 ? 31.37390  0.29416   20.78886  1.000 209.14993 ? 249 ILE A CB  1 
ATOM   1374 C CG1 . ILE A 1 249 ? 29.90505  -0.12763  20.78617  1.000 206.03513 ? 249 ILE A CG1 1 
ATOM   1375 C CG2 . ILE A 1 249 ? 31.60898  1.28640   21.91961  1.000 214.56448 ? 249 ILE A CG2 1 
ATOM   1376 C CD1 . ILE A 1 249 ? 29.49400  -0.94530  21.98754  1.000 209.06668 ? 249 ILE A CD1 1 
ATOM   1377 N N   . ILE A 1 250 ? 33.77568  1.98155   18.64256  1.000 204.78159 ? 250 ILE A N   1 
ATOM   1378 C CA  . ILE A 1 250 ? 35.15305  2.04410   18.17119  1.000 207.53874 ? 250 ILE A CA  1 
ATOM   1379 C C   . ILE A 1 250 ? 36.00120  2.75894   19.21441  1.000 213.32510 ? 250 ILE A C   1 
ATOM   1380 O O   . ILE A 1 250 ? 35.64456  3.84979   19.67797  1.000 213.75736 ? 250 ILE A O   1 
ATOM   1381 C CB  . ILE A 1 250 ? 35.23497  2.74088   16.80063  1.000 204.77602 ? 250 ILE A CB  1 
ATOM   1382 C CG1 . ILE A 1 250 ? 36.66377  3.19992   16.50326  1.000 208.45544 ? 250 ILE A CG1 1 
ATOM   1383 C CG2 . ILE A 1 250 ? 34.24773  3.89563   16.71898  1.000 202.32915 ? 250 ILE A CG2 1 
ATOM   1384 C CD1 . ILE A 1 250 ? 37.60541  2.07389   16.14437  1.000 209.92126 ? 250 ILE A CD1 1 
ATOM   1385 N N   . TYR A 1 251 ? 37.12036  2.13965   19.58996  1.000 219.07736 ? 251 TYR A N   1 
ATOM   1386 C CA  . TYR A 1 251 ? 38.01152  2.63428   20.64091  1.000 222.45224 ? 251 TYR A CA  1 
ATOM   1387 C C   . TYR A 1 251 ? 39.40825  2.83483   20.05994  1.000 222.50939 ? 251 TYR A C   1 
ATOM   1388 O O   . TYR A 1 251 ? 40.26718  1.95826   20.17413  1.000 223.40254 ? 251 TYR A O   1 
ATOM   1389 C CB  . TYR A 1 251 ? 38.05817  1.65810   21.83238  1.000 225.07507 ? 251 TYR A CB  1 
ATOM   1390 C CG  . TYR A 1 251 ? 36.81238  1.60204   22.68330  1.000 226.26126 ? 251 TYR A CG  1 
ATOM   1391 C CD1 . TYR A 1 251 ? 36.61696  2.50458   23.71999  1.000 229.62147 ? 251 TYR A CD1 1 
ATOM   1392 C CD2 . TYR A 1 251 ? 35.84565  0.62849   22.47019  1.000 224.45193 ? 251 TYR A CD2 1 
ATOM   1393 C CE1 . TYR A 1 251 ? 35.48749  2.44930   24.51043  1.000 231.15690 ? 251 TYR A CE1 1 
ATOM   1394 C CE2 . TYR A 1 251 ? 34.71267  0.56539   23.25627  1.000 225.65509 ? 251 TYR A CE2 1 
ATOM   1395 C CZ  . TYR A 1 251 ? 34.53805  1.47888   24.27422  1.000 229.02623 ? 251 TYR A CZ  1 
ATOM   1396 O OH  . TYR A 1 251 ? 33.41019  1.42112   25.05943  1.000 230.00917 ? 251 TYR A OH  1 
ATOM   1397 N N   . HIS A 1 252 ? 39.64498  3.99449   19.45528  1.000 225.78409 ? 252 HIS A N   1 
ATOM   1398 C CA  . HIS A 1 252 ? 40.98617  4.37329   19.03756  1.000 226.34115 ? 252 HIS A CA  1 
ATOM   1399 C C   . HIS A 1 252 ? 41.43850  5.60784   19.80538  1.000 229.10833 ? 252 HIS A C   1 
ATOM   1400 O O   . HIS A 1 252 ? 40.61819  6.41678   20.25016  1.000 229.93729 ? 252 HIS A O   1 
ATOM   1401 C CB  . HIS A 1 252 ? 41.06312  4.64489   17.53176  1.000 223.66418 ? 252 HIS A CB  1 
ATOM   1402 C CG  . HIS A 1 252 ? 42.46521  4.74890   17.01426  1.000 224.16127 ? 252 HIS A CG  1 
ATOM   1403 N ND1 . HIS A 1 252 ? 43.33803  3.68206   17.01616  1.000 224.66981 ? 252 HIS A ND1 1 
ATOM   1404 C CD2 . HIS A 1 252 ? 43.15124  5.79437   16.49418  1.000 224.38492 ? 252 HIS A CD2 1 
ATOM   1405 C CE1 . HIS A 1 252 ? 44.49817  4.06315   16.51219  1.000 225.11461 ? 252 HIS A CE1 1 
ATOM   1406 N NE2 . HIS A 1 252 ? 44.41144  5.34049   16.18742  1.000 224.93829 ? 252 HIS A NE2 1 
ATOM   1407 N N   . LYS A 1 253 ? 42.75529  5.73559   19.95998  1.000 223.69446 ? 253 LYS A N   1 
ATOM   1408 C CA  . LYS A 1 253 ? 43.38391  6.86755   20.65398  1.000 226.77642 ? 253 LYS A CA  1 
ATOM   1409 C C   . LYS A 1 253 ? 42.86057  6.85443   22.08882  1.000 230.31055 ? 253 LYS A C   1 
ATOM   1410 O O   . LYS A 1 253 ? 42.85850  5.78923   22.72671  1.000 231.29464 ? 253 LYS A O   1 
ATOM   1411 C CB  . LYS A 1 253 ? 43.12441  8.14880   19.86441  1.000 225.50419 ? 253 LYS A CB  1 
ATOM   1412 C CG  . LYS A 1 253 ? 44.00043  9.33243   20.24871  1.000 228.33436 ? 253 LYS A CG  1 
ATOM   1413 C CD  . LYS A 1 253 ? 43.31285  10.64753  19.91623  1.000 227.95605 ? 253 LYS A CD  1 
ATOM   1414 C CE  . LYS A 1 253 ? 42.81238  10.66605  18.48116  1.000 223.96620 ? 253 LYS A CE  1 
ATOM   1415 N NZ  . LYS A 1 253 ? 42.03811  11.90160  18.17876  1.000 223.65326 ? 253 LYS A NZ  1 
ATOM   1416 N N   . ASN A 1 254 ? 42.40890  7.97941   22.63026  1.000 215.43860 ? 254 ASN A N   1 
ATOM   1417 C CA  . ASN A 1 254 ? 41.78128  8.03213   23.94134  1.000 219.33782 ? 254 ASN A CA  1 
ATOM   1418 C C   . ASN A 1 254 ? 40.33426  8.49065   23.81333  1.000 217.76452 ? 254 ASN A C   1 
ATOM   1419 O O   . ASN A 1 254 ? 39.80364  9.17441   24.69246  1.000 220.68020 ? 254 ASN A O   1 
ATOM   1420 C CB  . ASN A 1 254 ? 42.57455  8.94940   24.87144  1.000 224.43702 ? 254 ASN A CB  1 
ATOM   1421 C CG  . ASN A 1 254 ? 42.27518  8.70044   26.32970  1.000 229.68535 ? 254 ASN A CG  1 
ATOM   1422 O OD1 . ASN A 1 254 ? 42.05568  9.63604   27.10045  1.000 230.79871 ? 254 ASN A OD1 1 
ATOM   1423 N ND2 . ASN A 1 254 ? 42.26358  7.43267   26.71955  1.000 232.07194 ? 254 ASN A ND2 1 
ATOM   1424 N N   . LEU A 1 255 ? 39.68994  8.11332   22.70995  1.000 213.00275 ? 255 LEU A N   1 
ATOM   1425 C CA  . LEU A 1 255 ? 38.37419  8.61962   22.33503  1.000 210.66410 ? 255 LEU A CA  1 
ATOM   1426 C C   . LEU A 1 255 ? 37.38891  7.46352   22.22286  1.000 208.41436 ? 255 LEU A C   1 
ATOM   1427 O O   . LEU A 1 255 ? 37.54529  6.58993   21.36247  1.000 205.47682 ? 255 LEU A O   1 
ATOM   1428 C CB  . LEU A 1 255 ? 38.44529  9.39303   21.01505  1.000 207.53465 ? 255 LEU A CB  1 
ATOM   1429 C CG  . LEU A 1 255 ? 38.75443  10.89227  21.07141  1.000 209.14681 ? 255 LEU A CG  1 
ATOM   1430 C CD1 . LEU A 1 255 ? 40.12699  11.16510  21.66716  1.000 212.64329 ? 255 LEU A CD1 1 
ATOM   1431 C CD2 . LEU A 1 255 ? 38.64184  11.50237  19.68300  1.000 206.03140 ? 255 LEU A CD2 1 
ATOM   1432 N N   . THR A 1 256 ? 36.37552  7.46710   23.08407  1.000 206.28219 ? 256 THR A N   1 
ATOM   1433 C CA  . THR A 1 256 ? 35.29164  6.49684   23.02102  1.000 203.32211 ? 256 THR A CA  1 
ATOM   1434 C C   . THR A 1 256 ? 34.18369  7.03637   22.12356  1.000 197.44143 ? 256 THR A C   1 
ATOM   1435 O O   . THR A 1 256 ? 33.74713  8.18040   22.28696  1.000 196.92237 ? 256 THR A O   1 
ATOM   1436 C CB  . THR A 1 256 ? 34.74882  6.20279   24.42051  1.000 206.68476 ? 256 THR A CB  1 
ATOM   1437 O OG1 . THR A 1 256 ? 35.76234  5.56048   25.20513  1.000 211.71095 ? 256 THR A OG1 1 
ATOM   1438 C CG2 . THR A 1 256 ? 33.52798  5.30977   24.34453  1.000 203.24296 ? 256 THR A CG2 1 
ATOM   1439 N N   . ILE A 1 257 ? 33.73315  6.21352   21.17755  1.000 198.22607 ? 257 ILE A N   1 
ATOM   1440 C CA  . ILE A 1 257 ? 32.78629  6.63385   20.15230  1.000 192.87327 ? 257 ILE A CA  1 
ATOM   1441 C C   . ILE A 1 257 ? 31.63608  5.63587   20.08869  1.000 189.23915 ? 257 ILE A C   1 
ATOM   1442 O O   . ILE A 1 257 ? 31.83634  4.42822   20.26097  1.000 189.82665 ? 257 ILE A O   1 
ATOM   1443 C CB  . ILE A 1 257 ? 33.47949  6.77261   18.77733  1.000 191.16841 ? 257 ILE A CB  1 
ATOM   1444 C CG1 . ILE A 1 257 ? 34.58593  7.82902   18.84106  1.000 195.54787 ? 257 ILE A CG1 1 
ATOM   1445 C CG2 . ILE A 1 257 ? 32.48138  7.12652   17.68953  1.000 186.95850 ? 257 ILE A CG2 1 
ATOM   1446 C CD1 . ILE A 1 257 ? 35.30475  8.04468   17.53155  1.000 194.64134 ? 257 ILE A CD1 1 
ATOM   1447 N N   . PHE A 1 258 ? 30.42906  6.14738   19.84246  1.000 193.62189 ? 258 PHE A N   1 
ATOM   1448 C CA  . PHE A 1 258 ? 29.21449  5.34379   19.75261  1.000 189.81465 ? 258 PHE A CA  1 
ATOM   1449 C C   . PHE A 1 258 ? 28.53177  5.65241   18.42772  1.000 184.81401 ? 258 PHE A C   1 
ATOM   1450 O O   . PHE A 1 258 ? 28.23816  6.81702   18.13825  1.000 184.23601 ? 258 PHE A O   1 
ATOM   1451 C CB  . PHE A 1 258 ? 28.27973  5.64734   20.93110  1.000 190.87762 ? 258 PHE A CB  1 
ATOM   1452 C CG  . PHE A 1 258 ? 27.05571  4.76668   20.99885  1.000 187.68176 ? 258 PHE A CG  1 
ATOM   1453 C CD1 . PHE A 1 258 ? 25.94279  5.03120   20.21387  1.000 183.02937 ? 258 PHE A CD1 1 
ATOM   1454 C CD2 . PHE A 1 258 ? 27.00615  3.69645   21.87782  1.000 190.15537 ? 258 PHE A CD2 1 
ATOM   1455 C CE1 . PHE A 1 258 ? 24.81797  4.23008   20.28460  1.000 180.37064 ? 258 PHE A CE1 1 
ATOM   1456 C CE2 . PHE A 1 258 ? 25.88253  2.89429   21.95598  1.000 188.49669 ? 258 PHE A CE2 1 
ATOM   1457 C CZ  . PHE A 1 258 ? 24.78642  3.16291   21.15950  1.000 182.55796 ? 258 PHE A CZ  1 
ATOM   1458 N N   . LYS A 1 259 ? 28.27635  4.61703   17.62811  1.000 200.13687 ? 259 LYS A N   1 
ATOM   1459 C CA  . LYS A 1 259 ? 27.56436  4.75927   16.36149  1.000 196.77429 ? 259 LYS A CA  1 
ATOM   1460 C C   . LYS A 1 259 ? 26.11093  4.35312   16.58097  1.000 192.48370 ? 259 LYS A C   1 
ATOM   1461 O O   . LYS A 1 259 ? 25.81736  3.17685   16.81460  1.000 190.48280 ? 259 LYS A O   1 
ATOM   1462 C CB  . LYS A 1 259 ? 28.21371  3.91882   15.26233  1.000 169.37327 ? 259 LYS A CB  1 
ATOM   1463 C CG  . LYS A 1 259 ? 27.55210  4.08080   13.89751  1.000 169.38562 ? 259 LYS A CG  1 
ATOM   1464 C CD  . LYS A 1 259 ? 28.55477  3.92169   12.76214  1.000 169.50082 ? 259 LYS A CD  1 
ATOM   1465 C CE  . LYS A 1 259 ? 28.58045  2.50348   12.21374  1.000 171.20999 ? 259 LYS A CE  1 
ATOM   1466 N NZ  . LYS A 1 259 ? 27.39933  2.21166   11.35313  1.000 186.34720 ? 259 LYS A NZ  1 
ATOM   1467 N N   . ALA A 1 260 ? 25.20784  5.32285   16.49761  1.000 183.79702 ? 260 ALA A N   1 
ATOM   1468 C CA  . ALA A 1 260 ? 23.80875  5.07502   16.83005  1.000 183.00797 ? 260 ALA A CA  1 
ATOM   1469 C C   . ALA A 1 260 ? 23.18229  4.10284   15.83581  1.000 181.92671 ? 260 ALA A C   1 
ATOM   1470 O O   . ALA A 1 260 ? 23.36525  4.25930   14.62252  1.000 181.87137 ? 260 ALA A O   1 
ATOM   1471 C CB  . ALA A 1 260 ? 23.02517  6.38530   16.84683  1.000 183.56465 ? 260 ALA A CB  1 
ATOM   1472 N N   . PRO A 1 261 ? 22.44503  3.09515   16.30152  1.000 189.76022 ? 261 PRO A N   1 
ATOM   1473 C CA  . PRO A 1 261 ? 21.73584  2.21317   15.36866  1.000 185.95769 ? 261 PRO A CA  1 
ATOM   1474 C C   . PRO A 1 261 ? 20.59069  2.95452   14.69970  1.000 183.16008 ? 261 PRO A C   1 
ATOM   1475 O O   . PRO A 1 261 ? 19.83009  3.67096   15.35362  1.000 183.05636 ? 261 PRO A O   1 
ATOM   1476 C CB  . PRO A 1 261 ? 21.22415  1.08451   16.26926  1.000 185.82580 ? 261 PRO A CB  1 
ATOM   1477 C CG  . PRO A 1 261 ? 21.06790  1.73161   17.60718  1.000 188.51271 ? 261 PRO A CG  1 
ATOM   1478 C CD  . PRO A 1 261 ? 22.18525  2.73952   17.70756  1.000 191.70382 ? 261 PRO A CD  1 
ATOM   1479 N N   . PHE A 1 262 ? 20.46885  2.76826   13.38143  1.000 200.23423 ? 262 PHE A N   1 
ATOM   1480 C CA  . PHE A 1 262 ? 19.50192  3.54551   12.61125  1.000 198.39126 ? 262 PHE A CA  1 
ATOM   1481 C C   . PHE A 1 262 ? 18.07598  3.32761   13.10325  1.000 195.74090 ? 262 PHE A C   1 
ATOM   1482 O O   . PHE A 1 262 ? 17.24378  4.23547   13.00520  1.000 195.45017 ? 262 PHE A O   1 
ATOM   1483 C CB  . PHE A 1 262 ? 19.61494  3.20803   11.12589  1.000 197.81631 ? 262 PHE A CB  1 
ATOM   1484 C CG  . PHE A 1 262 ? 18.96031  4.21574   10.22764  1.000 198.11937 ? 262 PHE A CG  1 
ATOM   1485 C CD1 . PHE A 1 262 ? 19.35393  5.54308   10.25651  1.000 200.99222 ? 262 PHE A CD1 1 
ATOM   1486 C CD2 . PHE A 1 262 ? 17.95917  3.83727   9.34964   1.000 196.13750 ? 262 PHE A CD2 1 
ATOM   1487 C CE1 . PHE A 1 262 ? 18.75712  6.47761   9.43050   1.000 202.12745 ? 262 PHE A CE1 1 
ATOM   1488 C CE2 . PHE A 1 262 ? 17.35918  4.76666   8.51879   1.000 197.12651 ? 262 PHE A CE2 1 
ATOM   1489 C CZ  . PHE A 1 262 ? 17.75884  6.08852   8.55962   1.000 200.32637 ? 262 PHE A CZ  1 
ATOM   1490 N N   . TYR A 1 263 ? 17.77701  2.14781   13.64090  1.000 199.03494 ? 263 TYR A N   1 
ATOM   1491 C CA  . TYR A 1 263 ? 16.47981  1.90641   14.26266  1.000 197.20313 ? 263 TYR A CA  1 
ATOM   1492 C C   . TYR A 1 263 ? 16.66203  0.88014   15.37023  1.000 198.65033 ? 263 TYR A C   1 
ATOM   1493 O O   . TYR A 1 263 ? 17.00649  -0.27292  15.09872  1.000 198.86165 ? 263 TYR A O   1 
ATOM   1494 C CB  . TYR A 1 263 ? 15.44688  1.43000   13.24278  1.000 194.30271 ? 263 TYR A CB  1 
ATOM   1495 C CG  . TYR A 1 263 ? 14.04401  1.35643   13.80634  1.000 192.82181 ? 263 TYR A CG  1 
ATOM   1496 C CD1 . TYR A 1 263 ? 13.24925  2.49291   13.88962  1.000 192.33935 ? 263 TYR A CD1 1 
ATOM   1497 C CD2 . TYR A 1 263 ? 13.51581  0.15359   14.25854  1.000 192.68493 ? 263 TYR A CD2 1 
ATOM   1498 C CE1 . TYR A 1 263 ? 11.96937  2.43294   14.40430  1.000 191.36731 ? 263 TYR A CE1 1 
ATOM   1499 C CE2 . TYR A 1 263 ? 12.23679  0.08551   14.77642  1.000 192.09402 ? 263 TYR A CE2 1 
ATOM   1500 C CZ  . TYR A 1 263 ? 11.46834  1.22875   14.84677  1.000 191.22107 ? 263 TYR A CZ  1 
ATOM   1501 O OH  . TYR A 1 263 ? 10.19317  1.17026   15.36077  1.000 190.82410 ? 263 TYR A OH  1 
ATOM   1502 N N   . VAL A 1 264 ? 16.43217  1.30132   16.61248  1.000 193.54570 ? 264 VAL A N   1 
ATOM   1503 C CA  . VAL A 1 264 ? 16.39050  0.40194   17.75960  1.000 196.35005 ? 264 VAL A CA  1 
ATOM   1504 C C   . VAL A 1 264 ? 14.92950  0.17676   18.12341  1.000 195.30262 ? 264 VAL A C   1 
ATOM   1505 O O   . VAL A 1 264 ? 14.10915  1.10187   18.05878  1.000 193.74424 ? 264 VAL A O   1 
ATOM   1506 C CB  . VAL A 1 264 ? 17.20074  0.96308   18.94676  1.000 200.80205 ? 264 VAL A CB  1 
ATOM   1507 C CG1 . VAL A 1 264 ? 16.63617  2.29758   19.41875  1.000 201.15070 ? 264 VAL A CG1 1 
ATOM   1508 C CG2 . VAL A 1 264 ? 17.25851  -0.04689  20.08719  1.000 204.96154 ? 264 VAL A CG2 1 
ATOM   1509 N N   . THR A 1 265 ? 14.59448  -1.06231  18.48592  1.000 197.86212 ? 265 THR A N   1 
ATOM   1510 C CA  . THR A 1 265 ? 13.19206  -1.44950  18.60793  1.000 197.20029 ? 265 THR A CA  1 
ATOM   1511 C C   . THR A 1 265 ? 12.58834  -1.01989  19.94125  1.000 200.20403 ? 265 THR A C   1 
ATOM   1512 O O   . THR A 1 265 ? 11.50608  -0.42413  19.97338  1.000 198.13640 ? 265 THR A O   1 
ATOM   1513 C CB  . THR A 1 265 ? 13.05123  -2.96159  18.42589  1.000 198.51387 ? 265 THR A CB  1 
ATOM   1514 O OG1 . THR A 1 265 ? 13.94776  -3.63707  19.31709  1.000 203.50034 ? 265 THR A OG1 1 
ATOM   1515 C CG2 . THR A 1 265 ? 13.37282  -3.35740  16.99322  1.000 195.29390 ? 265 THR A CG2 1 
ATOM   1516 N N   . SER A 1 266 ? 13.27069  -1.31425  21.04643  1.000 202.61808 ? 266 SER A N   1 
ATOM   1517 C CA  . SER A 1 266 ? 12.68285  -1.15680  22.37010  1.000 205.44313 ? 266 SER A CA  1 
ATOM   1518 C C   . SER A 1 266 ? 12.33108  0.30135   22.65803  1.000 203.96421 ? 266 SER A C   1 
ATOM   1519 O O   . SER A 1 266 ? 12.86653  1.23521   22.05460  1.000 202.24783 ? 266 SER A O   1 
ATOM   1520 C CB  . SER A 1 266 ? 13.63733  -1.68097  23.44225  1.000 211.35693 ? 266 SER A CB  1 
ATOM   1521 O OG  . SER A 1 266 ? 13.13770  -1.41669  24.74154  1.000 214.61785 ? 266 SER A OG  1 
ATOM   1522 N N   . LYS A 1 267 ? 11.40506  0.48395   23.60288  1.000 204.39218 ? 267 LYS A N   1 
ATOM   1523 C CA  . LYS A 1 267 ? 10.99396  1.82390   24.00637  1.000 205.12052 ? 267 LYS A CA  1 
ATOM   1524 C C   . LYS A 1 267 ? 12.04938  2.49559   24.87533  1.000 208.63668 ? 267 LYS A C   1 
ATOM   1525 O O   . LYS A 1 267 ? 12.35055  3.67922   24.68621  1.000 207.59085 ? 267 LYS A O   1 
ATOM   1526 C CB  . LYS A 1 267 ? 9.65983   1.76470   24.75286  1.000 208.13917 ? 267 LYS A CB  1 
ATOM   1527 C CG  . LYS A 1 267 ? 8.49262   1.24220   23.93025  1.000 205.71476 ? 267 LYS A CG  1 
ATOM   1528 C CD  . LYS A 1 267 ? 7.22324   1.17460   24.76904  1.000 206.37719 ? 267 LYS A CD  1 
ATOM   1529 C CE  . LYS A 1 267 ? 6.05976   0.59171   23.98197  1.000 204.71200 ? 267 LYS A CE  1 
ATOM   1530 N NZ  . LYS A 1 267 ? 4.84504   0.42459   24.82870  1.000 220.61119 ? 267 LYS A NZ  1 
ATOM   1531 N N   . ASP A 1 268 ? 12.61535  1.76226   25.83166  1.000 194.59666 ? 268 ASP A N   1 
ATOM   1532 C CA  . ASP A 1 268 ? 13.60373  2.29511   26.76167  1.000 198.89209 ? 268 ASP A CA  1 
ATOM   1533 C C   . ASP A 1 268 ? 14.88646  1.48597   26.64215  1.000 200.13749 ? 268 ASP A C   1 
ATOM   1534 O O   . ASP A 1 268 ? 14.88998  0.28067   26.91503  1.000 201.78661 ? 268 ASP A O   1 
ATOM   1535 C CB  . ASP A 1 268 ? 13.08476  2.25453   28.20126  1.000 208.17338 ? 268 ASP A CB  1 
ATOM   1536 C CG  . ASP A 1 268 ? 11.72907  2.91149   28.35536  1.000 221.44061 ? 268 ASP A CG  1 
ATOM   1537 O OD1 . ASP A 1 268 ? 11.40912  3.82218   27.56395  1.000 213.74431 ? 268 ASP A OD1 1 
ATOM   1538 O OD2 . ASP A 1 268 ? 10.98244  2.51348   29.27383  1.000 240.75305 ? 268 ASP A OD2 1 
ATOM   1539 N N   . VAL A 1 269 ? 15.96910  2.14856   26.23389  1.000 195.88562 ? 269 VAL A N   1 
ATOM   1540 C CA  . VAL A 1 269 ? 17.29843  1.54981   26.18130  1.000 197.78147 ? 269 VAL A CA  1 
ATOM   1541 C C   . VAL A 1 269 ? 18.30859  2.60739   26.60016  1.000 200.91704 ? 269 VAL A C   1 
ATOM   1542 O O   . VAL A 1 269 ? 18.13949  3.79628   26.31592  1.000 198.85621 ? 269 VAL A O   1 
ATOM   1543 C CB  . VAL A 1 269 ? 17.64451  0.99764   24.77957  1.000 191.92592 ? 269 VAL A CB  1 
ATOM   1544 C CG1 . VAL A 1 269 ? 16.89748  -0.29830  24.50912  1.000 188.61164 ? 269 VAL A CG1 1 
ATOM   1545 C CG2 . VAL A 1 269 ? 17.33310  2.03085   23.70704  1.000 190.63774 ? 269 VAL A CG2 1 
ATOM   1546 N N   . ASN A 1 270 ? 19.37061  2.16975   27.27445  1.000 193.76748 ? 270 ASN A N   1 
ATOM   1547 C CA  . ASN A 1 270 ? 20.34623  3.10493   27.81773  1.000 196.24806 ? 270 ASN A CA  1 
ATOM   1548 C C   . ASN A 1 270 ? 21.72051  2.45571   27.86426  1.000 200.44742 ? 270 ASN A C   1 
ATOM   1549 O O   . ASN A 1 270 ? 21.85878  1.23490   27.75788  1.000 202.00669 ? 270 ASN A O   1 
ATOM   1550 C CB  . ASN A 1 270 ? 19.94926  3.57665   29.22039  1.000 198.89567 ? 270 ASN A CB  1 
ATOM   1551 C CG  . ASN A 1 270 ? 20.18692  2.51759   30.27854  1.000 202.30222 ? 270 ASN A CG  1 
ATOM   1552 O OD1 . ASN A 1 270 ? 19.49932  1.49763   30.31880  1.000 203.34781 ? 270 ASN A OD1 1 
ATOM   1553 N ND2 . ASN A 1 270 ? 21.16561  2.75641   31.14442  1.000 204.12316 ? 270 ASN A ND2 1 
ATOM   1554 N N   . THR A 1 271 ? 22.74003  3.29553   28.03058  1.000 193.82971 ? 271 THR A N   1 
ATOM   1555 C CA  . THR A 1 271 ? 24.10556  2.82320   28.20036  1.000 198.45910 ? 271 THR A CA  1 
ATOM   1556 C C   . THR A 1 271 ? 24.86249  3.81151   29.07826  1.000 202.26511 ? 271 THR A C   1 
ATOM   1557 O O   . THR A 1 271 ? 24.70176  5.02734   28.94071  1.000 200.40740 ? 271 THR A O   1 
ATOM   1558 C CB  . THR A 1 271 ? 24.81058  2.63262   26.85023  1.000 195.92993 ? 271 THR A CB  1 
ATOM   1559 O OG1 . THR A 1 271 ? 26.13924  2.15128   27.07332  1.000 200.75980 ? 271 THR A OG1 1 
ATOM   1560 C CG2 . THR A 1 271 ? 24.86321  3.93543   26.05924  1.000 192.73714 ? 271 THR A CG2 1 
ATOM   1561 N N   . GLU A 1 272 ? 25.67136  3.28194   29.99071  1.000 200.05682 ? 272 GLU A N   1 
ATOM   1562 C CA  . GLU A 1 272 ? 26.40328  4.08674   30.95868  1.000 203.61000 ? 272 GLU A CA  1 
ATOM   1563 C C   . GLU A 1 272 ? 27.89806  3.99832   30.68388  1.000 207.13473 ? 272 GLU A C   1 
ATOM   1564 O O   . GLU A 1 272 ? 28.43975  2.90087   30.52896  1.000 209.63306 ? 272 GLU A O   1 
ATOM   1565 C CB  . GLU A 1 272 ? 26.11278  3.62264   32.38651  1.000 206.44344 ? 272 GLU A CB  1 
ATOM   1566 C CG  . GLU A 1 272 ? 24.65638  3.70477   32.79862  1.000 203.61290 ? 272 GLU A CG  1 
ATOM   1567 C CD  . GLU A 1 272 ? 24.45014  3.26842   34.23366  1.000 206.38137 ? 272 GLU A CD  1 
ATOM   1568 O OE1 . GLU A 1 272 ? 25.43912  2.84707   34.86981  1.000 210.27474 ? 272 GLU A OE1 1 
ATOM   1569 O OE2 . GLU A 1 272 ? 23.30626  3.34635   34.72733  1.000 204.51450 ? 272 GLU A OE2 1 
ATOM   1570 N N   . CYS A 1 273 ? 28.56353  5.14763   30.63745  1.000 210.31203 ? 273 CYS A N   1 
ATOM   1571 C CA  . CYS A 1 273 ? 30.01922  5.20980   30.53933  1.000 214.06334 ? 273 CYS A CA  1 
ATOM   1572 C C   . CYS A 1 273 ? 30.53052  5.96473   31.75948  1.000 217.65703 ? 273 CYS A C   1 
ATOM   1573 O O   . CYS A 1 273 ? 30.39664  7.18979   31.83681  1.000 217.07570 ? 273 CYS A O   1 
ATOM   1574 C CB  . CYS A 1 273 ? 30.45021  5.88597   29.24683  1.000 211.71943 ? 273 CYS A CB  1 
ATOM   1575 S SG  . CYS A 1 273 ? 32.18479  5.73583   28.82882  1.000 215.67760 ? 273 CYS A SG  1 
ATOM   1576 N N   . THR A 1 274 ? 31.10822  5.23843   32.71329  1.000 213.95228 ? 274 THR A N   1 
ATOM   1577 C CA  . THR A 1 274 ? 31.63297  5.85227   33.92995  1.000 217.20154 ? 274 THR A CA  1 
ATOM   1578 C C   . THR A 1 274 ? 33.10646  6.16595   33.68825  1.000 220.19788 ? 274 THR A C   1 
ATOM   1579 O O   . THR A 1 274 ? 33.97284  5.29317   33.78435  1.000 222.50457 ? 274 THR A O   1 
ATOM   1580 C CB  . THR A 1 274 ? 31.39757  4.95571   35.14805  1.000 218.85002 ? 274 THR A CB  1 
ATOM   1581 O OG1 . THR A 1 274 ? 32.05387  5.50496   36.30115  1.000 221.82508 ? 274 THR A OG1 1 
ATOM   1582 C CG2 . THR A 1 274 ? 31.85193  3.50376   34.91771  1.000 219.86645 ? 274 THR A CG2 1 
ATOM   1583 N N   . CYS A 1 275 ? 33.38725  7.41883   33.34493  1.000 226.53557 ? 275 CYS A N   1 
ATOM   1584 C CA  . CYS A 1 275 ? 34.73877  7.87153   33.06190  1.000 229.21281 ? 275 CYS A CA  1 
ATOM   1585 C C   . CYS A 1 275 ? 35.21996  8.77488   34.18648  1.000 231.73425 ? 275 CYS A C   1 
ATOM   1586 O O   . CYS A 1 275 ? 34.43441  9.50078   34.80229  1.000 230.77143 ? 275 CYS A O   1 
ATOM   1587 C CB  . CYS A 1 275 ? 34.81078  8.62767   31.73236  1.000 227.20287 ? 275 CYS A CB  1 
ATOM   1588 S SG  . CYS A 1 275 ? 36.43629  8.59712   30.93276  1.000 229.55866 ? 275 CYS A SG  1 
ATOM   1589 N N   . LYS A 1 276 ? 36.51979  8.72733   34.45018  1.000 224.96878 ? 276 LYS A N   1 
ATOM   1590 C CA  . LYS A 1 276 ? 37.12522  9.53682   35.49420  1.000 227.06097 ? 276 LYS A CA  1 
ATOM   1591 C C   . LYS A 1 276 ? 38.05322  10.57743  34.88156  1.000 228.47397 ? 276 LYS A C   1 
ATOM   1592 O O   . LYS A 1 276 ? 38.74843  10.30415  33.89785  1.000 227.98561 ? 276 LYS A O   1 
ATOM   1593 C CB  . LYS A 1 276 ? 37.89355  8.66395   36.48900  1.000 229.21999 ? 276 LYS A CB  1 
ATOM   1594 C CG  . LYS A 1 276 ? 38.27911  9.38923   37.76575  1.000 230.67498 ? 276 LYS A CG  1 
ATOM   1595 C CD  . LYS A 1 276 ? 38.80295  8.42604   38.81709  1.000 232.21584 ? 276 LYS A CD  1 
ATOM   1596 C CE  . LYS A 1 276 ? 39.13782  9.15235   40.11308  1.000 233.83046 ? 276 LYS A CE  1 
ATOM   1597 N NZ  . LYS A 1 276 ? 39.71507  8.23904   41.14023  1.000 235.21729 ? 276 LYS A NZ  1 
ATOM   1598 N N   . PHE A 1 277 ? 38.05074  11.77406  35.47263  1.000 233.94605 ? 277 PHE A N   1 
ATOM   1599 C CA  . PHE A 1 277 ? 38.92228  12.86962  35.06097  1.000 235.37952 ? 277 PHE A CA  1 
ATOM   1600 C C   . PHE A 1 277 ? 39.02905  13.91565  36.16916  1.000 236.12135 ? 277 PHE A C   1 
ATOM   1601 O O   . PHE A 1 277 ? 38.00904  14.32902  36.73052  1.000 234.13792 ? 277 PHE A O   1 
ATOM   1602 C CB  . PHE A 1 277 ? 38.40016  13.50019  33.77018  1.000 233.17981 ? 277 PHE A CB  1 
ATOM   1603 C CG  . PHE A 1 277 ? 39.16491  14.71246  33.32803  1.000 234.12938 ? 277 PHE A CG  1 
ATOM   1604 C CD1 . PHE A 1 277 ? 40.47101  14.60194  32.88017  1.000 235.56843 ? 277 PHE A CD1 1 
ATOM   1605 C CD2 . PHE A 1 277 ? 38.56685  15.95925  33.33683  1.000 232.21521 ? 277 PHE A CD2 1 
ATOM   1606 C CE1 . PHE A 1 277 ? 41.16615  15.71502  32.46413  1.000 236.11042 ? 277 PHE A CE1 1 
ATOM   1607 C CE2 . PHE A 1 277 ? 39.25498  17.07340  32.92268  1.000 233.24348 ? 277 PHE A CE2 1 
ATOM   1608 C CZ  . PHE A 1 277 ? 40.55729  16.95314  32.48511  1.000 235.26488 ? 277 PHE A CZ  1 
ATOM   1609 N N   . LYS A 1 278 ? 40.25174  14.34182  36.49947  1.000 238.76298 ? 278 LYS A N   1 
ATOM   1610 C CA  . LYS A 1 278 ? 40.47869  15.35105  37.54000  1.000 240.14491 ? 278 LYS A CA  1 
ATOM   1611 C C   . LYS A 1 278 ? 39.92409  14.88302  38.88625  1.000 239.87837 ? 278 LYS A C   1 
ATOM   1612 O O   . LYS A 1 278 ? 39.33759  15.65933  39.64322  1.000 239.07842 ? 278 LYS A O   1 
ATOM   1613 C CB  . LYS A 1 278 ? 39.87728  16.69980  37.13136  1.000 238.74556 ? 278 LYS A CB  1 
ATOM   1614 C CG  . LYS A 1 278 ? 40.47396  17.91473  37.81342  1.000 240.55741 ? 278 LYS A CG  1 
ATOM   1615 C CD  . LYS A 1 278 ? 39.75751  19.17586  37.36851  1.000 238.59178 ? 278 LYS A CD  1 
ATOM   1616 C CE  . LYS A 1 278 ? 40.21830  20.37374  38.16962  1.000 240.28131 ? 278 LYS A CE  1 
ATOM   1617 N NZ  . LYS A 1 278 ? 39.44413  21.59159  37.81747  1.000 238.41470 ? 278 LYS A NZ  1 
ATOM   1618 N N   . ASN A 1 279 ? 40.09395  13.59111  39.17188  1.000 241.76451 ? 279 ASN A N   1 
ATOM   1619 C CA  . ASN A 1 279 ? 39.62896  12.93092  40.38976  1.000 241.50517 ? 279 ASN A CA  1 
ATOM   1620 C C   . ASN A 1 279 ? 38.11409  12.98247  40.56308  1.000 238.54211 ? 279 ASN A C   1 
ATOM   1621 O O   . ASN A 1 279 ? 37.61289  12.69439  41.65834  1.000 238.30147 ? 279 ASN A O   1 
ATOM   1622 C CB  . ASN A 1 279 ? 40.31285  13.50267  41.63854  1.000 243.54208 ? 279 ASN A CB  1 
ATOM   1623 C CG  . ASN A 1 279 ? 41.67459  12.88678  41.88752  1.000 245.75844 ? 279 ASN A CG  1 
ATOM   1624 O OD1 . ASN A 1 279 ? 41.94625  11.76372  41.46290  1.000 245.36631 ? 279 ASN A OD1 1 
ATOM   1625 N ND2 . ASN A 1 279 ? 42.53612  13.61598  42.58604  1.000 247.49849 ? 279 ASN A ND2 1 
ATOM   1626 N N   . ASN A 1 280 ? 37.36984  13.33947  39.51930  1.000 238.51507 ? 280 ASN A N   1 
ATOM   1627 C CA  . ASN A 1 280 ? 35.91649  13.30036  39.53410  1.000 235.44559 ? 280 ASN A CA  1 
ATOM   1628 C C   . ASN A 1 280 ? 35.42638  12.13648  38.68338  1.000 233.99456 ? 280 ASN A C   1 
ATOM   1629 O O   . ASN A 1 280 ? 36.10230  11.70525  37.74750  1.000 234.87654 ? 280 ASN A O   1 
ATOM   1630 C CB  . ASN A 1 280 ? 35.31448  14.60715  39.00986  1.000 233.52435 ? 280 ASN A CB  1 
ATOM   1631 C CG  . ASN A 1 280 ? 35.69802  15.80616  39.85192  1.000 235.40380 ? 280 ASN A CG  1 
ATOM   1632 O OD1 . ASN A 1 280 ? 35.93289  15.68599  41.05360  1.000 236.49847 ? 280 ASN A OD1 1 
ATOM   1633 N ND2 . ASN A 1 280 ? 35.75870  16.97447  39.22378  1.000 235.83052 ? 280 ASN A ND2 1 
ATOM   1634 N N   . ASN A 1 281 ? 34.24149  11.62998  39.01181  1.000 232.01404 ? 281 ASN A N   1 
ATOM   1635 C CA  . ASN A 1 281 ? 33.63225  10.52688  38.28083  1.000 230.49443 ? 281 ASN A CA  1 
ATOM   1636 C C   . ASN A 1 281 ? 32.46225  11.06439  37.46899  1.000 226.99859 ? 281 ASN A C   1 
ATOM   1637 O O   . ASN A 1 281 ? 31.55095  11.68751  38.02362  1.000 225.12326 ? 281 ASN A O   1 
ATOM   1638 C CB  . ASN A 1 281 ? 33.17187  9.42093   39.23211  1.000 230.61460 ? 281 ASN A CB  1 
ATOM   1639 C CG  . ASN A 1 281 ? 32.67567  8.18818   38.49616  1.000 229.42009 ? 281 ASN A CG  1 
ATOM   1640 O OD1 . ASN A 1 281 ? 32.99848  7.97376   37.32568  1.000 228.15971 ? 281 ASN A OD1 1 
ATOM   1641 N ND2 . ASN A 1 281 ? 31.89122  7.36735   39.18343  1.000 229.89780 ? 281 ASN A ND2 1 
ATOM   1642 N N   . TYR A 1 282 ? 32.48776  10.81900  36.16228  1.000 222.56207 ? 282 TYR A N   1 
ATOM   1643 C CA  . TYR A 1 282 ? 31.46716  11.30745  35.24574  1.000 218.80356 ? 282 TYR A CA  1 
ATOM   1644 C C   . TYR A 1 282 ? 30.75718  10.12359  34.60625  1.000 216.76962 ? 282 TYR A C   1 
ATOM   1645 O O   . TYR A 1 282 ? 31.40970  9.21303   34.08532  1.000 218.07269 ? 282 TYR A O   1 
ATOM   1646 C CB  . TYR A 1 282 ? 32.08261  12.19988  34.16433  1.000 218.52239 ? 282 TYR A CB  1 
ATOM   1647 C CG  . TYR A 1 282 ? 32.99649  13.28128  34.69473  1.000 221.14831 ? 282 TYR A CG  1 
ATOM   1648 C CD1 . TYR A 1 282 ? 32.49620  14.52307  35.06366  1.000 219.90245 ? 282 TYR A CD1 1 
ATOM   1649 C CD2 . TYR A 1 282 ? 34.36185  13.06220  34.81856  1.000 224.89387 ? 282 TYR A CD2 1 
ATOM   1650 C CE1 . TYR A 1 282 ? 33.32982  15.51432  35.54591  1.000 222.34088 ? 282 TYR A CE1 1 
ATOM   1651 C CE2 . TYR A 1 282 ? 35.20210  14.04617  35.29952  1.000 227.14094 ? 282 TYR A CE2 1 
ATOM   1652 C CZ  . TYR A 1 282 ? 34.68164  15.27026  35.66132  1.000 225.87412 ? 282 TYR A CZ  1 
ATOM   1653 O OH  . TYR A 1 282 ? 35.51677  16.25308  36.14101  1.000 228.24685 ? 282 TYR A OH  1 
ATOM   1654 N N   . LYS A 1 283 ? 29.42705  10.13837  34.64277  1.000 206.84281 ? 283 LYS A N   1 
ATOM   1655 C CA  . LYS A 1 283 ? 28.60907  9.10209   34.02303  1.000 204.20162 ? 283 LYS A CA  1 
ATOM   1656 C C   . LYS A 1 283 ? 27.85809  9.70058   32.84146  1.000 199.59426 ? 283 LYS A C   1 
ATOM   1657 O O   . LYS A 1 283 ? 27.06348  10.63113  33.01389  1.000 197.43227 ? 283 LYS A O   1 
ATOM   1658 C CB  . LYS A 1 283 ? 27.62925  8.49029   35.02535  1.000 203.75085 ? 283 LYS A CB  1 
ATOM   1659 C CG  . LYS A 1 283 ? 26.64682  7.51509   34.38810  1.000 200.39177 ? 283 LYS A CG  1 
ATOM   1660 C CD  . LYS A 1 283 ? 26.23037  6.41108   35.34853  1.000 202.10856 ? 283 LYS A CD  1 
ATOM   1661 C CE  . LYS A 1 283 ? 24.84130  6.64706   35.91680  1.000 199.46247 ? 283 LYS A CE  1 
ATOM   1662 N NZ  . LYS A 1 283 ? 24.39243  5.49426   36.74785  1.000 200.80200 ? 283 LYS A NZ  1 
ATOM   1663 N N   . ILE A 1 284 ? 28.10453  9.16319   31.65117  1.000 193.30378 ? 284 ILE A N   1 
ATOM   1664 C CA  . ILE A 1 284 ? 27.46095  9.62246   30.42597  1.000 191.43252 ? 284 ILE A CA  1 
ATOM   1665 C C   . ILE A 1 284 ? 26.40242  8.59455   30.04590  1.000 189.48483 ? 284 ILE A C   1 
ATOM   1666 O O   . ILE A 1 284 ? 26.72786  7.46672   29.65795  1.000 188.21796 ? 284 ILE A O   1 
ATOM   1667 C CB  . ILE A 1 284 ? 28.47745  9.82357   29.29427  1.000 190.42406 ? 284 ILE A CB  1 
ATOM   1668 C CG1 . ILE A 1 284 ? 29.74175  10.50211  29.82385  1.000 192.44458 ? 284 ILE A CG1 1 
ATOM   1669 C CG2 . ILE A 1 284 ? 27.87438  10.66412  28.18486  1.000 189.39463 ? 284 ILE A CG2 1 
ATOM   1670 C CD1 . ILE A 1 284 ? 30.80090  10.73140  28.76310  1.000 191.68839 ? 284 ILE A CD1 1 
ATOM   1671 N N   . VAL A 1 285 ? 25.13339  8.97967   30.15748  1.000 193.55010 ? 285 VAL A N   1 
ATOM   1672 C CA  . VAL A 1 285 ? 24.00892  8.10855   29.83195  1.000 190.07148 ? 285 VAL A CA  1 
ATOM   1673 C C   . VAL A 1 285 ? 23.45318  8.52032   28.47695  1.000 185.03525 ? 285 VAL A C   1 
ATOM   1674 O O   . VAL A 1 285 ? 23.11875  9.69305   28.26395  1.000 183.55889 ? 285 VAL A O   1 
ATOM   1675 C CB  . VAL A 1 285 ? 22.92189  8.16961   30.92004  1.000 190.00828 ? 285 VAL A CB  1 
ATOM   1676 C CG1 . VAL A 1 285 ? 21.65642  7.47095   30.44931  1.000 185.75554 ? 285 VAL A CG1 1 
ATOM   1677 C CG2 . VAL A 1 285 ? 23.42987  7.53838   32.20764  1.000 194.70674 ? 285 VAL A CG2 1 
ATOM   1678 N N   . LEU A 1 286 ? 23.35724  7.56037   27.56116  1.000 193.20980 ? 286 LEU A N   1 
ATOM   1679 C CA  . LEU A 1 286 ? 22.88359  7.80214   26.20536  1.000 188.28785 ? 286 LEU A CA  1 
ATOM   1680 C C   . LEU A 1 286 ? 21.57104  7.06494   25.97189  1.000 184.42725 ? 286 LEU A C   1 
ATOM   1681 O O   . LEU A 1 286 ? 21.39469  5.93090   26.42606  1.000 185.30361 ? 286 LEU A O   1 
ATOM   1682 C CB  . LEU A 1 286 ? 23.91602  7.35728   25.16372  1.000 187.89217 ? 286 LEU A CB  1 
ATOM   1683 C CG  . LEU A 1 286 ? 25.03881  8.32679   24.78314  1.000 189.82852 ? 286 LEU A CG  1 
ATOM   1684 C CD1 . LEU A 1 286 ? 25.89808  8.66693   25.98267  1.000 195.49312 ? 286 LEU A CD1 1 
ATOM   1685 C CD2 . LEU A 1 286 ? 25.88861  7.73764   23.66831  1.000 188.53047 ? 286 LEU A CD2 1 
ATOM   1686 N N   . LYS A 1 287 ? 20.65410  7.71810   25.26115  1.000 189.41099 ? 287 LYS A N   1 
ATOM   1687 C CA  . LYS A 1 287 ? 19.35427  7.15170   24.93332  1.000 185.47171 ? 287 LYS A CA  1 
ATOM   1688 C C   . LYS A 1 287 ? 18.90843  7.70244   23.58985  1.000 181.94538 ? 287 LYS A C   1 
ATOM   1689 O O   . LYS A 1 287 ? 19.30244  8.81562   23.21810  1.000 181.64890 ? 287 LYS A O   1 
ATOM   1690 C CB  . LYS A 1 287 ? 18.30509  7.47139   26.01345  1.000 185.53813 ? 287 LYS A CB  1 
ATOM   1691 C CG  . LYS A 1 287 ? 18.49904  6.70639   27.31714  1.000 188.33414 ? 287 LYS A CG  1 
ATOM   1692 C CD  . LYS A 1 287 ? 17.46232  7.07731   28.36504  1.000 187.33378 ? 287 LYS A CD  1 
ATOM   1693 C CE  . LYS A 1 287 ? 16.05607  6.72313   27.92537  1.000 188.07252 ? 287 LYS A CE  1 
ATOM   1694 N NZ  . LYS A 1 287 ? 15.07499  7.07084   28.98383  1.000 191.94781 ? 287 LYS A NZ  1 
ATOM   1695 N N   . PRO A 1 288 ? 18.10677  6.95587   22.83629  1.000 194.01404 ? 288 PRO A N   1 
ATOM   1696 C CA  . PRO A 1 288 ? 17.65071  7.45470   21.53585  1.000 188.87545 ? 288 PRO A CA  1 
ATOM   1697 C C   . PRO A 1 288 ? 16.49197  8.43403   21.65956  1.000 188.03384 ? 288 PRO A C   1 
ATOM   1698 O O   . PRO A 1 288 ? 15.71859  8.40968   22.62049  1.000 189.07061 ? 288 PRO A O   1 
ATOM   1699 C CB  . PRO A 1 288 ? 17.21032  6.17711   20.81110  1.000 184.43720 ? 288 PRO A CB  1 
ATOM   1700 C CG  . PRO A 1 288 ? 16.76179  5.27933   21.90258  1.000 186.44209 ? 288 PRO A CG  1 
ATOM   1701 C CD  . PRO A 1 288 ? 17.67310  5.56944   23.07695  1.000 192.67065 ? 288 PRO A CD  1 
ATOM   1702 N N   . LYS A 1 289 ? 16.38361  9.29779   20.65547  1.000 199.20773 ? 289 LYS A N   1 
ATOM   1703 C CA  . LYS A 1 289 ? 15.25976  10.21189  20.53593  1.000 198.41768 ? 289 LYS A CA  1 
ATOM   1704 C C   . LYS A 1 289 ? 13.99366  9.42890   20.19444  1.000 193.39484 ? 289 LYS A C   1 
ATOM   1705 O O   . LYS A 1 289 ? 14.04381  8.24331   19.85640  1.000 190.70188 ? 289 LYS A O   1 
ATOM   1706 C CB  . LYS A 1 289 ? 15.54332  11.25714  19.45691  1.000 199.38622 ? 289 LYS A CB  1 
ATOM   1707 C CG  . LYS A 1 289 ? 14.69568  12.51992  19.51098  1.000 198.32377 ? 289 LYS A CG  1 
ATOM   1708 C CD  . LYS A 1 289 ? 15.08497  13.46930  18.38580  1.000 196.15416 ? 289 LYS A CD  1 
ATOM   1709 C CE  . LYS A 1 289 ? 14.32868  14.78463  18.45408  1.000 198.40684 ? 289 LYS A CE  1 
ATOM   1710 N NZ  . LYS A 1 289 ? 12.86748  14.59142  18.30284  1.000 201.45272 ? 289 LYS A NZ  1 
ATOM   1711 N N   . TYR A 1 290 ? 12.84290  10.09778  20.28841  1.000 245.98774 ? 290 TYR A N   1 
ATOM   1712 C CA  . TYR A 1 290 ? 11.63219  9.52005   19.72152  1.000 242.30416 ? 290 TYR A CA  1 
ATOM   1713 C C   . TYR A 1 290 ? 11.89386  9.23727   18.25532  1.000 239.31208 ? 290 TYR A C   1 
ATOM   1714 O O   . TYR A 1 290 ? 11.90965  10.16253  17.43635  1.000 239.74172 ? 290 TYR A O   1 
ATOM   1715 C CB  . TYR A 1 290 ? 10.42561  10.44372  19.86510  1.000 201.55102 ? 290 TYR A CB  1 
ATOM   1716 C CG  . TYR A 1 290 ? 9.31934   10.13274  18.87399  1.000 200.77453 ? 290 TYR A CG  1 
ATOM   1717 C CD1 . TYR A 1 290 ? 8.59002   8.95164   18.95729  1.000 199.20051 ? 290 TYR A CD1 1 
ATOM   1718 C CD2 . TYR A 1 290 ? 9.01136   11.02022  17.84984  1.000 201.82543 ? 290 TYR A CD2 1 
ATOM   1719 C CE1 . TYR A 1 290 ? 7.57862   8.66915   18.04674  1.000 198.60693 ? 290 TYR A CE1 1 
ATOM   1720 C CE2 . TYR A 1 290 ? 8.00683   10.74596  16.93765  1.000 201.33353 ? 290 TYR A CE2 1 
ATOM   1721 C CZ  . TYR A 1 290 ? 7.29329   9.57165   17.04031  1.000 199.67787 ? 290 TYR A CZ  1 
ATOM   1722 O OH  . TYR A 1 290 ? 6.29312   9.30323   16.13357  1.000 199.30298 ? 290 TYR A OH  1 
ATOM   1723 N N   . GLU A 1 291 ? 12.15146  7.98320   17.92430  1.000 227.20465 ? 291 GLU A N   1 
ATOM   1724 C CA  . GLU A 1 291 ? 12.50159  7.66272   16.55273  1.000 226.25141 ? 291 GLU A CA  1 
ATOM   1725 C C   . GLU A 1 291 ? 11.30401  7.92663   15.65251  1.000 227.79408 ? 291 GLU A C   1 
ATOM   1726 O O   . GLU A 1 291 ? 10.19656  7.45548   15.92176  1.000 233.65453 ? 291 GLU A O   1 
ATOM   1727 C CB  . GLU A 1 291 ? 12.97164  6.20571   16.44662  1.000 218.81948 ? 291 GLU A CB  1 
ATOM   1728 C CG  . GLU A 1 291 ? 11.91438  5.10217   16.56805  1.000 214.29463 ? 291 GLU A CG  1 
ATOM   1729 C CD  . GLU A 1 291 ? 11.34916  4.94301   17.96567  1.000 216.39942 ? 291 GLU A CD  1 
ATOM   1730 O OE1 . GLU A 1 291 ? 11.80539  5.64882   18.88595  1.000 216.18905 ? 291 GLU A OE1 1 
ATOM   1731 O OE2 . GLU A 1 291 ? 10.43658  4.11148   18.14556  1.000 226.28764 ? 291 GLU A OE2 1 
ATOM   1732 N N   . LYS A 1 292 ? 11.50149  8.74876   14.62918  1.000 228.35452 ? 292 LYS A N   1 
ATOM   1733 C CA  . LYS A 1 292 ? 10.50490  8.83660   13.58226  1.000 227.65387 ? 292 LYS A CA  1 
ATOM   1734 C C   . LYS A 1 292 ? 10.31392  7.45005   12.97816  1.000 224.08471 ? 292 LYS A C   1 
ATOM   1735 O O   . LYS A 1 292 ? 11.16390  6.97724   12.21572  1.000 223.81689 ? 292 LYS A O   1 
ATOM   1736 C CB  . LYS A 1 292 ? 10.91667  9.83574   12.50644  1.000 238.55841 ? 292 LYS A CB  1 
ATOM   1737 C CG  . LYS A 1 292 ? 10.96737  11.28103  12.98532  1.000 240.02039 ? 292 LYS A CG  1 
ATOM   1738 C CD  . LYS A 1 292 ? 11.23886  12.21787  11.81489  1.000 241.81442 ? 292 LYS A CD  1 
ATOM   1739 C CE  . LYS A 1 292 ? 11.34531  13.66466  12.26507  1.000 244.25153 ? 292 LYS A CE  1 
ATOM   1740 N NZ  . LYS A 1 292 ? 12.43331  13.90528  13.25393  1.000 243.56277 ? 292 LYS A NZ  1 
ATOM   1741 N N   . LYS A 1 293 ? 9.23101   6.77469   13.34679  1.000 228.81151 ? 293 LYS A N   1 
ATOM   1742 C CA  . LYS A 1 293 ? 8.90092   5.48361   12.77502  1.000 226.83793 ? 293 LYS A CA  1 
ATOM   1743 C C   . LYS A 1 293 ? 8.16065   5.72417   11.47148  1.000 225.76755 ? 293 LYS A C   1 
ATOM   1744 O O   . LYS A 1 293 ? 6.94084   5.55642   11.35082  1.000 224.45021 ? 293 LYS A O   1 
ATOM   1745 C CB  . LYS A 1 293 ? 8.09652   4.65628   13.75842  1.000 226.13360 ? 293 LYS A CB  1 
ATOM   1746 C CG  . LYS A 1 293 ? 8.81162   4.56106   15.09013  1.000 225.17179 ? 293 LYS A CG  1 
ATOM   1747 C CD  . LYS A 1 293 ? 7.95635   3.92589   16.15419  1.000 225.49984 ? 293 LYS A CD  1 
ATOM   1748 C CE  . LYS A 1 293 ? 6.61882   4.64654   16.25398  1.000 224.41240 ? 293 LYS A CE  1 
ATOM   1749 N NZ  . LYS A 1 293 ? 6.67050   5.71310   17.31570  1.000 223.62281 ? 293 LYS A NZ  1 
ATOM   1750 N N   . VAL A 1 294 ? 8.93818   6.12457   10.46972  1.000 214.75737 ? 294 VAL A N   1 
ATOM   1751 C CA  . VAL A 1 294 ? 8.42339   6.28369   9.11440   1.000 214.33907 ? 294 VAL A CA  1 
ATOM   1752 C C   . VAL A 1 294 ? 9.11169   5.25250   8.23555   1.000 212.28773 ? 294 VAL A C   1 
ATOM   1753 O O   . VAL A 1 294 ? 10.03818  5.57411   7.48619   1.000 214.52589 ? 294 VAL A O   1 
ATOM   1754 C CB  . VAL A 1 294 ? 8.63959   7.71434   8.60022   1.000 218.00405 ? 294 VAL A CB  1 
ATOM   1755 C CG1 . VAL A 1 294 ? 7.96937   7.89417   7.24328   1.000 219.80323 ? 294 VAL A CG1 1 
ATOM   1756 C CG2 . VAL A 1 294 ? 8.08214   8.70615   9.60468   1.000 217.20687 ? 294 VAL A CG2 1 
ATOM   1757 N N   . ILE A 1 295 ? 8.66514   4.00447   8.33323   1.000 202.14195 ? 295 ILE A N   1 
ATOM   1758 C CA  . ILE A 1 295 ? 9.26353   2.91655   7.56941   1.000 203.23261 ? 295 ILE A CA  1 
ATOM   1759 C C   . ILE A 1 295 ? 8.64655   2.92754   6.17566   1.000 203.68690 ? 295 ILE A C   1 
ATOM   1760 O O   . ILE A 1 295 ? 7.45988   2.63484   6.01180   1.000 201.99091 ? 295 ILE A O   1 
ATOM   1761 C CB  . ILE A 1 295 ? 9.05564   1.56051   8.25236   1.000 202.08597 ? 295 ILE A CB  1 
ATOM   1762 C CG1 . ILE A 1 295 ? 9.54478   1.60717   9.69854   1.000 201.14850 ? 295 ILE A CG1 1 
ATOM   1763 C CG2 . ILE A 1 295 ? 9.77578   0.46595   7.48349   1.000 197.13677 ? 295 ILE A CG2 1 
ATOM   1764 C CD1 . ILE A 1 295 ? 9.36626   0.30785   10.44507  1.000 189.17874 ? 295 ILE A CD1 1 
ATOM   1765 N N   . HIS A 1 296 ? 9.44750   3.27812   5.16907   1.000 190.28332 ? 296 HIS A N   1 
ATOM   1766 C CA  . HIS A 1 296 ? 9.00428   3.24717   3.77683   1.000 191.21427 ? 296 HIS A CA  1 
ATOM   1767 C C   . HIS A 1 296 ? 8.79729   1.78642   3.38679   1.000 190.82780 ? 296 HIS A C   1 
ATOM   1768 O O   . HIS A 1 296 ? 9.61283   1.16487   2.70145   1.000 192.60342 ? 296 HIS A O   1 
ATOM   1769 C CB  . HIS A 1 296 ? 10.01739  3.93532   2.86905   1.000 195.46724 ? 296 HIS A CB  1 
ATOM   1770 C CG  . HIS A 1 296 ? 10.54128  5.22715   3.41675   1.000 199.02757 ? 296 HIS A CG  1 
ATOM   1771 N ND1 . HIS A 1 296 ? 11.44235  5.28259   4.45844   1.000 198.65460 ? 296 HIS A ND1 1 
ATOM   1772 C CD2 . HIS A 1 296 ? 10.29287  6.51146   3.06659   1.000 202.49064 ? 296 HIS A CD2 1 
ATOM   1773 C CE1 . HIS A 1 296 ? 11.72417  6.54461   4.72831   1.000 201.56836 ? 296 HIS A CE1 1 
ATOM   1774 N NE2 . HIS A 1 296 ? 11.04071  7.31054   3.89727   1.000 204.47412 ? 296 HIS A NE2 1 
ATOM   1775 N N   . GLY A 1 297 ? 7.68542   1.23023   3.84495   1.000 177.94902 ? 297 GLY A N   1 
ATOM   1776 C CA  . GLY A 1 297 ? 7.40206   -0.16917  3.63676   1.000 177.22999 ? 297 GLY A CA  1 
ATOM   1777 C C   . GLY A 1 297 ? 5.92052   -0.46580  3.66651   1.000 177.03040 ? 297 GLY A C   1 
ATOM   1778 O O   . GLY A 1 297 ? 5.08468   0.43607   3.59326   1.000 177.72234 ? 297 GLY A O   1 
ATOM   1779 N N   . CYS A 1 298 ? 5.60381   -1.75437  3.78520   1.000 178.96977 ? 298 CYS A N   1 
ATOM   1780 C CA  . CYS A 1 298 ? 4.23503   -2.24692  3.70634   1.000 178.06960 ? 298 CYS A CA  1 
ATOM   1781 C C   . CYS A 1 298 ? 3.91281   -3.05905  4.95166   1.000 174.91554 ? 298 CYS A C   1 
ATOM   1782 O O   . CYS A 1 298 ? 4.69787   -3.92413  5.35150   1.000 174.22116 ? 298 CYS A O   1 
ATOM   1783 C CB  . CYS A 1 298 ? 4.04031   -3.10089  2.45020   1.000 179.22287 ? 298 CYS A CB  1 
ATOM   1784 S SG  . CYS A 1 298 ? 4.63210   -2.30933  0.93529   1.000 184.70452 ? 298 CYS A SG  1 
ATOM   1785 N N   . ASN A 1 299 ? 2.75713   -2.78641  5.55489   1.000 184.58708 ? 299 ASN A N   1 
ATOM   1786 C CA  . ASN A 1 299 ? 2.29675   -3.48108  6.75697   1.000 182.09995 ? 299 ASN A CA  1 
ATOM   1787 C C   . ASN A 1 299 ? 1.07241   -4.31346  6.39079   1.000 185.20422 ? 299 ASN A C   1 
ATOM   1788 O O   . ASN A 1 299 ? -0.04418  -3.79278  6.32266   1.000 185.77951 ? 299 ASN A O   1 
ATOM   1789 C CB  . ASN A 1 299 ? 1.97402   -2.49019  7.87329   1.000 184.35411 ? 299 ASN A CB  1 
ATOM   1790 C CG  . ASN A 1 299 ? 1.48228   -3.17379  9.14418   1.000 185.77793 ? 299 ASN A CG  1 
ATOM   1791 O OD1 . ASN A 1 299 ? 0.31920   -3.56937  9.24640   1.000 186.07051 ? 299 ASN A OD1 1 
ATOM   1792 N ND2 . ASN A 1 299 ? 2.36991   -3.30827  10.12130  1.000 188.07042 ? 299 ASN A ND2 1 
ATOM   1793 N N   . PHE A 1 300 ? 1.28476   -5.60643  6.15750   1.000 181.50561 ? 300 PHE A N   1 
ATOM   1794 C CA  . PHE A 1 300 ? 0.20075   -6.54245  5.89492   1.000 184.86953 ? 300 PHE A CA  1 
ATOM   1795 C C   . PHE A 1 300 ? -0.39202  -7.11498  7.17535   1.000 189.31364 ? 300 PHE A C   1 
ATOM   1796 O O   . PHE A 1 300 ? -1.14804  -8.08991  7.11405   1.000 191.33650 ? 300 PHE A O   1 
ATOM   1797 C CB  . PHE A 1 300 ? 0.68982   -7.68288  4.99798   1.000 187.45201 ? 300 PHE A CB  1 
ATOM   1798 C CG  . PHE A 1 300 ? 1.53257   -7.22788  3.84248   1.000 182.73985 ? 300 PHE A CG  1 
ATOM   1799 C CD1 . PHE A 1 300 ? 0.94777   -6.84951  2.64582   1.000 182.59123 ? 300 PHE A CD1 1 
ATOM   1800 C CD2 . PHE A 1 300 ? 2.91276   -7.18481  3.95174   1.000 178.57522 ? 300 PHE A CD2 1 
ATOM   1801 C CE1 . PHE A 1 300 ? 1.72407   -6.43417  1.57992   1.000 177.81332 ? 300 PHE A CE1 1 
ATOM   1802 C CE2 . PHE A 1 300 ? 3.69403   -6.77014  2.89138   1.000 176.62366 ? 300 PHE A CE2 1 
ATOM   1803 C CZ  . PHE A 1 300 ? 3.09917   -6.39593  1.70292   1.000 175.85454 ? 300 PHE A CZ  1 
ATOM   1804 N N   . SER A 1 301 ? -0.06924  -6.53061  8.32613   1.000 190.93079 ? 301 SER A N   1 
ATOM   1805 C CA  . SER A 1 301 ? -0.46958  -7.09399  9.60742   1.000 193.40672 ? 301 SER A CA  1 
ATOM   1806 C C   . SER A 1 301 ? -1.92929  -6.79548  9.91820   1.000 194.05756 ? 301 SER A C   1 
ATOM   1807 O O   . SER A 1 301 ? -2.44628  -5.72190  9.59587   1.000 191.69843 ? 301 SER A O   1 
ATOM   1808 C CB  . SER A 1 301 ? 0.41715   -6.55218  10.72583  1.000 193.14353 ? 301 SER A CB  1 
ATOM   1809 O OG  . SER A 1 301 ? 1.74564   -6.99734  10.55012  1.000 194.57260 ? 301 SER A OG  1 
ATOM   1810 N N   . SER A 1 302 ? -2.58757  -7.75767  10.56010  1.000 198.07583 ? 302 SER A N   1 
ATOM   1811 C CA  . SER A 1 302 ? -3.98172  -7.63538  10.98473  1.000 200.65929 ? 302 SER A CA  1 
ATOM   1812 C C   . SER A 1 302 ? -4.11175  -7.02217  12.37191  1.000 201.03475 ? 302 SER A C   1 
ATOM   1813 O O   . SER A 1 302 ? -4.95950  -7.43728  13.16791  1.000 201.70814 ? 302 SER A O   1 
ATOM   1814 C CB  . SER A 1 302 ? -4.64849  -9.00568  10.93189  1.000 203.35922 ? 302 SER A CB  1 
ATOM   1815 O OG  . SER A 1 302 ? -3.79729  -10.00058 11.47410  1.000 205.89506 ? 302 SER A OG  1 
ATOM   1816 N N   . ASN A 1 303 ? -3.28002  -6.03268  12.69027  1.000 211.61821 ? 303 ASN A N   1 
ATOM   1817 C CA  . ASN A 1 303 ? -3.28080  -5.40057  14.00058  1.000 211.79026 ? 303 ASN A CA  1 
ATOM   1818 C C   . ASN A 1 303 ? -3.13460  -3.89466  13.83732  1.000 206.66963 ? 303 ASN A C   1 
ATOM   1819 O O   . ASN A 1 303 ? -2.46223  -3.41663  12.92019  1.000 204.25168 ? 303 ASN A O   1 
ATOM   1820 C CB  . ASN A 1 303 ? -2.15524  -5.95633  14.88709  1.000 213.33687 ? 303 ASN A CB  1 
ATOM   1821 C CG  . ASN A 1 303 ? -1.76084  -5.00398  15.99778  1.000 210.99113 ? 303 ASN A CG  1 
ATOM   1822 O OD1 . ASN A 1 303 ? -0.74584  -4.31399  15.90545  1.000 213.11514 ? 303 ASN A OD1 1 
ATOM   1823 N ND2 . ASN A 1 303 ? -2.56845  -4.95317  17.05075  1.000 208.08086 ? 303 ASN A ND2 1 
ATOM   1824 N N   . VAL A 1 304 ? -3.77395  -3.15214  14.73602  1.000 214.47984 ? 304 VAL A N   1 
ATOM   1825 C CA  . VAL A 1 304 ? -3.73658  -1.69725  14.71246  1.000 211.42048 ? 304 VAL A CA  1 
ATOM   1826 C C   . VAL A 1 304 ? -2.68750  -1.14591  15.67095  1.000 211.04805 ? 304 VAL A C   1 
ATOM   1827 O O   . VAL A 1 304 ? -1.95936  -0.21414  15.32537  1.000 209.03546 ? 304 VAL A O   1 
ATOM   1828 C CB  . VAL A 1 304 ? -5.13989  -1.12433  15.01906  1.000 211.29545 ? 304 VAL A CB  1 
ATOM   1829 C CG1 . VAL A 1 304 ? -5.74860  -1.78951  16.25323  1.000 213.74632 ? 304 VAL A CG1 1 
ATOM   1830 C CG2 . VAL A 1 304 ? -5.08788  0.38941   15.18318  1.000 209.15196 ? 304 VAL A CG2 1 
ATOM   1831 N N   . SER A 1 305 ? -2.57754  -1.72825  16.86818  1.000 214.49807 ? 305 SER A N   1 
ATOM   1832 C CA  . SER A 1 305 ? -1.65900  -1.23254  17.89457  1.000 214.90419 ? 305 SER A CA  1 
ATOM   1833 C C   . SER A 1 305 ? -0.26711  -1.76701  17.58899  1.000 215.65207 ? 305 SER A C   1 
ATOM   1834 O O   . SER A 1 305 ? 0.18703   -2.78042  18.12464  1.000 218.33967 ? 305 SER A O   1 
ATOM   1835 C CB  . SER A 1 305 ? -2.11296  -1.63663  19.29022  1.000 217.31464 ? 305 SER A CB  1 
ATOM   1836 O OG  . SER A 1 305 ? -2.02543  -3.04055  19.47194  1.000 220.47266 ? 305 SER A OG  1 
ATOM   1837 N N   . SER A 1 306 ? 0.41977   -1.06109  16.70422  1.000 208.34916 ? 306 SER A N   1 
ATOM   1838 C CA  . SER A 1 306 ? 1.76812   -1.41943  16.30584  1.000 208.73185 ? 306 SER A CA  1 
ATOM   1839 C C   . SER A 1 306 ? 2.74605   -0.36853  16.80779  1.000 208.47159 ? 306 SER A C   1 
ATOM   1840 O O   . SER A 1 306 ? 2.47342   0.83165   16.73801  1.000 207.03707 ? 306 SER A O   1 
ATOM   1841 C CB  . SER A 1 306 ? 1.88339   -1.55389  14.78502  1.000 206.62169 ? 306 SER A CB  1 
ATOM   1842 O OG  . SER A 1 306 ? 3.24378   -1.68202  14.40574  1.000 206.06864 ? 306 SER A OG  1 
ATOM   1843 N N   . LYS A 1 307 ? 3.87988   -0.82250  17.32822  1.000 199.82299 ? 307 LYS A N   1 
ATOM   1844 C CA  . LYS A 1 307 ? 4.95921   0.08318   17.69317  1.000 200.19741 ? 307 LYS A CA  1 
ATOM   1845 C C   . LYS A 1 307 ? 5.72163   0.61055   16.48366  1.000 197.95846 ? 307 LYS A C   1 
ATOM   1846 O O   . LYS A 1 307 ? 6.73264   1.29674   16.66150  1.000 199.04646 ? 307 LYS A O   1 
ATOM   1847 C CB  . LYS A 1 307 ? 5.94358   -0.62506  18.62150  1.000 203.45478 ? 307 LYS A CB  1 
ATOM   1848 C CG  . LYS A 1 307 ? 5.35544   -1.16781  19.90354  1.000 205.98983 ? 307 LYS A CG  1 
ATOM   1849 C CD  . LYS A 1 307 ? 6.42393   -1.89440  20.69519  1.000 210.05924 ? 307 LYS A CD  1 
ATOM   1850 C CE  . LYS A 1 307 ? 5.81791   -2.62043  21.88488  1.000 213.41724 ? 307 LYS A CE  1 
ATOM   1851 N NZ  . LYS A 1 307 ? 6.84613   -3.38378  22.65203  1.000 218.23277 ? 307 LYS A NZ  1 
ATOM   1852 N N   . HIS A 1 308 ? 5.31030   0.26294   15.26658  1.000 199.28611 ? 308 HIS A N   1 
ATOM   1853 C CA  . HIS A 1 308 ? 6.02305   0.65596   14.05921  1.000 197.87003 ? 308 HIS A CA  1 
ATOM   1854 C C   . HIS A 1 308 ? 5.02093   1.15681   13.03122  1.000 193.78651 ? 308 HIS A C   1 
ATOM   1855 O O   . HIS A 1 308 ? 4.02555   0.48357   12.75251  1.000 193.19741 ? 308 HIS A O   1 
ATOM   1856 C CB  . HIS A 1 308 ? 6.83279   -0.51749  13.49380  1.000 198.33838 ? 308 HIS A CB  1 
ATOM   1857 C CG  . HIS A 1 308 ? 7.65347   -1.23475  14.52132  1.000 200.90929 ? 308 HIS A CG  1 
ATOM   1858 N ND1 . HIS A 1 308 ? 9.02599   -1.12863  14.58730  1.000 204.16022 ? 308 HIS A ND1 1 
ATOM   1859 C CD2 . HIS A 1 308 ? 7.29231   -2.06555  15.52772  1.000 201.29576 ? 308 HIS A CD2 1 
ATOM   1860 C CE1 . HIS A 1 308 ? 9.47458   -1.86477  15.58833  1.000 206.59590 ? 308 HIS A CE1 1 
ATOM   1861 N NE2 . HIS A 1 308 ? 8.44271   -2.44308  16.17541  1.000 204.91988 ? 308 HIS A NE2 1 
ATOM   1862 N N   . THR A 1 309 ? 5.28054   2.33188   12.46729  1.000 206.75226 ? 309 THR A N   1 
ATOM   1863 C CA  . THR A 1 309 ? 4.37306   2.95532   11.51083  1.000 206.17382 ? 309 THR A CA  1 
ATOM   1864 C C   . THR A 1 309 ? 4.96620   2.82452   10.11309  1.000 205.58851 ? 309 THR A C   1 
ATOM   1865 O O   . THR A 1 309 ? 5.99661   3.43544   9.80916   1.000 206.11265 ? 309 THR A O   1 
ATOM   1866 C CB  . THR A 1 309 ? 4.11961   4.42047   11.86454  1.000 207.57808 ? 309 THR A CB  1 
ATOM   1867 O OG1 . THR A 1 309 ? 3.39011   4.50207   13.09560  1.000 209.88923 ? 309 THR A OG1 1 
ATOM   1868 C CG2 . THR A 1 309 ? 3.32535   5.10798   10.76163  1.000 207.32091 ? 309 THR A CG2 1 
ATOM   1869 N N   . PHE A 1 310 ? 4.31934   2.02609   9.26906   1.000 198.84706 ? 310 PHE A N   1 
ATOM   1870 C CA  . PHE A 1 310 ? 4.73011   1.88338   7.88178   1.000 199.42003 ? 310 PHE A CA  1 
ATOM   1871 C C   . PHE A 1 310 ? 3.99116   2.89130   7.01261   1.000 200.16528 ? 310 PHE A C   1 
ATOM   1872 O O   . PHE A 1 310 ? 2.85594   3.27880   7.30171   1.000 200.37076 ? 310 PHE A O   1 
ATOM   1873 C CB  . PHE A 1 310 ? 4.46703   0.46464   7.37137   1.000 198.16317 ? 310 PHE A CB  1 
ATOM   1874 C CG  . PHE A 1 310 ? 5.28807   -0.58897  8.05723   1.000 200.53563 ? 310 PHE A CG  1 
ATOM   1875 C CD1 . PHE A 1 310 ? 6.50222   -0.99590  7.52894   1.000 199.88593 ? 310 PHE A CD1 1 
ATOM   1876 C CD2 . PHE A 1 310 ? 4.84755   -1.16926  9.23403   1.000 200.96262 ? 310 PHE A CD2 1 
ATOM   1877 C CE1 . PHE A 1 310 ? 7.25981   -1.96338  8.16318   1.000 190.39083 ? 310 PHE A CE1 1 
ATOM   1878 C CE2 . PHE A 1 310 ? 5.59903   -2.13586  9.87150   1.000 202.01824 ? 310 PHE A CE2 1 
ATOM   1879 C CZ  . PHE A 1 310 ? 6.80618   -2.53570  9.33458   1.000 196.75908 ? 310 PHE A CZ  1 
ATOM   1880 N N   . THR A 1 311 ? 4.65425   3.32161   5.93912   1.000 188.55690 ? 311 THR A N   1 
ATOM   1881 C CA  . THR A 1 311 ? 4.03762   4.26481   5.01668   1.000 189.85736 ? 311 THR A CA  1 
ATOM   1882 C C   . THR A 1 311 ? 2.91330   3.64086   4.20244   1.000 189.58803 ? 311 THR A C   1 
ATOM   1883 O O   . THR A 1 311 ? 2.19520   4.37362   3.51693   1.000 191.11334 ? 311 THR A O   1 
ATOM   1884 C CB  . THR A 1 311 ? 5.08809   4.84334   4.06845   1.000 192.82552 ? 311 THR A CB  1 
ATOM   1885 O OG1 . THR A 1 311 ? 5.69565   3.78291   3.31984   1.000 192.58830 ? 311 THR A OG1 1 
ATOM   1886 C CG2 . THR A 1 311 ? 6.15764   5.58393   4.85195   1.000 194.18858 ? 311 THR A CG2 1 
ATOM   1887 N N   . ASP A 1 312 ? 2.75774   2.31838   4.24240   1.000 180.23033 ? 312 ASP A N   1 
ATOM   1888 C CA  . ASP A 1 312 ? 1.71330   1.62990   3.49648   1.000 179.64900 ? 312 ASP A CA  1 
ATOM   1889 C C   . ASP A 1 312 ? 1.21403   0.46876   4.34176   1.000 178.15240 ? 312 ASP A C   1 
ATOM   1890 O O   . ASP A 1 312 ? 2.02388   -0.27476  4.90018   1.000 178.06500 ? 312 ASP A O   1 
ATOM   1891 C CB  . ASP A 1 312 ? 2.23904   1.11594   2.14939   1.000 180.47985 ? 312 ASP A CB  1 
ATOM   1892 C CG  . ASP A 1 312 ? 3.21571   2.08063   1.49359   1.000 183.19563 ? 312 ASP A CG  1 
ATOM   1893 O OD1 . ASP A 1 312 ? 2.85288   3.25650   1.28877   1.000 183.79731 ? 312 ASP A OD1 1 
ATOM   1894 O OD2 . ASP A 1 312 ? 4.35171   1.66348   1.18525   1.000 184.60441 ? 312 ASP A OD2 1 
ATOM   1895 N N   . SER A 1 313 ? -0.10479  0.30846   4.43533   1.000 178.72778 ? 313 SER A N   1 
ATOM   1896 C CA  . SER A 1 313 ? -0.69406  -0.74973  5.24299   1.000 178.53017 ? 313 SER A CA  1 
ATOM   1897 C C   . SER A 1 313 ? -1.76815  -1.47264  4.44182   1.000 180.08032 ? 313 SER A C   1 
ATOM   1898 O O   . SER A 1 313 ? -2.17920  -1.03105  3.36477   1.000 182.46289 ? 313 SER A O   1 
ATOM   1899 C CB  . SER A 1 313 ? -1.27432  -0.20015  6.55486   1.000 178.19111 ? 313 SER A CB  1 
ATOM   1900 O OG  . SER A 1 313 ? -0.26672  0.43227   7.32321   1.000 178.37704 ? 313 SER A OG  1 
ATOM   1901 N N   . LEU A 1 314 ? -2.22007  -2.59688  4.99600   1.000 176.97440 ? 314 LEU A N   1 
ATOM   1902 C CA  . LEU A 1 314 ? -3.20453  -3.48337  4.38679   1.000 178.24487 ? 314 LEU A CA  1 
ATOM   1903 C C   . LEU A 1 314 ? -3.37336  -4.68461  5.30793   1.000 179.33937 ? 314 LEU A C   1 
ATOM   1904 O O   . LEU A 1 314 ? -2.54465  -4.92492  6.18904   1.000 179.31061 ? 314 LEU A O   1 
ATOM   1905 C CB  . LEU A 1 314 ? -2.76920  -3.93012  2.98344   1.000 179.56157 ? 314 LEU A CB  1 
ATOM   1906 C CG  . LEU A 1 314 ? -3.48311  -5.06302  2.24196   1.000 180.68153 ? 314 LEU A CG  1 
ATOM   1907 C CD1 . LEU A 1 314 ? -4.94589  -4.71220  1.99715   1.000 182.70535 ? 314 LEU A CD1 1 
ATOM   1908 C CD2 . LEU A 1 314 ? -2.79347  -5.38745  0.93644   1.000 182.57240 ? 314 LEU A CD2 1 
ATOM   1909 N N   . ASP A 1 315 ? -4.45918  -5.42835  5.10402   1.000 185.60991 ? 315 ASP A N   1 
ATOM   1910 C CA  . ASP A 1 315 ? -4.65411  -6.73659  5.71376   1.000 190.65049 ? 315 ASP A CA  1 
ATOM   1911 C C   . ASP A 1 315 ? -4.57413  -7.81247  4.63888   1.000 192.30224 ? 315 ASP A C   1 
ATOM   1912 O O   . ASP A 1 315 ? -5.10927  -7.64286  3.53842   1.000 192.71096 ? 315 ASP A O   1 
ATOM   1913 C CB  . ASP A 1 315 ? -6.00204  -6.83022  6.43540   1.000 193.15415 ? 315 ASP A CB  1 
ATOM   1914 C CG  . ASP A 1 315 ? -6.25848  -8.20963  7.01013   1.000 198.72995 ? 315 ASP A CG  1 
ATOM   1915 O OD1 . ASP A 1 315 ? -5.47205  -8.64654  7.87438   1.000 200.90004 ? 315 ASP A OD1 1 
ATOM   1916 O OD2 . ASP A 1 315 ? -7.24386  -8.85642  6.59929   1.000 202.23994 ? 315 ASP A OD2 1 
ATOM   1917 N N   . ILE A 1 316 ? -3.89753  -8.91787  4.96395   1.000 194.07697 ? 316 ILE A N   1 
ATOM   1918 C CA  . ILE A 1 316 ? -3.72684  -10.04053 4.04692   1.000 194.97425 ? 316 ILE A CA  1 
ATOM   1919 C C   . ILE A 1 316 ? -4.67673  -11.19352 4.35902   1.000 199.80818 ? 316 ILE A C   1 
ATOM   1920 O O   . ILE A 1 316 ? -4.72116  -12.17725 3.60708   1.000 201.82185 ? 316 ILE A O   1 
ATOM   1921 C CB  . ILE A 1 316 ? -2.25570  -10.51423 4.06460   1.000 194.41157 ? 316 ILE A CB  1 
ATOM   1922 C CG1 . ILE A 1 316 ? -1.94276  -11.45040 2.89096   1.000 192.57746 ? 316 ILE A CG1 1 
ATOM   1923 C CG2 . ILE A 1 316 ? -1.91589  -11.16127 5.39884   1.000 196.94146 ? 316 ILE A CG2 1 
ATOM   1924 C CD1 . ILE A 1 316 ? -0.56227  -12.07578 2.96622   1.000 195.50787 ? 316 ILE A CD1 1 
ATOM   1925 N N   . SER A 1 317 ? -5.45492  -11.09174 5.43530   1.000 202.79074 ? 317 SER A N   1 
ATOM   1926 C CA  . SER A 1 317 ? -6.34422  -12.16342 5.86778   1.000 206.62332 ? 317 SER A CA  1 
ATOM   1927 C C   . SER A 1 317 ? -7.61434  -12.27697 5.02767   1.000 207.97026 ? 317 SER A C   1 
ATOM   1928 O O   . SER A 1 317 ? -8.43968  -13.15206 5.30448   1.000 210.81158 ? 317 SER A O   1 
ATOM   1929 C CB  . SER A 1 317 ? -6.72977  -11.95339 7.33567   1.000 207.32377 ? 317 SER A CB  1 
ATOM   1930 O OG  . SER A 1 317 ? -5.64932  -11.40798 8.07439   1.000 205.78196 ? 317 SER A OG  1 
ATOM   1931 N N   . LEU A 1 318 ? -7.78974  -11.43223 4.01022   1.000 210.96464 ? 318 LEU A N   1 
ATOM   1932 C CA  . LEU A 1 318 ? -9.06373  -11.30681 3.31387   1.000 212.20074 ? 318 LEU A CA  1 
ATOM   1933 C C   . LEU A 1 318 ? -9.02539  -11.67018 1.83375   1.000 210.02701 ? 318 LEU A C   1 
ATOM   1934 O O   . LEU A 1 318 ? -10.08181 -11.96907 1.26604   1.000 210.66104 ? 318 LEU A O   1 
ATOM   1935 C CB  . LEU A 1 318 ? -9.58702  -9.86729  3.45181   1.000 210.93845 ? 318 LEU A CB  1 
ATOM   1936 C CG  . LEU A 1 318 ? -8.52165  -8.77328  3.28713   1.000 207.51075 ? 318 LEU A CG  1 
ATOM   1937 C CD1 . LEU A 1 318 ? -8.32595  -8.38925  1.82594   1.000 203.87083 ? 318 LEU A CD1 1 
ATOM   1938 C CD2 . LEU A 1 318 ? -8.85607  -7.55043  4.12425   1.000 206.91284 ? 318 LEU A CD2 1 
ATOM   1939 N N   . VAL A 1 319 ? -7.85361  -11.65484 1.19807   1.000 209.23556 ? 319 VAL A N   1 
ATOM   1940 C CA  . VAL A 1 319 ? -7.72896  -11.74511 -0.25652  1.000 207.72684 ? 319 VAL A CA  1 
ATOM   1941 C C   . VAL A 1 319 ? -8.17566  -13.10829 -0.77420  1.000 210.53504 ? 319 VAL A C   1 
ATOM   1942 O O   . VAL A 1 319 ? -8.39719  -14.03997 0.00696   1.000 214.62135 ? 319 VAL A O   1 
ATOM   1943 C CB  . VAL A 1 319 ? -6.27946  -11.45248 -0.68976  1.000 204.00606 ? 319 VAL A CB  1 
ATOM   1944 C CG1 . VAL A 1 319 ? -5.80745  -10.13102 -0.11521  1.000 201.79809 ? 319 VAL A CG1 1 
ATOM   1945 C CG2 . VAL A 1 319 ? -5.35711  -12.57499 -0.25554  1.000 204.45041 ? 319 VAL A CG2 1 
ATOM   1946 N N   . ASP A 1 320 ? -8.32777  -13.22808 -2.09293  1.000 220.28849 ? 320 ASP A N   1 
ATOM   1947 C CA  . ASP A 1 320 ? -8.53704  -14.53580 -2.69587  1.000 222.35845 ? 320 ASP A CA  1 
ATOM   1948 C C   . ASP A 1 320 ? -7.32748  -15.42449 -2.43530  1.000 222.66488 ? 320 ASP A C   1 
ATOM   1949 O O   . ASP A 1 320 ? -6.21306  -14.94988 -2.20236  1.000 219.67190 ? 320 ASP A O   1 
ATOM   1950 C CB  . ASP A 1 320 ? -8.75967  -14.42766 -4.20651  1.000 219.86380 ? 320 ASP A CB  1 
ATOM   1951 C CG  . ASP A 1 320 ? -9.93386  -13.54256 -4.57380  1.000 218.28974 ? 320 ASP A CG  1 
ATOM   1952 O OD1 . ASP A 1 320 ? -10.86818 -13.41155 -3.75778  1.000 219.91121 ? 320 ASP A OD1 1 
ATOM   1953 O OD2 . ASP A 1 320 ? -9.91671  -12.96963 -5.68639  1.000 215.77908 ? 320 ASP A OD2 1 
ATOM   1954 N N   . ASP A 1 321 ? -7.55799  -16.73640 -2.48304  1.000 224.90374 ? 321 ASP A N   1 
ATOM   1955 C CA  . ASP A 1 321 ? -6.44243  -17.67291 -2.40870  1.000 226.34681 ? 321 ASP A CA  1 
ATOM   1956 C C   . ASP A 1 321 ? -5.50056  -17.51098 -3.59511  1.000 221.50116 ? 321 ASP A C   1 
ATOM   1957 O O   . ASP A 1 321 ? -4.29213  -17.73635 -3.46461  1.000 220.48054 ? 321 ASP A O   1 
ATOM   1958 C CB  . ASP A 1 321 ? -6.97188  -19.10237 -2.33162  1.000 231.02887 ? 321 ASP A CB  1 
ATOM   1959 C CG  . ASP A 1 321 ? -7.62598  -19.40897 -1.00364  1.000 234.19500 ? 321 ASP A CG  1 
ATOM   1960 O OD1 . ASP A 1 321 ? -7.47040  -18.60014 -0.06384  1.000 233.25151 ? 321 ASP A OD1 1 
ATOM   1961 O OD2 . ASP A 1 321 ? -8.28614  -20.46241 -0.90089  1.000 237.56430 ? 321 ASP A OD2 1 
ATOM   1962 N N   . SER A 1 322 ? -6.02924  -17.10129 -4.74816  1.000 235.29277 ? 322 SER A N   1 
ATOM   1963 C CA  . SER A 1 322 ? -5.24746  -16.87528 -5.96030  1.000 232.27045 ? 322 SER A CA  1 
ATOM   1964 C C   . SER A 1 322 ? -5.26630  -15.40788 -6.38363  1.000 229.24303 ? 322 SER A C   1 
ATOM   1965 O O   . SER A 1 322 ? -5.42224  -15.08979 -7.56379  1.000 227.16233 ? 322 SER A O   1 
ATOM   1966 C CB  . SER A 1 322 ? -5.75436  -17.75317 -7.09920  1.000 232.24271 ? 322 SER A CB  1 
ATOM   1967 O OG  . SER A 1 322 ? -7.12206  -17.50088 -7.36400  1.000 231.89645 ? 322 SER A OG  1 
ATOM   1968 N N   . ALA A 1 323 ? -5.10788  -14.49794 -5.42266  1.000 218.33297 ? 323 ALA A N   1 
ATOM   1969 C CA  . ALA A 1 323 ? -5.02795  -13.06376 -5.68484  1.000 215.57265 ? 323 ALA A CA  1 
ATOM   1970 C C   . ALA A 1 323 ? -3.64907  -12.56978 -5.26964  1.000 214.75883 ? 323 ALA A C   1 
ATOM   1971 O O   . ALA A 1 323 ? -3.34213  -12.50731 -4.07414  1.000 214.80691 ? 323 ALA A O   1 
ATOM   1972 C CB  . ALA A 1 323 ? -6.11765  -12.29631 -4.93850  1.000 215.96678 ? 323 ALA A CB  1 
ATOM   1973 N N   . HIS A 1 324 ? -2.82941  -12.20177 -6.25018  1.000 206.78217 ? 324 HIS A N   1 
ATOM   1974 C CA  . HIS A 1 324 ? -1.50302  -11.66893 -5.97890  1.000 205.02403 ? 324 HIS A CA  1 
ATOM   1975 C C   . HIS A 1 324 ? -1.59868  -10.18541 -5.63857  1.000 204.04237 ? 324 HIS A C   1 
ATOM   1976 O O   . HIS A 1 324 ? -2.22327  -9.40996  -6.37001  1.000 204.43444 ? 324 HIS A O   1 
ATOM   1977 C CB  . HIS A 1 324 ? -0.60252  -11.89914 -7.19270  1.000 205.29003 ? 324 HIS A CB  1 
ATOM   1978 C CG  . HIS A 1 324 ? -0.68377  -13.29044 -7.74502  1.000 206.08468 ? 324 HIS A CG  1 
ATOM   1979 N ND1 . HIS A 1 324 ? -1.76227  -13.74224 -8.47586  1.000 206.29597 ? 324 HIS A ND1 1 
ATOM   1980 C CD2 . HIS A 1 324 ? 0.17891   -14.33106 -7.66809  1.000 206.99186 ? 324 HIS A CD2 1 
ATOM   1981 C CE1 . HIS A 1 324 ? -1.55863  -14.99916 -8.82830  1.000 207.01339 ? 324 HIS A CE1 1 
ATOM   1982 N NE2 . HIS A 1 324 ? -0.38749  -15.38025 -8.35113  1.000 207.61348 ? 324 HIS A NE2 1 
ATOM   1983 N N   . ILE A 1 325 ? -0.97386  -9.78780  -4.52786  1.000 186.32373 ? 325 ILE A N   1 
ATOM   1984 C CA  . ILE A 1 325 ? -1.13277  -8.45444  -3.94296  1.000 186.08568 ? 325 ILE A CA  1 
ATOM   1985 C C   . ILE A 1 325 ? 0.20802   -7.72868  -4.02964  1.000 186.30609 ? 325 ILE A C   1 
ATOM   1986 O O   . ILE A 1 325 ? 1.24232   -8.26945  -3.61668  1.000 186.71461 ? 325 ILE A O   1 
ATOM   1987 C CB  . ILE A 1 325 ? -1.64985  -8.55148  -2.49071  1.000 186.95457 ? 325 ILE A CB  1 
ATOM   1988 C CG1 . ILE A 1 325 ? -2.91938  -9.41774  -2.40492  1.000 187.85954 ? 325 ILE A CG1 1 
ATOM   1989 C CG2 . ILE A 1 325 ? -1.93220  -7.18626  -1.92463  1.000 186.55945 ? 325 ILE A CG2 1 
ATOM   1990 C CD1 . ILE A 1 325 ? -4.02877  -9.02406  -3.38869  1.000 188.19955 ? 325 ILE A CD1 1 
ATOM   1991 N N   . SER A 1 326 ? 0.19324   -6.50363  -4.55572  1.000 170.82773 ? 326 SER A N   1 
ATOM   1992 C CA  . SER A 1 326 ? 1.41591   -5.84558  -5.03044  1.000 171.68282 ? 326 SER A CA  1 
ATOM   1993 C C   . SER A 1 326 ? 1.58947   -4.50289  -4.32614  1.000 170.88330 ? 326 SER A C   1 
ATOM   1994 O O   . SER A 1 326 ? 0.86574   -3.54956  -4.62540  1.000 171.82352 ? 326 SER A O   1 
ATOM   1995 C CB  . SER A 1 326 ? 1.34165   -5.67873  -6.55305  1.000 174.38164 ? 326 SER A CB  1 
ATOM   1996 O OG  . SER A 1 326 ? 1.33977   -6.93487  -7.21655  1.000 175.38388 ? 326 SER A OG  1 
ATOM   1997 N N   . CYS A 1 327 ? 2.54822   -4.42050  -3.40007  1.000 177.65560 ? 327 CYS A N   1 
ATOM   1998 C CA  . CYS A 1 327 ? 2.87185   -3.17196  -2.68420  1.000 178.21216 ? 327 CYS A CA  1 
ATOM   1999 C C   . CYS A 1 327 ? 4.28568   -2.75116  -3.09089  1.000 179.32205 ? 327 CYS A C   1 
ATOM   2000 O O   . CYS A 1 327 ? 5.26899   -3.35444  -2.64980  1.000 177.76980 ? 327 CYS A O   1 
ATOM   2001 C CB  . CYS A 1 327 ? 2.72994   -3.37016  -1.17072  1.000 176.04426 ? 327 CYS A CB  1 
ATOM   2002 S SG  . CYS A 1 327 ? 2.94117   -1.90333  -0.11214  1.000 177.27477 ? 327 CYS A SG  1 
ATOM   2003 N N   . ASN A 1 328 ? 4.39538   -1.71730  -3.92903  1.000 168.08040 ? 328 ASN A N   1 
ATOM   2004 C CA  . ASN A 1 328 ? 5.64232   -1.43061  -4.65571  1.000 171.51738 ? 328 ASN A CA  1 
ATOM   2005 C C   . ASN A 1 328 ? 6.20708   -0.04426  -4.34277  1.000 172.36343 ? 328 ASN A C   1 
ATOM   2006 O O   . ASN A 1 328 ? 5.95166   0.90513   -5.08539  1.000 174.06099 ? 328 ASN A O   1 
ATOM   2007 C CB  . ASN A 1 328 ? 5.41931   -1.57765  -6.16268  1.000 172.27128 ? 328 ASN A CB  1 
ATOM   2008 C CG  . ASN A 1 328 ? 4.82577   -2.91979  -6.53724  1.000 172.26495 ? 328 ASN A CG  1 
ATOM   2009 O OD1 . ASN A 1 328 ? 4.91794   -3.88318  -5.77912  1.000 171.43903 ? 328 ASN A OD1 1 
ATOM   2010 N ND2 . ASN A 1 328 ? 4.21446   -2.98933  -7.71430  1.000 173.73330 ? 328 ASN A ND2 1 
ATOM   2011 N N   . VAL A 1 329 ? 7.04507   0.04990   -3.30677  1.000 173.41510 ? 329 VAL A N   1 
ATOM   2012 C CA  . VAL A 1 329 ? 7.63894   1.33099   -2.92767  1.000 174.59187 ? 329 VAL A CA  1 
ATOM   2013 C C   . VAL A 1 329 ? 8.68370   1.75010   -3.95598  1.000 178.79481 ? 329 VAL A C   1 
ATOM   2014 O O   . VAL A 1 329 ? 9.49569   0.93400   -4.41479  1.000 181.82372 ? 329 VAL A O   1 
ATOM   2015 C CB  . VAL A 1 329 ? 8.25341   1.24686   -1.51972  1.000 172.61013 ? 329 VAL A CB  1 
ATOM   2016 C CG1 . VAL A 1 329 ? 8.83685   2.59349   -1.09716  1.000 175.06337 ? 329 VAL A CG1 1 
ATOM   2017 C CG2 . VAL A 1 329 ? 7.21749   0.78319   -0.51486  1.000 168.45294 ? 329 VAL A CG2 1 
ATOM   2018 N N   . HIS A 1 330 ? 8.66984   3.03480   -4.32054  1.000 176.11076 ? 330 HIS A N   1 
ATOM   2019 C CA  . HIS A 1 330 ? 9.63762   3.62108   -5.24276  1.000 180.42463 ? 330 HIS A CA  1 
ATOM   2020 C C   . HIS A 1 330 ? 10.26678  4.84803   -4.59647  1.000 183.70649 ? 330 HIS A C   1 
ATOM   2021 O O   . HIS A 1 330 ? 9.55323   5.76143   -4.17037  1.000 183.81081 ? 330 HIS A O   1 
ATOM   2022 C CB  . HIS A 1 330 ? 8.98080   4.01214   -6.57227  1.000 182.22807 ? 330 HIS A CB  1 
ATOM   2023 C CG  . HIS A 1 330 ? 8.75680   2.86069   -7.50252  1.000 183.81829 ? 330 HIS A CG  1 
ATOM   2024 N ND1 . HIS A 1 330 ? 8.08965   1.71571   -7.12444  1.000 181.91061 ? 330 HIS A ND1 1 
ATOM   2025 C CD2 . HIS A 1 330 ? 9.11306   2.67818   -8.79634  1.000 185.56413 ? 330 HIS A CD2 1 
ATOM   2026 C CE1 . HIS A 1 330 ? 8.04539   0.87699   -8.14423  1.000 182.40488 ? 330 HIS A CE1 1 
ATOM   2027 N NE2 . HIS A 1 330 ? 8.65929   1.43682   -9.17102  1.000 183.94759 ? 330 HIS A NE2 1 
ATOM   2028 N N   . LEU A 1 331 ? 11.59834  4.87248   -4.53614  1.000 182.00299 ? 331 LEU A N   1 
ATOM   2029 C CA  . LEU A 1 331 ? 12.34819  5.94265   -3.88727  1.000 185.96513 ? 331 LEU A CA  1 
ATOM   2030 C C   . LEU A 1 331 ? 13.34621  6.53626   -4.87457  1.000 192.22640 ? 331 LEU A C   1 
ATOM   2031 O O   . LEU A 1 331 ? 14.08608  5.79433   -5.52822  1.000 194.22187 ? 331 LEU A O   1 
ATOM   2032 C CB  . LEU A 1 331 ? 13.07629  5.41368   -2.64726  1.000 183.15711 ? 331 LEU A CB  1 
ATOM   2033 C CG  . LEU A 1 331 ? 12.23075  4.64509   -1.63136  1.000 177.68241 ? 331 LEU A CG  1 
ATOM   2034 C CD1 . LEU A 1 331 ? 13.12904  3.90266   -0.65445  1.000 175.79021 ? 331 LEU A CD1 1 
ATOM   2035 C CD2 . LEU A 1 331 ? 11.29962  5.59117   -0.89269  1.000 176.84183 ? 331 LEU A CD2 1 
ATOM   2036 N N   . SER A 1 332 ? 13.38836  7.87353   -4.95956  1.000 193.25247 ? 332 SER A N   1 
ATOM   2037 C CA  . SER A 1 332 ? 14.23623  8.57098   -5.93721  1.000 200.13305 ? 332 SER A CA  1 
ATOM   2038 C C   . SER A 1 332 ? 14.69309  9.90820   -5.34403  1.000 204.59011 ? 332 SER A C   1 
ATOM   2039 O O   . SER A 1 332 ? 13.99139  10.91680  -5.45991  1.000 206.17197 ? 332 SER A O   1 
ATOM   2040 C CB  . SER A 1 332 ? 13.48789  8.77930   -7.24762  1.000 201.56251 ? 332 SER A CB  1 
ATOM   2041 O OG  . SER A 1 332 ? 14.27849  9.48302   -8.18999  1.000 207.75353 ? 332 SER A OG  1 
ATOM   2042 N N   . GLU A 1 333 ? 15.88174  9.90644   -4.73777  1.000 201.05734 ? 333 GLU A N   1 
ATOM   2043 C CA  . GLU A 1 333 ? 16.47321  11.08745  -4.11691  1.000 204.79846 ? 333 GLU A CA  1 
ATOM   2044 C C   . GLU A 1 333 ? 17.98993  11.00262  -4.25917  1.000 208.93594 ? 333 GLU A C   1 
ATOM   2045 O O   . GLU A 1 333 ? 18.53322  9.92051   -4.51762  1.000 208.46206 ? 333 GLU A O   1 
ATOM   2046 C CB  . GLU A 1 333 ? 16.07980  11.21390  -2.63250  1.000 200.70081 ? 333 GLU A CB  1 
ATOM   2047 C CG  . GLU A 1 333 ? 14.58929  11.46454  -2.34341  1.000 198.10728 ? 333 GLU A CG  1 
ATOM   2048 C CD  . GLU A 1 333 ? 13.75560  10.19023  -2.33554  1.000 191.83602 ? 333 GLU A CD  1 
ATOM   2049 O OE1 . GLU A 1 333 ? 14.35675  9.10256   -2.42796  1.000 189.09508 ? 333 GLU A OE1 1 
ATOM   2050 O OE2 . GLU A 1 333 ? 12.50762  10.27269  -2.23813  1.000 189.98574 ? 333 GLU A OE2 1 
ATOM   2051 N N   . PRO A 1 334 ? 18.70493  12.13557  -4.10555  1.000 215.95903 ? 334 PRO A N   1 
ATOM   2052 C CA  . PRO A 1 334 ? 20.17707  12.11138  -4.12149  1.000 219.43759 ? 334 PRO A CA  1 
ATOM   2053 C C   . PRO A 1 334 ? 20.77084  11.38747  -2.91751  1.000 216.55442 ? 334 PRO A C   1 
ATOM   2054 O O   . PRO A 1 334 ? 21.54704  10.43609  -3.06795  1.000 216.86674 ? 334 PRO A O   1 
ATOM   2055 C CB  . PRO A 1 334 ? 20.54697  13.60323  -4.13061  1.000 223.21732 ? 334 PRO A CB  1 
ATOM   2056 C CG  . PRO A 1 334 ? 19.32082  14.28935  -4.70377  1.000 222.85046 ? 334 PRO A CG  1 
ATOM   2057 C CD  . PRO A 1 334 ? 18.17379  13.50828  -4.16991  1.000 217.46089 ? 334 PRO A CD  1 
ATOM   2058 N N   . LYS A 1 335 ? 20.41355  11.83734  -1.71286  1.000 219.03900 ? 335 LYS A N   1 
ATOM   2059 C CA  . LYS A 1 335 ? 20.82049  11.18649  -0.47455  1.000 215.28752 ? 335 LYS A CA  1 
ATOM   2060 C C   . LYS A 1 335 ? 19.66494  10.37168  0.09426   1.000 209.41342 ? 335 LYS A C   1 
ATOM   2061 O O   . LYS A 1 335 ? 18.49747  10.58345  -0.24543  1.000 208.57817 ? 335 LYS A O   1 
ATOM   2062 C CB  . LYS A 1 335 ? 21.30742  12.20705  0.56168   1.000 215.60372 ? 335 LYS A CB  1 
ATOM   2063 C CG  . LYS A 1 335 ? 22.79181  12.53536  0.46517   1.000 218.31616 ? 335 LYS A CG  1 
ATOM   2064 C CD  . LYS A 1 335 ? 23.19184  13.52022  1.54564   1.000 216.58505 ? 335 LYS A CD  1 
ATOM   2065 C CE  . LYS A 1 335 ? 24.70060  13.62020  1.70407   1.000 217.83719 ? 335 LYS A CE  1 
ATOM   2066 N NZ  . LYS A 1 335 ? 25.08724  14.54090  2.81570   1.000 216.45773 ? 335 LYS A NZ  1 
ATOM   2067 N N   . TYR A 1 336 ? 20.00509  9.41934   0.96591   1.000 206.21740 ? 336 TYR A N   1 
ATOM   2068 C CA  . TYR A 1 336 ? 19.03163  8.47172   1.50474   1.000 199.81308 ? 336 TYR A CA  1 
ATOM   2069 C C   . TYR A 1 336 ? 19.20953  8.34577   3.00952   1.000 195.85206 ? 336 TYR A C   1 
ATOM   2070 O O   . TYR A 1 336 ? 20.29686  8.00511   3.48365   1.000 196.18842 ? 336 TYR A O   1 
ATOM   2071 C CB  . TYR A 1 336 ? 19.16150  7.10310   0.82853   1.000 197.63035 ? 336 TYR A CB  1 
ATOM   2072 C CG  . TYR A 1 336 ? 18.34097  6.97740   -0.43192  1.000 199.24954 ? 336 TYR A CG  1 
ATOM   2073 C CD1 . TYR A 1 336 ? 18.75525  7.57491   -1.61000  1.000 205.57522 ? 336 TYR A CD1 1 
ATOM   2074 C CD2 . TYR A 1 336 ? 17.15153  6.26096   -0.44385  1.000 194.36282 ? 336 TYR A CD2 1 
ATOM   2075 C CE1 . TYR A 1 336 ? 18.00672  7.46922   -2.76423  1.000 206.77211 ? 336 TYR A CE1 1 
ATOM   2076 C CE2 . TYR A 1 336 ? 16.39532  6.14794   -1.59745  1.000 195.50448 ? 336 TYR A CE2 1 
ATOM   2077 C CZ  . TYR A 1 336 ? 16.82896  6.75532   -2.75451  1.000 201.47827 ? 336 TYR A CZ  1 
ATOM   2078 O OH  . TYR A 1 336 ? 16.08811  6.65343   -3.90836  1.000 202.79915 ? 336 TYR A OH  1 
ATOM   2079 N N   . ASN A 1 337 ? 18.14467  8.63060   3.75130   1.000 199.29512 ? 337 ASN A N   1 
ATOM   2080 C CA  . ASN A 1 337 ? 18.04491  8.37131   5.18485   1.000 195.21530 ? 337 ASN A CA  1 
ATOM   2081 C C   . ASN A 1 337 ? 16.76047  7.60680   5.47320   1.000 189.85411 ? 337 ASN A C   1 
ATOM   2082 O O   . ASN A 1 337 ? 15.97653  7.95461   6.35788   1.000 187.80439 ? 337 ASN A O   1 
ATOM   2083 C CB  . ASN A 1 337 ? 18.10058  9.67113   5.98221   1.000 197.09041 ? 337 ASN A CB  1 
ATOM   2084 C CG  . ASN A 1 337 ? 19.51596  10.15475  6.20793   1.000 201.29256 ? 337 ASN A CG  1 
ATOM   2085 O OD1 . ASN A 1 337 ? 20.40863  9.36768   6.52082   1.000 201.14780 ? 337 ASN A OD1 1 
ATOM   2086 N ND2 . ASN A 1 337 ? 19.73011  11.45497  6.05142   1.000 205.51515 ? 337 ASN A ND2 1 
ATOM   2087 N N   . HIS A 1 338 ? 16.52780  6.54730   4.70476   1.000 195.89605 ? 338 HIS A N   1 
ATOM   2088 C CA  . HIS A 1 338 ? 15.25264  5.84790   4.69584   1.000 190.21315 ? 338 HIS A CA  1 
ATOM   2089 C C   . HIS A 1 338 ? 15.34489  4.53100   5.45648   1.000 179.08299 ? 338 HIS A C   1 
ATOM   2090 O O   . HIS A 1 338 ? 16.40640  3.90766   5.53659   1.000 177.88253 ? 338 HIS A O   1 
ATOM   2091 C CB  . HIS A 1 338 ? 14.79192  5.57719   3.26016   1.000 191.26861 ? 338 HIS A CB  1 
ATOM   2092 C CG  . HIS A 1 338 ? 14.73841  6.79977   2.39619   1.000 197.06722 ? 338 HIS A CG  1 
ATOM   2093 N ND1 . HIS A 1 338 ? 15.84149  7.58867   2.14974   1.000 203.51259 ? 338 HIS A ND1 1 
ATOM   2094 C CD2 . HIS A 1 338 ? 13.71486  7.36195   1.71081   1.000 198.52891 ? 338 HIS A CD2 1 
ATOM   2095 C CE1 . HIS A 1 338 ? 15.49867  8.58795   1.35691   1.000 208.07443 ? 338 HIS A CE1 1 
ATOM   2096 N NE2 . HIS A 1 338 ? 14.21365  8.47293   1.07479   1.000 205.03054 ? 338 HIS A NE2 1 
ATOM   2097 N N   . LEU A 1 339 ? 14.21183  4.11440   6.01603   1.000 193.53169 ? 339 LEU A N   1 
ATOM   2098 C CA  . LEU A 1 339 ? 14.07182  2.81597   6.66306   1.000 183.59464 ? 339 LEU A CA  1 
ATOM   2099 C C   . LEU A 1 339 ? 13.06224  2.00466   5.86494   1.000 177.88270 ? 339 LEU A C   1 
ATOM   2100 O O   . LEU A 1 339 ? 11.91530  2.43208   5.69659   1.000 177.33588 ? 339 LEU A O   1 
ATOM   2101 C CB  . LEU A 1 339 ? 13.62384  2.96878   8.11790   1.000 182.67384 ? 339 LEU A CB  1 
ATOM   2102 C CG  . LEU A 1 339 ? 13.71782  1.72583   9.00434   1.000 181.94342 ? 339 LEU A CG  1 
ATOM   2103 C CD1 . LEU A 1 339 ? 15.16342  1.29116   9.15914   1.000 178.86002 ? 339 LEU A CD1 1 
ATOM   2104 C CD2 . LEU A 1 339 ? 13.09181  1.98718   10.36302  1.000 189.27808 ? 339 LEU A CD2 1 
ATOM   2105 N N   . VAL A 1 340 ? 13.48698  0.84537   5.36858   1.000 169.64933 ? 340 VAL A N   1 
ATOM   2106 C CA  . VAL A 1 340 ? 12.67896  0.02691   4.47210   1.000 170.48793 ? 340 VAL A CA  1 
ATOM   2107 C C   . VAL A 1 340 ? 12.46364  -1.33663  5.11055   1.000 166.52988 ? 340 VAL A C   1 
ATOM   2108 O O   . VAL A 1 340 ? 13.42889  -2.00736  5.49349   1.000 167.14239 ? 340 VAL A O   1 
ATOM   2109 C CB  . VAL A 1 340 ? 13.34035  -0.11897  3.08946   1.000 172.84183 ? 340 VAL A CB  1 
ATOM   2110 C CG1 . VAL A 1 340 ? 12.48450  -0.98772  2.18025   1.000 178.07818 ? 340 VAL A CG1 1 
ATOM   2111 C CG2 . VAL A 1 340 ? 13.57387  1.24840   2.46808   1.000 175.78191 ? 340 VAL A CG2 1 
ATOM   2112 N N   . GLY A 1 341 ? 11.20752  -1.74552  5.21116   1.000 158.55966 ? 341 GLY A N   1 
ATOM   2113 C CA  . GLY A 1 341 ? 10.89822  -3.04358  5.76562   1.000 157.78670 ? 341 GLY A CA  1 
ATOM   2114 C C   . GLY A 1 341 ? 9.44364   -3.40128  5.57645   1.000 157.55959 ? 341 GLY A C   1 
ATOM   2115 O O   . GLY A 1 341 ? 8.73392   -2.78608  4.77990   1.000 158.17966 ? 341 GLY A O   1 
ATOM   2116 N N   . LEU A 1 342 ? 9.00582   -4.41176  6.32390   1.000 164.70770 ? 342 LEU A N   1 
ATOM   2117 C CA  . LEU A 1 342 ? 7.62453   -4.86188  6.24902   1.000 167.76204 ? 342 LEU A CA  1 
ATOM   2118 C C   . LEU A 1 342 ? 7.27198   -5.60774  7.52613   1.000 171.62927 ? 342 LEU A C   1 
ATOM   2119 O O   . LEU A 1 342 ? 8.14224   -6.16957  8.19613   1.000 166.50316 ? 342 LEU A O   1 
ATOM   2120 C CB  . LEU A 1 342 ? 7.38796   -5.75239  5.02101   1.000 169.51491 ? 342 LEU A CB  1 
ATOM   2121 C CG  . LEU A 1 342 ? 8.23305   -7.02031  4.85981   1.000 169.98121 ? 342 LEU A CG  1 
ATOM   2122 C CD1 . LEU A 1 342 ? 7.55958   -8.22783  5.49880   1.000 177.66084 ? 342 LEU A CD1 1 
ATOM   2123 C CD2 . LEU A 1 342 ? 8.52824   -7.28826  3.39200   1.000 171.57570 ? 342 LEU A CD2 1 
ATOM   2124 N N   . ASN A 1 343 ? 5.98276   -5.60452  7.85135   1.000 177.06048 ? 343 ASN A N   1 
ATOM   2125 C CA  . ASN A 1 343 ? 5.44319   -6.39019  8.95734   1.000 176.54922 ? 343 ASN A CA  1 
ATOM   2126 C C   . ASN A 1 343 ? 4.48737   -7.41545  8.35621   1.000 176.32947 ? 343 ASN A C   1 
ATOM   2127 O O   . ASN A 1 343 ? 3.34273   -7.09202  8.02448   1.000 181.95097 ? 343 ASN A O   1 
ATOM   2128 C CB  . ASN A 1 343 ? 4.74942   -5.50262  9.98673   1.000 182.89518 ? 343 ASN A CB  1 
ATOM   2129 C CG  . ASN A 1 343 ? 4.43303   -6.23904  11.27476  1.000 190.68405 ? 343 ASN A CG  1 
ATOM   2130 O OD1 . ASN A 1 343 ? 4.35533   -7.46715  11.29762  1.000 193.69401 ? 343 ASN A OD1 1 
ATOM   2131 N ND2 . ASN A 1 343 ? 4.24318   -5.48954  12.35503  1.000 191.60947 ? 343 ASN A ND2 1 
ATOM   2132 N N   . CYS A 1 344 ? 4.96401   -8.65144  8.21447   1.000 170.50081 ? 344 CYS A N   1 
ATOM   2133 C CA  . CYS A 1 344 ? 4.17851   -9.72259  7.62410   1.000 179.77211 ? 344 CYS A CA  1 
ATOM   2134 C C   . CYS A 1 344 ? 3.62708   -10.61141 8.72371   1.000 187.29453 ? 344 CYS A C   1 
ATOM   2135 O O   . CYS A 1 344 ? 4.41269   -11.14520 9.52255   1.000 186.71707 ? 344 CYS A O   1 
ATOM   2136 C CB  . CYS A 1 344 ? 5.03400   -10.54095 6.66475   1.000 171.09290 ? 344 CYS A CB  1 
ATOM   2137 S SG  . CYS A 1 344 ? 4.29586   -12.08708 6.08776   1.000 185.09797 ? 344 CYS A SG  1 
ATOM   2138 N N   . PRO A 1 345 ? 2.30749   -10.79528 8.81809   1.000 184.73720 ? 345 PRO A N   1 
ATOM   2139 C CA  . PRO A 1 345 ? 1.77826   -11.70891 9.84093   1.000 189.56922 ? 345 PRO A CA  1 
ATOM   2140 C C   . PRO A 1 345 ? 2.10564   -13.16374 9.56323   1.000 191.98353 ? 345 PRO A C   1 
ATOM   2141 O O   . PRO A 1 345 ? 2.22305   -13.95134 10.51001  1.000 196.29246 ? 345 PRO A O   1 
ATOM   2142 C CB  . PRO A 1 345 ? 0.26674   -11.44728 9.79729   1.000 189.48856 ? 345 PRO A CB  1 
ATOM   2143 C CG  . PRO A 1 345 ? 0.01695   -10.94408 8.41679   1.000 186.56944 ? 345 PRO A CG  1 
ATOM   2144 C CD  . PRO A 1 345 ? 1.23871   -10.16011 8.02918   1.000 182.85227 ? 345 PRO A CD  1 
ATOM   2145 N N   . GLY A 1 346 ? 2.25753   -13.54431 8.29945   1.000 185.25302 ? 346 GLY A N   1 
ATOM   2146 C CA  . GLY A 1 346 ? 2.63991   -14.89083 7.93189   1.000 188.21336 ? 346 GLY A CA  1 
ATOM   2147 C C   . GLY A 1 346 ? 4.14299   -15.05214 7.85465   1.000 187.00883 ? 346 GLY A C   1 
ATOM   2148 O O   . GLY A 1 346 ? 4.90993   -14.30362 8.46514   1.000 186.26785 ? 346 GLY A O   1 
ATOM   2149 N N   . ASP A 1 347 ? 4.56736   -16.04847 7.08312   1.000 179.45185 ? 347 ASP A N   1 
ATOM   2150 C CA  . ASP A 1 347 ? 5.98746   -16.29901 6.90142   1.000 178.83171 ? 347 ASP A CA  1 
ATOM   2151 C C   . ASP A 1 347 ? 6.55484   -15.40070 5.80471   1.000 174.21112 ? 347 ASP A C   1 
ATOM   2152 O O   . ASP A 1 347 ? 5.84094   -14.93178 4.91405   1.000 172.98544 ? 347 ASP A O   1 
ATOM   2153 C CB  . ASP A 1 347 ? 6.23681   -17.76957 6.56621   1.000 183.22197 ? 347 ASP A CB  1 
ATOM   2154 C CG  . ASP A 1 347 ? 5.77069   -18.70379 7.66616   1.000 187.30727 ? 347 ASP A CG  1 
ATOM   2155 O OD1 . ASP A 1 347 ? 5.66329   -18.25281 8.82584   1.000 188.16018 ? 347 ASP A OD1 1 
ATOM   2156 O OD2 . ASP A 1 347 ? 5.51466   -19.89024 7.37359   1.000 189.49356 ? 347 ASP A OD2 1 
ATOM   2157 N N   . ILE A 1 348 ? 7.86257   -15.16575 5.88114   1.000 175.42887 ? 348 ILE A N   1 
ATOM   2158 C CA  . ILE A 1 348 ? 8.56837   -14.26282 4.97858   1.000 169.22573 ? 348 ILE A CA  1 
ATOM   2159 C C   . ILE A 1 348 ? 9.51190   -15.08065 4.10827   1.000 172.52699 ? 348 ILE A C   1 
ATOM   2160 O O   . ILE A 1 348 ? 10.32354  -15.86055 4.62186   1.000 177.72182 ? 348 ILE A O   1 
ATOM   2161 C CB  . ILE A 1 348 ? 9.32973   -13.17869 5.76053   1.000 165.07193 ? 348 ILE A CB  1 
ATOM   2162 C CG1 . ILE A 1 348 ? 8.33822   -12.19141 6.37896   1.000 162.22917 ? 348 ILE A CG1 1 
ATOM   2163 C CG2 . ILE A 1 348 ? 10.33056  -12.46510 4.86344   1.000 163.13427 ? 348 ILE A CG2 1 
ATOM   2164 C CD1 . ILE A 1 348 ? 8.93845   -11.30008 7.43604   1.000 164.41333 ? 348 ILE A CD1 1 
ATOM   2165 N N   . ILE A 1 349 ? 9.40121   -14.90482 2.79438   1.000 171.91684 ? 349 ILE A N   1 
ATOM   2166 C CA  . ILE A 1 349 ? 10.22239  -15.63356 1.82958   1.000 172.40661 ? 349 ILE A CA  1 
ATOM   2167 C C   . ILE A 1 349 ? 10.81519  -14.64023 0.83581   1.000 169.48501 ? 349 ILE A C   1 
ATOM   2168 O O   . ILE A 1 349 ? 10.07600  -13.82710 0.26372   1.000 169.07965 ? 349 ILE A O   1 
ATOM   2169 C CB  . ILE A 1 349 ? 9.40903   -16.71800 1.10281   1.000 172.97496 ? 349 ILE A CB  1 
ATOM   2170 C CG1 . ILE A 1 349 ? 8.88952   -17.76891 2.08846   1.000 176.00949 ? 349 ILE A CG1 1 
ATOM   2171 C CG2 . ILE A 1 349 ? 10.24414  -17.37718 0.01498   1.000 173.04672 ? 349 ILE A CG2 1 
ATOM   2172 C CD1 . ILE A 1 349 ? 7.49199   -17.49384 2.60741   1.000 176.88584 ? 349 ILE A CD1 1 
ATOM   2173 N N   . PRO A 1 350 ? 12.13791  -14.65004 0.60465   1.000 167.85139 ? 350 PRO A N   1 
ATOM   2174 C CA  . PRO A 1 350 ? 13.11812  -15.49018 1.30044   1.000 170.10480 ? 350 PRO A CA  1 
ATOM   2175 C C   . PRO A 1 350 ? 13.47036  -14.92265 2.67120   1.000 168.17158 ? 350 PRO A C   1 
ATOM   2176 O O   . PRO A 1 350 ? 12.66911  -14.18654 3.24545   1.000 164.21551 ? 350 PRO A O   1 
ATOM   2177 C CB  . PRO A 1 350 ? 14.32626  -15.46073 0.36430   1.000 171.57269 ? 350 PRO A CB  1 
ATOM   2178 C CG  . PRO A 1 350 ? 14.23190  -14.13727 -0.30426  1.000 170.13625 ? 350 PRO A CG  1 
ATOM   2179 C CD  . PRO A 1 350 ? 12.76260  -13.84526 -0.46055  1.000 166.75240 ? 350 PRO A CD  1 
ATOM   2180 N N   . ASP A 1 351 ? 14.65095  -15.25174 3.19374   1.000 170.05928 ? 351 ASP A N   1 
ATOM   2181 C CA  . ASP A 1 351 ? 15.06890  -14.73249 4.49575   1.000 170.51399 ? 351 ASP A CA  1 
ATOM   2182 C C   . ASP A 1 351 ? 15.43822  -13.25961 4.33737   1.000 162.40482 ? 351 ASP A C   1 
ATOM   2183 O O   . ASP A 1 351 ? 16.60765  -12.87132 4.27761   1.000 159.46065 ? 351 ASP A O   1 
ATOM   2184 C CB  . ASP A 1 351 ? 16.21488  -15.55386 5.07240   1.000 170.07268 ? 351 ASP A CB  1 
ATOM   2185 C CG  . ASP A 1 351 ? 15.72872  -16.81311 5.76188   1.000 176.67770 ? 351 ASP A CG  1 
ATOM   2186 O OD1 . ASP A 1 351 ? 14.60673  -17.26233 5.44502   1.000 178.60731 ? 351 ASP A OD1 1 
ATOM   2187 O OD2 . ASP A 1 351 ? 16.45552  -17.34251 6.62845   1.000 180.20312 ? 351 ASP A OD2 1 
ATOM   2188 N N   . CYS A 1 352 ? 14.40182  -12.42821 4.26422   1.000 173.19748 ? 352 CYS A N   1 
ATOM   2189 C CA  . CYS A 1 352 ? 14.57304  -10.98777 4.15341   1.000 165.19970 ? 352 CYS A CA  1 
ATOM   2190 C C   . CYS A 1 352 ? 15.02244  -10.41087 5.49593   1.000 163.98062 ? 352 CYS A C   1 
ATOM   2191 O O   . CYS A 1 352 ? 14.74872  -10.97673 6.55804   1.000 164.23047 ? 352 CYS A O   1 
ATOM   2192 C CB  . CYS A 1 352 ? 13.26031  -10.34952 3.66810   1.000 164.13720 ? 352 CYS A CB  1 
ATOM   2193 S SG  . CYS A 1 352 ? 12.89834  -10.73566 1.91817   1.000 174.19693 ? 352 CYS A SG  1 
ATOM   2194 N N   . PHE A 1 353 ? 15.73682  -9.28483  5.44816   1.000 166.04336 ? 353 PHE A N   1 
ATOM   2195 C CA  . PHE A 1 353 ? 16.00955  -8.55237  4.21316   1.000 166.12621 ? 353 PHE A CA  1 
ATOM   2196 C C   . PHE A 1 353 ? 17.39841  -8.81519  3.64462   1.000 169.49488 ? 353 PHE A C   1 
ATOM   2197 O O   . PHE A 1 353 ? 17.83113  -8.13004  2.72146   1.000 170.83826 ? 353 PHE A O   1 
ATOM   2198 C CB  . PHE A 1 353 ? 15.81618  -7.05185  4.43879   1.000 164.20326 ? 353 PHE A CB  1 
ATOM   2199 C CG  . PHE A 1 353 ? 14.54253  -6.51801  3.85359   1.000 161.94865 ? 353 PHE A CG  1 
ATOM   2200 C CD1 . PHE A 1 353 ? 13.33965  -6.67063  4.52217   1.000 159.73044 ? 353 PHE A CD1 1 
ATOM   2201 C CD2 . PHE A 1 353 ? 14.54587  -5.87579  2.62719   1.000 167.03323 ? 353 PHE A CD2 1 
ATOM   2202 C CE1 . PHE A 1 353 ? 12.16416  -6.18520  3.98154   1.000 159.09684 ? 353 PHE A CE1 1 
ATOM   2203 C CE2 . PHE A 1 353 ? 13.37486  -5.38699  2.08136   1.000 166.98844 ? 353 PHE A CE2 1 
ATOM   2204 C CZ  . PHE A 1 353 ? 12.18196  -5.54213  2.75933   1.000 161.61370 ? 353 PHE A CZ  1 
ATOM   2205 N N   . PHE A 1 354 ? 18.08943  -9.81677  4.18655   1.000 160.84980 ? 354 PHE A N   1 
ATOM   2206 C CA  . PHE A 1 354 ? 19.38150  -10.19552 3.62394   1.000 165.54351 ? 354 PHE A CA  1 
ATOM   2207 C C   . PHE A 1 354 ? 19.21687  -10.78099 2.22661   1.000 164.83979 ? 354 PHE A C   1 
ATOM   2208 O O   . PHE A 1 354 ? 19.96599  -10.43033 1.30793   1.000 174.79311 ? 354 PHE A O   1 
ATOM   2209 C CB  . PHE A 1 354 ? 20.08210  -11.19089 4.54747   1.000 179.19955 ? 354 PHE A CB  1 
ATOM   2210 C CG  . PHE A 1 354 ? 21.56189  -10.96258 4.68061   1.000 183.99159 ? 354 PHE A CG  1 
ATOM   2211 C CD1 . PHE A 1 354 ? 22.29816  -10.44030 3.62874   1.000 186.17934 ? 354 PHE A CD1 1 
ATOM   2212 C CD2 . PHE A 1 354 ? 22.21509  -11.26131 5.86413   1.000 185.40907 ? 354 PHE A CD2 1 
ATOM   2213 C CE1 . PHE A 1 354 ? 23.65983  -10.22813 3.75534   1.000 188.60797 ? 354 PHE A CE1 1 
ATOM   2214 C CE2 . PHE A 1 354 ? 23.57306  -11.05072 5.99736   1.000 187.80861 ? 354 PHE A CE2 1 
ATOM   2215 C CZ  . PHE A 1 354 ? 24.29715  -10.53281 4.94092   1.000 189.24317 ? 354 PHE A CZ  1 
ATOM   2216 N N   . GLN A 1 355 ? 18.23637  -11.66155 2.04480   1.000 166.18582 ? 355 GLN A N   1 
ATOM   2217 C CA  . GLN A 1 355 ? 17.96260  -12.29759 0.76347   1.000 167.68918 ? 355 GLN A CA  1 
ATOM   2218 C C   . GLN A 1 355 ? 16.67367  -11.74475 0.17127   1.000 167.10969 ? 355 GLN A C   1 
ATOM   2219 O O   . GLN A 1 355 ? 15.71228  -11.47799 0.89846   1.000 165.91757 ? 355 GLN A O   1 
ATOM   2220 C CB  . GLN A 1 355 ? 17.84776  -13.81562 0.91837   1.000 178.87854 ? 355 GLN A CB  1 
ATOM   2221 C CG  . GLN A 1 355 ? 19.14684  -14.50964 1.27629   1.000 183.44810 ? 355 GLN A CG  1 
ATOM   2222 C CD  . GLN A 1 355 ? 18.95313  -15.98370 1.56252   1.000 185.23417 ? 355 GLN A CD  1 
ATOM   2223 O OE1 . GLN A 1 355 ? 17.97799  -16.38064 2.20011   1.000 185.07388 ? 355 GLN A OE1 1 
ATOM   2224 N NE2 . GLN A 1 355 ? 19.88217  -16.80547 1.08924   1.000 189.08969 ? 355 GLN A NE2 1 
ATOM   2225 N N   . VAL A 1 356 ? 16.65237  -11.59116 -1.15342  1.000 165.79701 ? 356 VAL A N   1 
ATOM   2226 C CA  . VAL A 1 356 ? 15.50431  -11.02902 -1.85722  1.000 172.62988 ? 356 VAL A CA  1 
ATOM   2227 C C   . VAL A 1 356 ? 15.42063  -11.65563 -3.24254  1.000 178.04578 ? 356 VAL A C   1 
ATOM   2228 O O   . VAL A 1 356 ? 16.42927  -12.08009 -3.81219  1.000 179.98859 ? 356 VAL A O   1 
ATOM   2229 C CB  . VAL A 1 356 ? 15.59695  -9.48764  -1.96389  1.000 166.43647 ? 356 VAL A CB  1 
ATOM   2230 C CG1 . VAL A 1 356 ? 15.14982  -8.82166  -0.67007  1.000 159.85112 ? 356 VAL A CG1 1 
ATOM   2231 C CG2 . VAL A 1 356 ? 17.01745  -9.07043  -2.31943  1.000 178.19208 ? 356 VAL A CG2 1 
ATOM   2232 N N   . TYR A 1 357 ? 14.20454  -11.71038 -3.78522  1.000 178.19308 ? 357 TYR A N   1 
ATOM   2233 C CA  . TYR A 1 357 ? 14.01980  -12.13085 -5.16762  1.000 179.59159 ? 357 TYR A CA  1 
ATOM   2234 C C   . TYR A 1 357 ? 14.47619  -11.02859 -6.11848  1.000 182.11037 ? 357 TYR A C   1 
ATOM   2235 O O   . TYR A 1 357 ? 14.44704  -9.84033  -5.78764  1.000 182.62523 ? 357 TYR A O   1 
ATOM   2236 C CB  . TYR A 1 357 ? 12.55723  -12.48707 -5.43847  1.000 178.62058 ? 357 TYR A CB  1 
ATOM   2237 C CG  . TYR A 1 357 ? 12.21986  -13.95083 -5.24277  1.000 177.10989 ? 357 TYR A CG  1 
ATOM   2238 C CD1 . TYR A 1 357 ? 11.90055  -14.45203 -3.98688  1.000 173.11209 ? 357 TYR A CD1 1 
ATOM   2239 C CD2 . TYR A 1 357 ? 12.21073  -14.82938 -6.31921  1.000 180.11680 ? 357 TYR A CD2 1 
ATOM   2240 C CE1 . TYR A 1 357 ? 11.58666  -15.78967 -3.80871  1.000 171.77372 ? 357 TYR A CE1 1 
ATOM   2241 C CE2 . TYR A 1 357 ? 11.89811  -16.16699 -6.15094  1.000 179.19845 ? 357 TYR A CE2 1 
ATOM   2242 C CZ  . TYR A 1 357 ? 11.58702  -16.64119 -4.89388  1.000 174.78723 ? 357 TYR A CZ  1 
ATOM   2243 O OH  . TYR A 1 357 ? 11.27515  -17.97002 -4.71842  1.000 173.67725 ? 357 TYR A OH  1 
ATOM   2244 N N   . GLN A 1 358 ? 14.89871  -11.43804 -7.31968  1.000 185.05360 ? 358 GLN A N   1 
ATOM   2245 C CA  . GLN A 1 358 ? 15.52661  -10.48615 -8.23623  1.000 187.83967 ? 358 GLN A CA  1 
ATOM   2246 C C   . GLN A 1 358 ? 14.53953  -9.48603  -8.82878  1.000 188.22635 ? 358 GLN A C   1 
ATOM   2247 O O   . GLN A 1 358 ? 14.83708  -8.27900  -8.80827  1.000 190.81836 ? 358 GLN A O   1 
ATOM   2248 C CB  . GLN A 1 358 ? 16.29619  -11.24379 -9.32178  1.000 189.82344 ? 358 GLN A CB  1 
ATOM   2249 C CG  . GLN A 1 358 ? 17.52736  -11.96487 -8.79680  1.000 191.18710 ? 358 GLN A CG  1 
ATOM   2250 C CD  . GLN A 1 358 ? 18.20849  -12.81022 -9.85350  1.000 194.41935 ? 358 GLN A CD  1 
ATOM   2251 O OE1 . GLN A 1 358 ? 17.57668  -13.25547 -10.81164 1.000 193.87478 ? 358 GLN A OE1 1 
ATOM   2252 N NE2 . GLN A 1 358 ? 19.50719  -13.03362 -9.68546  1.000 197.42767 ? 358 GLN A NE2 1 
ATOM   2253 N N   . PRO A 1 359 ? 13.37541  -9.88630  -9.37771  1.000 193.33710 ? 359 PRO A N   1 
ATOM   2254 C CA  . PRO A 1 359 ? 12.78182  -11.21396 -9.57341  1.000 191.73339 ? 359 PRO A CA  1 
ATOM   2255 C C   . PRO A 1 359 ? 13.27351  -11.90282 -10.84365 1.000 193.36245 ? 359 PRO A C   1 
ATOM   2256 O O   . PRO A 1 359 ? 12.60515  -12.81833 -11.32490 1.000 191.51963 ? 359 PRO A O   1 
ATOM   2257 C CB  . PRO A 1 359 ? 11.28934  -10.90638 -9.66813  1.000 189.81470 ? 359 PRO A CB  1 
ATOM   2258 C CG  . PRO A 1 359 ? 11.25048  -9.57571  -10.32715 1.000 191.23781 ? 359 PRO A CG  1 
ATOM   2259 C CD  . PRO A 1 359 ? 12.46003  -8.82091  -9.82950  1.000 193.66289 ? 359 PRO A CD  1 
ATOM   2260 N N   . SER A 1 367 ? 12.80167  -19.27231 -7.69159  1.000 183.94478 ? 367 SER A N   1 
ATOM   2261 C CA  . SER A 1 367 ? 14.06527  -19.43180 -6.98144  1.000 186.23414 ? 367 SER A CA  1 
ATOM   2262 C C   . SER A 1 367 ? 15.15174  -18.54064 -7.57935  1.000 187.21537 ? 367 SER A C   1 
ATOM   2263 O O   . SER A 1 367 ? 16.05839  -19.02060 -8.25989  1.000 189.41754 ? 367 SER A O   1 
ATOM   2264 C CB  . SER A 1 367 ? 14.51146  -20.89554 -7.00454  1.000 189.06289 ? 367 SER A CB  1 
ATOM   2265 O OG  . SER A 1 367 ? 15.70321  -21.07841 -6.25982  1.000 190.57737 ? 367 SER A OG  1 
ATOM   2266 N N   . ASN A 1 368 ? 15.04695  -17.23706 -7.32260  1.000 189.16128 ? 368 ASN A N   1 
ATOM   2267 C CA  . ASN A 1 368 ? 16.04126  -16.27398 -7.78093  1.000 189.20344 ? 368 ASN A CA  1 
ATOM   2268 C C   . ASN A 1 368 ? 16.60728  -15.51716 -6.58668  1.000 188.57058 ? 368 ASN A C   1 
ATOM   2269 O O   . ASN A 1 368 ? 16.64083  -14.28246 -6.58046  1.000 187.64826 ? 368 ASN A O   1 
ATOM   2270 C CB  . ASN A 1 368 ? 15.42913  -15.30173 -8.79219  1.000 189.07966 ? 368 ASN A CB  1 
ATOM   2271 C CG  . ASN A 1 368 ? 14.74033  -16.01113 -9.94192  1.000 188.75013 ? 368 ASN A CG  1 
ATOM   2272 O OD1 . ASN A 1 368 ? 13.57007  -15.75914 -10.22973 1.000 186.91704 ? 368 ASN A OD1 1 
ATOM   2273 N ND2 . ASN A 1 368 ? 15.46467  -16.90380 -10.60642 1.000 189.86440 ? 368 ASN A ND2 1 
ATOM   2274 N N   . ILE A 1 369 ? 17.05930  -16.25533 -5.57711  1.000 173.41408 ? 369 ILE A N   1 
ATOM   2275 C CA  . ILE A 1 369 ? 17.41846  -15.67607 -4.28688  1.000 172.97967 ? 369 ILE A CA  1 
ATOM   2276 C C   . ILE A 1 369 ? 18.79844  -15.03355 -4.39500  1.000 176.03116 ? 369 ILE A C   1 
ATOM   2277 O O   . ILE A 1 369 ? 19.81692  -15.72759 -4.46241  1.000 180.01789 ? 369 ILE A O   1 
ATOM   2278 C CB  . ILE A 1 369 ? 17.37608  -16.72914 -3.17571  1.000 172.95396 ? 369 ILE A CB  1 
ATOM   2279 C CG1 . ILE A 1 369 ? 15.97504  -17.34274 -3.09615  1.000 170.93200 ? 369 ILE A CG1 1 
ATOM   2280 C CG2 . ILE A 1 369 ? 17.76881  -16.11748 -1.84621  1.000 173.16099 ? 369 ILE A CG2 1 
ATOM   2281 C CD1 . ILE A 1 369 ? 15.82934  -18.41036 -2.04130  1.000 171.56198 ? 369 ILE A CD1 1 
ATOM   2282 N N   . VAL A 1 370 ? 18.82888  -13.70321 -4.40027  1.000 174.76961 ? 370 VAL A N   1 
ATOM   2283 C CA  . VAL A 1 370 ? 20.06659  -12.94093 -4.46843  1.000 177.81939 ? 370 VAL A CA  1 
ATOM   2284 C C   . VAL A 1 370 ? 20.33216  -12.32685 -3.09269  1.000 176.82403 ? 370 VAL A C   1 
ATOM   2285 O O   . VAL A 1 370 ? 19.46246  -12.29122 -2.22204  1.000 173.09681 ? 370 VAL A O   1 
ATOM   2286 C CB  . VAL A 1 370 ? 20.01415  -11.85664 -5.56681  1.000 179.26346 ? 370 VAL A CB  1 
ATOM   2287 C CG1 . VAL A 1 370 ? 19.24408  -10.63113 -5.07915  1.000 177.77757 ? 370 VAL A CG1 1 
ATOM   2288 C CG2 . VAL A 1 370 ? 21.41314  -11.48273 -6.04911  1.000 184.85082 ? 370 VAL A CG2 1 
ATOM   2289 N N   . TYR A 1 371 ? 21.55611  -11.84265 -2.90134  1.000 179.11580 ? 371 TYR A N   1 
ATOM   2290 C CA  . TYR A 1 371 ? 21.96315  -11.19818 -1.65936  1.000 175.93145 ? 371 TYR A CA  1 
ATOM   2291 C C   . TYR A 1 371 ? 21.85836  -9.68360  -1.79232  1.000 175.75617 ? 371 TYR A C   1 
ATOM   2292 O O   . TYR A 1 371 ? 22.23512  -9.10966  -2.81871  1.000 182.42060 ? 371 TYR A O   1 
ATOM   2293 C CB  . TYR A 1 371 ? 23.38909  -11.60540 -1.27286  1.000 180.64555 ? 371 TYR A CB  1 
ATOM   2294 C CG  . TYR A 1 371 ? 23.44204  -12.87912 -0.45526  1.000 179.86787 ? 371 TYR A CG  1 
ATOM   2295 C CD1 . TYR A 1 371 ? 23.40868  -14.12763 -1.06627  1.000 181.85846 ? 371 TYR A CD1 1 
ATOM   2296 C CD2 . TYR A 1 371 ? 23.51686  -12.83177 0.93011   1.000 177.00040 ? 371 TYR A CD2 1 
ATOM   2297 C CE1 . TYR A 1 371 ? 23.45335  -15.29235 -0.31749  1.000 181.48280 ? 371 TYR A CE1 1 
ATOM   2298 C CE2 . TYR A 1 371 ? 23.56227  -13.99147 1.68715   1.000 177.13930 ? 371 TYR A CE2 1 
ATOM   2299 C CZ  . TYR A 1 371 ? 23.53036  -15.21797 1.05789   1.000 180.08632 ? 371 TYR A CZ  1 
ATOM   2300 O OH  . TYR A 1 371 ? 23.57524  -16.37412 1.80399   1.000 181.29725 ? 371 TYR A OH  1 
ATOM   2301 N N   . LEU A 1 372 ? 21.34641  -9.04014  -0.73945  1.000 180.24817 ? 372 LEU A N   1 
ATOM   2302 C CA  . LEU A 1 372 ? 20.98740  -7.62642  -0.83004  1.000 181.43815 ? 372 LEU A CA  1 
ATOM   2303 C C   . LEU A 1 372 ? 22.22181  -6.73442  -0.90004  1.000 187.36287 ? 372 LEU A C   1 
ATOM   2304 O O   . LEU A 1 372 ? 22.31147  -5.85576  -1.76554  1.000 191.81802 ? 372 LEU A O   1 
ATOM   2305 C CB  . LEU A 1 372 ? 20.10931  -7.23083  0.35629   1.000 171.44732 ? 372 LEU A CB  1 
ATOM   2306 C CG  . LEU A 1 372 ? 19.53019  -5.81923  0.25616   1.000 170.64543 ? 372 LEU A CG  1 
ATOM   2307 C CD1 . LEU A 1 372 ? 18.53841  -5.73361  -0.89384  1.000 171.45742 ? 372 LEU A CD1 1 
ATOM   2308 C CD2 . LEU A 1 372 ? 18.88410  -5.38519  1.56218   1.000 168.75834 ? 372 LEU A CD2 1 
ATOM   2309 N N   . ASP A 1 373 ? 23.18181  -6.94134  0.00905   1.000 184.63874 ? 373 ASP A N   1 
ATOM   2310 C CA  . ASP A 1 373 ? 24.35426  -6.06984  0.07444   1.000 190.53054 ? 373 ASP A CA  1 
ATOM   2311 C C   . ASP A 1 373 ? 25.07892  -5.99729  -1.26397  1.000 196.69467 ? 373 ASP A C   1 
ATOM   2312 O O   . ASP A 1 373 ? 25.57058  -4.93236  -1.65653  1.000 201.26077 ? 373 ASP A O   1 
ATOM   2313 C CB  . ASP A 1 373 ? 25.30808  -6.55166  1.16952   1.000 191.57170 ? 373 ASP A CB  1 
ATOM   2314 C CG  . ASP A 1 373 ? 24.68995  -6.48961  2.54981   1.000 188.83296 ? 373 ASP A CG  1 
ATOM   2315 O OD1 . ASP A 1 373 ? 23.73163  -7.24770  2.80516   1.000 185.92431 ? 373 ASP A OD1 1 
ATOM   2316 O OD2 . ASP A 1 373 ? 25.16322  -5.68544  3.37983   1.000 189.96599 ? 373 ASP A OD2 1 
ATOM   2317 N N   . SER A 1 374 ? 25.14929  -7.12005  -1.98195  1.000 190.87864 ? 374 SER A N   1 
ATOM   2318 C CA  . SER A 1 374 ? 25.77489  -7.12823  -3.30008  1.000 195.93791 ? 374 SER A CA  1 
ATOM   2319 C C   . SER A 1 374 ? 24.88513  -6.47223  -4.35008  1.000 197.46932 ? 374 SER A C   1 
ATOM   2320 O O   . SER A 1 374 ? 25.38618  -5.79556  -5.25500  1.000 202.45340 ? 374 SER A O   1 
ATOM   2321 C CB  . SER A 1 374 ? 26.11126  -8.56313  -3.70699  1.000 196.12206 ? 374 SER A CB  1 
ATOM   2322 O OG  . SER A 1 374 ? 24.98326  -9.41038  -3.56965  1.000 192.88525 ? 374 SER A OG  1 
ATOM   2323 N N   . GLN A 1 375 ? 23.56652  -6.66025  -4.24434  1.000 190.03354 ? 375 GLN A N   1 
ATOM   2324 C CA  . GLN A 1 375 ? 22.65007  -6.07325  -5.21719  1.000 189.67907 ? 375 GLN A CA  1 
ATOM   2325 C C   . GLN A 1 375 ? 22.64368  -4.55115  -5.12408  1.000 192.53827 ? 375 GLN A C   1 
ATOM   2326 O O   . GLN A 1 375 ? 22.62376  -3.86204  -6.15000  1.000 196.47190 ? 375 GLN A O   1 
ATOM   2327 C CB  . GLN A 1 375 ? 21.24380  -6.63785  -5.01013  1.000 184.50182 ? 375 GLN A CB  1 
ATOM   2328 C CG  . GLN A 1 375 ? 20.20189  -6.12135  -5.98812  1.000 184.90133 ? 375 GLN A CG  1 
ATOM   2329 C CD  . GLN A 1 375 ? 20.34646  -6.71256  -7.37541  1.000 186.30503 ? 375 GLN A CD  1 
ATOM   2330 O OE1 . GLN A 1 375 ? 20.95949  -7.76464  -7.55365  1.000 186.65005 ? 375 GLN A OE1 1 
ATOM   2331 N NE2 . GLN A 1 375 ? 19.77931  -6.03673  -8.36859  1.000 187.44710 ? 375 GLN A NE2 1 
ATOM   2332 N N   . ILE A 1 376 ? 22.65659  -4.00997  -3.90473  1.000 193.75511 ? 376 ILE A N   1 
ATOM   2333 C CA  . ILE A 1 376 ? 22.75232  -2.56398  -3.73321  1.000 196.37124 ? 376 ILE A CA  1 
ATOM   2334 C C   . ILE A 1 376 ? 24.18345  -2.08413  -3.94771  1.000 201.61616 ? 376 ILE A C   1 
ATOM   2335 O O   . ILE A 1 376 ? 24.40183  -0.97341  -4.44629  1.000 204.74851 ? 376 ILE A O   1 
ATOM   2336 C CB  . ILE A 1 376 ? 22.23964  -2.15203  -2.34229  1.000 192.21413 ? 376 ILE A CB  1 
ATOM   2337 C CG1 . ILE A 1 376 ? 20.97228  -2.92511  -1.96722  1.000 186.17315 ? 376 ILE A CG1 1 
ATOM   2338 C CG2 . ILE A 1 376 ? 21.97853  -0.65209  -2.29712  1.000 194.43802 ? 376 ILE A CG2 1 
ATOM   2339 C CD1 . ILE A 1 376 ? 19.71696  -2.38604  -2.60189  1.000 183.77499 ? 376 ILE A CD1 1 
ATOM   2340 N N   . ASN A 1 377 ? 25.16808  -2.90651  -3.57493  1.000 200.34967 ? 377 ASN A N   1 
ATOM   2341 C CA  . ASN A 1 377 ? 26.58884  -2.56020  -3.64488  1.000 204.21062 ? 377 ASN A CA  1 
ATOM   2342 C C   . ASN A 1 377 ? 26.91174  -1.36799  -2.74333  1.000 205.08879 ? 377 ASN A C   1 
ATOM   2343 O O   . ASN A 1 377 ? 27.48695  -0.36511  -3.17275  1.000 209.26001 ? 377 ASN A O   1 
ATOM   2344 C CB  . ASN A 1 377 ? 27.03564  -2.30322  -5.08725  1.000 208.68419 ? 377 ASN A CB  1 
ATOM   2345 C CG  . ASN A 1 377 ? 28.53602  -2.46094  -5.26622  1.000 212.07227 ? 377 ASN A CG  1 
ATOM   2346 O OD1 . ASN A 1 377 ? 29.23196  -2.94658  -4.37324  1.000 211.16716 ? 377 ASN A OD1 1 
ATOM   2347 N ND2 . ASN A 1 377 ? 29.03911  -2.06011  -6.42754  1.000 215.81939 ? 377 ASN A ND2 1 
ATOM   2348 N N   . ILE A 1 378 ? 26.53333  -1.49216  -1.47338  1.000 209.59366 ? 378 ILE A N   1 
ATOM   2349 C CA  . ILE A 1 378 ? 26.87964  -0.52886  -0.43367  1.000 209.50776 ? 378 ILE A CA  1 
ATOM   2350 C C   . ILE A 1 378 ? 27.31330  -1.31246  0.79597   1.000 206.24760 ? 378 ILE A C   1 
ATOM   2351 O O   . ILE A 1 378 ? 26.62282  -2.24698  1.21573   1.000 202.22103 ? 378 ILE A O   1 
ATOM   2352 C CB  . ILE A 1 378 ? 25.70536  0.40791   -0.08835  1.000 207.44019 ? 378 ILE A CB  1 
ATOM   2353 C CG1 . ILE A 1 378 ? 25.34701  1.28933   -1.28441  1.000 211.45033 ? 378 ILE A CG1 1 
ATOM   2354 C CG2 . ILE A 1 378 ? 26.04608  1.26877   1.11945   1.000 206.29940 ? 378 ILE A CG2 1 
ATOM   2355 C CD1 . ILE A 1 378 ? 24.06970  2.06262   -1.09010  1.000 209.51787 ? 378 ILE A CD1 1 
ATOM   2356 N N   . GLY A 1 379 ? 28.45365  -0.93816  1.36962   1.000 210.75438 ? 379 GLY A N   1 
ATOM   2357 C CA  . GLY A 1 379 ? 29.00059  -1.65738  2.50271   1.000 208.45316 ? 379 GLY A CA  1 
ATOM   2358 C C   . GLY A 1 379 ? 28.18569  -1.54675  3.77478   1.000 204.27127 ? 379 GLY A C   1 
ATOM   2359 O O   . GLY A 1 379 ? 27.74725  -2.56136  4.32559   1.000 201.15880 ? 379 GLY A O   1 
ATOM   2360 N N   . ASP A 1 380 ? 27.97194  -0.32057  4.25071   1.000 205.85554 ? 380 ASP A N   1 
ATOM   2361 C CA  . ASP A 1 380 ? 27.32432  -0.08938  5.54266   1.000 202.22744 ? 380 ASP A CA  1 
ATOM   2362 C C   . ASP A 1 380 ? 25.81423  -0.01941  5.35125   1.000 198.77377 ? 380 ASP A C   1 
ATOM   2363 O O   . ASP A 1 380 ? 25.22685  1.05461   5.19761   1.000 198.68543 ? 380 ASP A O   1 
ATOM   2364 C CB  . ASP A 1 380 ? 27.86901  1.17302   6.19883   1.000 204.12836 ? 380 ASP A CB  1 
ATOM   2365 C CG  . ASP A 1 380 ? 29.21358  0.94669   6.86420   1.000 204.28572 ? 380 ASP A CG  1 
ATOM   2366 O OD1 . ASP A 1 380 ? 29.62233  -0.22753  6.98408   1.000 202.14674 ? 380 ASP A OD1 1 
ATOM   2367 O OD2 . ASP A 1 380 ? 29.85866  1.93879   7.26651   1.000 206.97177 ? 380 ASP A OD2 1 
ATOM   2368 N N   . ILE A 1 381 ? 25.18165  -1.18898  5.36898   1.000 201.17006 ? 381 ILE A N   1 
ATOM   2369 C CA  . ILE A 1 381 ? 23.72976  -1.31743  5.38778   1.000 190.23963 ? 381 ILE A CA  1 
ATOM   2370 C C   . ILE A 1 381 ? 23.35491  -2.04596  6.66957   1.000 189.01004 ? 381 ILE A C   1 
ATOM   2371 O O   . ILE A 1 381 ? 23.70723  -3.21889  6.84612   1.000 192.91390 ? 381 ILE A O   1 
ATOM   2372 C CB  . ILE A 1 381 ? 23.19838  -2.07313  4.15988   1.000 186.30557 ? 381 ILE A CB  1 
ATOM   2373 C CG1 . ILE A 1 381 ? 23.64313  -1.38804  2.86896   1.000 190.76519 ? 381 ILE A CG1 1 
ATOM   2374 C CG2 . ILE A 1 381 ? 21.67957  -2.17089  4.21381   1.000 181.92826 ? 381 ILE A CG2 1 
ATOM   2375 C CD1 . ILE A 1 381 ? 23.31505  -2.17387  1.61868   1.000 197.62676 ? 381 ILE A CD1 1 
ATOM   2376 N N   . GLU A 1 382 ? 22.65467  -1.35552  7.56393   1.000 195.03323 ? 382 GLU A N   1 
ATOM   2377 C CA  . GLU A 1 382 ? 22.24661  -1.95979  8.82289   1.000 190.87391 ? 382 GLU A CA  1 
ATOM   2378 C C   . GLU A 1 382 ? 20.98544  -2.79574  8.63640   1.000 183.55282 ? 382 GLU A C   1 
ATOM   2379 O O   . GLU A 1 382 ? 20.15056  -2.51671  7.77187   1.000 180.82557 ? 382 GLU A O   1 
ATOM   2380 C CB  . GLU A 1 382 ? 22.01286  -0.88627  9.88627   1.000 197.07561 ? 382 GLU A CB  1 
ATOM   2381 C CG  . GLU A 1 382 ? 23.28820  -0.27912  10.45369  1.000 203.22206 ? 382 GLU A CG  1 
ATOM   2382 C CD  . GLU A 1 382 ? 23.81220  0.88724   9.63621   1.000 206.30382 ? 382 GLU A CD  1 
ATOM   2383 O OE1 . GLU A 1 382 ? 23.33468  1.08904   8.50002   1.000 206.35338 ? 382 GLU A OE1 1 
ATOM   2384 O OE2 . GLU A 1 382 ? 24.70167  1.60819   10.13683  1.000 209.15485 ? 382 GLU A OE2 1 
ATOM   2385 N N   . TYR A 1 383 ? 20.85758  -3.83520  9.45994   1.000 187.29781 ? 383 TYR A N   1 
ATOM   2386 C CA  . TYR A 1 383 ? 19.73546  -4.76343  9.39822   1.000 184.40808 ? 383 TYR A CA  1 
ATOM   2387 C C   . TYR A 1 383 ? 19.11460  -4.89518  10.77967  1.000 187.52538 ? 383 TYR A C   1 
ATOM   2388 O O   . TYR A 1 383 ? 19.83320  -5.04946  11.77235  1.000 193.11152 ? 383 TYR A O   1 
ATOM   2389 C CB  . TYR A 1 383 ? 20.18001  -6.13960  8.89269   1.000 182.58957 ? 383 TYR A CB  1 
ATOM   2390 C CG  . TYR A 1 383 ? 20.51179  -6.18647  7.41918   1.000 182.71397 ? 383 TYR A CG  1 
ATOM   2391 C CD1 . TYR A 1 383 ? 21.77536  -5.84007  6.95851   1.000 184.46300 ? 383 TYR A CD1 1 
ATOM   2392 C CD2 . TYR A 1 383 ? 19.56238  -6.58708  6.48871   1.000 180.70209 ? 383 TYR A CD2 1 
ATOM   2393 C CE1 . TYR A 1 383 ? 22.08163  -5.88690  5.61094   1.000 188.37498 ? 383 TYR A CE1 1 
ATOM   2394 C CE2 . TYR A 1 383 ? 19.85941  -6.63736  5.14066   1.000 183.97399 ? 383 TYR A CE2 1 
ATOM   2395 C CZ  . TYR A 1 383 ? 21.12003  -6.28652  4.70797   1.000 185.68397 ? 383 TYR A CZ  1 
ATOM   2396 O OH  . TYR A 1 383 ? 21.42187  -6.33480  3.36750   1.000 190.09745 ? 383 TYR A OH  1 
ATOM   2397 N N   . TYR A 1 384 ? 17.78467  -4.84228  10.84124  1.000 183.57581 ? 384 TYR A N   1 
ATOM   2398 C CA  . TYR A 1 384 ? 17.06597  -4.96027  12.10124  1.000 184.48163 ? 384 TYR A CA  1 
ATOM   2399 C C   . TYR A 1 384 ? 15.82076  -5.81302  11.90164  1.000 180.67963 ? 384 TYR A C   1 
ATOM   2400 O O   . TYR A 1 384 ? 15.23486  -5.84263  10.81676  1.000 180.29305 ? 384 TYR A O   1 
ATOM   2401 C CB  . TYR A 1 384 ? 16.67851  -3.58547  12.66364  1.000 183.61936 ? 384 TYR A CB  1 
ATOM   2402 C CG  . TYR A 1 384 ? 17.81959  -2.59381  12.68959  1.000 182.75611 ? 384 TYR A CG  1 
ATOM   2403 C CD1 . TYR A 1 384 ? 18.84809  -2.71382  13.61433  1.000 186.54272 ? 384 TYR A CD1 1 
ATOM   2404 C CD2 . TYR A 1 384 ? 17.86789  -1.53697  11.78966  1.000 183.24396 ? 384 TYR A CD2 1 
ATOM   2405 C CE1 . TYR A 1 384 ? 19.89490  -1.81164  13.64045  1.000 191.15068 ? 384 TYR A CE1 1 
ATOM   2406 C CE2 . TYR A 1 384 ? 18.91044  -0.62800  11.80929  1.000 190.01223 ? 384 TYR A CE2 1 
ATOM   2407 C CZ  . TYR A 1 384 ? 19.92060  -0.77060  12.73738  1.000 194.98707 ? 384 TYR A CZ  1 
ATOM   2408 O OH  . TYR A 1 384 ? 20.96162  0.12867   12.76488  1.000 199.47453 ? 384 TYR A OH  1 
ATOM   2409 N N   . GLU A 1 385 ? 15.42065  -6.50516  12.96614  1.000 178.22513 ? 385 GLU A N   1 
ATOM   2410 C CA  . GLU A 1 385 ? 14.27417  -7.39991  12.92881  1.000 177.11227 ? 385 GLU A CA  1 
ATOM   2411 C C   . GLU A 1 385 ? 13.50152  -7.27990  14.23406  1.000 176.65944 ? 385 GLU A C   1 
ATOM   2412 O O   . GLU A 1 385 ? 14.04967  -6.89733  15.27017  1.000 177.40075 ? 385 GLU A O   1 
ATOM   2413 C CB  . GLU A 1 385 ? 14.70727  -8.85406  12.69275  1.000 182.33360 ? 385 GLU A CB  1 
ATOM   2414 C CG  . GLU A 1 385 ? 15.81750  -9.32129  13.62022  1.000 196.66835 ? 385 GLU A CG  1 
ATOM   2415 C CD  . GLU A 1 385 ? 16.26579  -10.73978 13.32695  1.000 201.64174 ? 385 GLU A CD  1 
ATOM   2416 O OE1 . GLU A 1 385 ? 15.51373  -11.47922 12.65598  1.000 203.24928 ? 385 GLU A OE1 1 
ATOM   2417 O OE2 . GLU A 1 385 ? 17.37286  -11.11453 13.76672  1.000 202.59963 ? 385 GLU A OE2 1 
ATOM   2418 N N   . ASP A 1 386 ? 12.21459  -7.61694  14.17404  1.000 182.49206 ? 386 ASP A N   1 
ATOM   2419 C CA  . ASP A 1 386 ? 11.33896  -7.49764  15.33188  1.000 184.31484 ? 386 ASP A CA  1 
ATOM   2420 C C   . ASP A 1 386 ? 10.17097  -8.45552  15.15840  1.000 192.57545 ? 386 ASP A C   1 
ATOM   2421 O O   . ASP A 1 386 ? 9.86475   -8.89671  14.04652  1.000 198.99589 ? 386 ASP A O   1 
ATOM   2422 C CB  . ASP A 1 386 ? 10.85305  -6.05107  15.51321  1.000 198.72634 ? 386 ASP A CB  1 
ATOM   2423 C CG  . ASP A 1 386 ? 10.06308  -5.85050  16.79450  1.000 202.09519 ? 386 ASP A CG  1 
ATOM   2424 O OD1 . ASP A 1 386 ? 8.92361   -6.35327  16.88138  1.000 202.51188 ? 386 ASP A OD1 1 
ATOM   2425 O OD2 . ASP A 1 386 ? 10.58910  -5.19670  17.71934  1.000 204.33038 ? 386 ASP A OD2 1 
ATOM   2426 N N   . ALA A 1 387 ? 9.52593   -8.77802  16.27965  1.000 195.14909 ? 387 ALA A N   1 
ATOM   2427 C CA  . ALA A 1 387 ? 8.39034   -9.70102  16.29356  1.000 199.43866 ? 387 ALA A CA  1 
ATOM   2428 C C   . ALA A 1 387 ? 7.36341   -9.19741  17.30002  1.000 200.54478 ? 387 ALA A C   1 
ATOM   2429 O O   . ALA A 1 387 ? 7.56888   -9.31295  18.51300  1.000 204.59960 ? 387 ALA A O   1 
ATOM   2430 C CB  . ALA A 1 387 ? 8.84052   -11.12232 16.63525  1.000 204.08443 ? 387 ALA A CB  1 
ATOM   2431 N N   . GLU A 1 388 ? 6.26023   -8.63951  16.80073  1.000 204.14167 ? 388 GLU A N   1 
ATOM   2432 C CA  . GLU A 1 388 ? 5.15417   -8.20461  17.65407  1.000 204.60385 ? 388 GLU A CA  1 
ATOM   2433 C C   . GLU A 1 388 ? 4.25241   -9.40647  17.92599  1.000 208.52392 ? 388 GLU A C   1 
ATOM   2434 O O   . GLU A 1 388 ? 3.20645   -9.60218  17.30121  1.000 206.65154 ? 388 GLU A O   1 
ATOM   2435 C CB  . GLU A 1 388 ? 4.38300   -7.06036  17.00645  1.000 199.43982 ? 388 GLU A CB  1 
ATOM   2436 C CG  . GLU A 1 388 ? 5.13370   -5.73989  16.96045  1.000 196.00720 ? 388 GLU A CG  1 
ATOM   2437 C CD  . GLU A 1 388 ? 4.23068   -4.57489  16.60084  1.000 192.32462 ? 388 GLU A CD  1 
ATOM   2438 O OE1 . GLU A 1 388 ? 3.04455   -4.81556  16.29236  1.000 191.94381 ? 388 GLU A OE1 1 
ATOM   2439 O OE2 . GLU A 1 388 ? 4.70393   -3.41919  16.63201  1.000 190.35967 ? 388 GLU A OE2 1 
ATOM   2440 N N   . GLY A 1 389 ? 4.66988   -10.22234 18.89124  1.000 198.48213 ? 389 GLY A N   1 
ATOM   2441 C CA  . GLY A 1 389 ? 3.95191   -11.44017 19.21152  1.000 202.29710 ? 389 GLY A CA  1 
ATOM   2442 C C   . GLY A 1 389 ? 4.07394   -12.47320 18.11150  1.000 202.46901 ? 389 GLY A C   1 
ATOM   2443 O O   . GLY A 1 389 ? 5.04973   -13.22868 18.06652  1.000 204.81268 ? 389 GLY A O   1 
ATOM   2444 N N   . ASP A 1 390 ? 3.08639   -12.51385 17.21266  1.000 194.46734 ? 390 ASP A N   1 
ATOM   2445 C CA  . ASP A 1 390 ? 3.14504   -13.37724 16.04240  1.000 194.24625 ? 390 ASP A CA  1 
ATOM   2446 C C   . ASP A 1 390 ? 3.41571   -12.62735 14.74736  1.000 188.97037 ? 390 ASP A C   1 
ATOM   2447 O O   . ASP A 1 390 ? 3.80746   -13.25978 13.76176  1.000 188.41673 ? 390 ASP A O   1 
ATOM   2448 C CB  . ASP A 1 390 ? 1.84294   -14.17807 15.89186  1.000 196.54618 ? 390 ASP A CB  1 
ATOM   2449 C CG  . ASP A 1 390 ? 1.63742   -15.16863 17.01821  1.000 203.20849 ? 390 ASP A CG  1 
ATOM   2450 O OD1 . ASP A 1 390 ? 2.22354   -14.96662 18.10108  1.000 205.89180 ? 390 ASP A OD1 1 
ATOM   2451 O OD2 . ASP A 1 390 ? 0.89646   -16.15272 16.81964  1.000 206.32012 ? 390 ASP A OD2 1 
ATOM   2452 N N   . ASP A 1 391 ? 3.21793   -11.31013 14.72337  1.000 196.44392 ? 391 ASP A N   1 
ATOM   2453 C CA  . ASP A 1 391 ? 3.64726   -10.50774 13.58640  1.000 192.78152 ? 391 ASP A CA  1 
ATOM   2454 C C   . ASP A 1 391 ? 5.15854   -10.61622 13.40892  1.000 190.90846 ? 391 ASP A C   1 
ATOM   2455 O O   . ASP A 1 391 ? 5.90433   -10.83896 14.36690  1.000 194.87844 ? 391 ASP A O   1 
ATOM   2456 C CB  . ASP A 1 391 ? 3.24419   -9.04352  13.78185  1.000 190.17553 ? 391 ASP A CB  1 
ATOM   2457 C CG  . ASP A 1 391 ? 1.75310   -8.81579  13.60534  1.000 190.28321 ? 391 ASP A CG  1 
ATOM   2458 O OD1 . ASP A 1 391 ? 1.06425   -9.74146  13.13005  1.000 192.59163 ? 391 ASP A OD1 1 
ATOM   2459 O OD2 . ASP A 1 391 ? 1.26990   -7.71343  13.94300  1.000 187.84953 ? 391 ASP A OD2 1 
ATOM   2460 N N   . LYS A 1 392 ? 5.61077   -10.45923 12.16589  1.000 187.45101 ? 392 LYS A N   1 
ATOM   2461 C CA  . LYS A 1 392 ? 7.02209   -10.58200 11.82061  1.000 180.63007 ? 392 LYS A CA  1 
ATOM   2462 C C   . LYS A 1 392 ? 7.48120   -9.30185  11.14048  1.000 169.17694 ? 392 LYS A C   1 
ATOM   2463 O O   . LYS A 1 392 ? 6.96717   -8.94171  10.07635  1.000 167.97534 ? 392 LYS A O   1 
ATOM   2464 C CB  . LYS A 1 392 ? 7.26568   -11.79121 10.91689  1.000 185.21314 ? 392 LYS A CB  1 
ATOM   2465 C CG  . LYS A 1 392 ? 6.78593   -13.10042 11.51367  1.000 191.86660 ? 392 LYS A CG  1 
ATOM   2466 C CD  . LYS A 1 392 ? 7.22023   -14.28230 10.67234  1.000 194.38007 ? 392 LYS A CD  1 
ATOM   2467 C CE  . LYS A 1 392 ? 6.56107   -15.56458 11.14616  1.000 200.19841 ? 392 LYS A CE  1 
ATOM   2468 N NZ  . LYS A 1 392 ? 5.07574   -15.46478 11.10123  1.000 200.59736 ? 392 LYS A NZ  1 
ATOM   2469 N N   . ILE A 1 393 ? 8.44756   -8.62325  11.75314  1.000 183.75514 ? 393 ILE A N   1 
ATOM   2470 C CA  . ILE A 1 393 ? 8.99457   -7.37246  11.24306  1.000 178.61857 ? 393 ILE A CA  1 
ATOM   2471 C C   . ILE A 1 393 ? 10.41875  -7.62738  10.77160  1.000 175.47156 ? 393 ILE A C   1 
ATOM   2472 O O   . ILE A 1 393 ? 11.23454  -8.19084  11.51142  1.000 177.05364 ? 393 ILE A O   1 
ATOM   2473 C CB  . ILE A 1 393 ? 8.95725   -6.26518  12.31073  1.000 180.93845 ? 393 ILE A CB  1 
ATOM   2474 C CG1 . ILE A 1 393 ? 7.53068   -6.07359  12.82580  1.000 194.39837 ? 393 ILE A CG1 1 
ATOM   2475 C CG2 . ILE A 1 393 ? 9.50080   -4.95994  11.74827  1.000 177.15600 ? 393 ILE A CG2 1 
ATOM   2476 C CD1 . ILE A 1 393 ? 7.41756   -5.07900  13.95273  1.000 197.64543 ? 393 ILE A CD1 1 
ATOM   2477 N N   . LYS A 1 394 ? 10.71214  -7.21846  9.53924   1.000 164.30868 ? 394 LYS A N   1 
ATOM   2478 C CA  . LYS A 1 394 ? 12.04193  -7.33726  8.95448   1.000 165.04349 ? 394 LYS A CA  1 
ATOM   2479 C C   . LYS A 1 394 ? 12.32288  -6.07021  8.16513   1.000 165.17607 ? 394 LYS A C   1 
ATOM   2480 O O   . LYS A 1 394 ? 11.52760  -5.69661  7.29868   1.000 165.27929 ? 394 LYS A O   1 
ATOM   2481 C CB  . LYS A 1 394 ? 12.14282  -8.56491  8.04073   1.000 165.91255 ? 394 LYS A CB  1 
ATOM   2482 C CG  . LYS A 1 394 ? 12.04321  -9.90276  8.75595   1.000 169.28112 ? 394 LYS A CG  1 
ATOM   2483 C CD  . LYS A 1 394 ? 13.35974  -10.28206 9.40892   1.000 174.78824 ? 394 LYS A CD  1 
ATOM   2484 C CE  . LYS A 1 394 ? 13.34066  -11.72943 9.86814   1.000 185.90439 ? 394 LYS A CE  1 
ATOM   2485 N NZ  . LYS A 1 394 ? 14.68919  -12.19544 10.28908  1.000 193.38619 ? 394 LYS A NZ  1 
ATOM   2486 N N   . LEU A 1 395 ? 13.44288  -5.41100  8.45803   1.000 170.20465 ? 395 LEU A N   1 
ATOM   2487 C CA  . LEU A 1 395 ? 13.73639  -4.12743  7.83448   1.000 170.01336 ? 395 LEU A CA  1 
ATOM   2488 C C   . LEU A 1 395 ? 15.24097  -3.89708  7.79051   1.000 172.82111 ? 395 LEU A C   1 
ATOM   2489 O O   . LEU A 1 395 ? 16.02160  -4.59619  8.44122   1.000 176.73986 ? 395 LEU A O   1 
ATOM   2490 C CB  . LEU A 1 395 ? 13.02811  -2.98255  8.57111   1.000 169.58480 ? 395 LEU A CB  1 
ATOM   2491 C CG  . LEU A 1 395 ? 13.17045  -2.89821  10.09199  1.000 172.37562 ? 395 LEU A CG  1 
ATOM   2492 C CD1 . LEU A 1 395 ? 14.34098  -2.01260  10.47536  1.000 177.88899 ? 395 LEU A CD1 1 
ATOM   2493 C CD2 . LEU A 1 395 ? 11.88413  -2.38780  10.71863  1.000 171.72170 ? 395 LEU A CD2 1 
ATOM   2494 N N   . PHE A 1 396 ? 15.63731  -2.89580  7.00483   1.000 166.02694 ? 396 PHE A N   1 
ATOM   2495 C CA  . PHE A 1 396 ? 17.02885  -2.48494  6.88995   1.000 166.65095 ? 396 PHE A CA  1 
ATOM   2496 C C   . PHE A 1 396 ? 17.08487  -0.96865  6.76020   1.000 169.60925 ? 396 PHE A C   1 
ATOM   2497 O O   . PHE A 1 396 ? 16.07141  -0.30352  6.52737   1.000 168.88944 ? 396 PHE A O   1 
ATOM   2498 C CB  . PHE A 1 396 ? 17.72567  -3.15820  5.69810   1.000 167.66889 ? 396 PHE A CB  1 
ATOM   2499 C CG  . PHE A 1 396 ? 17.33729  -2.58799  4.36193   1.000 169.99362 ? 396 PHE A CG  1 
ATOM   2500 C CD1 . PHE A 1 396 ? 16.21050  -3.04493  3.70132   1.000 168.64596 ? 396 PHE A CD1 1 
ATOM   2501 C CD2 . PHE A 1 396 ? 18.10729  -1.60328  3.76104   1.000 171.37675 ? 396 PHE A CD2 1 
ATOM   2502 C CE1 . PHE A 1 396 ? 15.85327  -2.52705  2.47170   1.000 170.24642 ? 396 PHE A CE1 1 
ATOM   2503 C CE2 . PHE A 1 396 ? 17.75301  -1.07852  2.53309   1.000 174.33416 ? 396 PHE A CE2 1 
ATOM   2504 C CZ  . PHE A 1 396 ? 16.62460  -1.54175  1.88717   1.000 173.84673 ? 396 PHE A CZ  1 
ATOM   2505 N N   . GLY A 1 397 ? 18.28912  -0.42300  6.90315   1.000 170.36551 ? 397 GLY A N   1 
ATOM   2506 C CA  . GLY A 1 397 ? 18.47244  1.01420   6.84813   1.000 169.38692 ? 397 GLY A CA  1 
ATOM   2507 C C   . GLY A 1 397 ? 19.53127  1.45023   5.85450   1.000 175.16875 ? 397 GLY A C   1 
ATOM   2508 O O   . GLY A 1 397 ? 20.72094  1.20086   6.05906   1.000 180.34471 ? 397 GLY A O   1 
ATOM   2509 N N   . ILE A 1 398 ? 19.11526  2.10533   4.77368   1.000 172.98750 ? 398 ILE A N   1 
ATOM   2510 C CA  . ILE A 1 398 ? 20.02772  2.59515   3.74412   1.000 181.70679 ? 398 ILE A CA  1 
ATOM   2511 C C   . ILE A 1 398 ? 20.38878  4.04167   4.04685   1.000 190.49435 ? 398 ILE A C   1 
ATOM   2512 O O   . ILE A 1 398 ? 19.50390  4.89443   4.19375   1.000 190.20531 ? 398 ILE A O   1 
ATOM   2513 C CB  . ILE A 1 398 ? 19.40850  2.45863   2.34204   1.000 184.38068 ? 398 ILE A CB  1 
ATOM   2514 C CG1 . ILE A 1 398 ? 20.17040  3.31206   1.32552   1.000 199.62056 ? 398 ILE A CG1 1 
ATOM   2515 C CG2 . ILE A 1 398 ? 17.91752  2.80383   2.35110   1.000 183.75398 ? 398 ILE A CG2 1 
ATOM   2516 C CD1 . ILE A 1 398 ? 19.60767  3.24251   -0.08046  1.000 202.69265 ? 398 ILE A CD1 1 
ATOM   2517 N N   . VAL A 1 399 ? 21.68775  4.31864   4.15382   1.000 195.84154 ? 399 VAL A N   1 
ATOM   2518 C CA  . VAL A 1 399 ? 22.16616  5.67627   4.41050   1.000 200.95900 ? 399 VAL A CA  1 
ATOM   2519 C C   . VAL A 1 399 ? 23.27969  6.04541   3.43353   1.000 207.27004 ? 399 VAL A C   1 
ATOM   2520 O O   . VAL A 1 399 ? 24.40921  5.55869   3.55538   1.000 208.82026 ? 399 VAL A O   1 
ATOM   2521 C CB  . VAL A 1 399 ? 22.64369  5.82063   5.86692   1.000 198.63406 ? 399 VAL A CB  1 
ATOM   2522 C CG1 . VAL A 1 399 ? 23.23060  7.20131   6.10941   1.000 202.37196 ? 399 VAL A CG1 1 
ATOM   2523 C CG2 . VAL A 1 399 ? 21.49185  5.55777   6.83304   1.000 193.52115 ? 399 VAL A CG2 1 
ATOM   2524 N N   . GLY A 1 400 ? 22.97848  6.90046   2.46188   1.000 201.09683 ? 400 GLY A N   1 
ATOM   2525 C CA  . GLY A 1 400 ? 23.98420  7.38947   1.54243   1.000 206.87988 ? 400 GLY A CA  1 
ATOM   2526 C C   . GLY A 1 400 ? 23.53387  7.28743   0.09870   1.000 209.68422 ? 400 GLY A C   1 
ATOM   2527 O O   . GLY A 1 400 ? 22.37323  6.98837   -0.20295  1.000 207.07350 ? 400 GLY A O   1 
ATOM   2528 N N   . SER A 1 401 ? 24.47226  7.55211   -0.81031  1.000 210.77085 ? 401 SER A N   1 
ATOM   2529 C CA  . SER A 1 401 ? 24.22191  7.44318   -2.24044  1.000 213.98678 ? 401 SER A CA  1 
ATOM   2530 C C   . SER A 1 401 ? 24.06188  5.97674   -2.64841  1.000 212.17259 ? 401 SER A C   1 
ATOM   2531 O O   . SER A 1 401 ? 24.30450  5.05746   -1.86341  1.000 210.11889 ? 401 SER A O   1 
ATOM   2532 C CB  . SER A 1 401 ? 25.35751  8.09229   -3.03267  1.000 219.97290 ? 401 SER A CB  1 
ATOM   2533 O OG  . SER A 1 401 ? 25.23408  7.81681   -4.41697  1.000 224.02620 ? 401 SER A OG  1 
ATOM   2534 N N   . ILE A 1 402 ? 23.64993  5.76008   -3.89832  1.000 210.66965 ? 402 ILE A N   1 
ATOM   2535 C CA  . ILE A 1 402 ? 23.38779  4.41098   -4.40863  1.000 208.52297 ? 402 ILE A CA  1 
ATOM   2536 C C   . ILE A 1 402 ? 23.84299  4.30761   -5.86332  1.000 212.48601 ? 402 ILE A C   1 
ATOM   2537 O O   . ILE A 1 402 ? 23.53510  5.18560   -6.68350  1.000 215.12301 ? 402 ILE A O   1 
ATOM   2538 C CB  . ILE A 1 402 ? 21.90749  4.02102   -4.23231  1.000 203.25565 ? 402 ILE A CB  1 
ATOM   2539 C CG1 . ILE A 1 402 ? 21.65180  2.61149   -4.77713  1.000 201.99916 ? 402 ILE A CG1 1 
ATOM   2540 C CG2 . ILE A 1 402 ? 20.96448  5.04847   -4.86255  1.000 203.51340 ? 402 ILE A CG2 1 
ATOM   2541 C CD1 . ILE A 1 402 ? 20.34299  2.01720   -4.32203  1.000 196.52695 ? 402 ILE A CD1 1 
ATOM   2542 N N   . PRO A 1 403 ? 24.59459  3.26586   -6.22511  1.000 210.31685 ? 403 PRO A N   1 
ATOM   2543 C CA  . PRO A 1 403 ? 25.28486  3.27966   -7.52083  1.000 213.60314 ? 403 PRO A CA  1 
ATOM   2544 C C   . PRO A 1 403 ? 24.43998  2.80141   -8.69081  1.000 211.99428 ? 403 PRO A C   1 
ATOM   2545 O O   . PRO A 1 403 ? 24.63134  3.27622   -9.81304  1.000 214.78902 ? 403 PRO A O   1 
ATOM   2546 C CB  . PRO A 1 403 ? 26.48278  2.35750   -7.27342  1.000 213.77825 ? 403 PRO A CB  1 
ATOM   2547 C CG  . PRO A 1 403 ? 25.97586  1.37806   -6.27490  1.000 209.35645 ? 403 PRO A CG  1 
ATOM   2548 C CD  . PRO A 1 403 ? 25.08748  2.18405   -5.35235  1.000 207.64214 ? 403 PRO A CD  1 
ATOM   2549 N N   . LYS A 1 404 ? 23.49420  1.89271   -8.45992  1.000 202.36475 ? 404 LYS A N   1 
ATOM   2550 C CA  . LYS A 1 404 ? 22.70360  1.34407   -9.54953  1.000 200.65999 ? 404 LYS A CA  1 
ATOM   2551 C C   . LYS A 1 404 ? 21.23213  1.28860   -9.16500  1.000 196.63776 ? 404 LYS A C   1 
ATOM   2552 O O   . LYS A 1 404 ? 20.89227  1.04221   -8.00352  1.000 194.26625 ? 404 LYS A O   1 
ATOM   2553 C CB  . LYS A 1 404 ? 23.20537  -0.05290  -9.93499  1.000 199.74861 ? 404 LYS A CB  1 
ATOM   2554 C CG  . LYS A 1 404 ? 23.07120  -1.09592  -8.83093  1.000 200.58835 ? 404 LYS A CG  1 
ATOM   2555 C CD  . LYS A 1 404 ? 23.51896  -2.48147  -9.29280  1.000 199.54164 ? 404 LYS A CD  1 
ATOM   2556 C CE  . LYS A 1 404 ? 25.00861  -2.52541  -9.60361  1.000 202.57324 ? 404 LYS A CE  1 
ATOM   2557 N NZ  . LYS A 1 404 ? 25.45655  -3.88907  -10.00654 1.000 201.26125 ? 404 LYS A NZ  1 
ATOM   2558 N N   . THR A 1 405 ? 20.36311  1.51597   -10.14953 1.000 194.43826 ? 405 THR A N   1 
ATOM   2559 C CA  . THR A 1 405 ? 18.91985  1.42550   -9.93811  1.000 190.27648 ? 405 THR A CA  1 
ATOM   2560 C C   . THR A 1 405 ? 18.57016  -0.03032  -9.65956  1.000 186.28383 ? 405 THR A C   1 
ATOM   2561 O O   . THR A 1 405 ? 18.44420  -0.84538  -10.57653 1.000 186.13190 ? 405 THR A O   1 
ATOM   2562 C CB  . THR A 1 405 ? 18.15862  1.96599   -11.14473 1.000 191.14218 ? 405 THR A CB  1 
ATOM   2563 O OG1 . THR A 1 405 ? 18.44993  3.35963   -11.31305 1.000 194.68983 ? 405 THR A OG1 1 
ATOM   2564 C CG2 . THR A 1 405 ? 16.65290  1.79533   -10.95844 1.000 186.16222 ? 405 THR A CG2 1 
ATOM   2565 N N   . THR A 1 406 ? 18.42467  -0.36169  -8.38060  1.000 192.94562 ? 406 THR A N   1 
ATOM   2566 C CA  . THR A 1 406 ? 18.20671  -1.72820  -7.93143  1.000 189.46029 ? 406 THR A CA  1 
ATOM   2567 C C   . THR A 1 406 ? 16.72616  -1.96366  -7.65040  1.000 184.77490 ? 406 THR A C   1 
ATOM   2568 O O   . THR A 1 406 ? 16.02482  -1.07320  -7.16165  1.000 183.08450 ? 406 THR A O   1 
ATOM   2569 C CB  . THR A 1 406 ? 19.04883  -2.01422  -6.67938  1.000 189.06828 ? 406 THR A CB  1 
ATOM   2570 O OG1 . THR A 1 406 ? 20.38163  -2.37994  -7.06484  1.000 193.12501 ? 406 THR A OG1 1 
ATOM   2571 C CG2 . THR A 1 406 ? 18.44001  -3.11813  -5.83605  1.000 184.82400 ? 406 THR A CG2 1 
ATOM   2572 N N   . SER A 1 407 ? 16.24910  -3.16199  -7.98524  1.000 185.21287 ? 407 SER A N   1 
ATOM   2573 C CA  . SER A 1 407 ? 14.87817  -3.55964  -7.69948  1.000 180.75434 ? 407 SER A CA  1 
ATOM   2574 C C   . SER A 1 407 ? 14.88004  -4.97264  -7.13824  1.000 177.36402 ? 407 SER A C   1 
ATOM   2575 O O   . SER A 1 407 ? 15.49886  -5.86826  -7.71962  1.000 178.55350 ? 407 SER A O   1 
ATOM   2576 C CB  . SER A 1 407 ? 14.01223  -3.49019  -8.96215  1.000 179.99599 ? 407 SER A CB  1 
ATOM   2577 O OG  . SER A 1 407 ? 14.19860  -2.26037  -9.64275  1.000 183.10555 ? 407 SER A OG  1 
ATOM   2578 N N   . PHE A 1 408 ? 14.19409  -5.17131  -6.01278  1.000 177.06434 ? 408 PHE A N   1 
ATOM   2579 C CA  . PHE A 1 408 ? 14.08461  -6.49084  -5.40492  1.000 174.04859 ? 408 PHE A CA  1 
ATOM   2580 C C   . PHE A 1 408 ? 12.68821  -6.67343  -4.82526  1.000 170.57087 ? 408 PHE A C   1 
ATOM   2581 O O   . PHE A 1 408 ? 11.93889  -5.71160  -4.63855  1.000 168.57355 ? 408 PHE A O   1 
ATOM   2582 C CB  . PHE A 1 408 ? 15.15802  -6.72119  -4.32781  1.000 173.99394 ? 408 PHE A CB  1 
ATOM   2583 C CG  . PHE A 1 408 ? 15.29068  -5.59977  -3.33403  1.000 172.89828 ? 408 PHE A CG  1 
ATOM   2584 C CD1 . PHE A 1 408 ? 16.10338  -4.51096  -3.60331  1.000 176.28810 ? 408 PHE A CD1 1 
ATOM   2585 C CD2 . PHE A 1 408 ? 14.62568  -5.64726  -2.12004  1.000 164.68182 ? 408 PHE A CD2 1 
ATOM   2586 C CE1 . PHE A 1 408 ? 16.23644  -3.48213  -2.68996  1.000 169.26339 ? 408 PHE A CE1 1 
ATOM   2587 C CE2 . PHE A 1 408 ? 14.75722  -4.62270  -1.20022  1.000 164.69255 ? 408 PHE A CE2 1 
ATOM   2588 C CZ  . PHE A 1 408 ? 15.56377  -3.53895  -1.48618  1.000 166.15010 ? 408 PHE A CZ  1 
ATOM   2589 N N   . THR A 1 409 ? 12.34618  -7.93095  -4.54102  1.000 161.40697 ? 409 THR A N   1 
ATOM   2590 C CA  . THR A 1 409 ? 10.97958  -8.30908  -4.19230  1.000 160.49841 ? 409 THR A CA  1 
ATOM   2591 C C   . THR A 1 409 ? 10.99745  -9.36551  -3.09600  1.000 159.24903 ? 409 THR A C   1 
ATOM   2592 O O   . THR A 1 409 ? 11.63552  -10.41026 -3.25263  1.000 160.24293 ? 409 THR A O   1 
ATOM   2593 C CB  . THR A 1 409 ? 10.23326  -8.83083  -5.42786  1.000 162.41554 ? 409 THR A CB  1 
ATOM   2594 O OG1 . THR A 1 409 ? 10.17750  -7.80198  -6.42466  1.000 163.80990 ? 409 THR A OG1 1 
ATOM   2595 C CG2 . THR A 1 409 ? 8.81829   -9.26618  -5.07156  1.000 161.54146 ? 409 THR A CG2 1 
ATOM   2596 N N   . CYS A 1 410 ? 10.29830  -9.09683  -1.99440  1.000 160.24298 ? 410 CYS A N   1 
ATOM   2597 C CA  . CYS A 1 410 ? 10.10243  -10.05511 -0.91315  1.000 157.28532 ? 410 CYS A CA  1 
ATOM   2598 C C   . CYS A 1 410 ? 8.64185   -10.50061 -0.88823  1.000 160.70554 ? 410 CYS A C   1 
ATOM   2599 O O   . CYS A 1 410 ? 7.76850   -9.87786  -1.49801  1.000 161.19888 ? 410 CYS A O   1 
ATOM   2600 C CB  . CYS A 1 410 ? 10.51944  -9.45494  0.43945   1.000 156.82811 ? 410 CYS A CB  1 
ATOM   2601 S SG  . CYS A 1 410 ? 10.87190  -10.69029 1.73111   1.000 168.47936 ? 410 CYS A SG  1 
ATOM   2602 N N   . ILE A 1 411 ? 8.37696   -11.59490 -0.17283  1.000 169.99875 ? 411 ILE A N   1 
ATOM   2603 C CA  . ILE A 1 411 ? 7.08476   -12.27243 -0.22206  1.000 170.30038 ? 411 ILE A CA  1 
ATOM   2604 C C   . ILE A 1 411 ? 6.56136   -12.50084 1.19062   1.000 170.53450 ? 411 ILE A C   1 
ATOM   2605 O O   . ILE A 1 411 ? 7.31677   -12.87911 2.09297   1.000 169.77034 ? 411 ILE A O   1 
ATOM   2606 C CB  . ILE A 1 411 ? 7.18674   -13.60838 -0.99412  1.000 172.66759 ? 411 ILE A CB  1 
ATOM   2607 C CG1 . ILE A 1 411 ? 7.10711   -13.36001 -2.50132  1.000 171.22241 ? 411 ILE A CG1 1 
ATOM   2608 C CG2 . ILE A 1 411 ? 6.12153   -14.60555 -0.54528  1.000 170.75472 ? 411 ILE A CG2 1 
ATOM   2609 C CD1 . ILE A 1 411 ? 7.21277   -14.61678 -3.32931  1.000 171.93766 ? 411 ILE A CD1 1 
ATOM   2610 N N   . CYS A 1 412 ? 5.26166   -12.26755 1.37546   1.000 181.20840 ? 412 CYS A N   1 
ATOM   2611 C CA  . CYS A 1 412 ? 4.55305   -12.55361 2.61745   1.000 179.59436 ? 412 CYS A CA  1 
ATOM   2612 C C   . CYS A 1 412 ? 3.48690   -13.59975 2.32424   1.000 186.34578 ? 412 CYS A C   1 
ATOM   2613 O O   . CYS A 1 412 ? 2.62031   -13.38158 1.47055   1.000 186.03973 ? 412 CYS A O   1 
ATOM   2614 C CB  . CYS A 1 412 ? 3.92569   -11.28136 3.19230   1.000 181.27281 ? 412 CYS A CB  1 
ATOM   2615 S SG  . CYS A 1 412 ? 2.94060   -11.50733 4.69269   1.000 184.64837 ? 412 CYS A SG  1 
ATOM   2616 N N   . LYS A 1 413 ? 3.54926   -14.73174 3.02503   1.000 173.68140 ? 413 LYS A N   1 
ATOM   2617 C CA  . LYS A 1 413 ? 2.67022   -15.86761 2.75737   1.000 174.58803 ? 413 LYS A CA  1 
ATOM   2618 C C   . LYS A 1 413 ? 1.90967   -16.24652 4.02224   1.000 177.51998 ? 413 LYS A C   1 
ATOM   2619 O O   . LYS A 1 413 ? 2.50399   -16.74214 4.98631   1.000 180.38134 ? 413 LYS A O   1 
ATOM   2620 C CB  . LYS A 1 413 ? 3.46298   -17.06433 2.23395   1.000 176.48980 ? 413 LYS A CB  1 
ATOM   2621 C CG  . LYS A 1 413 ? 2.60850   -18.30048 2.02141   1.000 177.68613 ? 413 LYS A CG  1 
ATOM   2622 C CD  . LYS A 1 413 ? 3.45116   -19.54704 1.84574   1.000 181.69446 ? 413 LYS A CD  1 
ATOM   2623 C CE  . LYS A 1 413 ? 2.58159   -20.78639 1.90706   1.000 185.19234 ? 413 LYS A CE  1 
ATOM   2624 N NZ  . LYS A 1 413 ? 1.88561   -20.90279 3.21885   1.000 187.64490 ? 413 LYS A NZ  1 
ATOM   2625 N N   . LYS A 1 414 ? 0.59480   -16.03082 4.00628   1.000 186.91163 ? 414 LYS A N   1 
ATOM   2626 C CA  . LYS A 1 414 ? -0.31094  -16.48076 5.05992   1.000 191.50777 ? 414 LYS A CA  1 
ATOM   2627 C C   . LYS A 1 414 ? -1.23582  -17.53380 4.46075   1.000 193.99098 ? 414 LYS A C   1 
ATOM   2628 O O   . LYS A 1 414 ? -2.14023  -17.20137 3.68630   1.000 192.63044 ? 414 LYS A O   1 
ATOM   2629 C CB  . LYS A 1 414 ? -1.10546  -15.30997 5.63773   1.000 190.34984 ? 414 LYS A CB  1 
ATOM   2630 C CG  . LYS A 1 414 ? -2.20935  -15.71839 6.60337   1.000 193.54644 ? 414 LYS A CG  1 
ATOM   2631 C CD  . LYS A 1 414 ? -1.64460  -16.23559 7.91431   1.000 196.47710 ? 414 LYS A CD  1 
ATOM   2632 C CE  . LYS A 1 414 ? -0.93965  -15.13209 8.68485   1.000 194.33745 ? 414 LYS A CE  1 
ATOM   2633 N NZ  . LYS A 1 414 ? -1.86362  -14.01599 9.02838   1.000 191.63692 ? 414 LYS A NZ  1 
ATOM   2634 N N   . ASP A 1 415 ? -1.00311  -18.79255 4.81640   1.000 197.71470 ? 415 ASP A N   1 
ATOM   2635 C CA  . ASP A 1 415 ? -1.75352  -19.94462 4.28381   1.000 200.44673 ? 415 ASP A CA  1 
ATOM   2636 C C   . ASP A 1 415 ? -1.58772  -19.93159 2.75917   1.000 198.26772 ? 415 ASP A C   1 
ATOM   2637 O O   . ASP A 1 415 ? -0.47585  -19.68701 2.26653   1.000 195.98963 ? 415 ASP A O   1 
ATOM   2638 C CB  . ASP A 1 415 ? -3.18216  -19.90310 4.79090   1.000 202.88663 ? 415 ASP A CB  1 
ATOM   2639 C CG  . ASP A 1 415 ? -3.27278  -20.10356 6.29400   1.000 205.41331 ? 415 ASP A CG  1 
ATOM   2640 O OD1 . ASP A 1 415 ? -2.87772  -19.18480 7.04200   1.000 203.65591 ? 415 ASP A OD1 1 
ATOM   2641 O OD2 . ASP A 1 415 ? -3.72105  -21.18595 6.72824   1.000 209.48982 ? 415 ASP A OD2 1 
ATOM   2642 N N   . LYS A 1 416 ? -2.65205  -20.18094 1.99125   1.000 205.69130 ? 416 LYS A N   1 
ATOM   2643 C CA  . LYS A 1 416 ? -2.56741  -20.17378 0.53410   1.000 203.82136 ? 416 LYS A CA  1 
ATOM   2644 C C   . LYS A 1 416 ? -2.45499  -18.77013 -0.05155  1.000 199.88237 ? 416 LYS A C   1 
ATOM   2645 O O   . LYS A 1 416 ? -2.06287  -18.63147 -1.21457  1.000 197.25303 ? 416 LYS A O   1 
ATOM   2646 C CB  . LYS A 1 416 ? -3.78697  -20.88068 -0.06423  1.000 205.92170 ? 416 LYS A CB  1 
ATOM   2647 C CG  . LYS A 1 416 ? -3.77698  -22.39645 0.08685   1.000 208.82389 ? 416 LYS A CG  1 
ATOM   2648 C CD  . LYS A 1 416 ? -4.94834  -23.02087 -0.65778  1.000 211.34602 ? 416 LYS A CD  1 
ATOM   2649 C CE  . LYS A 1 416 ? -4.82699  -24.53453 -0.75080  1.000 214.37699 ? 416 LYS A CE  1 
ATOM   2650 N NZ  . LYS A 1 416 ? -5.59679  -25.24658 0.30242   1.000 218.27337 ? 416 LYS A NZ  1 
ATOM   2651 N N   . LYS A 1 417 ? -2.78202  -17.73476 0.71801   1.000 199.05540 ? 417 LYS A N   1 
ATOM   2652 C CA  . LYS A 1 417 ? -2.74518  -16.36980 0.21656   1.000 193.08192 ? 417 LYS A CA  1 
ATOM   2653 C C   . LYS A 1 417 ? -1.30546  -15.86585 0.12258   1.000 189.97941 ? 417 LYS A C   1 
ATOM   2654 O O   . LYS A 1 417 ? -0.38621  -16.40560 0.74471   1.000 191.75911 ? 417 LYS A O   1 
ATOM   2655 C CB  . LYS A 1 417 ? -3.58075  -15.45849 1.11427   1.000 192.91350 ? 417 LYS A CB  1 
ATOM   2656 C CG  . LYS A 1 417 ? -4.97128  -16.01463 1.38081   1.000 197.98671 ? 417 LYS A CG  1 
ATOM   2657 C CD  . LYS A 1 417 ? -5.79918  -15.12828 2.29320   1.000 198.90575 ? 417 LYS A CD  1 
ATOM   2658 C CE  . LYS A 1 417 ? -7.13078  -15.79191 2.61417   1.000 202.64095 ? 417 LYS A CE  1 
ATOM   2659 N NZ  . LYS A 1 417 ? -8.18890  -14.79841 2.94616   1.000 201.65197 ? 417 LYS A NZ  1 
ATOM   2660 N N   . SER A 1 418 ? -1.11787  -14.81266 -0.67249  1.000 190.66998 ? 418 SER A N   1 
ATOM   2661 C CA  . SER A 1 418 ? 0.20982   -14.29070 -0.96622  1.000 188.86145 ? 418 SER A CA  1 
ATOM   2662 C C   . SER A 1 418 ? 0.16623   -12.77037 -1.03296  1.000 186.75241 ? 418 SER A C   1 
ATOM   2663 O O   . SER A 1 418 ? -0.89106  -12.16504 -1.22447  1.000 186.71018 ? 418 SER A O   1 
ATOM   2664 C CB  . SER A 1 418 ? 0.75625   -14.85919 -2.28367  1.000 188.38398 ? 418 SER A CB  1 
ATOM   2665 O OG  . SER A 1 418 ? 1.91282   -14.15647 -2.70443  1.000 186.94424 ? 418 SER A OG  1 
ATOM   2666 N N   . ALA A 1 419 ? 1.33956   -12.15743 -0.87782  1.000 177.35301 ? 419 ALA A N   1 
ATOM   2667 C CA  . ALA A 1 419 ? 1.46053   -10.70163 -0.91957  1.000 176.06735 ? 419 ALA A CA  1 
ATOM   2668 C C   . ALA A 1 419 ? 2.86703   -10.35327 -1.38525  1.000 175.55033 ? 419 ALA A C   1 
ATOM   2669 O O   . ALA A 1 419 ? 3.84186   -10.64033 -0.68396  1.000 175.63452 ? 419 ALA A O   1 
ATOM   2670 C CB  . ALA A 1 419 ? 1.16547   -10.08421 0.44456   1.000 175.97315 ? 419 ALA A CB  1 
ATOM   2671 N N   . TYR A 1 420 ? 2.96855   -9.73614  -2.55843  1.000 178.84915 ? 420 TYR A N   1 
ATOM   2672 C CA  . TYR A 1 420 ? 4.24872   -9.33225  -3.11970  1.000 178.38198 ? 420 TYR A CA  1 
ATOM   2673 C C   . TYR A 1 420 ? 4.57966   -7.89853  -2.71998  1.000 173.56320 ? 420 TYR A C   1 
ATOM   2674 O O   . TYR A 1 420 ? 3.68998   -7.07026  -2.50831  1.000 174.08131 ? 420 TYR A O   1 
ATOM   2675 C CB  . TYR A 1 420 ? 4.22966   -9.45357  -4.64499  1.000 179.13291 ? 420 TYR A CB  1 
ATOM   2676 C CG  . TYR A 1 420 ? 3.96931   -10.85439 -5.15352  1.000 179.70788 ? 420 TYR A CG  1 
ATOM   2677 C CD1 . TYR A 1 420 ? 4.65767   -11.94311 -4.63524  1.000 180.14227 ? 420 TYR A CD1 1 
ATOM   2678 C CD2 . TYR A 1 420 ? 3.02918   -11.08802 -6.14825  1.000 179.88594 ? 420 TYR A CD2 1 
ATOM   2679 C CE1 . TYR A 1 420 ? 4.42095   -13.22532 -5.09830  1.000 180.95033 ? 420 TYR A CE1 1 
ATOM   2680 C CE2 . TYR A 1 420 ? 2.78610   -12.36505 -6.61651  1.000 180.33407 ? 420 TYR A CE2 1 
ATOM   2681 C CZ  . TYR A 1 420 ? 3.48304   -13.42988 -6.08842  1.000 181.18109 ? 420 TYR A CZ  1 
ATOM   2682 O OH  . TYR A 1 420 ? 3.24007   -14.70217 -6.55412  1.000 182.48101 ? 420 TYR A OH  1 
ATOM   2683 N N   . MET A 1 421 ? 5.87710   -7.61228  -2.61950  1.000 165.00224 ? 421 MET A N   1 
ATOM   2684 C CA  . MET A 1 421 ? 6.36016   -6.27619  -2.29154  1.000 166.35355 ? 421 MET A CA  1 
ATOM   2685 C C   . MET A 1 421 ? 7.59847   -5.97158  -3.11826  1.000 169.07693 ? 421 MET A C   1 
ATOM   2686 O O   . MET A 1 421 ? 8.53166   -6.77611  -3.14917  1.000 170.90687 ? 421 MET A O   1 
ATOM   2687 C CB  . MET A 1 421 ? 6.68484   -6.14500  -0.79945  1.000 162.56717 ? 421 MET A CB  1 
ATOM   2688 C CG  . MET A 1 421 ? 7.61927   -4.98651  -0.49377  1.000 163.43199 ? 421 MET A CG  1 
ATOM   2689 S SD  . MET A 1 421 ? 7.51955   -4.38154  1.19861   1.000 164.90381 ? 421 MET A SD  1 
ATOM   2690 C CE  . MET A 1 421 ? 8.52760   -2.90576  1.07325   1.000 165.96971 ? 421 MET A CE  1 
ATOM   2691 N N   . THR A 1 422 ? 7.61784   -4.80653  -3.76587  1.000 160.28484 ? 422 THR A N   1 
ATOM   2692 C CA  . THR A 1 422 ? 8.68927   -4.43428  -4.68664  1.000 164.71806 ? 422 THR A CA  1 
ATOM   2693 C C   . THR A 1 422 ? 9.31148   -3.11421  -4.24647  1.000 166.64969 ? 422 THR A C   1 
ATOM   2694 O O   . THR A 1 422 ? 8.67336   -2.06021  -4.33630  1.000 167.04799 ? 422 THR A O   1 
ATOM   2695 C CB  . THR A 1 422 ? 8.16242   -4.32926  -6.11748  1.000 166.60254 ? 422 THR A CB  1 
ATOM   2696 O OG1 . THR A 1 422 ? 7.60180   -5.58664  -6.51662  1.000 166.68440 ? 422 THR A OG1 1 
ATOM   2697 C CG2 . THR A 1 422 ? 9.28473   -3.95273  -7.07217  1.000 171.23702 ? 422 THR A CG2 1 
ATOM   2698 N N   . VAL A 1 423 ? 10.55615  -3.16958  -3.78522  1.000 163.94340 ? 423 VAL A N   1 
ATOM   2699 C CA  . VAL A 1 423 ? 11.33143  -1.96979  -3.49636  1.000 166.56898 ? 423 VAL A CA  1 
ATOM   2700 C C   . VAL A 1 423 ? 12.09184  -1.57880  -4.75612  1.000 170.59877 ? 423 VAL A C   1 
ATOM   2701 O O   . VAL A 1 423 ? 12.69463  -2.43187  -5.41934  1.000 172.25763 ? 423 VAL A O   1 
ATOM   2702 C CB  . VAL A 1 423 ? 12.29076  -2.20023  -2.31627  1.000 162.21078 ? 423 VAL A CB  1 
ATOM   2703 C CG1 . VAL A 1 423 ? 13.11059  -0.94835  -2.04231  1.000 160.30504 ? 423 VAL A CG1 1 
ATOM   2704 C CG2 . VAL A 1 423 ? 11.51671  -2.60869  -1.07657  1.000 158.20043 ? 423 VAL A CG2 1 
ATOM   2705 N N   . THR A 1 424 ? 12.05992  -0.28911  -5.09288  1.000 167.91294 ? 424 THR A N   1 
ATOM   2706 C CA  . THR A 1 424 ? 12.69649  0.23454   -6.30236  1.000 170.33172 ? 424 THR A CA  1 
ATOM   2707 C C   . THR A 1 424 ? 13.49306  1.47645   -5.91421  1.000 170.44744 ? 424 THR A C   1 
ATOM   2708 O O   . THR A 1 424 ? 12.96254  2.58854   -5.90972  1.000 171.13272 ? 424 THR A O   1 
ATOM   2709 C CB  . THR A 1 424 ? 11.65868  0.54713   -7.37945  1.000 172.34579 ? 424 THR A CB  1 
ATOM   2710 O OG1 . THR A 1 424 ? 10.77337  -0.57009  -7.52999  1.000 171.95616 ? 424 THR A OG1 1 
ATOM   2711 C CG2 . THR A 1 424 ? 12.34104  0.82625   -8.71068  1.000 175.14317 ? 424 THR A CG2 1 
ATOM   2712 N N   . ILE A 1 425 ? 14.76706  1.28359   -5.59230  1.000 177.65131 ? 425 ILE A N   1 
ATOM   2713 C CA  . ILE A 1 425 ? 15.64442  2.37574   -5.19031  1.000 181.89109 ? 425 ILE A CA  1 
ATOM   2714 C C   . ILE A 1 425 ? 16.34420  2.91569   -6.43021  1.000 187.30722 ? 425 ILE A C   1 
ATOM   2715 O O   . ILE A 1 425 ? 17.13736  2.21250   -7.06520  1.000 189.08115 ? 425 ILE A O   1 
ATOM   2716 C CB  . ILE A 1 425 ? 16.66164  1.91562   -4.14015  1.000 181.19608 ? 425 ILE A CB  1 
ATOM   2717 C CG1 . ILE A 1 425 ? 16.06352  0.81873   -3.25840  1.000 174.68600 ? 425 ILE A CG1 1 
ATOM   2718 C CG2 . ILE A 1 425 ? 17.09444  3.09123   -3.27706  1.000 183.17207 ? 425 ILE A CG2 1 
ATOM   2719 C CD1 . ILE A 1 425 ? 16.99382  0.32047   -2.18000  1.000 167.59962 ? 425 ILE A CD1 1 
ATOM   2720 N N   . ASP A 1 426 ? 16.04992  4.16633   -6.77434  1.000 186.03436 ? 426 ASP A N   1 
ATOM   2721 C CA  . ASP A 1 426 ? 16.58164  4.80020   -7.96763  1.000 192.06035 ? 426 ASP A CA  1 
ATOM   2722 C C   . ASP A 1 426 ? 17.96032  5.39721   -7.70076  1.000 197.73329 ? 426 ASP A C   1 
ATOM   2723 O O   . ASP A 1 426 ? 18.32822  5.70232   -6.56445  1.000 197.54403 ? 426 ASP A O   1 
ATOM   2724 C CB  . ASP A 1 426 ? 15.62023  5.88170   -8.45936  1.000 193.20867 ? 426 ASP A CB  1 
ATOM   2725 C CG  . ASP A 1 426 ? 14.24225  5.33179   -8.77515  1.000 188.21125 ? 426 ASP A CG  1 
ATOM   2726 O OD1 . ASP A 1 426 ? 14.14909  4.42231   -9.62567  1.000 186.47707 ? 426 ASP A OD1 1 
ATOM   2727 O OD2 . ASP A 1 426 ? 13.25367  5.79233   -8.16578  1.000 185.68514 ? 426 ASP A OD2 1 
ATOM   2728 N N   . SER A 1 427 ? 18.72580  5.56478   -8.77803  1.000 206.20179 ? 427 SER A N   1 
ATOM   2729 C CA  . SER A 1 427 ? 20.08307  6.09664   -8.71454  1.000 210.76072 ? 427 SER A CA  1 
ATOM   2730 C C   . SER A 1 427 ? 20.16420  7.34719   -9.57791  1.000 216.00620 ? 427 SER A C   1 
ATOM   2731 O O   . SER A 1 427 ? 19.94173  7.28290   -10.79204 1.000 216.64206 ? 427 SER A O   1 
ATOM   2732 C CB  . SER A 1 427 ? 21.10159  5.05184   -9.17537  1.000 212.16602 ? 427 SER A CB  1 
ATOM   2733 O OG  . SER A 1 427 ? 20.71924  4.48164   -10.41518 1.000 210.01074 ? 427 SER A OG  1 
ATOM   2734 N N   . ALA A 1 428 ? 20.48174  8.47672   -8.95341  1.000 209.04400 ? 428 ALA A N   1 
ATOM   2735 C CA  . ALA A 1 428 ? 20.58430  9.74492   -9.66523  1.000 214.41294 ? 428 ALA A CA  1 
ATOM   2736 C C   . ALA A 1 428 ? 21.69445  10.60957  -9.07742  1.000 214.24992 ? 428 ALA A C   1 
ATOM   2737 O O   . ALA A 1 428 ? 21.49641  11.79520  -8.81210  1.000 214.84811 ? 428 ALA A O   1 
ATOM   2738 C CB  . ALA A 1 428 ? 19.25532  10.48449  -9.62487  1.000 218.07658 ? 428 ALA A CB  1 
ATOM   2739 N N   . VAL B 2 2   ? 20.77299  -33.76975 -5.91064  1.000 182.91254 ? 2   VAL B N   1 
ATOM   2740 C CA  . VAL B 2 2   ? 20.33927  -33.58925 -4.53153  1.000 181.57696 ? 2   VAL B CA  1 
ATOM   2741 C C   . VAL B 2 2   ? 20.57899  -34.86843 -3.73692  1.000 182.36970 ? 2   VAL B C   1 
ATOM   2742 O O   . VAL B 2 2   ? 20.31653  -35.96909 -4.22210  1.000 185.33283 ? 2   VAL B O   1 
ATOM   2743 C CB  . VAL B 2 2   ? 18.85927  -33.17033 -4.46489  1.000 177.45496 ? 2   VAL B CB  1 
ATOM   2744 C CG1 . VAL B 2 2   ? 18.46684  -32.81558 -3.03718  1.000 173.39010 ? 2   VAL B CG1 1 
ATOM   2745 C CG2 . VAL B 2 2   ? 18.59723  -32.00233 -5.40353  1.000 181.05020 ? 2   VAL B CG2 1 
ATOM   2746 N N   . GLN B 2 3   ? 21.08402  -34.71687 -2.51450  1.000 183.63503 ? 3   GLN B N   1 
ATOM   2747 C CA  . GLN B 2 3   ? 21.35482  -35.85694 -1.65144  1.000 184.27085 ? 3   GLN B CA  1 
ATOM   2748 C C   . GLN B 2 3   ? 21.46233  -35.36873 -0.21439  1.000 171.69721 ? 3   GLN B C   1 
ATOM   2749 O O   . GLN B 2 3   ? 22.02061  -34.29899 0.04199   1.000 169.07343 ? 3   GLN B O   1 
ATOM   2750 C CB  . GLN B 2 3   ? 22.63788  -36.58378 -2.07389  1.000 185.12432 ? 3   GLN B CB  1 
ATOM   2751 C CG  . GLN B 2 3   ? 22.97299  -37.80135 -1.23030  1.000 186.60248 ? 3   GLN B CG  1 
ATOM   2752 C CD  . GLN B 2 3   ? 23.97635  -38.71757 -1.90175  1.000 188.71155 ? 3   GLN B CD  1 
ATOM   2753 O OE1 . GLN B 2 3   ? 23.89671  -39.93943 -1.77606  1.000 190.71900 ? 3   GLN B OE1 1 
ATOM   2754 N NE2 . GLN B 2 3   ? 24.92719  -38.13181 -2.62087  1.000 187.62631 ? 3   GLN B NE2 1 
ATOM   2755 N N   . LEU B 2 4   ? 20.92218  -36.15740 0.71338   1.000 185.64745 ? 4   LEU B N   1 
ATOM   2756 C CA  . LEU B 2 4   ? 20.91409  -35.82120 2.13369   1.000 181.28105 ? 4   LEU B CA  1 
ATOM   2757 C C   . LEU B 2 4   ? 21.54820  -36.97002 2.90677   1.000 182.91803 ? 4   LEU B C   1 
ATOM   2758 O O   . LEU B 2 4   ? 20.95517  -38.04633 3.02779   1.000 185.54004 ? 4   LEU B O   1 
ATOM   2759 C CB  . LEU B 2 4   ? 19.49264  -35.54521 2.62256   1.000 174.97166 ? 4   LEU B CB  1 
ATOM   2760 C CG  . LEU B 2 4   ? 18.80683  -34.34530 1.96731   1.000 173.68691 ? 4   LEU B CG  1 
ATOM   2761 C CD1 . LEU B 2 4   ? 17.34616  -34.26156 2.37879   1.000 169.75255 ? 4   LEU B CD1 1 
ATOM   2762 C CD2 . LEU B 2 4   ? 19.53820  -33.06033 2.32157   1.000 172.73017 ? 4   LEU B CD2 1 
ATOM   2763 N N   . VAL B 2 5   ? 22.74935  -36.73971 3.42869   1.000 181.04039 ? 5   VAL B N   1 
ATOM   2764 C CA  . VAL B 2 5   ? 23.52018  -37.75238 4.14501   1.000 184.39937 ? 5   VAL B CA  1 
ATOM   2765 C C   . VAL B 2 5   ? 23.26468  -37.59577 5.63649   1.000 180.72155 ? 5   VAL B C   1 
ATOM   2766 O O   . VAL B 2 5   ? 23.62798  -36.57554 6.23168   1.000 180.85178 ? 5   VAL B O   1 
ATOM   2767 C CB  . VAL B 2 5   ? 25.01817  -37.63577 3.83554   1.000 187.95913 ? 5   VAL B CB  1 
ATOM   2768 C CG1 . VAL B 2 5   ? 25.81874  -38.61447 4.68542   1.000 197.07326 ? 5   VAL B CG1 1 
ATOM   2769 C CG2 . VAL B 2 5   ? 25.27685  -37.87648 2.35449   1.000 194.62776 ? 5   VAL B CG2 1 
ATOM   2770 N N   . GLU B 2 6   ? 22.64859  -38.60644 6.24439   1.000 191.55710 ? 6   GLU B N   1 
ATOM   2771 C CA  . GLU B 2 6   ? 22.31943  -38.58561 7.66092   1.000 190.09097 ? 6   GLU B CA  1 
ATOM   2772 C C   . GLU B 2 6   ? 23.38877  -39.31052 8.46992   1.000 193.78014 ? 6   GLU B C   1 
ATOM   2773 O O   . GLU B 2 6   ? 23.98485  -40.28881 8.01308   1.000 195.88025 ? 6   GLU B O   1 
ATOM   2774 C CB  . GLU B 2 6   ? 20.95031  -39.22457 7.90752   1.000 187.56420 ? 6   GLU B CB  1 
ATOM   2775 C CG  . GLU B 2 6   ? 19.84695  -38.65917 7.02509   1.000 185.10359 ? 6   GLU B CG  1 
ATOM   2776 C CD  . GLU B 2 6   ? 18.54103  -38.47065 7.77165   1.000 179.99477 ? 6   GLU B CD  1 
ATOM   2777 O OE1 . GLU B 2 6   ? 18.57468  -38.36913 9.01625   1.000 178.19625 ? 6   GLU B OE1 1 
ATOM   2778 O OE2 . GLU B 2 6   ? 17.47993  -38.42958 7.11402   1.000 177.46723 ? 6   GLU B OE2 1 
ATOM   2779 N N   . SER B 2 7   ? 23.62564  -38.81863 9.68553   1.000 186.04654 ? 7   SER B N   1 
ATOM   2780 C CA  . SER B 2 7   ? 24.68353  -39.34113 10.53903  1.000 193.30379 ? 7   SER B CA  1 
ATOM   2781 C C   . SER B 2 7   ? 24.21340  -39.35685 11.98590  1.000 190.00690 ? 7   SER B C   1 
ATOM   2782 O O   . SER B 2 7   ? 23.22305  -38.71730 12.34637  1.000 183.75261 ? 7   SER B O   1 
ATOM   2783 C CB  . SER B 2 7   ? 25.96814  -38.51124 10.41033  1.000 202.77852 ? 7   SER B CB  1 
ATOM   2784 O OG  . SER B 2 7   ? 26.94002  -38.92828 11.35229  1.000 205.69798 ? 7   SER B OG  1 
ATOM   2785 N N   . GLY B 2 8   ? 24.94348  -40.09570 12.81356  1.000 200.60227 ? 8   GLY B N   1 
ATOM   2786 C CA  . GLY B 2 8   ? 24.62895  -40.18876 14.22410  1.000 197.82078 ? 8   GLY B CA  1 
ATOM   2787 C C   . GLY B 2 8   ? 23.78043  -41.40166 14.55193  1.000 193.41841 ? 8   GLY B C   1 
ATOM   2788 O O   . GLY B 2 8   ? 23.72551  -42.38735 13.81077  1.000 193.11556 ? 8   GLY B O   1 
ATOM   2789 N N   . GLY B 2 9   ? 23.11299  -41.32227 15.70148  1.000 200.63717 ? 9   GLY B N   1 
ATOM   2790 C CA  . GLY B 2 9   ? 22.17775  -42.35364 16.10713  1.000 200.89735 ? 9   GLY B CA  1 
ATOM   2791 C C   . GLY B 2 9   ? 22.80236  -43.52403 16.83939  1.000 207.19625 ? 9   GLY B C   1 
ATOM   2792 O O   . GLY B 2 9   ? 23.92261  -43.93872 16.52659  1.000 210.78011 ? 9   GLY B O   1 
ATOM   2793 N N   . GLY B 2 10  ? 22.08023  -44.06715 17.81429  1.000 207.35370 ? 10  GLY B N   1 
ATOM   2794 C CA  . GLY B 2 10  ? 22.57493  -45.20842 18.56130  1.000 213.57431 ? 10  GLY B CA  1 
ATOM   2795 C C   . GLY B 2 10  ? 21.72379  -45.45084 19.79207  1.000 211.50031 ? 10  GLY B C   1 
ATOM   2796 O O   . GLY B 2 10  ? 20.56402  -45.03847 19.85143  1.000 204.77651 ? 10  GLY B O   1 
ATOM   2797 N N   . LEU B 2 11  ? 22.32042  -46.12944 20.76891  1.000 206.91964 ? 11  LEU B N   1 
ATOM   2798 C CA  . LEU B 2 11  ? 21.66673  -46.38623 22.04481  1.000 206.61148 ? 11  LEU B CA  1 
ATOM   2799 C C   . LEU B 2 11  ? 21.98246  -45.25402 23.01214  1.000 205.37581 ? 11  LEU B C   1 
ATOM   2800 O O   . LEU B 2 11  ? 23.14684  -44.87574 23.17662  1.000 207.77395 ? 11  LEU B O   1 
ATOM   2801 C CB  . LEU B 2 11  ? 22.11672  -47.72790 22.62947  1.000 211.24421 ? 11  LEU B CB  1 
ATOM   2802 C CG  . LEU B 2 11  ? 21.49820  -48.19279 23.95502  1.000 211.21773 ? 11  LEU B CG  1 
ATOM   2803 C CD1 . LEU B 2 11  ? 21.38669  -49.70776 23.98036  1.000 214.43601 ? 11  LEU B CD1 1 
ATOM   2804 C CD2 . LEU B 2 11  ? 22.30019  -47.71188 25.16190  1.000 212.81810 ? 11  LEU B CD2 1 
ATOM   2805 N N   . LEU B 2 12  ? 20.94445  -44.72148 23.65256  1.000 211.50764 ? 12  LEU B N   1 
ATOM   2806 C CA  . LEU B 2 12  ? 21.10021  -43.66400 24.63827  1.000 210.65674 ? 12  LEU B CA  1 
ATOM   2807 C C   . LEU B 2 12  ? 20.10269  -43.87453 25.76606  1.000 210.15376 ? 12  LEU B C   1 
ATOM   2808 O O   . LEU B 2 12  ? 18.99270  -44.36951 25.55396  1.000 208.57510 ? 12  LEU B O   1 
ATOM   2809 C CB  . LEU B 2 12  ? 20.90521  -42.27398 24.02048  1.000 207.45931 ? 12  LEU B CB  1 
ATOM   2810 C CG  . LEU B 2 12  ? 21.97097  -41.81380 23.02572  1.000 208.43952 ? 12  LEU B CG  1 
ATOM   2811 C CD1 . LEU B 2 12  ? 21.55723  -40.50385 22.39689  1.000 207.06063 ? 12  LEU B CD1 1 
ATOM   2812 C CD2 . LEU B 2 12  ? 23.32709  -41.68065 23.70235  1.000 212.01850 ? 12  LEU B CD2 1 
ATOM   2813 N N   . GLN B 2 13  ? 20.51184  -43.49478 26.96086  1.000 206.19880 ? 13  GLN B N   1 
ATOM   2814 C CA  . GLN B 2 13  ? 19.70860  -43.59871 28.16458  1.000 206.56146 ? 13  GLN B CA  1 
ATOM   2815 C C   . GLN B 2 13  ? 19.14303  -42.23468 28.53872  1.000 204.43997 ? 13  GLN B C   1 
ATOM   2816 O O   . GLN B 2 13  ? 19.65982  -41.20125 28.10416  1.000 203.14809 ? 13  GLN B O   1 
ATOM   2817 C CB  . GLN B 2 13  ? 20.55927  -44.17374 29.30347  1.000 210.25226 ? 13  GLN B CB  1 
ATOM   2818 C CG  . GLN B 2 13  ? 20.98603  -45.61409 29.03968  1.000 212.87839 ? 13  GLN B CG  1 
ATOM   2819 C CD  . GLN B 2 13  ? 21.96949  -46.14602 30.06129  1.000 217.30730 ? 13  GLN B CD  1 
ATOM   2820 O OE1 . GLN B 2 13  ? 22.93056  -45.47021 30.42790  1.000 218.57342 ? 13  GLN B OE1 1 
ATOM   2821 N NE2 . GLN B 2 13  ? 21.73525  -47.36882 30.52442  1.000 220.07802 ? 13  GLN B NE2 1 
ATOM   2822 N N   . PRO B 2 14  ? 18.05741  -42.19314 29.31740  1.000 204.65930 ? 14  PRO B N   1 
ATOM   2823 C CA  . PRO B 2 14  ? 17.37807  -40.91542 29.57548  1.000 203.28926 ? 14  PRO B CA  1 
ATOM   2824 C C   . PRO B 2 14  ? 18.31971  -39.84740 30.11546  1.000 204.20052 ? 14  PRO B C   1 
ATOM   2825 O O   . PRO B 2 14  ? 19.20157  -40.11952 30.93277  1.000 206.76746 ? 14  PRO B O   1 
ATOM   2826 C CB  . PRO B 2 14  ? 16.30772  -41.29078 30.60469  1.000 204.90377 ? 14  PRO B CB  1 
ATOM   2827 C CG  . PRO B 2 14  ? 16.01105  -42.71519 30.31780  1.000 205.55792 ? 14  PRO B CG  1 
ATOM   2828 C CD  . PRO B 2 14  ? 17.31766  -43.32981 29.89726  1.000 206.20641 ? 14  PRO B CD  1 
ATOM   2829 N N   . GLY B 2 15  ? 18.12434  -38.61756 29.63991  1.000 202.92722 ? 15  GLY B N   1 
ATOM   2830 C CA  . GLY B 2 15  ? 18.93592  -37.49310 30.03725  1.000 203.96222 ? 15  GLY B CA  1 
ATOM   2831 C C   . GLY B 2 15  ? 20.12611  -37.21367 29.14479  1.000 203.59220 ? 15  GLY B C   1 
ATOM   2832 O O   . GLY B 2 15  ? 20.63156  -36.08575 29.14812  1.000 203.96765 ? 15  GLY B O   1 
ATOM   2833 N N   . ARG B 2 16  ? 20.58772  -38.19960 28.37902  1.000 199.11646 ? 16  ARG B N   1 
ATOM   2834 C CA  . ARG B 2 16  ? 21.73682  -37.98348 27.51371  1.000 199.76139 ? 16  ARG B CA  1 
ATOM   2835 C C   . ARG B 2 16  ? 21.35930  -37.08332 26.33644  1.000 196.91261 ? 16  ARG B C   1 
ATOM   2836 O O   . ARG B 2 16  ? 20.18623  -36.81027 26.07226  1.000 194.29697 ? 16  ARG B O   1 
ATOM   2837 C CB  . ARG B 2 16  ? 22.29565  -39.31374 27.01061  1.000 201.32685 ? 16  ARG B CB  1 
ATOM   2838 C CG  . ARG B 2 16  ? 22.69186  -40.29300 28.10711  1.000 204.62693 ? 16  ARG B CG  1 
ATOM   2839 C CD  . ARG B 2 16  ? 23.49551  -39.63750 29.22677  1.000 207.41320 ? 16  ARG B CD  1 
ATOM   2840 N NE  . ARG B 2 16  ? 24.68472  -38.94439 28.74504  1.000 208.92437 ? 16  ARG B NE  1 
ATOM   2841 C CZ  . ARG B 2 16  ? 24.91154  -37.64706 28.90281  1.000 208.75559 ? 16  ARG B CZ  1 
ATOM   2842 N NH1 . ARG B 2 16  ? 24.05683  -36.86840 29.54641  1.000 207.26830 ? 16  ARG B NH1 1 
ATOM   2843 N NH2 . ARG B 2 16  ? 26.02828  -37.11906 28.41033  1.000 210.64950 ? 16  ARG B NH2 1 
ATOM   2844 N N   . SER B 2 17  ? 22.38169  -36.62069 25.62211  1.000 209.69275 ? 17  SER B N   1 
ATOM   2845 C CA  . SER B 2 17  ? 22.21046  -35.67414 24.52974  1.000 207.54743 ? 17  SER B CA  1 
ATOM   2846 C C   . SER B 2 17  ? 23.02264  -36.12007 23.32335  1.000 207.02432 ? 17  SER B C   1 
ATOM   2847 O O   . SER B 2 17  ? 24.18385  -36.51881 23.45848  1.000 210.04909 ? 17  SER B O   1 
ATOM   2848 C CB  . SER B 2 17  ? 22.63429  -34.26008 24.95060  1.000 208.89339 ? 17  SER B CB  1 
ATOM   2849 O OG  . SER B 2 17  ? 22.32999  -33.31306 23.94123  1.000 207.50746 ? 17  SER B OG  1 
ATOM   2850 N N   . LEU B 2 18  ? 22.40739  -36.04126 22.14563  1.000 199.38354 ? 18  LEU B N   1 
ATOM   2851 C CA  . LEU B 2 18  ? 23.03769  -36.42704 20.89160  1.000 199.88655 ? 18  LEU B CA  1 
ATOM   2852 C C   . LEU B 2 18  ? 22.75608  -35.36539 19.83860  1.000 196.98513 ? 18  LEU B C   1 
ATOM   2853 O O   . LEU B 2 18  ? 21.72200  -34.69335 19.87342  1.000 194.02214 ? 18  LEU B O   1 
ATOM   2854 C CB  . LEU B 2 18  ? 22.53029  -37.79382 20.40938  1.000 194.99299 ? 18  LEU B CB  1 
ATOM   2855 C CG  . LEU B 2 18  ? 23.11295  -38.38882 19.12496  1.000 190.11946 ? 18  LEU B CG  1 
ATOM   2856 C CD1 . LEU B 2 18  ? 24.61766  -38.57477 19.24382  1.000 190.70069 ? 18  LEU B CD1 1 
ATOM   2857 C CD2 . LEU B 2 18  ? 22.43082  -39.70589 18.78704  1.000 188.55990 ? 18  LEU B CD2 1 
ATOM   2858 N N   . LYS B 2 19  ? 23.69089  -35.21473 18.90472  1.000 192.35294 ? 19  LYS B N   1 
ATOM   2859 C CA  . LYS B 2 19  ? 23.57419  -34.25310 17.81666  1.000 188.63286 ? 19  LYS B CA  1 
ATOM   2860 C C   . LYS B 2 19  ? 23.55949  -35.01129 16.49724  1.000 181.29840 ? 19  LYS B C   1 
ATOM   2861 O O   . LYS B 2 19  ? 24.55124  -35.65502 16.13771  1.000 183.37623 ? 19  LYS B O   1 
ATOM   2862 C CB  . LYS B 2 19  ? 24.72613  -33.24697 17.85110  1.000 194.67076 ? 19  LYS B CB  1 
ATOM   2863 C CG  . LYS B 2 19  ? 24.42281  -31.93347 17.15510  1.000 193.17282 ? 19  LYS B CG  1 
ATOM   2864 C CD  . LYS B 2 19  ? 25.66149  -31.05697 17.06874  1.000 197.38861 ? 19  LYS B CD  1 
ATOM   2865 C CE  . LYS B 2 19  ? 25.32108  -29.66937 16.54992  1.000 197.11997 ? 19  LYS B CE  1 
ATOM   2866 N NZ  . LYS B 2 19  ? 26.54230  -28.87698 16.23534  1.000 201.04261 ? 19  LYS B NZ  1 
ATOM   2867 N N   . LEU B 2 20  ? 22.43953  -34.93602 15.78164  1.000 185.22786 ? 20  LEU B N   1 
ATOM   2868 C CA  . LEU B 2 20  ? 22.29010  -35.61363 14.50039  1.000 183.41879 ? 20  LEU B CA  1 
ATOM   2869 C C   . LEU B 2 20  ? 22.66984  -34.67045 13.36568  1.000 183.39462 ? 20  LEU B C   1 
ATOM   2870 O O   . LEU B 2 20  ? 22.21656  -33.52217 13.32587  1.000 181.41621 ? 20  LEU B O   1 
ATOM   2871 C CB  . LEU B 2 20  ? 20.85668  -36.11356 14.31639  1.000 179.55266 ? 20  LEU B CB  1 
ATOM   2872 C CG  . LEU B 2 20  ? 20.37588  -37.18377 15.29829  1.000 177.82093 ? 20  LEU B CG  1 
ATOM   2873 C CD1 . LEU B 2 20  ? 18.96305  -37.62943 14.95688  1.000 174.68923 ? 20  LEU B CD1 1 
ATOM   2874 C CD2 . LEU B 2 20  ? 21.32766  -38.37009 15.30774  1.000 182.28649 ? 20  LEU B CD2 1 
ATOM   2875 N N   . SER B 2 21  ? 23.49416  -35.16067 12.44400  1.000 179.80794 ? 21  SER B N   1 
ATOM   2876 C CA  . SER B 2 21  ? 23.99195  -34.36911 11.32980  1.000 183.28855 ? 21  SER B CA  1 
ATOM   2877 C C   . SER B 2 21  ? 23.31774  -34.79261 10.03010  1.000 178.37543 ? 21  SER B C   1 
ATOM   2878 O O   . SER B 2 21  ? 22.90189  -35.94392 9.87071   1.000 178.29247 ? 21  SER B O   1 
ATOM   2879 C CB  . SER B 2 21  ? 25.51243  -34.50236 11.19882  1.000 191.03362 ? 21  SER B CB  1 
ATOM   2880 O OG  . SER B 2 21  ? 26.16374  -34.05603 12.37613  1.000 201.65219 ? 21  SER B OG  1 
ATOM   2881 N N   . CYS B 2 22  ? 23.21793  -33.84319 9.09694   1.000 177.69757 ? 22  CYS B N   1 
ATOM   2882 C CA  . CYS B 2 22  ? 22.53728  -34.07513 7.82223   1.000 176.99938 ? 22  CYS B CA  1 
ATOM   2883 C C   . CYS B 2 22  ? 23.27850  -33.27715 6.75118   1.000 183.32644 ? 22  CYS B C   1 
ATOM   2884 O O   . CYS B 2 22  ? 23.03128  -32.07895 6.58696   1.000 182.04326 ? 22  CYS B O   1 
ATOM   2885 C CB  . CYS B 2 22  ? 21.07037  -33.67407 7.90909   1.000 174.51140 ? 22  CYS B CB  1 
ATOM   2886 S SG  . CYS B 2 22  ? 20.13767  -33.75745 6.35723   1.000 177.82190 ? 22  CYS B SG  1 
ATOM   2887 N N   . VAL B 2 23  ? 24.17859  -33.94518 6.02992   1.000 174.96224 ? 23  VAL B N   1 
ATOM   2888 C CA  . VAL B 2 23  ? 24.99073  -33.28903 5.01047   1.000 176.43928 ? 23  VAL B CA  1 
ATOM   2889 C C   . VAL B 2 23  ? 24.16340  -33.09832 3.74646   1.000 173.86502 ? 23  VAL B C   1 
ATOM   2890 O O   . VAL B 2 23  ? 23.42988  -33.99902 3.32115   1.000 174.55098 ? 23  VAL B O   1 
ATOM   2891 C CB  . VAL B 2 23  ? 26.26631  -34.10503 4.72957   1.000 182.20755 ? 23  VAL B CB  1 
ATOM   2892 C CG1 . VAL B 2 23  ? 27.19868  -33.34129 3.79963   1.000 187.70119 ? 23  VAL B CG1 1 
ATOM   2893 C CG2 . VAL B 2 23  ? 26.97304  -34.45812 6.03219   1.000 185.54151 ? 23  VAL B CG2 1 
ATOM   2894 N N   . ALA B 2 24  ? 24.27734  -31.91876 3.14161   1.000 172.66320 ? 24  ALA B N   1 
ATOM   2895 C CA  . ALA B 2 24  ? 23.56017  -31.57858 1.92148   1.000 168.08833 ? 24  ALA B CA  1 
ATOM   2896 C C   . ALA B 2 24  ? 24.42960  -31.83340 0.69435   1.000 175.92481 ? 24  ALA B C   1 
ATOM   2897 O O   . ALA B 2 24  ? 25.64825  -31.99997 0.78683   1.000 185.55269 ? 24  ALA B O   1 
ATOM   2898 C CB  . ALA B 2 24  ? 23.10966  -30.11539 1.95029   1.000 164.63618 ? 24  ALA B CB  1 
ATOM   2899 N N   . SER B 2 25  ? 23.78130  -31.86294 -0.46894  1.000 176.63882 ? 25  SER B N   1 
ATOM   2900 C CA  . SER B 2 25  ? 24.47947  -32.14665 -1.71589  1.000 182.09328 ? 25  SER B CA  1 
ATOM   2901 C C   . SER B 2 25  ? 23.69422  -31.57002 -2.88512  1.000 182.22898 ? 25  SER B C   1 
ATOM   2902 O O   . SER B 2 25  ? 22.46742  -31.69572 -2.93322  1.000 184.00426 ? 25  SER B O   1 
ATOM   2903 C CB  . SER B 2 25  ? 24.66956  -33.65562 -1.91450  1.000 184.42840 ? 25  SER B CB  1 
ATOM   2904 O OG  . SER B 2 25  ? 25.16611  -34.28419 -0.74551  1.000 185.66267 ? 25  SER B OG  1 
ATOM   2905 N N   . GLY B 2 26  ? 24.40866  -30.94989 -3.82221  1.000 185.83342 ? 26  GLY B N   1 
ATOM   2906 C CA  . GLY B 2 26  ? 23.83318  -30.55767 -5.09586  1.000 185.48606 ? 26  GLY B CA  1 
ATOM   2907 C C   . GLY B 2 26  ? 23.21853  -29.17393 -5.14832  1.000 184.38173 ? 26  GLY B C   1 
ATOM   2908 O O   . GLY B 2 26  ? 23.71731  -28.29183 -5.85359  1.000 181.85056 ? 26  GLY B O   1 
ATOM   2909 N N   . PHE B 2 27  ? 22.12884  -28.97492 -4.41270  1.000 195.98920 ? 27  PHE B N   1 
ATOM   2910 C CA  . PHE B 2 27  ? 21.36239  -27.74236 -4.50344  1.000 194.75093 ? 27  PHE B CA  1 
ATOM   2911 C C   . PHE B 2 27  ? 22.08979  -26.59282 -3.80641  1.000 190.91856 ? 27  PHE B C   1 
ATOM   2912 O O   . PHE B 2 27  ? 23.05212  -26.78464 -3.05751  1.000 186.75585 ? 27  PHE B O   1 
ATOM   2913 C CB  . PHE B 2 27  ? 19.97675  -27.93405 -3.88852  1.000 187.60089 ? 27  PHE B CB  1 
ATOM   2914 C CG  . PHE B 2 27  ? 20.00110  -28.18245 -2.40486  1.000 175.72969 ? 27  PHE B CG  1 
ATOM   2915 C CD1 . PHE B 2 27  ? 20.30168  -29.43758 -1.90138  1.000 176.13535 ? 27  PHE B CD1 1 
ATOM   2916 C CD2 . PHE B 2 27  ? 19.72121  -27.16066 -1.51381  1.000 172.88400 ? 27  PHE B CD2 1 
ATOM   2917 C CE1 . PHE B 2 27  ? 20.32668  -29.66578 -0.53827  1.000 174.44548 ? 27  PHE B CE1 1 
ATOM   2918 C CE2 . PHE B 2 27  ? 19.74184  -27.38337 -0.15069  1.000 171.22882 ? 27  PHE B CE2 1 
ATOM   2919 C CZ  . PHE B 2 27  ? 20.04579  -28.63693 0.33769   1.000 171.22555 ? 27  PHE B CZ  1 
ATOM   2920 N N   . THR B 2 28  ? 21.60976  -25.37746 -4.06631  1.000 179.74514 ? 28  THR B N   1 
ATOM   2921 C CA  . THR B 2 28  ? 22.08673  -24.19359 -3.35784  1.000 174.48724 ? 28  THR B CA  1 
ATOM   2922 C C   . THR B 2 28  ? 21.53176  -24.22056 -1.93897  1.000 170.40651 ? 28  THR B C   1 
ATOM   2923 O O   . THR B 2 28  ? 20.32167  -24.08068 -1.73707  1.000 172.38572 ? 28  THR B O   1 
ATOM   2924 C CB  . THR B 2 28  ? 21.65768  -22.92602 -4.09141  1.000 181.24690 ? 28  THR B CB  1 
ATOM   2925 O OG1 . THR B 2 28  ? 21.95871  -23.05407 -5.48675  1.000 184.40453 ? 28  THR B OG1 1 
ATOM   2926 C CG2 . THR B 2 28  ? 22.38990  -21.71355 -3.53417  1.000 179.84647 ? 28  THR B CG2 1 
ATOM   2927 N N   . PHE B 2 29  ? 22.41436  -24.39565 -0.95234  1.000 173.67906 ? 29  PHE B N   1 
ATOM   2928 C CA  . PHE B 2 29  ? 21.95943  -24.70141 0.40147   1.000 170.81606 ? 29  PHE B CA  1 
ATOM   2929 C C   . PHE B 2 29  ? 21.20224  -23.53592 1.02843   1.000 170.66420 ? 29  PHE B C   1 
ATOM   2930 O O   . PHE B 2 29  ? 20.15112  -23.73791 1.64724   1.000 167.09376 ? 29  PHE B O   1 
ATOM   2931 C CB  . PHE B 2 29  ? 23.14503  -25.10207 1.27622   1.000 172.37490 ? 29  PHE B CB  1 
ATOM   2932 C CG  . PHE B 2 29  ? 22.74946  -25.60014 2.63427   1.000 173.69611 ? 29  PHE B CG  1 
ATOM   2933 C CD1 . PHE B 2 29  ? 21.67688  -26.46387 2.78005   1.000 173.25158 ? 29  PHE B CD1 1 
ATOM   2934 C CD2 . PHE B 2 29  ? 23.45288  -25.21560 3.76294   1.000 174.86996 ? 29  PHE B CD2 1 
ATOM   2935 C CE1 . PHE B 2 29  ? 21.30636  -26.92818 4.02664   1.000 171.91799 ? 29  PHE B CE1 1 
ATOM   2936 C CE2 . PHE B 2 29  ? 23.08888  -25.67913 5.01379   1.000 173.64706 ? 29  PHE B CE2 1 
ATOM   2937 C CZ  . PHE B 2 29  ? 22.01392  -26.53651 5.14522   1.000 173.27263 ? 29  PHE B CZ  1 
ATOM   2938 N N   . ASN B 2 30  ? 21.71011  -22.31287 0.88275   1.000 179.97955 ? 30  ASN B N   1 
ATOM   2939 C CA  . ASN B 2 30  ? 21.09573  -21.14884 1.51254   1.000 176.73616 ? 30  ASN B CA  1 
ATOM   2940 C C   . ASN B 2 30  ? 19.83901  -20.66580 0.79684   1.000 174.08946 ? 30  ASN B C   1 
ATOM   2941 O O   . ASN B 2 30  ? 19.40169  -19.53637 1.04767   1.000 172.83976 ? 30  ASN B O   1 
ATOM   2942 C CB  . ASN B 2 30  ? 22.10644  -20.00372 1.60701   1.000 176.76860 ? 30  ASN B CB  1 
ATOM   2943 C CG  . ASN B 2 30  ? 23.14749  -20.23378 2.68358   1.000 176.77779 ? 30  ASN B CG  1 
ATOM   2944 O OD1 . ASN B 2 30  ? 23.44923  -21.37383 3.03778   1.000 178.07524 ? 30  ASN B OD1 1 
ATOM   2945 N ND2 . ASN B 2 30  ? 23.69515  -19.14830 3.21937   1.000 177.99455 ? 30  ASN B ND2 1 
ATOM   2946 N N   . ASN B 2 31  ? 19.24547  -21.48057 -0.07614  1.000 165.64765 ? 31  ASN B N   1 
ATOM   2947 C CA  . ASN B 2 31  ? 18.06212  -21.08376 -0.82935  1.000 168.25952 ? 31  ASN B CA  1 
ATOM   2948 C C   . ASN B 2 31  ? 16.86347  -21.99082 -0.57942  1.000 169.94699 ? 31  ASN B C   1 
ATOM   2949 O O   . ASN B 2 31  ? 15.85606  -21.87069 -1.28660  1.000 171.17543 ? 31  ASN B O   1 
ATOM   2950 C CB  . ASN B 2 31  ? 18.37430  -21.04540 -2.32915  1.000 172.73717 ? 31  ASN B CB  1 
ATOM   2951 C CG  . ASN B 2 31  ? 19.25678  -19.87445 -2.71246  1.000 171.08083 ? 31  ASN B CG  1 
ATOM   2952 O OD1 . ASN B 2 31  ? 19.82975  -19.20470 -1.85323  1.000 165.82974 ? 31  ASN B OD1 1 
ATOM   2953 N ND2 . ASN B 2 31  ? 19.37151  -19.62203 -4.01084  1.000 175.07933 ? 31  ASN B ND2 1 
ATOM   2954 N N   . TYR B 2 32  ? 16.93535  -22.89054 0.40036   1.000 157.93898 ? 32  TYR B N   1 
ATOM   2955 C CA  . TYR B 2 32  ? 15.85664  -23.83660 0.64966   1.000 156.34130 ? 32  TYR B CA  1 
ATOM   2956 C C   . TYR B 2 32  ? 15.68525  -24.05536 2.14550   1.000 157.59248 ? 32  TYR B C   1 
ATOM   2957 O O   . TYR B 2 32  ? 16.66881  -24.20497 2.87596   1.000 156.12173 ? 32  TYR B O   1 
ATOM   2958 C CB  . TYR B 2 32  ? 16.12176  -25.17922 -0.04497  1.000 158.28358 ? 32  TYR B CB  1 
ATOM   2959 C CG  . TYR B 2 32  ? 16.18890  -25.09071 -1.55309  1.000 164.03091 ? 32  TYR B CG  1 
ATOM   2960 C CD1 . TYR B 2 32  ? 15.04925  -25.24920 -2.32869  1.000 165.67908 ? 32  TYR B CD1 1 
ATOM   2961 C CD2 . TYR B 2 32  ? 17.39216  -24.84995 -2.20072  1.000 168.54558 ? 32  TYR B CD2 1 
ATOM   2962 C CE1 . TYR B 2 32  ? 15.10685  -25.16895 -3.70718  1.000 174.20352 ? 32  TYR B CE1 1 
ATOM   2963 C CE2 . TYR B 2 32  ? 17.46091  -24.76874 -3.57750  1.000 173.14948 ? 32  TYR B CE2 1 
ATOM   2964 C CZ  . TYR B 2 32  ? 16.31540  -24.92834 -4.32628  1.000 178.02547 ? 32  TYR B CZ  1 
ATOM   2965 O OH  . TYR B 2 32  ? 16.37885  -24.84755 -5.69862  1.000 193.38696 ? 32  TYR B OH  1 
ATOM   2966 N N   . TRP B 2 33  ? 14.43117  -24.07033 2.59332   1.000 153.82014 ? 33  TRP B N   1 
ATOM   2967 C CA  . TRP B 2 33  ? 14.13123  -24.38985 3.98180   1.000 153.00466 ? 33  TRP B CA  1 
ATOM   2968 C C   . TRP B 2 33  ? 14.47025  -25.84642 4.28227   1.000 154.12590 ? 33  TRP B C   1 
ATOM   2969 O O   . TRP B 2 33  ? 14.45460  -26.70757 3.39890   1.000 158.41241 ? 33  TRP B O   1 
ATOM   2970 C CB  . TRP B 2 33  ? 12.65409  -24.13621 4.29074   1.000 153.36910 ? 33  TRP B CB  1 
ATOM   2971 C CG  . TRP B 2 33  ? 12.31709  -22.71970 4.65897   1.000 150.35871 ? 33  TRP B CG  1 
ATOM   2972 C CD1 . TRP B 2 33  ? 12.77821  -21.58111 4.06546   1.000 154.41830 ? 33  TRP B CD1 1 
ATOM   2973 C CD2 . TRP B 2 33  ? 11.44538  -22.29648 5.71535   1.000 147.19787 ? 33  TRP B CD2 1 
ATOM   2974 N NE1 . TRP B 2 33  ? 12.24376  -20.47522 4.68410   1.000 150.94143 ? 33  TRP B NE1 1 
ATOM   2975 C CE2 . TRP B 2 33  ? 11.42227  -20.88816 5.70010   1.000 149.78434 ? 33  TRP B CE2 1 
ATOM   2976 C CE3 . TRP B 2 33  ? 10.68202  -22.97301 6.67166   1.000 148.10771 ? 33  TRP B CE3 1 
ATOM   2977 C CZ2 . TRP B 2 33  ? 10.66643  -20.14413 6.60482   1.000 153.09046 ? 33  TRP B CZ2 1 
ATOM   2978 C CZ3 . TRP B 2 33  ? 9.93245   -22.23373 7.56782   1.000 147.96328 ? 33  TRP B CZ3 1 
ATOM   2979 C CH2 . TRP B 2 33  ? 9.93002   -20.83413 7.52839   1.000 151.00240 ? 33  TRP B CH2 1 
ATOM   2980 N N   . MET B 2 34  ? 14.77122  -26.11902 5.54910   1.000 153.06190 ? 34  MET B N   1 
ATOM   2981 C CA  . MET B 2 34  ? 15.08525  -27.46178 6.01124   1.000 154.16513 ? 34  MET B CA  1 
ATOM   2982 C C   . MET B 2 34  ? 14.16740  -27.83620 7.16818   1.000 149.58089 ? 34  MET B C   1 
ATOM   2983 O O   . MET B 2 34  ? 13.60302  -26.97261 7.84535   1.000 148.28768 ? 34  MET B O   1 
ATOM   2984 C CB  . MET B 2 34  ? 16.55274  -27.57306 6.44625   1.000 157.54200 ? 34  MET B CB  1 
ATOM   2985 C CG  . MET B 2 34  ? 17.55519  -27.13487 5.38839   1.000 162.05299 ? 34  MET B CG  1 
ATOM   2986 S SD  . MET B 2 34  ? 17.50959  -28.16629 3.91079   1.000 164.84646 ? 34  MET B SD  1 
ATOM   2987 C CE  . MET B 2 34  ? 17.96851  -29.75504 4.59808   1.000 162.53565 ? 34  MET B CE  1 
ATOM   2988 N N   . SER B 2 35  ? 14.02409  -29.14118 7.39264   1.000 151.20739 ? 35  SER B N   1 
ATOM   2989 C CA  . SER B 2 35  ? 13.14335  -29.63424 8.44137   1.000 150.31379 ? 35  SER B CA  1 
ATOM   2990 C C   . SER B 2 35  ? 13.64400  -30.98079 8.94318   1.000 150.71935 ? 35  SER B C   1 
ATOM   2991 O O   . SER B 2 35  ? 14.45457  -31.64814 8.29534   1.000 150.74054 ? 35  SER B O   1 
ATOM   2992 C CB  . SER B 2 35  ? 11.69477  -29.75808 7.95033   1.000 149.10215 ? 35  SER B CB  1 
ATOM   2993 O OG  . SER B 2 35  ? 11.12249  -28.48481 7.70651   1.000 149.63551 ? 35  SER B OG  1 
ATOM   2994 N N   . TRP B 2 36  ? 13.14507  -31.36964 10.11612  1.000 158.68951 ? 36  TRP B N   1 
ATOM   2995 C CA  . TRP B 2 36  ? 13.43122  -32.66797 10.71636  1.000 155.93271 ? 36  TRP B CA  1 
ATOM   2996 C C   . TRP B 2 36  ? 12.11091  -33.34636 11.04697  1.000 158.44678 ? 36  TRP B C   1 
ATOM   2997 O O   . TRP B 2 36  ? 11.30092  -32.79418 11.79861  1.000 158.82475 ? 36  TRP B O   1 
ATOM   2998 C CB  . TRP B 2 36  ? 14.28477  -32.52682 11.98037  1.000 155.28386 ? 36  TRP B CB  1 
ATOM   2999 C CG  . TRP B 2 36  ? 15.70002  -32.10516 11.73447  1.000 161.52932 ? 36  TRP B CG  1 
ATOM   3000 C CD1 . TRP B 2 36  ? 16.18509  -30.83076 11.72296  1.000 164.99160 ? 36  TRP B CD1 1 
ATOM   3001 C CD2 . TRP B 2 36  ? 16.81928  -32.96295 11.48127  1.000 163.30359 ? 36  TRP B CD2 1 
ATOM   3002 N NE1 . TRP B 2 36  ? 17.53569  -30.84078 11.47481  1.000 165.78219 ? 36  TRP B NE1 1 
ATOM   3003 C CE2 . TRP B 2 36  ? 17.94936  -32.13758 11.32000  1.000 165.64880 ? 36  TRP B CE2 1 
ATOM   3004 C CE3 . TRP B 2 36  ? 16.97453  -34.34812 11.37207  1.000 163.40423 ? 36  TRP B CE3 1 
ATOM   3005 C CZ2 . TRP B 2 36  ? 19.21707  -32.65097 11.05550  1.000 169.14108 ? 36  TRP B CZ2 1 
ATOM   3006 C CZ3 . TRP B 2 36  ? 18.23360  -34.85580 11.11033  1.000 168.17121 ? 36  TRP B CZ3 1 
ATOM   3007 C CH2 . TRP B 2 36  ? 19.33814  -34.00942 10.95541  1.000 170.03677 ? 36  TRP B CH2 1 
ATOM   3008 N N   . ILE B 2 37  ? 11.89489  -34.53636 10.48962  1.000 166.04733 ? 37  ILE B N   1 
ATOM   3009 C CA  . ILE B 2 37  ? 10.67447  -35.30533 10.70203  1.000 165.15283 ? 37  ILE B CA  1 
ATOM   3010 C C   . ILE B 2 37  ? 11.05642  -36.67972 11.23405  1.000 164.86132 ? 37  ILE B C   1 
ATOM   3011 O O   . ILE B 2 37  ? 12.00541  -37.30089 10.74384  1.000 166.79942 ? 37  ILE B O   1 
ATOM   3012 C CB  . ILE B 2 37  ? 9.84631   -35.43408 9.40512   1.000 164.24989 ? 37  ILE B CB  1 
ATOM   3013 C CG1 . ILE B 2 37  ? 9.82073   -34.10823 8.64002   1.000 162.59295 ? 37  ILE B CG1 1 
ATOM   3014 C CG2 . ILE B 2 37  ? 8.42680   -35.87494 9.72044   1.000 164.43881 ? 37  ILE B CG2 1 
ATOM   3015 C CD1 . ILE B 2 37  ? 9.10058   -32.99107 9.36540   1.000 163.20043 ? 37  ILE B CD1 1 
ATOM   3016 N N   . ARG B 2 38  ? 10.31567  -37.15596 12.23374  1.000 178.34478 ? 38  ARG B N   1 
ATOM   3017 C CA  . ARG B 2 38  ? 10.59856  -38.43581 12.86711  1.000 180.47624 ? 38  ARG B CA  1 
ATOM   3018 C C   . ARG B 2 38  ? 9.35274   -39.31059 12.85633  1.000 180.97280 ? 38  ARG B C   1 
ATOM   3019 O O   . ARG B 2 38  ? 8.23275   -38.83394 12.65554  1.000 178.76670 ? 38  ARG B O   1 
ATOM   3020 C CB  . ARG B 2 38  ? 11.08970  -38.25997 14.31132  1.000 178.52766 ? 38  ARG B CB  1 
ATOM   3021 C CG  . ARG B 2 38  ? 9.99060   -37.91017 15.30411  1.000 179.45558 ? 38  ARG B CG  1 
ATOM   3022 C CD  . ARG B 2 38  ? 10.53235  -37.85847 16.72249  1.000 181.51057 ? 38  ARG B CD  1 
ATOM   3023 N NE  . ARG B 2 38  ? 9.51475   -37.48111 17.69578  1.000 185.49973 ? 38  ARG B NE  1 
ATOM   3024 C CZ  . ARG B 2 38  ? 9.76355   -37.21531 18.97085  1.000 185.90347 ? 38  ARG B CZ  1 
ATOM   3025 N NH1 . ARG B 2 38  ? 10.99138  -37.26817 19.46097  1.000 184.76676 ? 38  ARG B NH1 1 
ATOM   3026 N NH2 . ARG B 2 38  ? 8.75594   -36.88540 19.77365  1.000 188.88330 ? 38  ARG B NH2 1 
ATOM   3027 N N   . GLN B 2 39  ? 9.56356   -40.60695 13.08173  1.000 187.56835 ? 39  GLN B N   1 
ATOM   3028 C CA  . GLN B 2 39  ? 8.47200   -41.57175 13.15755  1.000 192.16595 ? 39  GLN B CA  1 
ATOM   3029 C C   . GLN B 2 39  ? 8.79535   -42.60428 14.22475  1.000 194.56442 ? 39  GLN B C   1 
ATOM   3030 O O   . GLN B 2 39  ? 9.81590   -43.29368 14.13410  1.000 197.28636 ? 39  GLN B O   1 
ATOM   3031 C CB  . GLN B 2 39  ? 8.23494   -42.26370 11.81208  1.000 192.22808 ? 39  GLN B CB  1 
ATOM   3032 C CG  . GLN B 2 39  ? 7.06878   -43.23900 11.84535  1.000 195.25716 ? 39  GLN B CG  1 
ATOM   3033 C CD  . GLN B 2 39  ? 7.11870   -44.26705 10.73403  1.000 199.14868 ? 39  GLN B CD  1 
ATOM   3034 O OE1 . GLN B 2 39  ? 7.86122   -44.11820 9.76422   1.000 200.72141 ? 39  GLN B OE1 1 
ATOM   3035 N NE2 . GLN B 2 39  ? 6.32845   -45.32519 10.87512  1.000 203.89002 ? 39  GLN B NE2 1 
ATOM   3036 N N   . ALA B 2 40  ? 7.92587   -42.71162 15.22777  1.000 192.54945 ? 40  ALA B N   1 
ATOM   3037 C CA  . ALA B 2 40  ? 8.05636   -43.74488 16.24089  1.000 193.14260 ? 40  ALA B CA  1 
ATOM   3038 C C   . ALA B 2 40  ? 7.45449   -45.05589 15.73580  1.000 199.21232 ? 40  ALA B C   1 
ATOM   3039 O O   . ALA B 2 40  ? 6.54308   -45.04446 14.90302  1.000 205.47584 ? 40  ALA B O   1 
ATOM   3040 C CB  . ALA B 2 40  ? 7.36676   -43.31412 17.53128  1.000 194.57513 ? 40  ALA B CB  1 
ATOM   3041 N N   . PRO B 2 41  ? 7.95540   -46.19684 16.21402  1.000 202.11632 ? 41  PRO B N   1 
ATOM   3042 C CA  . PRO B 2 41  ? 7.47734   -47.49415 15.70302  1.000 208.21678 ? 41  PRO B CA  1 
ATOM   3043 C C   . PRO B 2 41  ? 5.97445   -47.65859 15.88062  1.000 212.38834 ? 41  PRO B C   1 
ATOM   3044 O O   . PRO B 2 41  ? 5.45269   -47.61559 16.99712  1.000 218.23161 ? 41  PRO B O   1 
ATOM   3045 C CB  . PRO B 2 41  ? 8.26356   -48.51041 16.54052  1.000 210.39007 ? 41  PRO B CB  1 
ATOM   3046 C CG  . PRO B 2 41  ? 9.49048   -47.78395 16.95690  1.000 204.81878 ? 41  PRO B CG  1 
ATOM   3047 C CD  . PRO B 2 41  ? 9.07180   -46.35715 17.16183  1.000 199.37498 ? 41  PRO B CD  1 
ATOM   3048 N N   . GLY B 2 42  ? 5.27862   -47.84707 14.76045  1.000 204.66423 ? 42  GLY B N   1 
ATOM   3049 C CA  . GLY B 2 42  ? 3.83957   -48.00840 14.77814  1.000 212.87774 ? 42  GLY B CA  1 
ATOM   3050 C C   . GLY B 2 42  ? 3.05513   -46.74250 15.02513  1.000 212.55635 ? 42  GLY B C   1 
ATOM   3051 O O   . GLY B 2 42  ? 1.92226   -46.81661 15.50944  1.000 215.81839 ? 42  GLY B O   1 
ATOM   3052 N N   . LYS B 2 43  ? 3.62420   -45.57819 14.71644  1.000 206.50735 ? 43  LYS B N   1 
ATOM   3053 C CA  . LYS B 2 43  ? 2.95033   -44.30507 14.92427  1.000 204.29646 ? 43  LYS B CA  1 
ATOM   3054 C C   . LYS B 2 43  ? 3.15759   -43.42740 13.69759  1.000 201.40956 ? 43  LYS B C   1 
ATOM   3055 O O   . LYS B 2 43  ? 4.06478   -43.65424 12.89399  1.000 199.17337 ? 43  LYS B O   1 
ATOM   3056 C CB  . LYS B 2 43  ? 3.45855   -43.60041 16.19112  1.000 201.45986 ? 43  LYS B CB  1 
ATOM   3057 C CG  . LYS B 2 43  ? 3.26048   -44.40873 17.46736  1.000 209.03139 ? 43  LYS B CG  1 
ATOM   3058 C CD  . LYS B 2 43  ? 4.00123   -43.80309 18.64556  1.000 209.83989 ? 43  LYS B CD  1 
ATOM   3059 C CE  . LYS B 2 43  ? 4.01386   -44.75345 19.83220  1.000 213.47442 ? 43  LYS B CE  1 
ATOM   3060 N NZ  . LYS B 2 43  ? 4.93872   -44.29268 20.90463  1.000 212.59172 ? 43  LYS B NZ  1 
ATOM   3061 N N   . GLY B 2 44  ? 2.30382   -42.41889 13.55969  1.000 199.20593 ? 44  GLY B N   1 
ATOM   3062 C CA  . GLY B 2 44  ? 2.33078   -41.56020 12.39471  1.000 198.26847 ? 44  GLY B CA  1 
ATOM   3063 C C   . GLY B 2 44  ? 3.55205   -40.65668 12.35367  1.000 190.18765 ? 44  GLY B C   1 
ATOM   3064 O O   . GLY B 2 44  ? 4.38406   -40.61957 13.26080  1.000 183.98838 ? 44  GLY B O   1 
ATOM   3065 N N   . LEU B 2 45  ? 3.65254   -39.90819 11.25731  1.000 193.17516 ? 45  LEU B N   1 
ATOM   3066 C CA  . LEU B 2 45  ? 4.75266   -38.96924 11.09068  1.000 181.70676 ? 45  LEU B CA  1 
ATOM   3067 C C   . LEU B 2 45  ? 4.56402   -37.75694 11.99303  1.000 180.31580 ? 45  LEU B C   1 
ATOM   3068 O O   . LEU B 2 45  ? 3.45946   -37.22179 12.12334  1.000 186.75165 ? 45  LEU B O   1 
ATOM   3069 C CB  . LEU B 2 45  ? 4.86339   -38.52528 9.63242   1.000 178.26036 ? 45  LEU B CB  1 
ATOM   3070 C CG  . LEU B 2 45  ? 5.86824   -39.28224 8.76187   1.000 180.24281 ? 45  LEU B CG  1 
ATOM   3071 C CD1 . LEU B 2 45  ? 6.06020   -38.57468 7.42845   1.000 179.61351 ? 45  LEU B CD1 1 
ATOM   3072 C CD2 . LEU B 2 45  ? 7.19746   -39.43829 9.48605   1.000 180.77071 ? 45  LEU B CD2 1 
ATOM   3073 N N   . GLU B 2 46  ? 5.65691   -37.32241 12.61536  1.000 174.13939 ? 46  GLU B N   1 
ATOM   3074 C CA  . GLU B 2 46  ? 5.64109   -36.20320 13.54636  1.000 175.72039 ? 46  GLU B CA  1 
ATOM   3075 C C   . GLU B 2 46  ? 6.70361   -35.19370 13.14248  1.000 174.73632 ? 46  GLU B C   1 
ATOM   3076 O O   . GLU B 2 46  ? 7.86449   -35.55990 12.93297  1.000 174.98636 ? 46  GLU B O   1 
ATOM   3077 C CB  . GLU B 2 46  ? 5.88420   -36.67761 14.98277  1.000 175.89612 ? 46  GLU B CB  1 
ATOM   3078 C CG  . GLU B 2 46  ? 6.04345   -35.55075 15.98877  1.000 179.71865 ? 46  GLU B CG  1 
ATOM   3079 C CD  . GLU B 2 46  ? 6.43928   -36.05033 17.36356  1.000 187.06957 ? 46  GLU B CD  1 
ATOM   3080 O OE1 . GLU B 2 46  ? 6.43632   -37.28184 17.57197  1.000 194.95569 ? 46  GLU B OE1 1 
ATOM   3081 O OE2 . GLU B 2 46  ? 6.75655   -35.21217 18.23406  1.000 192.27080 ? 46  GLU B OE2 1 
ATOM   3082 N N   . TRP B 2 47  ? 6.30505   -33.92923 13.03448  1.000 167.72924 ? 47  TRP B N   1 
ATOM   3083 C CA  . TRP B 2 47  ? 7.24801   -32.85718 12.75273  1.000 164.44973 ? 47  TRP B CA  1 
ATOM   3084 C C   . TRP B 2 47  ? 7.97843   -32.45542 14.02869  1.000 167.71249 ? 47  TRP B C   1 
ATOM   3085 O O   . TRP B 2 47  ? 7.39165   -32.42768 15.11418  1.000 170.43975 ? 47  TRP B O   1 
ATOM   3086 C CB  . TRP B 2 47  ? 6.52291   -31.65438 12.14875  1.000 165.38098 ? 47  TRP B CB  1 
ATOM   3087 C CG  . TRP B 2 47  ? 7.36381   -30.42237 12.09591  1.000 164.52961 ? 47  TRP B CG  1 
ATOM   3088 C CD1 . TRP B 2 47  ? 8.49262   -30.23280 11.35554  1.000 164.81697 ? 47  TRP B CD1 1 
ATOM   3089 C CD2 . TRP B 2 47  ? 7.14443   -29.20268 12.81361  1.000 165.88670 ? 47  TRP B CD2 1 
ATOM   3090 N NE1 . TRP B 2 47  ? 8.99201   -28.97186 11.56846  1.000 162.52549 ? 47  TRP B NE1 1 
ATOM   3091 C CE2 . TRP B 2 47  ? 8.18404   -28.31947 12.46192  1.000 165.76148 ? 47  TRP B CE2 1 
ATOM   3092 C CE3 . TRP B 2 47  ? 6.17073   -28.77208 13.71993  1.000 170.25159 ? 47  TRP B CE3 1 
ATOM   3093 C CZ2 . TRP B 2 47  ? 8.27622   -27.02993 12.98162  1.000 168.99198 ? 47  TRP B CZ2 1 
ATOM   3094 C CZ3 . TRP B 2 47  ? 6.26310   -27.49090 14.23408  1.000 173.00941 ? 47  TRP B CZ3 1 
ATOM   3095 C CH2 . TRP B 2 47  ? 7.30943   -26.63605 13.86525  1.000 173.20245 ? 47  TRP B CH2 1 
ATOM   3096 N N   . ILE B 2 48  ? 9.27035   -32.14505 13.89385  1.000 163.50022 ? 48  ILE B N   1 
ATOM   3097 C CA  . ILE B 2 48  ? 10.14598  -31.91694 15.03424  1.000 165.32452 ? 48  ILE B CA  1 
ATOM   3098 C C   . ILE B 2 48  ? 10.78230  -30.53302 15.00540  1.000 164.57102 ? 48  ILE B C   1 
ATOM   3099 O O   . ILE B 2 48  ? 10.89475  -29.87753 16.04781  1.000 165.87857 ? 48  ILE B O   1 
ATOM   3100 C CB  . ILE B 2 48  ? 11.23168  -33.01279 15.12304  1.000 165.61974 ? 48  ILE B CB  1 
ATOM   3101 C CG1 . ILE B 2 48  ? 10.60308  -34.33714 15.55415  1.000 167.42424 ? 48  ILE B CG1 1 
ATOM   3102 C CG2 . ILE B 2 48  ? 12.34208  -32.61253 16.08545  1.000 163.82827 ? 48  ILE B CG2 1 
ATOM   3103 C CD1 . ILE B 2 48  ? 9.87878   -34.25582 16.88121  1.000 171.59487 ? 48  ILE B CD1 1 
ATOM   3104 N N   . ALA B 2 49  ? 11.21015  -30.06776 13.83499  1.000 155.72433 ? 49  ALA B N   1 
ATOM   3105 C CA  . ALA B 2 49  ? 11.85939  -28.76651 13.74700  1.000 154.83599 ? 49  ALA B CA  1 
ATOM   3106 C C   . ALA B 2 49  ? 11.91496  -28.33111 12.29248  1.000 153.41452 ? 49  ALA B C   1 
ATOM   3107 O O   . ALA B 2 49  ? 11.94626  -29.16511 11.38345  1.000 152.30668 ? 49  ALA B O   1 
ATOM   3108 C CB  . ALA B 2 49  ? 13.27384  -28.79928 14.34062  1.000 158.21910 ? 49  ALA B CB  1 
ATOM   3109 N N   . SER B 2 50  ? 11.92764  -27.01553 12.08850  1.000 146.12352 ? 50  SER B N   1 
ATOM   3110 C CA  . SER B 2 50  ? 12.06092  -26.42470 10.76580  1.000 145.71472 ? 50  SER B CA  1 
ATOM   3111 C C   . SER B 2 50  ? 12.91090  -25.16868 10.86723  1.000 146.40946 ? 50  SER B C   1 
ATOM   3112 O O   . SER B 2 50  ? 12.81285  -24.42082 11.84402  1.000 147.01029 ? 50  SER B O   1 
ATOM   3113 C CB  . SER B 2 50  ? 10.69480  -26.08604 10.15541  1.000 145.13215 ? 50  SER B CB  1 
ATOM   3114 O OG  . SER B 2 50  ? 9.93779   -27.25929 9.91756   1.000 144.92803 ? 50  SER B OG  1 
ATOM   3115 N N   . ILE B 2 51  ? 13.74709  -24.94357 9.85438   1.000 151.28904 ? 51  ILE B N   1 
ATOM   3116 C CA  . ILE B 2 51  ? 14.61264  -23.77530 9.80005   1.000 150.92643 ? 51  ILE B CA  1 
ATOM   3117 C C   . ILE B 2 51  ? 14.41196  -23.08856 8.45530   1.000 153.49801 ? 51  ILE B C   1 
ATOM   3118 O O   . ILE B 2 51  ? 13.99102  -23.70207 7.47203   1.000 152.40693 ? 51  ILE B O   1 
ATOM   3119 C CB  . ILE B 2 51  ? 16.09869  -24.14184 10.01985  1.000 152.00295 ? 51  ILE B CB  1 
ATOM   3120 C CG1 . ILE B 2 51  ? 16.92271  -22.89579 10.35756  1.000 151.38431 ? 51  ILE B CG1 1 
ATOM   3121 C CG2 . ILE B 2 51  ? 16.65821  -24.86148 8.80196   1.000 154.73559 ? 51  ILE B CG2 1 
ATOM   3122 C CD1 . ILE B 2 51  ? 17.97222  -23.12499 11.42322  1.000 151.20662 ? 51  ILE B CD1 1 
ATOM   3123 N N   . SER B 2 52  ? 14.70484  -21.79214 8.42804   1.000 156.44781 ? 52  SER B N   1 
ATOM   3124 C CA  . SER B 2 52  ? 14.52903  -20.98468 7.23184   1.000 155.77086 ? 52  SER B CA  1 
ATOM   3125 C C   . SER B 2 52  ? 15.76819  -21.09705 6.34230   1.000 158.46974 ? 52  SER B C   1 
ATOM   3126 O O   . SER B 2 52  ? 16.60318  -21.98989 6.51083   1.000 162.83569 ? 52  SER B O   1 
ATOM   3127 C CB  . SER B 2 52  ? 14.22714  -19.53977 7.61953   1.000 156.31963 ? 52  SER B CB  1 
ATOM   3128 O OG  . SER B 2 52  ? 15.28496  -18.98748 8.38198   1.000 158.01916 ? 52  SER B OG  1 
ATOM   3129 N N   . ASN B 2 53  ? 15.89708  -20.18128 5.37848   1.000 157.79198 ? 53  ASN B N   1 
ATOM   3130 C CA  . ASN B 2 53  ? 17.01988  -20.23073 4.44603   1.000 158.12684 ? 53  ASN B CA  1 
ATOM   3131 C C   . ASN B 2 53  ? 18.33859  -19.93769 5.15050   1.000 158.95413 ? 53  ASN B C   1 
ATOM   3132 O O   . ASN B 2 53  ? 19.31245  -20.68513 5.00375   1.000 160.09432 ? 53  ASN B O   1 
ATOM   3133 C CB  . ASN B 2 53  ? 16.79234  -19.24741 3.29713   1.000 157.21886 ? 53  ASN B CB  1 
ATOM   3134 C CG  . ASN B 2 53  ? 15.80413  -19.76752 2.27270   1.000 157.25079 ? 53  ASN B CG  1 
ATOM   3135 O OD1 . ASN B 2 53  ? 15.67890  -20.97553 2.07275   1.000 158.45113 ? 53  ASN B OD1 1 
ATOM   3136 N ND2 . ASN B 2 53  ? 15.09371  -18.85653 1.61905   1.000 156.41173 ? 53  ASN B ND2 1 
ATOM   3137 N N   . ILE B 2 54  ? 18.39156  -18.84982 5.91351   1.000 159.45575 ? 54  ILE B N   1 
ATOM   3138 C CA  . ILE B 2 54  ? 19.58338  -18.46751 6.65259   1.000 161.22037 ? 54  ILE B CA  1 
ATOM   3139 C C   . ILE B 2 54  ? 19.42577  -18.72719 8.14500   1.000 163.24698 ? 54  ILE B C   1 
ATOM   3140 O O   . ILE B 2 54  ? 20.36987  -19.16754 8.80438   1.000 170.60187 ? 54  ILE B O   1 
ATOM   3141 C CB  . ILE B 2 54  ? 19.93863  -16.98753 6.38728   1.000 162.55894 ? 54  ILE B CB  1 
ATOM   3142 C CG1 . ILE B 2 54  ? 20.15324  -16.74422 4.89270   1.000 158.48725 ? 54  ILE B CG1 1 
ATOM   3143 C CG2 . ILE B 2 54  ? 21.17864  -16.57611 7.17016   1.000 178.38736 ? 54  ILE B CG2 1 
ATOM   3144 C CD1 . ILE B 2 54  ? 20.56191  -15.32755 4.56206   1.000 162.16239 ? 54  ILE B CD1 1 
ATOM   3145 N N   . GLY B 2 55  ? 18.24024  -18.47355 8.68997   1.000 160.85548 ? 55  GLY B N   1 
ATOM   3146 C CA  . GLY B 2 55  ? 18.02455  -18.58880 10.11763  1.000 155.64318 ? 55  GLY B CA  1 
ATOM   3147 C C   . GLY B 2 55  ? 17.34411  -17.36507 10.69406  1.000 156.72340 ? 55  GLY B C   1 
ATOM   3148 O O   . GLY B 2 55  ? 17.69906  -16.89195 11.77887  1.000 166.36273 ? 55  GLY B O   1 
ATOM   3149 N N   . GLY B 2 56  ? 16.37058  -16.83472 9.95933   1.000 163.81400 ? 56  GLY B N   1 
ATOM   3150 C CA  . GLY B 2 56  ? 15.59828  -15.69905 10.41964  1.000 162.55726 ? 56  GLY B CA  1 
ATOM   3151 C C   . GLY B 2 56  ? 14.33353  -16.13445 11.12695  1.000 170.57613 ? 56  GLY B C   1 
ATOM   3152 O O   . GLY B 2 56  ? 13.83584  -15.44206 12.02024  1.000 176.24254 ? 56  GLY B O   1 
ATOM   3153 N N   . THR B 2 57  ? 13.81059  -17.29389 10.73385  1.000 155.38802 ? 57  THR B N   1 
ATOM   3154 C CA  . THR B 2 57  ? 12.61278  -17.86854 11.33004  1.000 157.81397 ? 57  THR B CA  1 
ATOM   3155 C C   . THR B 2 57  ? 12.86306  -19.33558 11.64304  1.000 157.92962 ? 57  THR B C   1 
ATOM   3156 O O   . THR B 2 57  ? 13.36989  -20.07809 10.79579  1.000 157.78027 ? 57  THR B O   1 
ATOM   3157 C CB  . THR B 2 57  ? 11.40052  -17.72554 10.40165  1.000 156.76303 ? 57  THR B CB  1 
ATOM   3158 O OG1 . THR B 2 57  ? 11.81345  -17.88401 9.03809   1.000 156.77939 ? 57  THR B OG1 1 
ATOM   3159 C CG2 . THR B 2 57  ? 10.74591  -16.36403 10.57989  1.000 157.58484 ? 57  THR B CG2 1 
ATOM   3160 N N   . ILE B 2 58  ? 12.51382  -19.74578 12.86020  1.000 153.05519 ? 58  ILE B N   1 
ATOM   3161 C CA  . ILE B 2 58  ? 12.67987  -21.12271 13.31334  1.000 153.29488 ? 58  ILE B CA  1 
ATOM   3162 C C   . ILE B 2 58  ? 11.47244  -21.49347 14.16164  1.000 154.42553 ? 58  ILE B C   1 
ATOM   3163 O O   . ILE B 2 58  ? 11.10726  -20.75709 15.08410  1.000 158.85194 ? 58  ILE B O   1 
ATOM   3164 C CB  . ILE B 2 58  ? 13.98109  -21.31928 14.11913  1.000 152.59326 ? 58  ILE B CB  1 
ATOM   3165 C CG1 . ILE B 2 58  ? 15.21210  -21.21918 13.21419  1.000 151.72909 ? 58  ILE B CG1 1 
ATOM   3166 C CG2 . ILE B 2 58  ? 13.96933  -22.65651 14.83540  1.000 152.84335 ? 58  ILE B CG2 1 
ATOM   3167 C CD1 . ILE B 2 58  ? 15.86090  -19.85154 13.20220  1.000 151.86149 ? 58  ILE B CD1 1 
ATOM   3168 N N   . TYR B 2 59  ? 10.85197  -22.62984 13.85331  1.000 159.67989 ? 59  TYR B N   1 
ATOM   3169 C CA  . TYR B 2 59  ? 9.71930   -23.12702 14.61876  1.000 158.54701 ? 59  TYR B CA  1 
ATOM   3170 C C   . TYR B 2 59  ? 10.01501  -24.52000 15.15884  1.000 158.34984 ? 59  TYR B C   1 
ATOM   3171 O O   . TYR B 2 59  ? 10.71438  -25.31629 14.52579  1.000 154.87406 ? 59  TYR B O   1 
ATOM   3172 C CB  . TYR B 2 59  ? 8.43748   -23.18678 13.77511  1.000 157.76869 ? 59  TYR B CB  1 
ATOM   3173 C CG  . TYR B 2 59  ? 8.25505   -22.05105 12.79489  1.000 159.60484 ? 59  TYR B CG  1 
ATOM   3174 C CD1 . TYR B 2 59  ? 8.21190   -20.73152 13.22450  1.000 161.60114 ? 59  TYR B CD1 1 
ATOM   3175 C CD2 . TYR B 2 59  ? 8.09700   -22.30396 11.43856  1.000 161.37895 ? 59  TYR B CD2 1 
ATOM   3176 C CE1 . TYR B 2 59  ? 8.03648   -19.69395 12.32666  1.000 165.00105 ? 59  TYR B CE1 1 
ATOM   3177 C CE2 . TYR B 2 59  ? 7.91917   -21.27535 10.53509  1.000 161.64965 ? 59  TYR B CE2 1 
ATOM   3178 C CZ  . TYR B 2 59  ? 7.88969   -19.97247 10.98371  1.000 166.03407 ? 59  TYR B CZ  1 
ATOM   3179 O OH  . TYR B 2 59  ? 7.71351   -18.94497 10.08576  1.000 167.78172 ? 59  TYR B OH  1 
ATOM   3180 N N   . TYR B 2 60  ? 9.46884   -24.80530 16.33655  1.000 170.60076 ? 60  TYR B N   1 
ATOM   3181 C CA  . TYR B 2 60  ? 9.42816   -26.13876 16.91509  1.000 167.25136 ? 60  TYR B CA  1 
ATOM   3182 C C   . TYR B 2 60  ? 8.02850   -26.40741 17.44408  1.000 170.75435 ? 60  TYR B C   1 
ATOM   3183 O O   . TYR B 2 60  ? 7.33638   -25.47669 17.86850  1.000 172.97763 ? 60  TYR B O   1 
ATOM   3184 C CB  . TYR B 2 60  ? 10.42323  -26.30441 18.07435  1.000 165.08500 ? 60  TYR B CB  1 
ATOM   3185 C CG  . TYR B 2 60  ? 11.84138  -25.85587 17.80962  1.000 164.64333 ? 60  TYR B CG  1 
ATOM   3186 C CD1 . TYR B 2 60  ? 12.76709  -26.71159 17.22602  1.000 163.27396 ? 60  TYR B CD1 1 
ATOM   3187 C CD2 . TYR B 2 60  ? 12.26354  -24.58553 18.17480  1.000 166.32532 ? 60  TYR B CD2 1 
ATOM   3188 C CE1 . TYR B 2 60  ? 14.06943  -26.30491 16.99516  1.000 164.38768 ? 60  TYR B CE1 1 
ATOM   3189 C CE2 . TYR B 2 60  ? 13.56139  -24.17130 17.95051  1.000 168.38304 ? 60  TYR B CE2 1 
ATOM   3190 C CZ  . TYR B 2 60  ? 14.45997  -25.03284 17.35989  1.000 168.65274 ? 60  TYR B CZ  1 
ATOM   3191 O OH  . TYR B 2 60  ? 15.75234  -24.61659 17.13646  1.000 171.92875 ? 60  TYR B OH  1 
ATOM   3192 N N   . PRO B 2 61  ? 7.58355   -27.66221 17.43250  1.000 174.40182 ? 61  PRO B N   1 
ATOM   3193 C CA  . PRO B 2 61  ? 6.36282   -28.00530 18.16452  1.000 178.63980 ? 61  PRO B CA  1 
ATOM   3194 C C   . PRO B 2 61  ? 6.62082   -27.97303 19.66108  1.000 192.28825 ? 61  PRO B C   1 
ATOM   3195 O O   . PRO B 2 61  ? 7.75027   -28.15067 20.12409  1.000 189.97786 ? 61  PRO B O   1 
ATOM   3196 C CB  . PRO B 2 61  ? 6.04119   -29.42374 17.67934  1.000 173.57923 ? 61  PRO B CB  1 
ATOM   3197 C CG  . PRO B 2 61  ? 7.35911   -29.98684 17.29608  1.000 168.10879 ? 61  PRO B CG  1 
ATOM   3198 C CD  . PRO B 2 61  ? 8.15425   -28.83092 16.74228  1.000 168.77828 ? 61  PRO B CD  1 
ATOM   3199 N N   . ASP B 2 62  ? 5.55018   -27.73573 20.42175  1.000 199.31441 ? 62  ASP B N   1 
ATOM   3200 C CA  . ASP B 2 62  ? 5.68199   -27.57883 21.86609  1.000 202.47640 ? 62  ASP B CA  1 
ATOM   3201 C C   . ASP B 2 62  ? 6.20051   -28.83880 22.54625  1.000 199.81637 ? 62  ASP B C   1 
ATOM   3202 O O   . ASP B 2 62  ? 6.69352   -28.75997 23.67677  1.000 203.08694 ? 62  ASP B O   1 
ATOM   3203 C CB  . ASP B 2 62  ? 4.33740   -27.17951 22.47264  1.000 210.09409 ? 62  ASP B CB  1 
ATOM   3204 C CG  . ASP B 2 62  ? 3.69111   -26.02566 21.73731  1.000 212.36457 ? 62  ASP B CG  1 
ATOM   3205 O OD1 . ASP B 2 62  ? 4.42955   -25.16724 21.21147  1.000 210.33139 ? 62  ASP B OD1 1 
ATOM   3206 O OD2 . ASP B 2 62  ? 2.44458   -25.98124 21.68018  1.000 216.58631 ? 62  ASP B OD2 1 
ATOM   3207 N N   . SER B 2 63  ? 6.10954   -29.99490 21.88415  1.000 195.34166 ? 63  SER B N   1 
ATOM   3208 C CA  . SER B 2 63  ? 6.55596   -31.24024 22.49679  1.000 198.42609 ? 63  SER B CA  1 
ATOM   3209 C C   . SER B 2 63  ? 8.05152   -31.23454 22.78783  1.000 196.48874 ? 63  SER B C   1 
ATOM   3210 O O   . SER B 2 63  ? 8.49346   -31.84365 23.77001  1.000 200.32452 ? 63  SER B O   1 
ATOM   3211 C CB  . SER B 2 63  ? 6.19638   -32.42251 21.59532  1.000 194.51816 ? 63  SER B CB  1 
ATOM   3212 O OG  . SER B 2 63  ? 6.71436   -32.25243 20.28456  1.000 189.06987 ? 63  SER B OG  1 
ATOM   3213 N N   . VAL B 2 64  ? 8.84498   -30.56512 21.95551  1.000 198.57206 ? 64  VAL B N   1 
ATOM   3214 C CA  . VAL B 2 64  ? 10.29810  -30.58037 22.10185  1.000 194.34290 ? 64  VAL B CA  1 
ATOM   3215 C C   . VAL B 2 64  ? 10.80845  -29.17856 22.40826  1.000 197.41151 ? 64  VAL B C   1 
ATOM   3216 O O   . VAL B 2 64  ? 11.94796  -28.83491 22.07232  1.000 190.98236 ? 64  VAL B O   1 
ATOM   3217 C CB  . VAL B 2 64  ? 10.97560  -31.14191 20.83842  1.000 183.37597 ? 64  VAL B CB  1 
ATOM   3218 C CG1 . VAL B 2 64  ? 10.62421  -32.61178 20.65422  1.000 181.56117 ? 64  VAL B CG1 1 
ATOM   3219 C CG2 . VAL B 2 64  ? 10.57041  -30.33489 19.61872  1.000 183.20212 ? 64  VAL B CG2 1 
ATOM   3220 N N   . LYS B 2 65  ? 9.97240   -28.37127 23.05151  1.000 191.37684 ? 65  LYS B N   1 
ATOM   3221 C CA  . LYS B 2 65  ? 10.32544  -26.99231 23.34562  1.000 194.34931 ? 65  LYS B CA  1 
ATOM   3222 C C   . LYS B 2 65  ? 11.53466  -26.94083 24.26939  1.000 196.22313 ? 65  LYS B C   1 
ATOM   3223 O O   . LYS B 2 65  ? 11.49154  -27.45287 25.39260  1.000 198.22272 ? 65  LYS B O   1 
ATOM   3224 C CB  . LYS B 2 65  ? 9.13730   -26.27022 23.98163  1.000 199.82856 ? 65  LYS B CB  1 
ATOM   3225 C CG  . LYS B 2 65  ? 9.23898   -24.76047 23.96687  1.000 202.05930 ? 65  LYS B CG  1 
ATOM   3226 C CD  . LYS B 2 65  ? 7.92619   -24.11751 24.39763  1.000 206.02014 ? 65  LYS B CD  1 
ATOM   3227 C CE  . LYS B 2 65  ? 7.89605   -22.62541 24.09001  1.000 207.97209 ? 65  LYS B CE  1 
ATOM   3228 N NZ  . LYS B 2 65  ? 6.54384   -22.04841 24.33732  1.000 212.00276 ? 65  LYS B NZ  1 
ATOM   3229 N N   . GLY B 2 66  ? 12.62149  -26.34594 23.78197  1.000 197.12673 ? 66  GLY B N   1 
ATOM   3230 C CA  . GLY B 2 66  ? 13.84882  -26.25152 24.54753  1.000 198.03791 ? 66  GLY B CA  1 
ATOM   3231 C C   . GLY B 2 66  ? 14.67769  -27.51642 24.48691  1.000 196.04633 ? 66  GLY B C   1 
ATOM   3232 O O   . GLY B 2 66  ? 15.90542  -27.45701 24.37235  1.000 195.87121 ? 66  GLY B O   1 
ATOM   3233 N N   . ARG B 2 67  ? 14.00628  -28.66964 24.56366  1.000 197.82495 ? 67  ARG B N   1 
ATOM   3234 C CA  . ARG B 2 67  ? 14.69727  -29.95363 24.52202  1.000 196.18342 ? 67  ARG B CA  1 
ATOM   3235 C C   . ARG B 2 67  ? 15.50680  -30.12016 23.24411  1.000 188.85977 ? 67  ARG B C   1 
ATOM   3236 O O   . ARG B 2 67  ? 16.56710  -30.75644 23.25800  1.000 188.66297 ? 67  ARG B O   1 
ATOM   3237 C CB  . ARG B 2 67  ? 13.68168  -31.08694 24.64437  1.000 196.86488 ? 67  ARG B CB  1 
ATOM   3238 C CG  . ARG B 2 67  ? 12.62790  -30.86081 25.71271  1.000 200.01836 ? 67  ARG B CG  1 
ATOM   3239 C CD  . ARG B 2 67  ? 11.46188  -31.81753 25.53712  1.000 200.00728 ? 67  ARG B CD  1 
ATOM   3240 N NE  . ARG B 2 67  ? 11.91113  -33.14746 25.14421  1.000 197.97292 ? 67  ARG B NE  1 
ATOM   3241 C CZ  . ARG B 2 67  ? 12.42794  -34.04050 25.97690  1.000 199.04955 ? 67  ARG B CZ  1 
ATOM   3242 N NH1 . ARG B 2 67  ? 12.58343  -33.77689 27.26406  1.000 201.65455 ? 67  ARG B NH1 1 
ATOM   3243 N NH2 . ARG B 2 67  ? 12.80151  -35.22668 25.50580  1.000 193.98194 ? 67  ARG B NH2 1 
ATOM   3244 N N   . PHE B 2 68  ? 15.02278  -29.56882 22.13593  1.000 193.42798 ? 68  PHE B N   1 
ATOM   3245 C CA  . PHE B 2 68  ? 15.67005  -29.68656 20.84083  1.000 182.32973 ? 68  PHE B CA  1 
ATOM   3246 C C   . PHE B 2 68  ? 16.12777  -28.31194 20.37050  1.000 185.71757 ? 68  PHE B C   1 
ATOM   3247 O O   . PHE B 2 68  ? 15.61126  -27.27869 20.80503  1.000 191.42052 ? 68  PHE B O   1 
ATOM   3248 C CB  . PHE B 2 68  ? 14.72744  -30.31897 19.80518  1.000 178.01422 ? 68  PHE B CB  1 
ATOM   3249 C CG  . PHE B 2 68  ? 14.58106  -31.81281 19.94281  1.000 179.78683 ? 68  PHE B CG  1 
ATOM   3250 C CD1 . PHE B 2 68  ? 14.26137  -32.38738 21.16310  1.000 187.16931 ? 68  PHE B CD1 1 
ATOM   3251 C CD2 . PHE B 2 68  ? 14.74851  -32.64068 18.84507  1.000 177.02580 ? 68  PHE B CD2 1 
ATOM   3252 C CE1 . PHE B 2 68  ? 14.12439  -33.75624 21.28966  1.000 184.04787 ? 68  PHE B CE1 1 
ATOM   3253 C CE2 . PHE B 2 68  ? 14.60980  -34.01214 18.96458  1.000 175.98350 ? 68  PHE B CE2 1 
ATOM   3254 C CZ  . PHE B 2 68  ? 14.29714  -34.56976 20.18889  1.000 178.06527 ? 68  PHE B CZ  1 
ATOM   3255 N N   . THR B 2 69  ? 17.11401  -28.30966 19.47507  1.000 173.14248 ? 69  THR B N   1 
ATOM   3256 C CA  . THR B 2 69  ? 17.69374  -27.06438 18.97635  1.000 174.77831 ? 69  THR B CA  1 
ATOM   3257 C C   . THR B 2 69  ? 18.21770  -27.31322 17.56896  1.000 170.10198 ? 69  THR B C   1 
ATOM   3258 O O   . THR B 2 69  ? 19.24853  -27.97073 17.39831  1.000 170.17567 ? 69  THR B O   1 
ATOM   3259 C CB  . THR B 2 69  ? 18.80910  -26.56961 19.89595  1.000 179.97180 ? 69  THR B CB  1 
ATOM   3260 O OG1 . THR B 2 69  ? 18.29766  -26.39424 21.22355  1.000 186.86975 ? 69  THR B OG1 1 
ATOM   3261 C CG2 . THR B 2 69  ? 19.36465  -25.24548 19.39609  1.000 180.07499 ? 69  THR B CG2 1 
ATOM   3262 N N   . ILE B 2 70  ? 17.51359  -26.78534 16.56716  1.000 168.19653 ? 70  ILE B N   1 
ATOM   3263 C CA  . ILE B 2 70  ? 17.91998  -26.97482 15.18014  1.000 163.94997 ? 70  ILE B CA  1 
ATOM   3264 C C   . ILE B 2 70  ? 19.08985  -26.05025 14.85210  1.000 167.78201 ? 70  ILE B C   1 
ATOM   3265 O O   . ILE B 2 70  ? 19.30936  -25.02156 15.49754  1.000 170.80022 ? 70  ILE B O   1 
ATOM   3266 C CB  . ILE B 2 70  ? 16.73314  -26.74512 14.22493  1.000 162.49477 ? 70  ILE B CB  1 
ATOM   3267 C CG1 . ILE B 2 70  ? 16.99506  -27.39808 12.86555  1.000 163.16617 ? 70  ILE B CG1 1 
ATOM   3268 C CG2 . ILE B 2 70  ? 16.45512  -25.25869 14.05823  1.000 164.62392 ? 70  ILE B CG2 1 
ATOM   3269 C CD1 . ILE B 2 70  ? 15.84362  -27.26873 11.89669  1.000 160.78260 ? 70  ILE B CD1 1 
ATOM   3270 N N   . SER B 2 71  ? 19.85958  -26.43343 13.83522  1.000 167.35807 ? 71  SER B N   1 
ATOM   3271 C CA  . SER B 2 71  ? 21.02603  -25.66266 13.42773  1.000 169.55632 ? 71  SER B CA  1 
ATOM   3272 C C   . SER B 2 71  ? 21.36395  -26.00480 11.98408  1.000 169.06652 ? 71  SER B C   1 
ATOM   3273 O O   . SER B 2 71  ? 21.00821  -27.07337 11.48022  1.000 167.71192 ? 71  SER B O   1 
ATOM   3274 C CB  . SER B 2 71  ? 22.22387  -25.93423 14.34569  1.000 172.73555 ? 71  SER B CB  1 
ATOM   3275 O OG  . SER B 2 71  ? 23.32344  -25.10295 14.01822  1.000 175.39271 ? 71  SER B OG  1 
ATOM   3276 N N   . ARG B 2 72  ? 22.05591  -25.07780 11.32410  1.000 164.89594 ? 72  ARG B N   1 
ATOM   3277 C CA  . ARG B 2 72  ? 22.47722  -25.27812 9.94502   1.000 166.98030 ? 72  ARG B CA  1 
ATOM   3278 C C   . ARG B 2 72  ? 23.68890  -24.40179 9.66275   1.000 172.35411 ? 72  ARG B C   1 
ATOM   3279 O O   . ARG B 2 72  ? 23.75077  -23.25409 10.11104  1.000 174.10584 ? 72  ARG B O   1 
ATOM   3280 C CB  . ARG B 2 72  ? 21.34655  -24.96282 8.95849   1.000 164.87009 ? 72  ARG B CB  1 
ATOM   3281 C CG  . ARG B 2 72  ? 20.74839  -23.57461 9.10166   1.000 164.42126 ? 72  ARG B CG  1 
ATOM   3282 C CD  . ARG B 2 72  ? 19.76198  -23.30639 7.98226   1.000 160.18991 ? 72  ARG B CD  1 
ATOM   3283 N NE  . ARG B 2 72  ? 20.41028  -23.33377 6.67716   1.000 156.69786 ? 72  ARG B NE  1 
ATOM   3284 C CZ  . ARG B 2 72  ? 19.78548  -23.58559 5.53528   1.000 155.63115 ? 72  ARG B CZ  1 
ATOM   3285 N NH1 . ARG B 2 72  ? 18.49301  -23.86606 5.50161   1.000 155.34017 ? 72  ARG B NH1 1 
ATOM   3286 N NH2 . ARG B 2 72  ? 20.47525  -23.55748 4.39860   1.000 157.19586 ? 72  ARG B NH2 1 
ATOM   3287 N N   . ASP B 2 73  ? 24.64395  -24.95253 8.91666   1.000 168.32549 ? 73  ASP B N   1 
ATOM   3288 C CA  . ASP B 2 73  ? 25.89478  -24.27692 8.59408   1.000 180.97735 ? 73  ASP B CA  1 
ATOM   3289 C C   . ASP B 2 73  ? 26.01566  -24.16152 7.08177   1.000 180.42027 ? 73  ASP B C   1 
ATOM   3290 O O   . ASP B 2 73  ? 25.94274  -25.16986 6.37075   1.000 180.10588 ? 73  ASP B O   1 
ATOM   3291 C CB  . ASP B 2 73  ? 27.08902  -25.03590 9.17675   1.000 185.41869 ? 73  ASP B CB  1 
ATOM   3292 C CG  . ASP B 2 73  ? 28.41489  -24.35735 8.88764   1.000 189.50744 ? 73  ASP B CG  1 
ATOM   3293 O OD1 . ASP B 2 73  ? 28.41625  -23.16829 8.50489   1.000 188.50457 ? 73  ASP B OD1 1 
ATOM   3294 O OD2 . ASP B 2 73  ? 29.46136  -25.01988 9.04329   1.000 192.54339 ? 73  ASP B OD2 1 
ATOM   3295 N N   . SER B 2 74  ? 26.21206  -22.93364 6.59634   1.000 175.31538 ? 74  SER B N   1 
ATOM   3296 C CA  . SER B 2 74  ? 26.31362  -22.71194 5.15769   1.000 173.31347 ? 74  SER B CA  1 
ATOM   3297 C C   . SER B 2 74  ? 27.65429  -23.18591 4.61000   1.000 178.07676 ? 74  SER B C   1 
ATOM   3298 O O   . SER B 2 74  ? 27.71314  -23.76546 3.51910   1.000 177.93034 ? 74  SER B O   1 
ATOM   3299 C CB  . SER B 2 74  ? 26.10441  -21.23166 4.84046   1.000 172.62020 ? 74  SER B CB  1 
ATOM   3300 O OG  . SER B 2 74  ? 26.32933  -20.97104 3.46570   1.000 173.42769 ? 74  SER B OG  1 
ATOM   3301 N N   . ALA B 2 75  ? 28.73982  -22.95094 5.35227   1.000 183.61800 ? 75  ALA B N   1 
ATOM   3302 C CA  . ALA B 2 75  ? 30.07479  -23.22973 4.83019   1.000 184.51589 ? 75  ALA B CA  1 
ATOM   3303 C C   . ALA B 2 75  ? 30.28898  -24.71945 4.58820   1.000 186.19218 ? 75  ALA B C   1 
ATOM   3304 O O   . ALA B 2 75  ? 30.96587  -25.10412 3.62740   1.000 186.38521 ? 75  ALA B O   1 
ATOM   3305 C CB  . ALA B 2 75  ? 31.13472  -22.68482 5.78673   1.000 187.33895 ? 75  ALA B CB  1 
ATOM   3306 N N   . GLN B 2 76  ? 29.72671  -25.57275 5.44283   1.000 185.63213 ? 76  GLN B N   1 
ATOM   3307 C CA  . GLN B 2 76  ? 29.90546  -27.01304 5.32337   1.000 186.38007 ? 76  GLN B CA  1 
ATOM   3308 C C   . GLN B 2 76  ? 28.65356  -27.74363 4.85535   1.000 183.32546 ? 76  GLN B C   1 
ATOM   3309 O O   . GLN B 2 76  ? 28.69326  -28.97085 4.71300   1.000 183.08124 ? 76  GLN B O   1 
ATOM   3310 C CB  . GLN B 2 76  ? 30.38195  -27.60130 6.65716   1.000 189.79816 ? 76  GLN B CB  1 
ATOM   3311 C CG  . GLN B 2 76  ? 31.87789  -27.44457 6.90673   1.000 193.08935 ? 76  GLN B CG  1 
ATOM   3312 C CD  . GLN B 2 76  ? 32.19796  -26.39193 7.95125   1.000 195.36326 ? 76  GLN B CD  1 
ATOM   3313 O OE1 . GLN B 2 76  ? 31.96020  -25.20170 7.74665   1.000 195.33548 ? 76  GLN B OE1 1 
ATOM   3314 N NE2 . GLN B 2 76  ? 32.74195  -26.82916 9.08129   1.000 197.24327 ? 76  GLN B NE2 1 
ATOM   3315 N N   . ASN B 2 77  ? 27.54912  -27.02972 4.61762   1.000 179.42694 ? 77  ASN B N   1 
ATOM   3316 C CA  . ASN B 2 77  ? 26.33942  -27.60387 4.02013   1.000 176.26786 ? 77  ASN B CA  1 
ATOM   3317 C C   . ASN B 2 77  ? 25.80681  -28.77912 4.84022   1.000 167.45430 ? 77  ASN B C   1 
ATOM   3318 O O   . ASN B 2 77  ? 25.60516  -29.88230 4.32831   1.000 168.41792 ? 77  ASN B O   1 
ATOM   3319 C CB  . ASN B 2 77  ? 26.59485  -28.02752 2.57042   1.000 177.72422 ? 77  ASN B CB  1 
ATOM   3320 C CG  . ASN B 2 77  ? 26.69051  -26.84950 1.62239   1.000 179.21577 ? 77  ASN B CG  1 
ATOM   3321 O OD1 . ASN B 2 77  ? 25.83884  -26.66976 0.75318   1.000 176.12419 ? 77  ASN B OD1 1 
ATOM   3322 N ND2 . ASN B 2 77  ? 27.73140  -26.04140 1.78249   1.000 180.52925 ? 77  ASN B ND2 1 
ATOM   3323 N N   . THR B 2 78  ? 25.57496  -28.53704 6.12875   1.000 171.63632 ? 78  THR B N   1 
ATOM   3324 C CA  . THR B 2 78  ? 25.10939  -29.58398 7.02593   1.000 171.80943 ? 78  THR B CA  1 
ATOM   3325 C C   . THR B 2 78  ? 23.99258  -29.05388 7.91299   1.000 169.01420 ? 78  THR B C   1 
ATOM   3326 O O   . THR B 2 78  ? 23.91687  -27.85668 8.20159   1.000 168.24428 ? 78  THR B O   1 
ATOM   3327 C CB  . THR B 2 78  ? 26.24560  -30.13594 7.90069   1.000 175.97557 ? 78  THR B CB  1 
ATOM   3328 O OG1 . THR B 2 78  ? 26.92929  -29.05252 8.54181   1.000 187.98864 ? 78  THR B OG1 1 
ATOM   3329 C CG2 . THR B 2 78  ? 27.23500  -30.93271 7.06107   1.000 176.49880 ? 78  THR B CG2 1 
ATOM   3330 N N   . LEU B 2 79  ? 23.12772  -29.96824 8.34135   1.000 178.24418 ? 79  LEU B N   1 
ATOM   3331 C CA  . LEU B 2 79  ? 22.01251  -29.67748 9.22744   1.000 172.55225 ? 79  LEU B CA  1 
ATOM   3332 C C   . LEU B 2 79  ? 22.23773  -30.37871 10.56163  1.000 171.85722 ? 79  LEU B C   1 
ATOM   3333 O O   . LEU B 2 79  ? 22.85675  -31.44448 10.61976  1.000 174.62302 ? 79  LEU B O   1 
ATOM   3334 C CB  . LEU B 2 79  ? 20.69237  -30.13562 8.59861   1.000 167.11326 ? 79  LEU B CB  1 
ATOM   3335 C CG  . LEU B 2 79  ? 19.37817  -29.50846 9.05968   1.000 163.26303 ? 79  LEU B CG  1 
ATOM   3336 C CD1 . LEU B 2 79  ? 19.37397  -28.01442 8.79226   1.000 161.65722 ? 79  LEU B CD1 1 
ATOM   3337 C CD2 . LEU B 2 79  ? 18.21283  -30.18306 8.35382   1.000 160.74031 ? 79  LEU B CD2 1 
ATOM   3338 N N   . TYR B 2 80  ? 21.73948  -29.77316 11.63847  1.000 168.51674 ? 80  TYR B N   1 
ATOM   3339 C CA  . TYR B 2 80  ? 21.96980  -30.29666 12.97755  1.000 168.52150 ? 80  TYR B CA  1 
ATOM   3340 C C   . TYR B 2 80  ? 20.68063  -30.24808 13.78403  1.000 163.30087 ? 80  TYR B C   1 
ATOM   3341 O O   . TYR B 2 80  ? 19.77147  -29.46407 13.50093  1.000 160.84305 ? 80  TYR B O   1 
ATOM   3342 C CB  . TYR B 2 80  ? 23.07627  -29.52002 13.70486  1.000 172.63108 ? 80  TYR B CB  1 
ATOM   3343 C CG  . TYR B 2 80  ? 24.39621  -29.51045 12.96759  1.000 180.16759 ? 80  TYR B CG  1 
ATOM   3344 C CD1 . TYR B 2 80  ? 25.29756  -30.55967 13.09973  1.000 191.55035 ? 80  TYR B CD1 1 
ATOM   3345 C CD2 . TYR B 2 80  ? 24.73951  -28.45333 12.13598  1.000 188.56247 ? 80  TYR B CD2 1 
ATOM   3346 C CE1 . TYR B 2 80  ? 26.50500  -30.55432 12.42415  1.000 195.91652 ? 80  TYR B CE1 1 
ATOM   3347 C CE2 . TYR B 2 80  ? 25.94284  -28.43903 11.45755  1.000 194.14642 ? 80  TYR B CE2 1 
ATOM   3348 C CZ  . TYR B 2 80  ? 26.82171  -29.49136 11.60483  1.000 197.34990 ? 80  TYR B CZ  1 
ATOM   3349 O OH  . TYR B 2 80  ? 28.02094  -29.48004 10.92995  1.000 201.13809 ? 80  TYR B OH  1 
ATOM   3350 N N   . LEU B 2 81  ? 20.61862  -31.10315 14.80669  1.000 169.45012 ? 81  LEU B N   1 
ATOM   3351 C CA  . LEU B 2 81  ? 19.45557  -31.17191 15.69343  1.000 168.17716 ? 81  LEU B CA  1 
ATOM   3352 C C   . LEU B 2 81  ? 19.96222  -31.59705 17.07347  1.000 170.28319 ? 81  LEU B C   1 
ATOM   3353 O O   . LEU B 2 81  ? 19.99094  -32.78596 17.39860  1.000 170.39957 ? 81  LEU B O   1 
ATOM   3354 C CB  . LEU B 2 81  ? 18.40357  -32.13190 15.15891  1.000 165.95527 ? 81  LEU B CB  1 
ATOM   3355 C CG  . LEU B 2 81  ? 17.02127  -32.03284 15.80400  1.000 164.67717 ? 81  LEU B CG  1 
ATOM   3356 C CD1 . LEU B 2 81  ? 16.40358  -30.67222 15.52075  1.000 163.92175 ? 81  LEU B CD1 1 
ATOM   3357 C CD2 . LEU B 2 81  ? 16.11523  -33.15163 15.31549  1.000 163.19204 ? 81  LEU B CD2 1 
ATOM   3358 N N   . GLN B 2 82  ? 20.36349  -30.61080 17.87277  1.000 181.93080 ? 82  GLN B N   1 
ATOM   3359 C CA  . GLN B 2 82  ? 20.86594  -30.86407 19.21947  1.000 189.97851 ? 82  GLN B CA  1 
ATOM   3360 C C   . GLN B 2 82  ? 19.68643  -31.13946 20.14384  1.000 191.64609 ? 82  GLN B C   1 
ATOM   3361 O O   . GLN B 2 82  ? 18.89479  -30.23793 20.43807  1.000 193.30026 ? 82  GLN B O   1 
ATOM   3362 C CB  . GLN B 2 82  ? 21.68971  -29.67960 19.71635  1.000 198.79380 ? 82  GLN B CB  1 
ATOM   3363 C CG  . GLN B 2 82  ? 22.27650  -29.88027 21.10450  1.000 203.02731 ? 82  GLN B CG  1 
ATOM   3364 C CD  . GLN B 2 82  ? 23.02889  -31.19154 21.23115  1.000 205.07678 ? 82  GLN B CD  1 
ATOM   3365 O OE1 . GLN B 2 82  ? 22.50156  -32.17575 21.75064  1.000 204.46988 ? 82  GLN B OE1 1 
ATOM   3366 N NE2 . GLN B 2 82  ? 24.26757  -31.21192 20.75310  1.000 207.82972 ? 82  GLN B NE2 1 
ATOM   3367 N N   . MET B 2 83  ? 19.57013  -32.38070 20.60697  1.000 197.87751 ? 83  MET B N   1 
ATOM   3368 C CA  . MET B 2 83  ? 18.46715  -32.80843 21.45658  1.000 196.54885 ? 83  MET B CA  1 
ATOM   3369 C C   . MET B 2 83  ? 18.99031  -33.14610 22.84721  1.000 201.68219 ? 83  MET B C   1 
ATOM   3370 O O   . MET B 2 83  ? 19.97267  -33.88255 22.98605  1.000 202.88754 ? 83  MET B O   1 
ATOM   3371 C CB  . MET B 2 83  ? 17.74157  -34.00895 20.84041  1.000 188.09515 ? 83  MET B CB  1 
ATOM   3372 C CG  . MET B 2 83  ? 18.63691  -35.19478 20.51227  1.000 185.53411 ? 83  MET B CG  1 
ATOM   3373 S SD  . MET B 2 83  ? 17.86616  -36.38610 19.40004  1.000 184.74194 ? 83  MET B SD  1 
ATOM   3374 C CE  . MET B 2 83  ? 17.96449  -35.50397 17.84430  1.000 186.68596 ? 83  MET B CE  1 
ATOM   3375 N N   . ASN B 2 84  ? 18.33801  -32.60064 23.86930  1.000 191.56683 ? 84  ASN B N   1 
ATOM   3376 C CA  . ASN B 2 84  ? 18.72560  -32.79609 25.25750  1.000 195.89364 ? 84  ASN B CA  1 
ATOM   3377 C C   . ASN B 2 84  ? 17.64447  -33.55999 26.01055  1.000 196.31954 ? 84  ASN B C   1 
ATOM   3378 O O   . ASN B 2 84  ? 16.49097  -33.63372 25.57750  1.000 193.60653 ? 84  ASN B O   1 
ATOM   3379 C CB  . ASN B 2 84  ? 18.97177  -31.45344 25.95658  1.000 199.83704 ? 84  ASN B CB  1 
ATOM   3380 C CG  . ASN B 2 84  ? 20.04000  -30.62272 25.27708  1.000 199.39232 ? 84  ASN B CG  1 
ATOM   3381 O OD1 . ASN B 2 84  ? 21.10428  -31.12789 24.92318  1.000 199.20924 ? 84  ASN B OD1 1 
ATOM   3382 N ND2 . ASN B 2 84  ? 19.76270  -29.33459 25.09792  1.000 199.80847 ? 84  ASN B ND2 1 
ATOM   3383 N N   . SER B 2 85  ? 18.04306  -34.12613 27.15260  1.000 198.15663 ? 85  SER B N   1 
ATOM   3384 C CA  . SER B 2 85  ? 17.12217  -34.71763 28.12578  1.000 200.18834 ? 85  SER B CA  1 
ATOM   3385 C C   . SER B 2 85  ? 16.14940  -35.68989 27.46035  1.000 196.30202 ? 85  SER B C   1 
ATOM   3386 O O   . SER B 2 85  ? 14.92778  -35.56302 27.56952  1.000 196.40601 ? 85  SER B O   1 
ATOM   3387 C CB  . SER B 2 85  ? 16.37150  -33.62203 28.88206  1.000 203.16335 ? 85  SER B CB  1 
ATOM   3388 O OG  . SER B 2 85  ? 15.58177  -34.16816 29.92038  1.000 206.53638 ? 85  SER B OG  1 
ATOM   3389 N N   . LEU B 2 86  ? 16.70931  -36.66827 26.75541  1.000 195.17362 ? 86  LEU B N   1 
ATOM   3390 C CA  . LEU B 2 86  ? 15.90685  -37.57795 25.95139  1.000 191.67875 ? 86  LEU B CA  1 
ATOM   3391 C C   . LEU B 2 86  ? 15.01782  -38.45453 26.82746  1.000 194.25915 ? 86  LEU B C   1 
ATOM   3392 O O   . LEU B 2 86  ? 15.38035  -38.83261 27.94467  1.000 198.67157 ? 86  LEU B O   1 
ATOM   3393 C CB  . LEU B 2 86  ? 16.81345  -38.44599 25.08154  1.000 190.02244 ? 86  LEU B CB  1 
ATOM   3394 C CG  . LEU B 2 86  ? 17.64697  -37.65322 24.07368  1.000 187.60706 ? 86  LEU B CG  1 
ATOM   3395 C CD1 . LEU B 2 86  ? 18.66487  -38.54764 23.39049  1.000 188.76817 ? 86  LEU B CD1 1 
ATOM   3396 C CD2 . LEU B 2 86  ? 16.74065  -36.98508 23.05000  1.000 185.32746 ? 86  LEU B CD2 1 
ATOM   3397 N N   . ARG B 2 87  ? 13.83774  -38.77547 26.30174  1.000 194.66104 ? 87  ARG B N   1 
ATOM   3398 C CA  . ARG B 2 87  ? 12.84218  -39.56859 27.00527  1.000 196.88605 ? 87  ARG B CA  1 
ATOM   3399 C C   . ARG B 2 87  ? 12.39428  -40.72287 26.11750  1.000 196.31413 ? 87  ARG B C   1 
ATOM   3400 O O   . ARG B 2 87  ? 12.71390  -40.78257 24.92692  1.000 194.04336 ? 87  ARG B O   1 
ATOM   3401 C CB  . ARG B 2 87  ? 11.64335  -38.70506 27.42409  1.000 198.13239 ? 87  ARG B CB  1 
ATOM   3402 C CG  . ARG B 2 87  ? 12.02276  -37.54115 28.32973  1.000 199.27442 ? 87  ARG B CG  1 
ATOM   3403 C CD  . ARG B 2 87  ? 10.83596  -36.64627 28.65203  1.000 201.23048 ? 87  ARG B CD  1 
ATOM   3404 N NE  . ARG B 2 87  ? 10.22859  -36.07674 27.45519  1.000 199.33958 ? 87  ARG B NE  1 
ATOM   3405 C CZ  . ARG B 2 87  ? 9.61791   -34.90025 27.41567  1.000 200.13951 ? 87  ARG B CZ  1 
ATOM   3406 N NH1 . ARG B 2 87  ? 9.55300   -34.11939 28.48175  1.000 202.50187 ? 87  ARG B NH1 1 
ATOM   3407 N NH2 . ARG B 2 87  ? 9.06957   -34.49132 26.27502  1.000 198.87184 ? 87  ARG B NH2 1 
ATOM   3408 N N   . SER B 2 88  ? 11.63375  -41.64518 26.71582  1.000 201.06642 ? 88  SER B N   1 
ATOM   3409 C CA  . SER B 2 88  ? 11.20753  -42.84335 25.99766  1.000 201.34267 ? 88  SER B CA  1 
ATOM   3410 C C   . SER B 2 88  ? 10.32893  -42.50818 24.79925  1.000 199.44219 ? 88  SER B C   1 
ATOM   3411 O O   . SER B 2 88  ? 10.26068  -43.29021 23.84401  1.000 198.56961 ? 88  SER B O   1 
ATOM   3412 C CB  . SER B 2 88  ? 10.46860  -43.78767 26.94628  1.000 205.30781 ? 88  SER B CB  1 
ATOM   3413 O OG  . SER B 2 88  ? 9.31961   -43.16446 27.49329  1.000 207.42425 ? 88  SER B OG  1 
ATOM   3414 N N   . GLU B 2 89  ? 9.64918   -41.35932 24.82944  1.000 206.10236 ? 89  GLU B N   1 
ATOM   3415 C CA  . GLU B 2 89  ? 8.82180   -40.95952 23.69626  1.000 204.77127 ? 89  GLU B CA  1 
ATOM   3416 C C   . GLU B 2 89  ? 9.66216   -40.66915 22.45951  1.000 200.12954 ? 89  GLU B C   1 
ATOM   3417 O O   . GLU B 2 89  ? 9.19433   -40.86921 21.33266  1.000 198.90209 ? 89  GLU B O   1 
ATOM   3418 C CB  . GLU B 2 89  ? 7.98576   -39.73471 24.06518  1.000 206.14174 ? 89  GLU B CB  1 
ATOM   3419 C CG  . GLU B 2 89  ? 7.05822   -39.94749 25.24884  1.000 211.07680 ? 89  GLU B CG  1 
ATOM   3420 C CD  . GLU B 2 89  ? 6.40035   -38.66163 25.70765  1.000 213.19146 ? 89  GLU B CD  1 
ATOM   3421 O OE1 . GLU B 2 89  ? 6.88592   -37.57614 25.32515  1.000 210.53840 ? 89  GLU B OE1 1 
ATOM   3422 O OE2 . GLU B 2 89  ? 5.39780   -38.73596 26.44882  1.000 218.11201 ? 89  GLU B OE2 1 
ATOM   3423 N N   . ASP B 2 90  ? 10.89929  -40.20739 22.64633  1.000 206.90689 ? 90  ASP B N   1 
ATOM   3424 C CA  . ASP B 2 90  ? 11.77547  -39.86806 21.53122  1.000 194.23110 ? 90  ASP B CA  1 
ATOM   3425 C C   . ASP B 2 90  ? 12.34402  -41.09078 20.82214  1.000 192.22214 ? 90  ASP B C   1 
ATOM   3426 O O   . ASP B 2 90  ? 13.15483  -40.92426 19.90378  1.000 189.17434 ? 90  ASP B O   1 
ATOM   3427 C CB  . ASP B 2 90  ? 12.91858  -38.97791 22.02251  1.000 191.38988 ? 90  ASP B CB  1 
ATOM   3428 C CG  . ASP B 2 90  ? 12.42568  -37.77874 22.80766  1.000 191.81849 ? 90  ASP B CG  1 
ATOM   3429 O OD1 . ASP B 2 90  ? 11.96865  -37.96564 23.95496  1.000 203.86382 ? 90  ASP B OD1 1 
ATOM   3430 O OD2 . ASP B 2 90  ? 12.49305  -36.65002 22.27793  1.000 190.90594 ? 90  ASP B OD2 1 
ATOM   3431 N N   . THR B 2 91  ? 11.95002  -42.29909 21.21752  1.000 199.56281 ? 91  THR B N   1 
ATOM   3432 C CA  . THR B 2 91  ? 12.41948  -43.52519 20.57523  1.000 200.30662 ? 91  THR B CA  1 
ATOM   3433 C C   . THR B 2 91  ? 11.83911  -43.58902 19.16877  1.000 195.15063 ? 91  THR B C   1 
ATOM   3434 O O   . THR B 2 91  ? 10.71051  -44.04344 18.96912  1.000 197.93190 ? 91  THR B O   1 
ATOM   3435 C CB  . THR B 2 91  ? 12.01104  -44.74466 21.39462  1.000 205.31273 ? 91  THR B CB  1 
ATOM   3436 O OG1 . THR B 2 91  ? 12.37161  -44.54324 22.76711  1.000 212.54976 ? 91  THR B OG1 1 
ATOM   3437 C CG2 . THR B 2 91  ? 12.70504  -45.99541 20.87392  1.000 205.83503 ? 91  THR B CG2 1 
ATOM   3438 N N   . ALA B 2 92  ? 12.60898  -43.13219 18.18390  1.000 196.47601 ? 92  ALA B N   1 
ATOM   3439 C CA  . ALA B 2 92  ? 12.11086  -43.03440 16.81892  1.000 198.13078 ? 92  ALA B CA  1 
ATOM   3440 C C   . ALA B 2 92  ? 13.28768  -42.90987 15.86131  1.000 198.48173 ? 92  ALA B C   1 
ATOM   3441 O O   . ALA B 2 92  ? 14.43465  -42.71958 16.27254  1.000 201.44872 ? 92  ALA B O   1 
ATOM   3442 C CB  . ALA B 2 92  ? 11.15707  -41.84578 16.66498  1.000 198.42956 ? 92  ALA B CB  1 
ATOM   3443 N N   . THR B 2 93  ? 12.98163  -43.02263 14.57042  1.000 196.33754 ? 93  THR B N   1 
ATOM   3444 C CA  . THR B 2 93  ? 13.94213  -42.78925 13.49961  1.000 196.25696 ? 93  THR B CA  1 
ATOM   3445 C C   . THR B 2 93  ? 13.73199  -41.38258 12.95492  1.000 194.64393 ? 93  THR B C   1 
ATOM   3446 O O   . THR B 2 93  ? 12.60393  -41.00424 12.62243  1.000 193.82163 ? 93  THR B O   1 
ATOM   3447 C CB  . THR B 2 93  ? 13.78554  -43.82275 12.38188  1.000 198.14472 ? 93  THR B CB  1 
ATOM   3448 O OG1 . THR B 2 93  ? 14.00642  -45.13747 12.90826  1.000 202.49530 ? 93  THR B OG1 1 
ATOM   3449 C CG2 . THR B 2 93  ? 14.78088  -43.55663 11.26194  1.000 200.59219 ? 93  THR B CG2 1 
ATOM   3450 N N   . TYR B 2 94  ? 14.81362  -40.61417 12.86766  1.000 188.65342 ? 94  TYR B N   1 
ATOM   3451 C CA  . TYR B 2 94  ? 14.75137  -39.19125 12.56139  1.000 183.93678 ? 94  TYR B CA  1 
ATOM   3452 C C   . TYR B 2 94  ? 15.23589  -38.93624 11.14047  1.000 186.06533 ? 94  TYR B C   1 
ATOM   3453 O O   . TYR B 2 94  ? 16.29422  -39.43302 10.74060  1.000 195.19906 ? 94  TYR B O   1 
ATOM   3454 C CB  . TYR B 2 94  ? 15.58404  -38.38958 13.56484  1.000 184.02955 ? 94  TYR B CB  1 
ATOM   3455 C CG  . TYR B 2 94  ? 14.99383  -38.36027 14.95956  1.000 183.15121 ? 94  TYR B CG  1 
ATOM   3456 C CD1 . TYR B 2 94  ? 14.97629  -39.50013 15.75466  1.000 186.41833 ? 94  TYR B CD1 1 
ATOM   3457 C CD2 . TYR B 2 94  ? 14.45869  -37.19084 15.48230  1.000 184.60113 ? 94  TYR B CD2 1 
ATOM   3458 C CE1 . TYR B 2 94  ? 14.43656  -39.47720 17.02641  1.000 190.01639 ? 94  TYR B CE1 1 
ATOM   3459 C CE2 . TYR B 2 94  ? 13.92087  -37.15726 16.75490  1.000 186.09070 ? 94  TYR B CE2 1 
ATOM   3460 C CZ  . TYR B 2 94  ? 13.91121  -38.30322 17.52186  1.000 188.65771 ? 94  TYR B CZ  1 
ATOM   3461 O OH  . TYR B 2 94  ? 13.37425  -38.27435 18.78848  1.000 192.34198 ? 94  TYR B OH  1 
ATOM   3462 N N   . TYR B 2 95  ? 14.46313  -38.15323 10.38972  1.000 174.35227 ? 95  TYR B N   1 
ATOM   3463 C CA  . TYR B 2 95  ? 14.74973  -37.83428 8.99808   1.000 177.51746 ? 95  TYR B CA  1 
ATOM   3464 C C   . TYR B 2 95  ? 14.91821  -36.32968 8.84046   1.000 176.23880 ? 95  TYR B C   1 
ATOM   3465 O O   . TYR B 2 95  ? 14.23805  -35.54722 9.51164   1.000 173.94490 ? 95  TYR B O   1 
ATOM   3466 C CB  . TYR B 2 95  ? 13.62193  -38.31103 8.06760   1.000 176.60033 ? 95  TYR B CB  1 
ATOM   3467 C CG  . TYR B 2 95  ? 13.30662  -39.79126 8.12426   1.000 181.71925 ? 95  TYR B CG  1 
ATOM   3468 C CD1 . TYR B 2 95  ? 12.61925  -40.33746 9.20215   1.000 180.49592 ? 95  TYR B CD1 1 
ATOM   3469 C CD2 . TYR B 2 95  ? 13.66393  -40.63551 7.08107   1.000 186.16135 ? 95  TYR B CD2 1 
ATOM   3470 C CE1 . TYR B 2 95  ? 12.32059  -41.68559 9.25127   1.000 181.48569 ? 95  TYR B CE1 1 
ATOM   3471 C CE2 . TYR B 2 95  ? 13.36797  -41.98478 7.12035   1.000 187.97555 ? 95  TYR B CE2 1 
ATOM   3472 C CZ  . TYR B 2 95  ? 12.69605  -42.50423 8.20729   1.000 186.53468 ? 95  TYR B CZ  1 
ATOM   3473 O OH  . TYR B 2 95  ? 12.39929  -43.84720 8.25002   1.000 190.70013 ? 95  TYR B OH  1 
ATOM   3474 N N   . CYS B 2 96  ? 15.81891  -35.92667 7.94793   1.000 169.80228 ? 96  CYS B N   1 
ATOM   3475 C CA  . CYS B 2 96  ? 15.94526  -34.53573 7.53578   1.000 169.55974 ? 96  CYS B CA  1 
ATOM   3476 C C   . CYS B 2 96  ? 15.40692  -34.37777 6.11991   1.000 172.68152 ? 96  CYS B C   1 
ATOM   3477 O O   . CYS B 2 96  ? 15.60097  -35.25295 5.26999   1.000 181.36124 ? 96  CYS B O   1 
ATOM   3478 C CB  . CYS B 2 96  ? 17.39820  -34.05189 7.60857   1.000 171.33445 ? 96  CYS B CB  1 
ATOM   3479 S SG  . CYS B 2 96  ? 18.62720  -35.06363 6.73877   1.000 182.97985 ? 96  CYS B SG  1 
ATOM   3480 N N   . THR B 2 97  ? 14.71393  -33.26595 5.87498   1.000 153.30168 ? 97  THR B N   1 
ATOM   3481 C CA  . THR B 2 97  ? 14.07316  -33.01207 4.59309   1.000 158.32181 ? 97  THR B CA  1 
ATOM   3482 C C   . THR B 2 97  ? 14.40802  -31.61052 4.10599   1.000 157.91701 ? 97  THR B C   1 
ATOM   3483 O O   . THR B 2 97  ? 14.65738  -30.70051 4.90155   1.000 156.54871 ? 97  THR B O   1 
ATOM   3484 C CB  . THR B 2 97  ? 12.53875  -33.14651 4.67438   1.000 161.93485 ? 97  THR B CB  1 
ATOM   3485 O OG1 . THR B 2 97  ? 11.98178  -31.95685 5.24846   1.000 159.47802 ? 97  THR B OG1 1 
ATOM   3486 C CG2 . THR B 2 97  ? 12.13702  -34.34126 5.52543   1.000 158.76823 ? 97  THR B CG2 1 
ATOM   3487 N N   . ARG B 2 98  ? 14.40363  -31.44676 2.78627   1.000 152.40854 ? 98  ARG B N   1 
ATOM   3488 C CA  . ARG B 2 98  ? 14.39659  -30.13336 2.15808   1.000 153.96321 ? 98  ARG B CA  1 
ATOM   3489 C C   . ARG B 2 98  ? 12.95644  -29.78342 1.81188   1.000 156.15322 ? 98  ARG B C   1 
ATOM   3490 O O   . ARG B 2 98  ? 12.24011  -30.60268 1.22761   1.000 159.88790 ? 98  ARG B O   1 
ATOM   3491 C CB  . ARG B 2 98  ? 15.26648  -30.10575 0.89953   1.000 157.46842 ? 98  ARG B CB  1 
ATOM   3492 C CG  . ARG B 2 98  ? 15.42799  -28.71351 0.30735   1.000 160.50009 ? 98  ARG B CG  1 
ATOM   3493 C CD  . ARG B 2 98  ? 16.18864  -28.71878 -1.01238  1.000 165.71829 ? 98  ARG B CD  1 
ATOM   3494 N NE  . ARG B 2 98  ? 15.32162  -28.98983 -2.15326  1.000 170.13794 ? 98  ARG B NE  1 
ATOM   3495 C CZ  . ARG B 2 98  ? 15.62033  -28.68288 -3.40853  1.000 173.35001 ? 98  ARG B CZ  1 
ATOM   3496 N NH1 . ARG B 2 98  ? 16.75480  -28.07953 -3.72116  1.000 177.90093 ? 98  ARG B NH1 1 
ATOM   3497 N NH2 . ARG B 2 98  ? 14.75504  -28.98037 -4.37345  1.000 176.55117 ? 98  ARG B NH2 1 
ATOM   3498 N N   . ASP B 2 99  ? 12.52723  -28.58387 2.19112   1.000 164.73590 ? 99  ASP B N   1 
ATOM   3499 C CA  . ASP B 2 99  ? 11.16029  -28.15032 1.95702   1.000 165.33564 ? 99  ASP B CA  1 
ATOM   3500 C C   . ASP B 2 99  ? 11.13046  -26.89771 1.09496   1.000 168.65163 ? 99  ASP B C   1 
ATOM   3501 O O   . ASP B 2 99  ? 12.05752  -26.08369 1.11159   1.000 166.74254 ? 99  ASP B O   1 
ATOM   3502 C CB  . ASP B 2 99  ? 10.41375  -27.86439 3.26875   1.000 161.88089 ? 99  ASP B CB  1 
ATOM   3503 C CG  . ASP B 2 99  ? 11.29267  -28.01743 4.49131   1.000 161.23514 ? 99  ASP B CG  1 
ATOM   3504 O OD1 . ASP B 2 99  ? 12.02593  -29.02407 4.58131   1.000 162.56197 ? 99  ASP B OD1 1 
ATOM   3505 O OD2 . ASP B 2 99  ? 11.24521  -27.12626 5.36590   1.000 158.15904 ? 99  ASP B OD2 1 
ATOM   3506 N N   . LEU B 2 100 ? 10.04533  -26.75894 0.34037   1.000 165.57257 ? 100 LEU B N   1 
ATOM   3507 C CA  . LEU B 2 100 ? 9.70438   -25.51784 -0.33542  1.000 168.25429 ? 100 LEU B CA  1 
ATOM   3508 C C   . LEU B 2 100 ? 8.64938   -24.82148 0.51368   1.000 168.31407 ? 100 LEU B C   1 
ATOM   3509 O O   . LEU B 2 100 ? 7.53106   -25.32620 0.65946   1.000 168.88284 ? 100 LEU B O   1 
ATOM   3510 C CB  . LEU B 2 100 ? 9.18673   -25.78157 -1.74941  1.000 172.14976 ? 100 LEU B CB  1 
ATOM   3511 C CG  . LEU B 2 100 ? 10.06879  -26.62386 -2.67199  1.000 174.98177 ? 100 LEU B CG  1 
ATOM   3512 C CD1 . LEU B 2 100 ? 9.46794   -26.69085 -4.06784  1.000 180.30368 ? 100 LEU B CD1 1 
ATOM   3513 C CD2 . LEU B 2 100 ? 11.48470  -26.07552 -2.72107  1.000 175.70585 ? 100 LEU B CD2 1 
ATOM   3514 N N   . ARG B 2 101 ? 9.00854   -23.67235 1.08863   1.000 173.39415 ? 101 ARG B N   1 
ATOM   3515 C CA  . ARG B 2 101 ? 8.06093   -22.94582 1.92463   1.000 170.82752 ? 101 ARG B CA  1 
ATOM   3516 C C   . ARG B 2 101 ? 6.87361   -22.42484 1.12537   1.000 176.29573 ? 101 ARG B C   1 
ATOM   3517 O O   . ARG B 2 101 ? 5.80514   -22.19615 1.70202   1.000 179.22369 ? 101 ARG B O   1 
ATOM   3518 C CB  . ARG B 2 101 ? 8.76695   -21.79376 2.64440   1.000 168.93836 ? 101 ARG B CB  1 
ATOM   3519 C CG  . ARG B 2 101 ? 7.89569   -21.02132 3.63487   1.000 168.70024 ? 101 ARG B CG  1 
ATOM   3520 C CD  . ARG B 2 101 ? 7.65950   -21.77385 4.94621   1.000 169.17851 ? 101 ARG B CD  1 
ATOM   3521 N NE  . ARG B 2 101 ? 6.72752   -22.88912 4.81837   1.000 172.11649 ? 101 ARG B NE  1 
ATOM   3522 C CZ  . ARG B 2 101 ? 7.05037   -24.16316 4.99883   1.000 169.95319 ? 101 ARG B CZ  1 
ATOM   3523 N NH1 . ARG B 2 101 ? 8.27620   -24.52487 5.33973   1.000 164.92112 ? 101 ARG B NH1 1 
ATOM   3524 N NH2 . ARG B 2 101 ? 6.11836   -25.09798 4.83785   1.000 168.91690 ? 101 ARG B NH2 1 
ATOM   3525 N N   . MET B 2 102 ? 7.02804   -22.24956 -0.18897  1.000 165.70920 ? 102 MET B N   1 
ATOM   3526 C CA  . MET B 2 102 ? 5.91108   -21.77567 -0.99893  1.000 169.96718 ? 102 MET B CA  1 
ATOM   3527 C C   . MET B 2 102 ? 4.88033   -22.87443 -1.22352  1.000 177.93395 ? 102 MET B C   1 
ATOM   3528 O O   . MET B 2 102 ? 3.67308   -22.60837 -1.21970  1.000 181.42168 ? 102 MET B O   1 
ATOM   3529 C CB  . MET B 2 102 ? 6.41766   -21.23217 -2.33461  1.000 173.82571 ? 102 MET B CB  1 
ATOM   3530 C CG  . MET B 2 102 ? 7.15770   -19.91280 -2.21467  1.000 177.01186 ? 102 MET B CG  1 
ATOM   3531 S SD  . MET B 2 102 ? 6.24255   -18.71649 -1.22157  1.000 175.60746 ? 102 MET B SD  1 
ATOM   3532 C CE  . MET B 2 102 ? 4.72987   -18.56230 -2.17016  1.000 182.24659 ? 102 MET B CE  1 
ATOM   3533 N N   . SER B 2 103 ? 5.33048   -24.11115 -1.41944  1.000 172.21145 ? 103 SER B N   1 
ATOM   3534 C CA  . SER B 2 103 ? 4.43133   -25.23200 -1.65344  1.000 173.73017 ? 103 SER B CA  1 
ATOM   3535 C C   . SER B 2 103 ? 4.15416   -26.04501 -0.39508  1.000 170.41053 ? 103 SER B C   1 
ATOM   3536 O O   . SER B 2 103 ? 3.40227   -27.02292 -0.46183  1.000 177.13359 ? 103 SER B O   1 
ATOM   3537 C CB  . SER B 2 103 ? 4.99870   -26.13992 -2.74811  1.000 175.08816 ? 103 SER B CB  1 
ATOM   3538 O OG  . SER B 2 103 ? 5.19048   -25.42397 -3.95601  1.000 194.92963 ? 103 SER B OG  1 
ATOM   3539 N N   . ASP B 2 104 ? 4.74332   -25.66396 0.73992   1.000 172.48749 ? 104 ASP B N   1 
ATOM   3540 C CA  . ASP B 2 104 ? 4.48664   -26.29277 2.03815   1.000 170.81619 ? 104 ASP B CA  1 
ATOM   3541 C C   . ASP B 2 104 ? 4.64087   -27.80993 1.97147   1.000 171.02771 ? 104 ASP B C   1 
ATOM   3542 O O   . ASP B 2 104 ? 3.79964   -28.56707 2.46086   1.000 171.76930 ? 104 ASP B O   1 
ATOM   3543 C CB  . ASP B 2 104 ? 3.09948   -25.91786 2.56452   1.000 174.07784 ? 104 ASP B CB  1 
ATOM   3544 C CG  . ASP B 2 104 ? 2.83702   -24.43108 2.50879   1.000 179.53923 ? 104 ASP B CG  1 
ATOM   3545 O OD1 . ASP B 2 104 ? 3.51590   -23.74419 1.72009   1.000 180.53544 ? 104 ASP B OD1 1 
ATOM   3546 O OD2 . ASP B 2 104 ? 1.95709   -23.95033 3.25449   1.000 182.98969 ? 104 ASP B OD2 1 
ATOM   3547 N N   . TYR B 2 105 ? 5.73230   -28.26146 1.35916   1.000 167.51467 ? 105 TYR B N   1 
ATOM   3548 C CA  . TYR B 2 105 ? 5.93213   -29.69202 1.18651   1.000 166.35712 ? 105 TYR B CA  1 
ATOM   3549 C C   . TYR B 2 105 ? 7.41964   -30.00122 1.11070   1.000 164.77175 ? 105 TYR B C   1 
ATOM   3550 O O   . TYR B 2 105 ? 8.25554   -29.11501 0.91897   1.000 168.21561 ? 105 TYR B O   1 
ATOM   3551 C CB  . TYR B 2 105 ? 5.19719   -30.20856 -0.05552  1.000 169.12826 ? 105 TYR B CB  1 
ATOM   3552 C CG  . TYR B 2 105 ? 6.04192   -30.28681 -1.30467  1.000 173.95114 ? 105 TYR B CG  1 
ATOM   3553 C CD1 . TYR B 2 105 ? 6.37155   -29.14420 -2.01656  1.000 177.91479 ? 105 TYR B CD1 1 
ATOM   3554 C CD2 . TYR B 2 105 ? 6.49168   -31.50880 -1.78305  1.000 174.99272 ? 105 TYR B CD2 1 
ATOM   3555 C CE1 . TYR B 2 105 ? 7.13448   -29.21283 -3.16348  1.000 182.52331 ? 105 TYR B CE1 1 
ATOM   3556 C CE2 . TYR B 2 105 ? 7.25534   -31.58886 -2.92832  1.000 178.07331 ? 105 TYR B CE2 1 
ATOM   3557 C CZ  . TYR B 2 105 ? 7.57501   -30.43773 -3.61466  1.000 182.78213 ? 105 TYR B CZ  1 
ATOM   3558 O OH  . TYR B 2 105 ? 8.33660   -30.51321 -4.75754  1.000 198.28108 ? 105 TYR B OH  1 
ATOM   3559 N N   . PHE B 2 106 ? 7.73676   -31.28650 1.26186   1.000 171.25671 ? 106 PHE B N   1 
ATOM   3560 C CA  . PHE B 2 106 ? 9.10907   -31.78386 1.26972   1.000 170.77432 ? 106 PHE B CA  1 
ATOM   3561 C C   . PHE B 2 106 ? 9.36277   -32.50016 -0.05085  1.000 174.70891 ? 106 PHE B C   1 
ATOM   3562 O O   . PHE B 2 106 ? 8.74743   -33.53564 -0.32789  1.000 175.48609 ? 106 PHE B O   1 
ATOM   3563 C CB  . PHE B 2 106 ? 9.34447   -32.72870 2.44768   1.000 167.05194 ? 106 PHE B CB  1 
ATOM   3564 C CG  . PHE B 2 106 ? 8.93149   -32.16679 3.77936   1.000 163.75264 ? 106 PHE B CG  1 
ATOM   3565 C CD1 . PHE B 2 106 ? 9.03125   -30.81364 4.04228   1.000 163.50088 ? 106 PHE B CD1 1 
ATOM   3566 C CD2 . PHE B 2 106 ? 8.44418   -32.99976 4.77097   1.000 161.40211 ? 106 PHE B CD2 1 
ATOM   3567 C CE1 . PHE B 2 106 ? 8.65222   -30.29895 5.26729   1.000 161.40364 ? 106 PHE B CE1 1 
ATOM   3568 C CE2 . PHE B 2 106 ? 8.06346   -32.49393 5.99667   1.000 159.21385 ? 106 PHE B CE2 1 
ATOM   3569 C CZ  . PHE B 2 106 ? 8.16765   -31.14103 6.24604   1.000 159.39815 ? 106 PHE B CZ  1 
ATOM   3570 N N   . ASP B 2 107 ? 10.27000  -31.95645 -0.86217  1.000 170.12039 ? 107 ASP B N   1 
ATOM   3571 C CA  . ASP B 2 107 ? 10.58829  -32.60375 -2.13040  1.000 175.31822 ? 107 ASP B CA  1 
ATOM   3572 C C   . ASP B 2 107 ? 11.56039  -33.76353 -1.93569  1.000 172.98327 ? 107 ASP B C   1 
ATOM   3573 O O   . ASP B 2 107 ? 11.28521  -34.88924 -2.36483  1.000 179.52359 ? 107 ASP B O   1 
ATOM   3574 C CB  . ASP B 2 107 ? 11.14172  -31.57771 -3.12474  1.000 177.83574 ? 107 ASP B CB  1 
ATOM   3575 C CG  . ASP B 2 107 ? 12.15302  -30.63815 -2.50084  1.000 177.49121 ? 107 ASP B CG  1 
ATOM   3576 O OD1 . ASP B 2 107 ? 12.70457  -30.97414 -1.43409  1.000 174.73761 ? 107 ASP B OD1 1 
ATOM   3577 O OD2 . ASP B 2 107 ? 12.39265  -29.55662 -3.07946  1.000 179.83662 ? 107 ASP B OD2 1 
ATOM   3578 N N   . TYR B 2 108 ? 12.68906  -33.51683 -1.27681  1.000 167.79842 ? 108 TYR B N   1 
ATOM   3579 C CA  . TYR B 2 108 ? 13.70925  -34.53306 -1.06810  1.000 171.02224 ? 108 TYR B CA  1 
ATOM   3580 C C   . TYR B 2 108 ? 13.83597  -34.86766 0.41317   1.000 166.53915 ? 108 TYR B C   1 
ATOM   3581 O O   . TYR B 2 108 ? 13.64319  -34.01198 1.28214   1.000 164.80591 ? 108 TYR B O   1 
ATOM   3582 C CB  . TYR B 2 108 ? 15.06164  -34.07302 -1.62204  1.000 169.69818 ? 108 TYR B CB  1 
ATOM   3583 C CG  . TYR B 2 108 ? 15.02228  -33.73092 -3.09435  1.000 177.72565 ? 108 TYR B CG  1 
ATOM   3584 C CD1 . TYR B 2 108 ? 15.16640  -34.71705 -4.06164  1.000 186.26576 ? 108 TYR B CD1 1 
ATOM   3585 C CD2 . TYR B 2 108 ? 14.83368  -32.42280 -3.51693  1.000 179.01579 ? 108 TYR B CD2 1 
ATOM   3586 C CE1 . TYR B 2 108 ? 15.12611  -34.40790 -5.40877  1.000 199.05292 ? 108 TYR B CE1 1 
ATOM   3587 C CE2 . TYR B 2 108 ? 14.79162  -32.10507 -4.86018  1.000 194.16290 ? 108 TYR B CE2 1 
ATOM   3588 C CZ  . TYR B 2 108 ? 14.93854  -33.09975 -5.80134  1.000 200.68355 ? 108 TYR B CZ  1 
ATOM   3589 O OH  . TYR B 2 108 ? 14.89738  -32.78260 -7.13935  1.000 204.11747 ? 108 TYR B OH  1 
ATOM   3590 N N   . TRP B 2 109 ? 14.15999  -36.12913 0.68957   1.000 177.49690 ? 109 TRP B N   1 
ATOM   3591 C CA  . TRP B 2 109 ? 14.27676  -36.64540 2.04572   1.000 174.42989 ? 109 TRP B CA  1 
ATOM   3592 C C   . TRP B 2 109 ? 15.62896  -37.32702 2.21544   1.000 176.79373 ? 109 TRP B C   1 
ATOM   3593 O O   . TRP B 2 109 ? 16.35207  -37.57650 1.24740   1.000 178.85820 ? 109 TRP B O   1 
ATOM   3594 C CB  . TRP B 2 109 ? 13.14462  -37.63162 2.37016   1.000 175.20793 ? 109 TRP B CB  1 
ATOM   3595 C CG  . TRP B 2 109 ? 11.77331  -37.01927 2.41384   1.000 172.61507 ? 109 TRP B CG  1 
ATOM   3596 C CD1 . TRP B 2 109 ? 11.14835  -36.32800 1.41636   1.000 174.77650 ? 109 TRP B CD1 1 
ATOM   3597 C CD2 . TRP B 2 109 ? 10.84668  -37.07187 3.50515   1.000 166.47775 ? 109 TRP B CD2 1 
ATOM   3598 N NE1 . TRP B 2 109 ? 9.89760   -35.93354 1.82475   1.000 172.21618 ? 109 TRP B NE1 1 
ATOM   3599 C CE2 . TRP B 2 109 ? 9.68745   -36.37931 3.10309   1.000 167.24261 ? 109 TRP B CE2 1 
ATOM   3600 C CE3 . TRP B 2 109 ? 10.88737  -37.63254 4.78528   1.000 163.88295 ? 109 TRP B CE3 1 
ATOM   3601 C CZ2 . TRP B 2 109 ? 8.57880   -36.23477 3.93419   1.000 164.24529 ? 109 TRP B CZ2 1 
ATOM   3602 C CZ3 . TRP B 2 109 ? 9.78718   -37.48532 5.60965   1.000 163.21071 ? 109 TRP B CZ3 1 
ATOM   3603 C CH2 . TRP B 2 109 ? 8.64897   -36.79152 5.18145   1.000 163.44403 ? 109 TRP B CH2 1 
ATOM   3604 N N   . GLY B 2 110 ? 15.96716  -37.63520 3.46863   1.000 182.37227 ? 110 GLY B N   1 
ATOM   3605 C CA  . GLY B 2 110 ? 17.20777  -38.29655 3.80142   1.000 180.28305 ? 110 GLY B CA  1 
ATOM   3606 C C   . GLY B 2 110 ? 16.98766  -39.73369 4.25399   1.000 180.91214 ? 110 GLY B C   1 
ATOM   3607 O O   . GLY B 2 110 ? 15.86383  -40.18071 4.47310   1.000 181.52654 ? 110 GLY B O   1 
ATOM   3608 N N   . GLN B 2 111 ? 18.10659  -40.45222 4.39891   1.000 183.20584 ? 111 GLN B N   1 
ATOM   3609 C CA  . GLN B 2 111 ? 18.06220  -41.86240 4.78234   1.000 184.45468 ? 111 GLN B CA  1 
ATOM   3610 C C   . GLN B 2 111 ? 17.24828  -42.07444 6.05294   1.000 179.53312 ? 111 GLN B C   1 
ATOM   3611 O O   . GLN B 2 111 ? 16.34467  -42.91706 6.09598   1.000 181.48601 ? 111 GLN B O   1 
ATOM   3612 C CB  . GLN B 2 111 ? 19.48187  -42.39852 4.97633   1.000 190.10879 ? 111 GLN B CB  1 
ATOM   3613 C CG  . GLN B 2 111 ? 20.28938  -42.56645 3.70400   1.000 193.39451 ? 111 GLN B CG  1 
ATOM   3614 C CD  . GLN B 2 111 ? 21.68279  -43.09907 3.98127   1.000 200.92978 ? 111 GLN B CD  1 
ATOM   3615 O OE1 . GLN B 2 111 ? 22.20973  -42.94274 5.08345   1.000 200.07791 ? 111 GLN B OE1 1 
ATOM   3616 N NE2 . GLN B 2 111 ? 22.28305  -43.74040 2.98494   1.000 206.74721 ? 111 GLN B NE2 1 
ATOM   3617 N N   . GLY B 2 112 ? 17.55914  -41.31788 7.10025   1.000 193.54123 ? 112 GLY B N   1 
ATOM   3618 C CA  . GLY B 2 112 ? 16.88974  -41.48495 8.37304   1.000 185.81997 ? 112 GLY B CA  1 
ATOM   3619 C C   . GLY B 2 112 ? 17.61979  -42.44498 9.28758   1.000 189.60832 ? 112 GLY B C   1 
ATOM   3620 O O   . GLY B 2 112 ? 17.55391  -43.66365 9.09893   1.000 194.86078 ? 112 GLY B O   1 
ATOM   3621 N N   . VAL B 2 113 ? 18.32569  -41.90902 10.27764  1.000 206.15202 ? 113 VAL B N   1 
ATOM   3622 C CA  . VAL B 2 113 ? 19.05985  -42.72197 11.23975  1.000 209.51809 ? 113 VAL B CA  1 
ATOM   3623 C C   . VAL B 2 113 ? 18.16797  -42.98449 12.44568  1.000 207.50775 ? 113 VAL B C   1 
ATOM   3624 O O   . VAL B 2 113 ? 17.34020  -42.15214 12.83255  1.000 204.97139 ? 113 VAL B O   1 
ATOM   3625 C CB  . VAL B 2 113 ? 20.38914  -42.04801 11.64401  1.000 169.96645 ? 113 VAL B CB  1 
ATOM   3626 C CG1 . VAL B 2 113 ? 21.33053  -41.97033 10.44888  1.000 171.60050 ? 113 VAL B CG1 1 
ATOM   3627 C CG2 . VAL B 2 113 ? 20.13797  -40.66336 12.21929  1.000 168.96704 ? 113 VAL B CG2 1 
ATOM   3628 N N   . MET B 2 114 ? 18.33167  -44.16287 13.04003  1.000 206.63378 ? 114 MET B N   1 
ATOM   3629 C CA  . MET B 2 114 ? 17.49402  -44.60954 14.14374  1.000 204.98248 ? 114 MET B CA  1 
ATOM   3630 C C   . MET B 2 114 ? 18.06991  -44.15156 15.47956  1.000 205.82890 ? 114 MET B C   1 
ATOM   3631 O O   . MET B 2 114 ? 19.28780  -44.06194 15.65654  1.000 212.49311 ? 114 MET B O   1 
ATOM   3632 C CB  . MET B 2 114 ? 17.35628  -46.13501 14.11872  1.000 211.35528 ? 114 MET B CB  1 
ATOM   3633 C CG  . MET B 2 114 ? 16.58086  -46.73120 15.28174  1.000 213.87067 ? 114 MET B CG  1 
ATOM   3634 S SD  . MET B 2 114 ? 14.91744  -46.05914 15.44641  1.000 213.86226 ? 114 MET B SD  1 
ATOM   3635 C CE  . MET B 2 114 ? 14.37788  -46.88464 16.94098  1.000 216.98645 ? 114 MET B CE  1 
ATOM   3636 N N   . VAL B 2 115 ? 17.17468  -43.85385 16.42014  1.000 206.92462 ? 115 VAL B N   1 
ATOM   3637 C CA  . VAL B 2 115 ? 17.53947  -43.39419 17.75609  1.000 208.36976 ? 115 VAL B CA  1 
ATOM   3638 C C   . VAL B 2 115 ? 16.78601  -44.24113 18.77256  1.000 212.67003 ? 115 VAL B C   1 
ATOM   3639 O O   . VAL B 2 115 ? 15.55216  -44.31659 18.72914  1.000 211.28981 ? 115 VAL B O   1 
ATOM   3640 C CB  . VAL B 2 115 ? 17.22578  -41.90186 17.95580  1.000 203.77551 ? 115 VAL B CB  1 
ATOM   3641 C CG1 . VAL B 2 115 ? 17.33632  -41.52513 19.42403  1.000 204.58246 ? 115 VAL B CG1 1 
ATOM   3642 C CG2 . VAL B 2 115 ? 18.15947  -41.04827 17.11228  1.000 201.29985 ? 115 VAL B CG2 1 
ATOM   3643 N N   . THR B 2 116 ? 17.52197  -44.87045 19.68517  1.000 206.34822 ? 116 THR B N   1 
ATOM   3644 C CA  . THR B 2 116 ? 16.94974  -45.73318 20.71249  1.000 207.16482 ? 116 THR B CA  1 
ATOM   3645 C C   . THR B 2 116 ? 17.11879  -45.06555 22.07147  1.000 208.91635 ? 116 THR B C   1 
ATOM   3646 O O   . THR B 2 116 ? 18.24587  -44.77470 22.48597  1.000 215.65656 ? 116 THR B O   1 
ATOM   3647 C CB  . THR B 2 116 ? 17.61497  -47.10959 20.70729  1.000 210.94431 ? 116 THR B CB  1 
ATOM   3648 O OG1 . THR B 2 116 ? 17.47009  -47.70994 19.41361  1.000 210.65026 ? 116 THR B OG1 1 
ATOM   3649 C CG2 . THR B 2 116 ? 16.98031  -48.01334 21.75345  1.000 212.70705 ? 116 THR B CG2 1 
ATOM   3650 N N   . VAL B 2 117 ? 16.00553  -44.82945 22.76154  1.000 200.88387 ? 117 VAL B N   1 
ATOM   3651 C CA  . VAL B 2 117 ? 16.00786  -44.18798 24.07074  1.000 205.73316 ? 117 VAL B CA  1 
ATOM   3652 C C   . VAL B 2 117 ? 15.37467  -45.17098 25.04714  1.000 211.98878 ? 117 VAL B C   1 
ATOM   3653 O O   . VAL B 2 117 ? 14.14504  -45.24387 25.16464  1.000 211.75255 ? 117 VAL B O   1 
ATOM   3654 C CB  . VAL B 2 117 ? 15.26277  -42.84687 24.06811  1.000 202.66886 ? 117 VAL B CB  1 
ATOM   3655 C CG1 . VAL B 2 117 ? 15.63208  -42.03520 25.30256  1.000 207.86183 ? 117 VAL B CG1 1 
ATOM   3656 C CG2 . VAL B 2 117 ? 15.55836  -42.07115 22.79507  1.000 197.39871 ? 117 VAL B CG2 1 
ATOM   3657 N N   . SER B 2 118 ? 16.20782  -45.92733 25.75757  1.000 204.87383 ? 118 SER B N   1 
ATOM   3658 C CA  . SER B 2 118 ? 15.73036  -46.88801 26.74128  1.000 207.46884 ? 118 SER B CA  1 
ATOM   3659 C C   . SER B 2 118 ? 16.71073  -46.95631 27.90271  1.000 209.96118 ? 118 SER B C   1 
ATOM   3660 O O   . SER B 2 118 ? 17.92373  -46.83776 27.71184  1.000 210.71181 ? 118 SER B O   1 
ATOM   3661 C CB  . SER B 2 118 ? 15.54519  -48.28483 26.12769  1.000 209.04935 ? 118 SER B CB  1 
ATOM   3662 O OG  . SER B 2 118 ? 15.08761  -49.21094 27.10030  1.000 212.22663 ? 118 SER B OG  1 
ATOM   3663 N N   . SER B 2 119 ? 16.17672  -47.14428 29.10975  1.000 208.41694 ? 119 SER B N   1 
ATOM   3664 C CA  . SER B 2 119 ? 16.98540  -47.31117 30.30845  1.000 213.69792 ? 119 SER B CA  1 
ATOM   3665 C C   . SER B 2 119 ? 17.34606  -48.76743 30.56917  1.000 217.44506 ? 119 SER B C   1 
ATOM   3666 O O   . SER B 2 119 ? 17.66556  -49.12324 31.70989  1.000 222.80025 ? 119 SER B O   1 
ATOM   3667 C CB  . SER B 2 119 ? 16.25539  -46.73344 31.52283  1.000 217.64503 ? 119 SER B CB  1 
ATOM   3668 O OG  . SER B 2 119 ? 15.09251  -47.48676 31.81518  1.000 220.36211 ? 119 SER B OG  1 
ATOM   3669 N N   . ALA B 2 120 ? 17.30716  -49.61085 29.54215  1.000 215.03914 ? 120 ALA B N   1 
ATOM   3670 C CA  . ALA B 2 120 ? 17.49191  -51.04294 29.72159  1.000 218.91977 ? 120 ALA B CA  1 
ATOM   3671 C C   . ALA B 2 120 ? 18.96804  -51.40328 29.81329  1.000 222.17921 ? 120 ALA B C   1 
ATOM   3672 O O   . ALA B 2 120 ? 19.80589  -50.85904 29.08719  1.000 219.90325 ? 120 ALA B O   1 
ATOM   3673 C CB  . ALA B 2 120 ? 16.84029  -51.80944 28.57062  1.000 215.73828 ? 120 ALA B CB  1 
ATOM   3674 N N   . GLU B 2 121 ? 19.27862  -52.33241 30.71345  1.000 221.45563 ? 121 GLU B N   1 
ATOM   3675 C CA  . GLU B 2 121 ? 20.62287  -52.86931 30.86754  1.000 225.64821 ? 121 GLU B CA  1 
ATOM   3676 C C   . GLU B 2 121 ? 20.71173  -54.23069 30.19101  1.000 229.22973 ? 121 GLU B C   1 
ATOM   3677 O O   . GLU B 2 121 ? 19.75342  -55.00880 30.20467  1.000 229.89066 ? 121 GLU B O   1 
ATOM   3678 C CB  . GLU B 2 121 ? 21.00226  -52.98796 32.34550  1.000 229.01556 ? 121 GLU B CB  1 
ATOM   3679 C CG  . GLU B 2 121 ? 21.12598  -51.65663 33.07402  1.000 226.50219 ? 121 GLU B CG  1 
ATOM   3680 C CD  . GLU B 2 121 ? 19.79977  -51.15448 33.61033  1.000 223.78704 ? 121 GLU B CD  1 
ATOM   3681 O OE1 . GLU B 2 121 ? 18.83406  -51.94562 33.64740  1.000 224.59242 ? 121 GLU B OE1 1 
ATOM   3682 O OE2 . GLU B 2 121 ? 19.72394  -49.96967 33.99850  1.000 221.40298 ? 121 GLU B OE2 1 
ATOM   3683 N N   . THR B 2 122 ? 21.87064  -54.51263 29.60132  1.000 213.48927 ? 122 THR B N   1 
ATOM   3684 C CA  . THR B 2 122 ? 22.06777  -55.72551 28.80522  1.000 217.32558 ? 122 THR B CA  1 
ATOM   3685 C C   . THR B 2 122 ? 22.10321  -56.94921 29.71609  1.000 222.96049 ? 122 THR B C   1 
ATOM   3686 O O   . THR B 2 122 ? 23.08688  -57.17506 30.42717  1.000 227.59950 ? 122 THR B O   1 
ATOM   3687 C CB  . THR B 2 122 ? 23.35411  -55.60968 27.99623  1.000 219.59316 ? 122 THR B CB  1 
ATOM   3688 O OG1 . THR B 2 122 ? 24.47544  -55.54678 28.88493  1.000 223.39480 ? 122 THR B OG1 1 
ATOM   3689 C CG2 . THR B 2 122 ? 23.33204  -54.34675 27.14026  1.000 213.11414 ? 122 THR B CG2 1 
ATOM   3690 N N   . THR B 2 123 ? 21.03517  -57.74992 29.69134  1.000 220.90864 ? 123 THR B N   1 
ATOM   3691 C CA  . THR B 2 123 ? 20.90416  -58.90429 30.56924  1.000 226.15238 ? 123 THR B CA  1 
ATOM   3692 C C   . THR B 2 123 ? 20.48562  -60.13922 29.77945  1.000 228.73990 ? 123 THR B C   1 
ATOM   3693 O O   . THR B 2 123 ? 19.95122  -60.04692 28.67154  1.000 225.48098 ? 123 THR B O   1 
ATOM   3694 C CB  . THR B 2 123 ? 19.89351  -58.64388 31.69742  1.000 224.55652 ? 123 THR B CB  1 
ATOM   3695 O OG1 . THR B 2 123 ? 18.64310  -58.22722 31.13738  1.000 219.78626 ? 123 THR B OG1 1 
ATOM   3696 C CG2 . THR B 2 123 ? 20.40870  -57.56747 32.64013  1.000 223.06140 ? 123 THR B CG2 1 
ATOM   3697 N N   . ALA B 2 124 ? 20.72183  -61.30239 30.38147  1.000 227.86384 ? 124 ALA B N   1 
ATOM   3698 C CA  . ALA B 2 124 ? 20.49371  -62.59255 29.73955  1.000 230.88237 ? 124 ALA B CA  1 
ATOM   3699 C C   . ALA B 2 124 ? 19.03893  -63.02159 29.89478  1.000 229.51578 ? 124 ALA B C   1 
ATOM   3700 O O   . ALA B 2 124 ? 18.29003  -62.45787 30.69477  1.000 227.49904 ? 124 ALA B O   1 
ATOM   3701 C CB  . ALA B 2 124 ? 21.44541  -63.62863 30.33620  1.000 237.58309 ? 124 ALA B CB  1 
ATOM   3702 N N   . PRO B 2 125 ? 18.59025  -64.03190 29.11792  1.000 233.93407 ? 125 PRO B N   1 
ATOM   3703 C CA  . PRO B 2 125 ? 17.18325  -64.45152 29.20389  1.000 227.93957 ? 125 PRO B CA  1 
ATOM   3704 C C   . PRO B 2 125 ? 16.93056  -65.61607 30.15004  1.000 231.51346 ? 125 PRO B C   1 
ATOM   3705 O O   . PRO B 2 125 ? 17.85883  -66.16764 30.74958  1.000 237.08344 ? 125 PRO B O   1 
ATOM   3706 C CB  . PRO B 2 125 ? 16.86638  -64.85029 27.75954  1.000 207.61924 ? 125 PRO B CB  1 
ATOM   3707 C CG  . PRO B 2 125 ? 18.15195  -65.42148 27.27150  1.000 211.84285 ? 125 PRO B CG  1 
ATOM   3708 C CD  . PRO B 2 125 ? 19.25416  -64.62239 27.93990  1.000 229.03185 ? 125 PRO B CD  1 
ATOM   3709 N N   . SER B 2 126 ? 15.65894  -65.99750 30.27402  1.000 222.56094 ? 126 SER B N   1 
ATOM   3710 C CA  . SER B 2 126 ? 15.23591  -67.14713 31.06649  1.000 229.29941 ? 126 SER B CA  1 
ATOM   3711 C C   . SER B 2 126 ? 14.34043  -68.01829 30.19826  1.000 228.14288 ? 126 SER B C   1 
ATOM   3712 O O   . SER B 2 126 ? 13.29971  -67.55592 29.71928  1.000 226.62052 ? 126 SER B O   1 
ATOM   3713 C CB  . SER B 2 126 ? 14.49933  -66.70516 32.33428  1.000 235.19788 ? 126 SER B CB  1 
ATOM   3714 O OG  . SER B 2 126 ? 13.40345  -65.86366 32.01841  1.000 231.92403 ? 126 SER B OG  1 
ATOM   3715 N N   . VAL B 2 127 ? 14.74043  -69.27292 29.99990  1.000 223.70986 ? 127 VAL B N   1 
ATOM   3716 C CA  . VAL B 2 127 ? 14.07048  -70.17265 29.06719  1.000 222.77101 ? 127 VAL B CA  1 
ATOM   3717 C C   . VAL B 2 127 ? 12.95924  -70.92608 29.78662  1.000 225.74520 ? 127 VAL B C   1 
ATOM   3718 O O   . VAL B 2 127 ? 13.05767  -71.24103 30.97738  1.000 229.07269 ? 127 VAL B O   1 
ATOM   3719 C CB  . VAL B 2 127 ? 15.08549  -71.14101 28.42260  1.000 222.71201 ? 127 VAL B CB  1 
ATOM   3720 C CG1 . VAL B 2 127 ? 14.47228  -71.84306 27.21900  1.000 220.11797 ? 127 VAL B CG1 1 
ATOM   3721 C CG2 . VAL B 2 127 ? 16.35052  -70.39580 28.02501  1.000 221.10014 ? 127 VAL B CG2 1 
ATOM   3722 N N   . TYR B 2 128 ? 11.88204  -71.21666 29.05115  1.000 223.08903 ? 128 TYR B N   1 
ATOM   3723 C CA  . TYR B 2 128 ? 10.75329  -71.98104 29.56933  1.000 225.60805 ? 128 TYR B CA  1 
ATOM   3724 C C   . TYR B 2 128 ? 10.25282  -72.96405 28.51612  1.000 224.02227 ? 128 TYR B C   1 
ATOM   3725 O O   . TYR B 2 128 ? 9.80613   -72.54556 27.44030  1.000 222.08303 ? 128 TYR B O   1 
ATOM   3726 C CB  . TYR B 2 128 ? 9.61328   -71.05363 29.99644  1.000 227.27655 ? 128 TYR B CB  1 
ATOM   3727 C CG  . TYR B 2 128 ? 9.98879   -70.03062 31.04425  1.000 228.90726 ? 128 TYR B CG  1 
ATOM   3728 C CD1 . TYR B 2 128 ? 10.06788  -70.37890 32.38581  1.000 232.12954 ? 128 TYR B CD1 1 
ATOM   3729 C CD2 . TYR B 2 128 ? 10.24803  -68.71223 30.69348  1.000 227.20187 ? 128 TYR B CD2 1 
ATOM   3730 C CE1 . TYR B 2 128 ? 10.40529  -69.44563 33.34769  1.000 233.84646 ? 128 TYR B CE1 1 
ATOM   3731 C CE2 . TYR B 2 128 ? 10.58510  -67.77173 31.64826  1.000 228.23659 ? 128 TYR B CE2 1 
ATOM   3732 C CZ  . TYR B 2 128 ? 10.66228  -68.14382 32.97345  1.000 231.88677 ? 128 TYR B CZ  1 
ATOM   3733 O OH  . TYR B 2 128 ? 10.99791  -67.21110 33.92780  1.000 232.59505 ? 128 TYR B OH  1 
ATOM   3734 N N   . PRO B 2 129 ? 10.30680  -74.26855 28.78071  1.000 225.02690 ? 129 PRO B N   1 
ATOM   3735 C CA  . PRO B 2 129 ? 9.77354   -75.23867 27.81710  1.000 225.46672 ? 129 PRO B CA  1 
ATOM   3736 C C   . PRO B 2 129 ? 8.25495   -75.30706 27.87643  1.000 227.08012 ? 129 PRO B C   1 
ATOM   3737 O O   . PRO B 2 129 ? 7.64823   -75.21826 28.94664  1.000 229.33637 ? 129 PRO B O   1 
ATOM   3738 C CB  . PRO B 2 129 ? 10.40826  -76.56063 28.26433  1.000 227.78970 ? 129 PRO B CB  1 
ATOM   3739 C CG  . PRO B 2 129 ? 10.61030  -76.38486 29.73220  1.000 228.63451 ? 129 PRO B CG  1 
ATOM   3740 C CD  . PRO B 2 129 ? 10.93275  -74.92553 29.94196  1.000 227.13710 ? 129 PRO B CD  1 
ATOM   3741 N N   . LEU B 2 130 ? 7.64030   -75.47135 26.70634  0.000 233.20538 ? 130 LEU B N   1 
ATOM   3742 C CA  . LEU B 2 130 ? 6.19057   -75.49382 26.58203  0.000 235.77580 ? 130 LEU B CA  1 
ATOM   3743 C C   . LEU B 2 130 ? 5.75455   -76.73655 25.81923  0.000 236.04303 ? 130 LEU B C   1 
ATOM   3744 O O   . LEU B 2 130 ? 6.47280   -77.23598 24.94873  0.000 233.30486 ? 130 LEU B O   1 
ATOM   3745 C CB  . LEU B 2 130 ? 5.67194   -74.23611 25.87023  0.000 234.85388 ? 130 LEU B CB  1 
ATOM   3746 C CG  . LEU B 2 130 ? 6.13030   -72.89544 26.44800  0.000 234.19526 ? 130 LEU B CG  1 
ATOM   3747 C CD1 . LEU B 2 130 ? 5.98616   -71.78810 25.41690  0.000 231.57479 ? 130 LEU B CD1 1 
ATOM   3748 C CD2 . LEU B 2 130 ? 5.34753   -72.55922 27.70570  0.000 238.32176 ? 130 LEU B CD2 1 
ATOM   3749 N N   . ALA B 2 131 ? 4.56566   -77.22845 26.15402  0.000 238.32531 ? 131 ALA B N   1 
ATOM   3750 C CA  . ALA B 2 131 ? 4.01480   -78.41413 25.50751  0.000 239.33961 ? 131 ALA B CA  1 
ATOM   3751 C C   . ALA B 2 131 ? 2.50709   -78.28342 25.32024  0.000 243.08780 ? 131 ALA B C   1 
ATOM   3752 O O   . ALA B 2 131 ? 1.72573   -78.83082 26.09795  0.000 247.09620 ? 131 ALA B O   1 
ATOM   3753 C CB  . ALA B 2 131 ? 4.34268   -79.65989 26.31551  0.000 240.48763 ? 131 ALA B CB  1 
ATOM   3754 N N   . THR B 2 143 ? 2.66005   -79.81235 19.01487  0.000 246.56536 ? 143 THR B N   1 
ATOM   3755 C CA  . THR B 2 143 ? 3.75002   -78.88040 18.75267  0.000 242.40481 ? 143 THR B CA  1 
ATOM   3756 C C   . THR B 2 143 ? 4.39226   -78.41966 20.05800  0.000 241.64741 ? 143 THR B C   1 
ATOM   3757 O O   . THR B 2 143 ? 3.69879   -78.11530 21.02904  0.000 244.08101 ? 143 THR B O   1 
ATOM   3758 C CB  . THR B 2 143 ? 3.26082   -77.65282 17.95689  0.000 241.29109 ? 143 THR B CB  1 
ATOM   3759 O OG1 . THR B 2 143 ? 2.66386   -78.08571 16.72839  0.000 242.17854 ? 143 THR B OG1 1 
ATOM   3760 C CG2 . THR B 2 143 ? 4.41640   -76.71272 17.64549  0.000 237.21374 ? 143 THR B CG2 1 
ATOM   3761 N N   . LEU B 2 144 ? 5.72148   -78.38107 20.07619  0.000 242.00731 ? 144 LEU B N   1 
ATOM   3762 C CA  . LEU B 2 144 ? 6.48639   -77.93629 21.23099  0.000 241.31641 ? 144 LEU B CA  1 
ATOM   3763 C C   . LEU B 2 144 ? 7.18602   -76.62407 20.90675  0.000 238.48954 ? 144 LEU B C   1 
ATOM   3764 O O   . LEU B 2 144 ? 7.68253   -76.43392 19.79226  0.000 236.09218 ? 144 LEU B O   1 
ATOM   3765 C CB  . LEU B 2 144 ? 7.51803   -78.98820 21.64491  0.000 240.66260 ? 144 LEU B CB  1 
ATOM   3766 C CG  . LEU B 2 144 ? 6.97916   -80.39864 21.88323  0.000 243.02109 ? 144 LEU B CG  1 
ATOM   3767 C CD1 . LEU B 2 144 ? 8.11476   -81.34833 22.22295  0.000 241.87837 ? 144 LEU B CD1 1 
ATOM   3768 C CD2 . LEU B 2 144 ? 5.92774   -80.39487 22.98071  0.000 246.51550 ? 144 LEU B CD2 1 
ATOM   3769 N N   . GLY B 2 145 ? 7.22404   -75.72422 21.87829  0.000 234.29183 ? 145 GLY B N   1 
ATOM   3770 C CA  . GLY B 2 145 ? 7.86851   -74.43833 21.68890  0.000 231.87837 ? 145 GLY B CA  1 
ATOM   3771 C C   . GLY B 2 145 ? 8.59986   -74.00070 22.93860  0.000 232.35987 ? 145 GLY B C   1 
ATOM   3772 O O   . GLY B 2 145 ? 8.20838   -74.32926 24.05953  0.000 235.06626 ? 145 GLY B O   1 
ATOM   3773 N N   . CYS B 2 146 ? 9.68158   -73.25438 22.73429  1.000 224.21924 ? 146 CYS B N   1 
ATOM   3774 C CA  . CYS B 2 146 ? 10.39495  -72.66552 23.85600  1.000 224.90868 ? 146 CYS B CA  1 
ATOM   3775 C C   . CYS B 2 146 ? 9.81693   -71.29093 24.17998  1.000 225.13714 ? 146 CYS B C   1 
ATOM   3776 O O   . CYS B 2 146 ? 8.94628   -70.76929 23.47978  1.000 224.35355 ? 146 CYS B O   1 
ATOM   3777 C CB  . CYS B 2 146 ? 11.89211  -72.54737 23.56567  1.000 223.18894 ? 146 CYS B CB  1 
ATOM   3778 S SG  . CYS B 2 146 ? 12.61684  -73.84711 22.54439  1.000 221.83662 ? 146 CYS B SG  1 
ATOM   3779 N N   . LEU B 2 147 ? 10.32332  -70.69807 25.25823  1.000 220.32039 ? 147 LEU B N   1 
ATOM   3780 C CA  . LEU B 2 147 ? 9.89113   -69.37568 25.69453  1.000 215.67842 ? 147 LEU B CA  1 
ATOM   3781 C C   . LEU B 2 147 ? 11.10684  -68.60265 26.17742  1.000 212.06500 ? 147 LEU B C   1 
ATOM   3782 O O   . LEU B 2 147 ? 11.73425  -68.98544 27.16883  1.000 221.85289 ? 147 LEU B O   1 
ATOM   3783 C CB  . LEU B 2 147 ? 8.83566   -69.47536 26.80013  1.000 219.73994 ? 147 LEU B CB  1 
ATOM   3784 C CG  . LEU B 2 147 ? 8.46031   -68.19507 27.55096  1.000 222.28954 ? 147 LEU B CG  1 
ATOM   3785 C CD1 . LEU B 2 147 ? 8.05380   -67.08948 26.59195  1.000 217.21097 ? 147 LEU B CD1 1 
ATOM   3786 C CD2 . LEU B 2 147 ? 7.34298   -68.47546 28.54350  1.000 229.85208 ? 147 LEU B CD2 1 
ATOM   3787 N N   . VAL B 2 148 ? 11.43597  -67.52401 25.47817  1.000 209.31232 ? 148 VAL B N   1 
ATOM   3788 C CA  . VAL B 2 148 ? 12.55067  -66.65375 25.82902  1.000 212.93565 ? 148 VAL B CA  1 
ATOM   3789 C C   . VAL B 2 148 ? 11.94557  -65.39747 26.44277  1.000 221.63637 ? 148 VAL B C   1 
ATOM   3790 O O   . VAL B 2 148 ? 11.50574  -64.49112 25.72678  1.000 219.71391 ? 148 VAL B O   1 
ATOM   3791 C CB  . VAL B 2 148 ? 13.42538  -66.32674 24.61364  1.000 205.21476 ? 148 VAL B CB  1 
ATOM   3792 C CG1 . VAL B 2 148 ? 14.62697  -65.49821 25.02845  1.000 213.43218 ? 148 VAL B CG1 1 
ATOM   3793 C CG2 . VAL B 2 148 ? 13.86430  -67.60688 23.91740  1.000 204.55285 ? 148 VAL B CG2 1 
ATOM   3794 N N   . LYS B 2 149 ? 11.92097  -65.33542 27.77064  1.000 216.97569 ? 149 LYS B N   1 
ATOM   3795 C CA  . LYS B 2 149 ? 11.26301  -64.25504 28.49130  1.000 218.57636 ? 149 LYS B CA  1 
ATOM   3796 C C   . LYS B 2 149 ? 12.30013  -63.29224 29.05463  1.000 216.68332 ? 149 LYS B C   1 
ATOM   3797 O O   . LYS B 2 149 ? 13.23779  -63.71188 29.74134  1.000 219.51603 ? 149 LYS B O   1 
ATOM   3798 C CB  . LYS B 2 149 ? 10.38934  -64.81209 29.61672  1.000 223.06976 ? 149 LYS B CB  1 
ATOM   3799 C CG  . LYS B 2 149 ? 9.46584   -63.78953 30.26116  1.000 222.47514 ? 149 LYS B CG  1 
ATOM   3800 C CD  . LYS B 2 149 ? 8.63407   -64.42553 31.36411  1.000 227.68296 ? 149 LYS B CD  1 
ATOM   3801 C CE  . LYS B 2 149 ? 7.71089   -63.41269 32.01906  1.000 227.77164 ? 149 LYS B CE  1 
ATOM   3802 N NZ  . LYS B 2 149 ? 6.97124   -64.00458 33.16762  1.000 233.18411 ? 149 LYS B NZ  1 
ATOM   3803 N N   . GLY B 2 150 ? 12.12730  -62.00567 28.75809  1.000 223.93701 ? 150 GLY B N   1 
ATOM   3804 C CA  . GLY B 2 150 ? 12.96905  -60.96244 29.31099  1.000 224.14401 ? 150 GLY B CA  1 
ATOM   3805 C C   . GLY B 2 150 ? 14.42396  -61.01896 28.89250  1.000 223.90138 ? 150 GLY B C   1 
ATOM   3806 O O   . GLY B 2 150 ? 15.28376  -61.42605 29.68006  1.000 227.34808 ? 150 GLY B O   1 
ATOM   3807 N N   . TYR B 2 151 ? 14.71842  -60.60558 27.66070  1.000 228.75136 ? 151 TYR B N   1 
ATOM   3808 C CA  . TYR B 2 151 ? 16.08835  -60.54004 27.17531  1.000 229.56631 ? 151 TYR B CA  1 
ATOM   3809 C C   . TYR B 2 151 ? 16.33651  -59.19540 26.50683  1.000 226.91678 ? 151 TYR B C   1 
ATOM   3810 O O   . TYR B 2 151 ? 15.42714  -58.58717 25.93562  1.000 223.39370 ? 151 TYR B O   1 
ATOM   3811 C CB  . TYR B 2 151 ? 16.40746  -61.68764 26.19891  1.000 227.45650 ? 151 TYR B CB  1 
ATOM   3812 C CG  . TYR B 2 151 ? 15.89734  -61.50326 24.78622  1.000 211.19889 ? 151 TYR B CG  1 
ATOM   3813 C CD1 . TYR B 2 151 ? 14.59786  -61.85093 24.44416  1.000 212.45953 ? 151 TYR B CD1 1 
ATOM   3814 C CD2 . TYR B 2 151 ? 16.72771  -61.00910 23.78737  1.000 208.43370 ? 151 TYR B CD2 1 
ATOM   3815 C CE1 . TYR B 2 151 ? 14.13514  -61.69647 23.15241  1.000 208.12613 ? 151 TYR B CE1 1 
ATOM   3816 C CE2 . TYR B 2 151 ? 16.27285  -60.84837 22.49392  1.000 205.56019 ? 151 TYR B CE2 1 
ATOM   3817 C CZ  . TYR B 2 151 ? 14.97579  -61.19280 22.18153  1.000 206.53253 ? 151 TYR B CZ  1 
ATOM   3818 O OH  . TYR B 2 151 ? 14.51892  -61.03492 20.89323  1.000 208.41771 ? 151 TYR B OH  1 
ATOM   3819 N N   . PHE B 2 152 ? 17.58698  -58.74177 26.58947  1.000 225.26615 ? 152 PHE B N   1 
ATOM   3820 C CA  . PHE B 2 152 ? 18.04115  -57.46528 26.05104  1.000 222.61124 ? 152 PHE B CA  1 
ATOM   3821 C C   . PHE B 2 152 ? 19.56498  -57.43696 26.08402  1.000 226.49702 ? 152 PHE B C   1 
ATOM   3822 O O   . PHE B 2 152 ? 20.16714  -57.85501 27.08031  1.000 230.55585 ? 152 PHE B O   1 
ATOM   3823 C CB  . PHE B 2 152 ? 17.45294  -56.29920 26.85280  1.000 219.29640 ? 152 PHE B CB  1 
ATOM   3824 C CG  . PHE B 2 152 ? 18.04300  -54.95626 26.50962  1.000 215.46904 ? 152 PHE B CG  1 
ATOM   3825 C CD1 . PHE B 2 152 ? 19.13911  -54.46802 27.20299  1.000 216.94930 ? 152 PHE B CD1 1 
ATOM   3826 C CD2 . PHE B 2 152 ? 17.49406  -54.17706 25.50440  1.000 210.63064 ? 152 PHE B CD2 1 
ATOM   3827 C CE1 . PHE B 2 152 ? 19.68431  -53.23752 26.89453  1.000 213.78990 ? 152 PHE B CE1 1 
ATOM   3828 C CE2 . PHE B 2 152 ? 18.03480  -52.94276 25.19153  1.000 207.47260 ? 152 PHE B CE2 1 
ATOM   3829 C CZ  . PHE B 2 152 ? 19.13104  -52.47295 25.88839  1.000 209.11773 ? 152 PHE B CZ  1 
ATOM   3830 N N   . PRO B 2 153 ? 20.23086  -56.94115 25.02999  1.000 220.10717 ? 153 PRO B N   1 
ATOM   3831 C CA  . PRO B 2 153 ? 19.62582  -56.37835 23.82146  1.000 212.58544 ? 153 PRO B CA  1 
ATOM   3832 C C   . PRO B 2 153 ? 19.34471  -57.42466 22.74812  1.000 208.73980 ? 153 PRO B C   1 
ATOM   3833 O O   . PRO B 2 153 ? 19.83425  -58.55040 22.84108  1.000 217.20985 ? 153 PRO B O   1 
ATOM   3834 C CB  . PRO B 2 153 ? 20.68677  -55.38761 23.34612  1.000 214.06454 ? 153 PRO B CB  1 
ATOM   3835 C CG  . PRO B 2 153 ? 21.97207  -56.03822 23.73767  1.000 223.18129 ? 153 PRO B CG  1 
ATOM   3836 C CD  . PRO B 2 153 ? 21.69853  -56.80666 25.01398  1.000 226.90758 ? 153 PRO B CD  1 
ATOM   3837 N N   . GLU B 2 154 ? 18.55763  -57.03917 21.74572  1.000 200.56233 ? 154 GLU B N   1 
ATOM   3838 C CA  . GLU B 2 154 ? 18.27122  -57.91328 20.62005  1.000 198.09377 ? 154 GLU B CA  1 
ATOM   3839 C C   . GLU B 2 154 ? 19.56569  -58.25824 19.88222  1.000 202.52061 ? 154 GLU B C   1 
ATOM   3840 O O   . GLU B 2 154 ? 20.48408  -57.43611 19.81267  1.000 207.89517 ? 154 GLU B O   1 
ATOM   3841 C CB  . GLU B 2 154 ? 17.28948  -57.22471 19.66924  1.000 194.01055 ? 154 GLU B CB  1 
ATOM   3842 C CG  . GLU B 2 154 ? 16.40929  -58.15720 18.85207  1.000 198.01358 ? 154 GLU B CG  1 
ATOM   3843 C CD  . GLU B 2 154 ? 15.45601  -57.41688 17.94094  1.000 194.68683 ? 154 GLU B CD  1 
ATOM   3844 O OE1 . GLU B 2 154 ? 15.24722  -56.20536 18.15535  1.000 190.15875 ? 154 GLU B OE1 1 
ATOM   3845 O OE2 . GLU B 2 154 ? 14.91668  -58.04814 17.00797  1.000 195.59611 ? 154 GLU B OE2 1 
ATOM   3846 N N   . PRO B 2 155 ? 19.67292  -59.47340 19.31550  1.000 199.27840 ? 155 PRO B N   1 
ATOM   3847 C CA  . PRO B 2 155 ? 18.73449  -60.59476 19.39410  1.000 198.47737 ? 155 PRO B CA  1 
ATOM   3848 C C   . PRO B 2 155 ? 19.25790  -61.81287 20.15384  1.000 203.83811 ? 155 PRO B C   1 
ATOM   3849 O O   . PRO B 2 155 ? 20.33647  -61.77373 20.74427  1.000 211.15200 ? 155 PRO B O   1 
ATOM   3850 C CB  . PRO B 2 155 ? 18.51949  -60.94285 17.92424  1.000 197.45594 ? 155 PRO B CB  1 
ATOM   3851 C CG  . PRO B 2 155 ? 19.87874  -60.69403 17.31403  1.000 201.00918 ? 155 PRO B CG  1 
ATOM   3852 C CD  . PRO B 2 155 ? 20.56803  -59.62450 18.15327  1.000 201.58414 ? 155 PRO B CD  1 
ATOM   3853 N N   . VAL B 2 156 ? 18.47724  -62.89137 20.11356  1.000 205.91471 ? 156 VAL B N   1 
ATOM   3854 C CA  . VAL B 2 156 ? 18.78562  -64.14270 20.79262  1.000 208.05336 ? 156 VAL B CA  1 
ATOM   3855 C C   . VAL B 2 156 ? 18.66493  -65.27664 19.78300  1.000 206.44917 ? 156 VAL B C   1 
ATOM   3856 O O   . VAL B 2 156 ? 17.84256  -65.22431 18.86308  1.000 200.99330 ? 156 VAL B O   1 
ATOM   3857 C CB  . VAL B 2 156 ? 17.85099  -64.36835 22.00980  1.000 209.20547 ? 156 VAL B CB  1 
ATOM   3858 C CG1 . VAL B 2 156 ? 17.23105  -65.76497 21.99677  1.000 211.55202 ? 156 VAL B CG1 1 
ATOM   3859 C CG2 . VAL B 2 156 ? 18.59627  -64.12470 23.31023  1.000 216.06145 ? 156 VAL B CG2 1 
ATOM   3860 N N   . THR B 2 157 ? 19.50397  -66.29916 19.94467  1.000 215.61705 ? 157 THR B N   1 
ATOM   3861 C CA  . THR B 2 157 ? 19.47764  -67.47301 19.08187  1.000 215.42247 ? 157 THR B CA  1 
ATOM   3862 C C   . THR B 2 157 ? 18.69037  -68.59621 19.74543  1.000 218.43440 ? 157 THR B C   1 
ATOM   3863 O O   . THR B 2 157 ? 18.77031  -68.79129 20.96186  1.000 217.97742 ? 157 THR B O   1 
ATOM   3864 C CB  . THR B 2 157 ? 20.89263  -67.95988 18.76593  1.000 214.72950 ? 157 THR B CB  1 
ATOM   3865 O OG1 . THR B 2 157 ? 21.34955  -68.81091 19.82349  1.000 217.48029 ? 157 THR B OG1 1 
ATOM   3866 C CG2 . THR B 2 157 ? 21.84092  -66.78056 18.63342  1.000 211.01942 ? 157 THR B CG2 1 
ATOM   3867 N N   . VAL B 2 158 ? 17.92920  -69.33280 18.93682  1.000 215.18211 ? 158 VAL B N   1 
ATOM   3868 C CA  . VAL B 2 158 ? 17.14628  -70.47422 19.40177  1.000 217.21546 ? 158 VAL B CA  1 
ATOM   3869 C C   . VAL B 2 158 ? 17.30464  -71.59702 18.38582  1.000 216.40941 ? 158 VAL B C   1 
ATOM   3870 O O   . VAL B 2 158 ? 17.00913  -71.41018 17.20027  1.000 214.94135 ? 158 VAL B O   1 
ATOM   3871 C CB  . VAL B 2 158 ? 15.65725  -70.13018 19.58789  1.000 217.72548 ? 158 VAL B CB  1 
ATOM   3872 C CG1 . VAL B 2 158 ? 14.84198  -71.39758 19.80089  1.000 220.13125 ? 158 VAL B CG1 1 
ATOM   3873 C CG2 . VAL B 2 158 ? 15.46871  -69.17172 20.75650  1.000 219.21454 ? 158 VAL B CG2 1 
ATOM   3874 N N   . THR B 2 159 ? 17.77114  -72.75768 18.84240  1.000 230.98723 ? 159 THR B N   1 
ATOM   3875 C CA  . THR B 2 159 ? 17.93786  -73.91881 17.98127  1.000 228.12453 ? 159 THR B CA  1 
ATOM   3876 C C   . THR B 2 159 ? 17.38953  -75.15007 18.68812  1.000 233.80169 ? 159 THR B C   1 
ATOM   3877 O O   . THR B 2 159 ? 17.25231  -75.17978 19.91318  1.000 235.22282 ? 159 THR B O   1 
ATOM   3878 C CB  . THR B 2 159 ? 19.40871  -74.14490 17.59870  1.000 227.26125 ? 159 THR B CB  1 
ATOM   3879 O OG1 . THR B 2 159 ? 20.20962  -74.21687 18.78430  1.000 231.44532 ? 159 THR B OG1 1 
ATOM   3880 C CG2 . THR B 2 159 ? 19.91739  -73.01493 16.71522  1.000 217.17554 ? 159 THR B CG2 1 
ATOM   3881 N N   . TRP B 2 160 ? 17.07707  -76.17244 17.89685  1.000 232.99581 ? 160 TRP B N   1 
ATOM   3882 C CA  . TRP B 2 160 ? 16.54059  -77.43079 18.39964  1.000 234.08732 ? 160 TRP B CA  1 
ATOM   3883 C C   . TRP B 2 160 ? 17.55843  -78.53499 18.15010  1.000 234.03014 ? 160 TRP B C   1 
ATOM   3884 O O   . TRP B 2 160 ? 17.95608  -78.76626 17.00294  1.000 233.14484 ? 160 TRP B O   1 
ATOM   3885 C CB  . TRP B 2 160 ? 15.20905  -77.76574 17.72844  1.000 234.46702 ? 160 TRP B CB  1 
ATOM   3886 C CG  . TRP B 2 160 ? 14.11892  -76.77999 18.01666  1.000 234.70253 ? 160 TRP B CG  1 
ATOM   3887 C CD1 . TRP B 2 160 ? 13.81997  -75.65476 17.30502  1.000 233.49283 ? 160 TRP B CD1 1 
ATOM   3888 C CD2 . TRP B 2 160 ? 13.17878  -76.83416 19.09508  1.000 236.27989 ? 160 TRP B CD2 1 
ATOM   3889 N NE1 . TRP B 2 160 ? 12.75127  -75.00452 17.87420  1.000 234.09406 ? 160 TRP B NE1 1 
ATOM   3890 C CE2 . TRP B 2 160 ? 12.34070  -75.70771 18.97610  1.000 235.98733 ? 160 TRP B CE2 1 
ATOM   3891 C CE3 . TRP B 2 160 ? 12.96464  -77.72591 20.15006  1.000 238.02887 ? 160 TRP B CE3 1 
ATOM   3892 C CZ2 . TRP B 2 160 ? 11.30324  -75.45259 19.86980  1.000 237.54949 ? 160 TRP B CZ2 1 
ATOM   3893 C CZ3 . TRP B 2 160 ? 11.93725  -77.46925 21.03726  1.000 239.68101 ? 160 TRP B CZ3 1 
ATOM   3894 C CH2 . TRP B 2 160 ? 11.11748  -76.34437 20.89038  1.000 239.53896 ? 160 TRP B CH2 1 
ATOM   3895 N N   . ASN B 2 161 ? 17.97023  -79.21342 19.22434  1.000 234.19404 ? 161 ASN B N   1 
ATOM   3896 C CA  . ASN B 2 161 ? 18.99262  -80.26136 19.16290  1.000 234.17251 ? 161 ASN B CA  1 
ATOM   3897 C C   . ASN B 2 161 ? 20.28676  -79.73847 18.54278  1.000 233.46644 ? 161 ASN B C   1 
ATOM   3898 O O   . ASN B 2 161 ? 20.97951  -80.45255 17.81423  1.000 236.06647 ? 161 ASN B O   1 
ATOM   3899 C CB  . ASN B 2 161 ? 18.48768  -81.49454 18.40940  1.000 236.46128 ? 161 ASN B CB  1 
ATOM   3900 C CG  . ASN B 2 161 ? 17.43845  -82.26470 19.18569  1.000 237.43834 ? 161 ASN B CG  1 
ATOM   3901 O OD1 . ASN B 2 161 ? 16.67824  -81.68958 19.96372  1.000 235.69823 ? 161 ASN B OD1 1 
ATOM   3902 N ND2 . ASN B 2 161 ? 17.39625  -83.57647 18.98149  1.000 240.74566 ? 161 ASN B ND2 1 
ATOM   3903 N N   . SER B 2 162 ? 20.60987  -78.47704 18.83851  1.000 244.88068 ? 162 SER B N   1 
ATOM   3904 C CA  . SER B 2 162 ? 21.82945  -77.82726 18.35347  1.000 244.88809 ? 162 SER B CA  1 
ATOM   3905 C C   . SER B 2 162 ? 21.90252  -77.84459 16.82752  1.000 243.31110 ? 162 SER B C   1 
ATOM   3906 O O   . SER B 2 162 ? 22.96436  -78.05925 16.23908  1.000 243.00732 ? 162 SER B O   1 
ATOM   3907 C CB  . SER B 2 162 ? 23.07831  -78.46370 18.96905  1.000 246.16632 ? 162 SER B CB  1 
ATOM   3908 O OG  . SER B 2 162 ? 24.23902  -77.71141 18.66147  1.000 247.01785 ? 162 SER B OG  1 
ATOM   3909 N N   . GLY B 2 163 ? 20.76218  -77.61676 16.18190  1.000 243.28516 ? 163 GLY B N   1 
ATOM   3910 C CA  . GLY B 2 163 ? 20.70839  -77.55734 14.73587  1.000 242.11548 ? 163 GLY B CA  1 
ATOM   3911 C C   . GLY B 2 163 ? 20.42429  -78.86758 14.04132  1.000 242.20322 ? 163 GLY B C   1 
ATOM   3912 O O   . GLY B 2 163 ? 20.71263  -78.99084 12.84544  1.000 241.49550 ? 163 GLY B O   1 
ATOM   3913 N N   . ALA B 2 164 ? 19.86939  -79.85262 14.74619  1.000 241.66980 ? 164 ALA B N   1 
ATOM   3914 C CA  . ALA B 2 164 ? 19.56009  -81.13786 14.13366  1.000 242.02349 ? 164 ALA B CA  1 
ATOM   3915 C C   . ALA B 2 164 ? 18.13415  -81.21126 13.60861  1.000 242.71678 ? 164 ALA B C   1 
ATOM   3916 O O   . ALA B 2 164 ? 17.86059  -81.99395 12.69129  1.000 243.53902 ? 164 ALA B O   1 
ATOM   3917 C CB  . ALA B 2 164 ? 19.79726  -82.27271 15.13325  1.000 242.57147 ? 164 ALA B CB  1 
ATOM   3918 N N   . LEU B 2 165 ? 17.22067  -80.42118 14.16794  1.000 244.72363 ? 165 LEU B N   1 
ATOM   3919 C CA  . LEU B 2 165 ? 15.84298  -80.35874 13.69044  1.000 245.80821 ? 165 LEU B CA  1 
ATOM   3920 C C   . LEU B 2 165 ? 15.76036  -79.28247 12.61441  1.000 245.14948 ? 165 LEU B C   1 
ATOM   3921 O O   . LEU B 2 165 ? 15.83894  -78.08653 12.91404  1.000 243.94678 ? 165 LEU B O   1 
ATOM   3922 C CB  . LEU B 2 165 ? 14.87836  -80.07006 14.83874  1.000 246.45822 ? 165 LEU B CB  1 
ATOM   3923 C CG  . LEU B 2 165 ? 14.31672  -81.25617 15.63057  1.000 248.04101 ? 165 LEU B CG  1 
ATOM   3924 C CD1 . LEU B 2 165 ? 15.41971  -82.04480 16.31771  1.000 247.64961 ? 165 LEU B CD1 1 
ATOM   3925 C CD2 . LEU B 2 165 ? 13.28775  -80.77994 16.64631  1.000 248.89746 ? 165 LEU B CD2 1 
ATOM   3926 N N   . SER B 2 166 ? 15.60515  -79.70714 11.36093  1.000 250.00016 ? 166 SER B N   1 
ATOM   3927 C CA  . SER B 2 166 ? 15.60471  -78.78329 10.23056  1.000 249.72883 ? 166 SER B CA  1 
ATOM   3928 C C   . SER B 2 166 ? 14.20857  -78.23379 9.94590   1.000 250.29309 ? 166 SER B C   1 
ATOM   3929 O O   . SER B 2 166 ? 14.00475  -77.01592 9.93368   1.000 249.15185 ? 166 SER B O   1 
ATOM   3930 C CB  . SER B 2 166 ? 16.17556  -79.47839 8.98930   1.000 250.71176 ? 166 SER B CB  1 
ATOM   3931 O OG  . SER B 2 166 ? 15.43898  -80.64729 8.67631   1.000 252.53178 ? 166 SER B OG  1 
ATOM   3932 N N   . SER B 2 167 ? 13.24292  -79.11774 9.71409   1.000 248.62480 ? 167 SER B N   1 
ATOM   3933 C CA  . SER B 2 167 ? 11.89556  -78.68762 9.37968   1.000 249.54718 ? 167 SER B CA  1 
ATOM   3934 C C   . SER B 2 167 ? 11.12204  -78.29895 10.63671  1.000 249.16104 ? 167 SER B C   1 
ATOM   3935 O O   . SER B 2 167 ? 11.43455  -78.72534 11.75176  1.000 248.94580 ? 167 SER B O   1 
ATOM   3936 C CB  . SER B 2 167 ? 11.15043  -79.79085 8.62678   1.000 252.27171 ? 167 SER B CB  1 
ATOM   3937 O OG  . SER B 2 167 ? 9.83380   -79.38523 8.29439   1.000 253.52811 ? 167 SER B OG  1 
ATOM   3938 N N   . GLY B 2 168 ? 10.09827  -77.46831 10.44019  1.000 242.15637 ? 168 GLY B N   1 
ATOM   3939 C CA  . GLY B 2 168 ? 9.20586   -77.07987 11.50981  1.000 242.32256 ? 168 GLY B CA  1 
ATOM   3940 C C   . GLY B 2 168 ? 9.65434   -75.90322 12.34689  1.000 240.18555 ? 168 GLY B C   1 
ATOM   3941 O O   . GLY B 2 168 ? 8.84902   -75.38672 13.13184  1.000 240.56323 ? 168 GLY B O   1 
ATOM   3942 N N   . VAL B 2 169 ? 10.90348  -75.45784 12.21175  1.000 242.04456 ? 169 VAL B N   1 
ATOM   3943 C CA  . VAL B 2 169 ? 11.42509  -74.34932 13.00578  1.000 240.37791 ? 169 VAL B CA  1 
ATOM   3944 C C   . VAL B 2 169 ? 10.60290  -73.09603 12.73664  1.000 239.36519 ? 169 VAL B C   1 
ATOM   3945 O O   . VAL B 2 169 ? 10.72036  -72.47757 11.67294  1.000 238.24020 ? 169 VAL B O   1 
ATOM   3946 C CB  . VAL B 2 169 ? 12.91570  -74.10575 12.70930  1.000 238.96866 ? 169 VAL B CB  1 
ATOM   3947 C CG1 . VAL B 2 169 ? 13.44091  -72.95064 13.54732  1.000 236.76519 ? 169 VAL B CG1 1 
ATOM   3948 C CG2 . VAL B 2 169 ? 13.71883  -75.36901 12.97153  1.000 239.94290 ? 169 VAL B CG2 1 
ATOM   3949 N N   . HIS B 2 170 ? 9.75947   -72.71493 13.70122  1.000 234.97101 ? 170 HIS B N   1 
ATOM   3950 C CA  . HIS B 2 170 ? 8.84284   -71.57908 13.56490  1.000 233.97046 ? 170 HIS B CA  1 
ATOM   3951 C C   . HIS B 2 170 ? 9.07056   -70.63019 14.74117  1.000 233.09913 ? 170 HIS B C   1 
ATOM   3952 O O   . HIS B 2 170 ? 8.34229   -70.66287 15.73464  1.000 234.66796 ? 170 HIS B O   1 
ATOM   3953 C CB  . HIS B 2 170 ? 7.39100   -72.06078 13.49142  1.000 236.19594 ? 170 HIS B CB  1 
ATOM   3954 C CG  . HIS B 2 170 ? 7.10042   -72.92459 12.30357  1.000 238.52204 ? 170 HIS B CG  1 
ATOM   3955 N ND1 . HIS B 2 170 ? 7.92214   -72.97036 11.19798  1.000 238.97729 ? 170 HIS B ND1 1 
ATOM   3956 C CD2 . HIS B 2 170 ? 6.08031   -73.77780 12.04914  1.000 240.64842 ? 170 HIS B CD2 1 
ATOM   3957 C CE1 . HIS B 2 170 ? 7.42057   -73.81348 10.31345  1.000 240.99345 ? 170 HIS B CE1 1 
ATOM   3958 N NE2 . HIS B 2 170 ? 6.30296   -74.31674 10.80535  1.000 242.01655 ? 170 HIS B NE2 1 
ATOM   3959 N N   . THR B 2 171 ? 10.08468  -69.77877 14.62168  1.000 231.63712 ? 171 THR B N   1 
ATOM   3960 C CA  . THR B 2 171 ? 10.39608  -68.80220 15.65864  1.000 229.44489 ? 171 THR B CA  1 
ATOM   3961 C C   . THR B 2 171 ? 9.56844   -67.53795 15.44468  1.000 225.09957 ? 171 THR B C   1 
ATOM   3962 O O   . THR B 2 171 ? 9.57692   -66.96158 14.35321  1.000 221.03124 ? 171 THR B O   1 
ATOM   3963 C CB  . THR B 2 171 ? 11.88912  -68.46769 15.65627  1.000 219.30589 ? 171 THR B CB  1 
ATOM   3964 O OG1 . THR B 2 171 ? 12.64683  -69.64403 15.96708  1.000 216.85151 ? 171 THR B OG1 1 
ATOM   3965 C CG2 . THR B 2 171 ? 12.19400  -67.39020 16.68652  1.000 219.09449 ? 171 THR B CG2 1 
ATOM   3966 N N   . PHE B 2 172 ? 8.86364   -67.11225 16.48430  1.000 220.04868 ? 172 PHE B N   1 
ATOM   3967 C CA  . PHE B 2 172 ? 7.94933   -65.97988 16.41947  1.000 223.31824 ? 172 PHE B CA  1 
ATOM   3968 C C   . PHE B 2 172 ? 8.69302   -64.68425 16.71972  1.000 212.70679 ? 172 PHE B C   1 
ATOM   3969 O O   . PHE B 2 172 ? 9.82020   -64.70178 17.21246  1.000 219.39343 ? 172 PHE B O   1 
ATOM   3970 C CB  . PHE B 2 172 ? 6.79648   -66.21339 17.39283  1.000 213.12395 ? 172 PHE B CB  1 
ATOM   3971 C CG  . PHE B 2 172 ? 5.67482   -67.01847 16.80955  1.000 232.24706 ? 172 PHE B CG  1 
ATOM   3972 C CD1 . PHE B 2 172 ? 5.83420   -68.36917 16.55189  1.000 238.08932 ? 172 PHE B CD1 1 
ATOM   3973 C CD2 . PHE B 2 172 ? 4.46260   -66.42165 16.51052  1.000 235.51561 ? 172 PHE B CD2 1 
ATOM   3974 C CE1 . PHE B 2 172 ? 4.80664   -69.10988 16.00954  1.000 240.52167 ? 172 PHE B CE1 1 
ATOM   3975 C CE2 . PHE B 2 172 ? 3.42748   -67.15844 15.96939  1.000 238.82022 ? 172 PHE B CE2 1 
ATOM   3976 C CZ  . PHE B 2 172 ? 3.60111   -68.50491 15.71672  1.000 240.70523 ? 172 PHE B CZ  1 
ATOM   3977 N N   . PRO B 2 173 ? 8.08533   -63.51401 16.41746  1.000 212.72639 ? 173 PRO B N   1 
ATOM   3978 C CA  . PRO B 2 173 ? 8.79813   -62.24121 16.62940  1.000 205.31754 ? 173 PRO B CA  1 
ATOM   3979 C C   . PRO B 2 173 ? 8.94897   -61.87785 18.10573  1.000 206.22109 ? 173 PRO B C   1 
ATOM   3980 O O   . PRO B 2 173 ? 8.48219   -62.59299 18.99106  1.000 210.85030 ? 173 PRO B O   1 
ATOM   3981 C CB  . PRO B 2 173 ? 7.92329   -61.22781 15.89192  1.000 205.32031 ? 173 PRO B CB  1 
ATOM   3982 C CG  . PRO B 2 173 ? 6.56336   -61.81053 15.94716  1.000 218.62519 ? 173 PRO B CG  1 
ATOM   3983 C CD  . PRO B 2 173 ? 6.77599   -63.29043 15.77595  1.000 221.70748 ? 173 PRO B CD  1 
ATOM   3984 N N   . ALA B 2 174 ? 9.61547   -60.74806 18.35941  1.000 208.75519 ? 174 ALA B N   1 
ATOM   3985 C CA  . ALA B 2 174 ? 9.82109   -60.24470 19.70675  1.000 203.32634 ? 174 ALA B CA  1 
ATOM   3986 C C   . ALA B 2 174 ? 8.80283   -59.15852 20.03905  1.000 198.52030 ? 174 ALA B C   1 
ATOM   3987 O O   . ALA B 2 174 ? 8.08456   -58.65141 19.17491  1.000 196.86531 ? 174 ALA B O   1 
ATOM   3988 C CB  . ALA B 2 174 ? 11.24732  -59.70448 19.86015  1.000 200.95103 ? 174 ALA B CB  1 
ATOM   3989 N N   . VAL B 2 175 ? 8.75174   -58.80146 21.32194  1.000 195.81590 ? 175 VAL B N   1 
ATOM   3990 C CA  . VAL B 2 175 ? 7.81441   -57.79477 21.80519  1.000 204.82815 ? 175 VAL B CA  1 
ATOM   3991 C C   . VAL B 2 175 ? 8.38815   -57.19778 23.08063  1.000 207.38189 ? 175 VAL B C   1 
ATOM   3992 O O   . VAL B 2 175 ? 9.07756   -57.87705 23.84467  1.000 204.67485 ? 175 VAL B O   1 
ATOM   3993 C CB  . VAL B 2 175 ? 6.40450   -58.40160 22.02899  1.000 214.58132 ? 175 VAL B CB  1 
ATOM   3994 C CG1 . VAL B 2 175 ? 6.42674   -59.40271 23.17048  1.000 217.31829 ? 175 VAL B CG1 1 
ATOM   3995 C CG2 . VAL B 2 175 ? 5.37303   -57.30867 22.28215  1.000 223.59341 ? 175 VAL B CG2 1 
ATOM   3996 N N   . LEU B 2 176 ? 8.11222   -55.91409 23.30346  1.000 207.98230 ? 176 LEU B N   1 
ATOM   3997 C CA  . LEU B 2 176 ? 8.62344   -55.18451 24.46282  1.000 213.70653 ? 176 LEU B CA  1 
ATOM   3998 C C   . LEU B 2 176 ? 7.53321   -55.14408 25.52834  1.000 217.62498 ? 176 LEU B C   1 
ATOM   3999 O O   . LEU B 2 176 ? 6.59103   -54.35257 25.44102  1.000 217.11209 ? 176 LEU B O   1 
ATOM   4000 C CB  . LEU B 2 176 ? 9.07333   -53.78370 24.06288  1.000 208.31950 ? 176 LEU B CB  1 
ATOM   4001 C CG  . LEU B 2 176 ? 10.40300  -53.70924 23.31129  1.000 203.50894 ? 176 LEU B CG  1 
ATOM   4002 C CD1 . LEU B 2 176 ? 10.62187  -52.31950 22.73744  1.000 200.62001 ? 176 LEU B CD1 1 
ATOM   4003 C CD2 . LEU B 2 176 ? 11.54637  -54.09356 24.23587  1.000 204.54465 ? 176 LEU B CD2 1 
ATOM   4004 N N   . GLN B 2 177 ? 7.66986   -56.00115 26.54083  1.000 209.92298 ? 177 GLN B N   1 
ATOM   4005 C CA  . GLN B 2 177 ? 6.68047   -56.06612 27.61651  1.000 214.56860 ? 177 GLN B CA  1 
ATOM   4006 C C   . GLN B 2 177 ? 6.82256   -54.87922 28.56534  1.000 212.88354 ? 177 GLN B C   1 
ATOM   4007 O O   . GLN B 2 177 ? 5.93397   -54.02628 28.65261  1.000 213.21573 ? 177 GLN B O   1 
ATOM   4008 C CB  . GLN B 2 177 ? 6.81809   -57.39233 28.37153  1.000 219.91368 ? 177 GLN B CB  1 
ATOM   4009 C CG  . GLN B 2 177 ? 6.61495   -58.62260 27.50333  1.000 222.38333 ? 177 GLN B CG  1 
ATOM   4010 C CD  . GLN B 2 177 ? 6.89359   -59.91260 28.24854  1.000 227.51849 ? 177 GLN B CD  1 
ATOM   4011 O OE1 . GLN B 2 177 ? 7.60695   -59.92157 29.25165  1.000 228.27387 ? 177 GLN B OE1 1 
ATOM   4012 N NE2 . GLN B 2 177 ? 6.32412   -61.01048 27.76500  1.000 231.21418 ? 177 GLN B NE2 1 
ATOM   4013 N N   . SER B 2 178 ? 7.93892   -54.81730 29.29047  1.000 218.34104 ? 178 SER B N   1 
ATOM   4014 C CA  . SER B 2 178 ? 8.21380   -53.73328 30.22426  1.000 216.87190 ? 178 SER B CA  1 
ATOM   4015 C C   . SER B 2 178 ? 9.69073   -53.35011 30.11200  1.000 212.90589 ? 178 SER B C   1 
ATOM   4016 O O   . SER B 2 178 ? 10.46005  -53.40939 31.06716  1.000 214.16459 ? 178 SER B O   1 
ATOM   4017 C CB  . SER B 2 178 ? 7.84146   -54.13123 31.65152  1.000 222.10697 ? 178 SER B CB  1 
ATOM   4018 O OG  . SER B 2 178 ? 6.47377   -54.49200 31.74095  1.000 226.89401 ? 178 SER B OG  1 
ATOM   4019 N N   . GLY B 2 179 ? 10.09632  -52.95249 28.90618  1.000 212.17769 ? 179 GLY B N   1 
ATOM   4020 C CA  . GLY B 2 179 ? 11.46262  -52.58001 28.62826  1.000 209.13237 ? 179 GLY B CA  1 
ATOM   4021 C C   . GLY B 2 179 ? 12.32441  -53.68560 28.05571  1.000 210.57829 ? 179 GLY B C   1 
ATOM   4022 O O   . GLY B 2 179 ? 13.40521  -53.39819 27.52935  1.000 208.61271 ? 179 GLY B O   1 
ATOM   4023 N N   . LEU B 2 180 ? 11.87933  -54.93699 28.13564  1.000 211.22685 ? 180 LEU B N   1 
ATOM   4024 C CA  . LEU B 2 180 ? 12.65387  -56.07965 27.67762  1.000 211.97459 ? 180 LEU B CA  1 
ATOM   4025 C C   . LEU B 2 180 ? 11.91467  -56.80582 26.56227  1.000 210.09929 ? 180 LEU B C   1 
ATOM   4026 O O   . LEU B 2 180 ? 10.68532  -56.74433 26.46606  1.000 213.41981 ? 180 LEU B O   1 
ATOM   4027 C CB  . LEU B 2 180 ? 12.93471  -57.05643 28.82700  1.000 218.96750 ? 180 LEU B CB  1 
ATOM   4028 C CG  . LEU B 2 180 ? 13.69577  -56.50457 30.03312  1.000 219.61474 ? 180 LEU B CG  1 
ATOM   4029 C CD1 . LEU B 2 180 ? 13.81226  -57.56114 31.11974  1.000 225.12384 ? 180 LEU B CD1 1 
ATOM   4030 C CD2 . LEU B 2 180 ? 15.06961  -56.00794 29.61624  1.000 217.90185 ? 180 LEU B CD2 1 
ATOM   4031 N N   . TYR B 2 181 ? 12.67743  -57.49982 25.72175  1.000 216.75055 ? 181 TYR B N   1 
ATOM   4032 C CA  . TYR B 2 181 ? 12.09030  -58.30453 24.66365  1.000 208.91998 ? 181 TYR B CA  1 
ATOM   4033 C C   . TYR B 2 181 ? 11.64067  -59.65998 25.20832  1.000 220.33140 ? 181 TYR B C   1 
ATOM   4034 O O   . TYR B 2 181 ? 12.07391  -60.10714 26.27371  1.000 227.13254 ? 181 TYR B O   1 
ATOM   4035 C CB  . TYR B 2 181 ? 13.08329  -58.51659 23.52008  1.000 202.89367 ? 181 TYR B CB  1 
ATOM   4036 C CG  . TYR B 2 181 ? 13.71292  -57.26161 22.95743  1.000 200.17085 ? 181 TYR B CG  1 
ATOM   4037 C CD1 . TYR B 2 181 ? 13.03391  -56.46837 22.04189  1.000 196.39772 ? 181 TYR B CD1 1 
ATOM   4038 C CD2 . TYR B 2 181 ? 15.00167  -56.88931 23.31736  1.000 200.21400 ? 181 TYR B CD2 1 
ATOM   4039 C CE1 . TYR B 2 181 ? 13.61386  -55.32771 21.51680  1.000 192.64766 ? 181 TYR B CE1 1 
ATOM   4040 C CE2 . TYR B 2 181 ? 15.58958  -55.75294 22.79769  1.000 198.27774 ? 181 TYR B CE2 1 
ATOM   4041 C CZ  . TYR B 2 181 ? 14.89223  -54.97611 21.89801  1.000 195.39676 ? 181 TYR B CZ  1 
ATOM   4042 O OH  . TYR B 2 181 ? 15.47682  -53.84361 21.37960  1.000 198.21978 ? 181 TYR B OH  1 
ATOM   4043 N N   . THR B 2 182 ? 10.76053  -60.31679 24.45297  1.000 206.61788 ? 182 THR B N   1 
ATOM   4044 C CA  . THR B 2 182 ? 10.25797  -61.63922 24.80450  1.000 212.47393 ? 182 THR B CA  1 
ATOM   4045 C C   . THR B 2 182 ? 9.72589   -62.30347 23.54122  1.000 202.31986 ? 182 THR B C   1 
ATOM   4046 O O   . THR B 2 182 ? 9.03841   -61.66043 22.74413  1.000 205.10740 ? 182 THR B O   1 
ATOM   4047 C CB  . THR B 2 182 ? 9.15870   -61.55896 25.87473  1.000 217.42032 ? 182 THR B CB  1 
ATOM   4048 O OG1 . THR B 2 182 ? 9.70715   -61.03410 27.09062  1.000 229.32928 ? 182 THR B OG1 1 
ATOM   4049 C CG2 . THR B 2 182 ? 8.56327   -62.93426 26.14874  1.000 224.86090 ? 182 THR B CG2 1 
ATOM   4050 N N   . LEU B 2 183 ? 10.04848  -63.58438 23.36055  1.000 201.87074 ? 183 LEU B N   1 
ATOM   4051 C CA  . LEU B 2 183 ? 9.65104   -64.29432 22.15287  1.000 209.49877 ? 183 LEU B CA  1 
ATOM   4052 C C   . LEU B 2 183 ? 9.40603   -65.76368 22.47072  1.000 217.13455 ? 183 LEU B C   1 
ATOM   4053 O O   . LEU B 2 183 ? 9.70779   -66.24957 23.56379  1.000 226.39851 ? 183 LEU B O   1 
ATOM   4054 C CB  . LEU B 2 183 ? 10.70855  -64.15079 21.05006  1.000 199.82205 ? 183 LEU B CB  1 
ATOM   4055 C CG  . LEU B 2 183 ? 11.99701  -64.96963 21.18514  1.000 200.58963 ? 183 LEU B CG  1 
ATOM   4056 C CD1 . LEU B 2 183 ? 11.95465  -66.21273 20.30423  1.000 202.37393 ? 183 LEU B CD1 1 
ATOM   4057 C CD2 . LEU B 2 183 ? 13.21365  -64.12541 20.85063  1.000 199.02400 ? 183 LEU B CD2 1 
ATOM   4058 N N   . THR B 2 184 ? 8.85070   -66.46726 21.48461  1.000 214.31362 ? 184 THR B N   1 
ATOM   4059 C CA  . THR B 2 184 ? 8.63421   -67.90496 21.54671  1.000 218.71874 ? 184 THR B CA  1 
ATOM   4060 C C   . THR B 2 184 ? 9.03614   -68.51844 20.21358  1.000 214.38980 ? 184 THR B C   1 
ATOM   4061 O O   . THR B 2 184 ? 9.02091   -67.84886 19.17774  1.000 214.04815 ? 184 THR B O   1 
ATOM   4062 C CB  . THR B 2 184 ? 7.17140   -68.25331 21.86001  1.000 234.68667 ? 184 THR B CB  1 
ATOM   4063 O OG1 . THR B 2 184 ? 6.30207   -67.40276 21.10143  1.000 233.92224 ? 184 THR B OG1 1 
ATOM   4064 C CG2 . THR B 2 184 ? 6.88151   -68.08187 23.34134  1.000 238.21468 ? 184 THR B CG2 1 
ATOM   4065 N N   . SER B 2 185 ? 9.39285   -69.80119 20.24590  1.000 217.50324 ? 185 SER B N   1 
ATOM   4066 C CA  . SER B 2 185 ? 9.83843   -70.51499 19.05100  0.000 220.81204 ? 185 SER B CA  1 
ATOM   4067 C C   . SER B 2 185 ? 9.29806   -71.93603 19.10742  0.000 232.12087 ? 185 SER B C   1 
ATOM   4068 O O   . SER B 2 185 ? 9.75215   -72.74031 19.92639  0.000 233.45385 ? 185 SER B O   1 
ATOM   4069 C CB  . SER B 2 185 ? 11.36328  -70.51603 18.94517  0.000 225.27113 ? 185 SER B CB  1 
ATOM   4070 O OG  . SER B 2 185 ? 11.79506  -71.29224 17.84203  0.000 227.36761 ? 185 SER B OG  1 
ATOM   4071 N N   . SER B 2 186 ? 8.34571   -72.24646 18.23328  0.000 233.04088 ? 186 SER B N   1 
ATOM   4072 C CA  . SER B 2 186 ? 7.70740   -73.55286 18.18446  0.000 235.28091 ? 186 SER B CA  1 
ATOM   4073 C C   . SER B 2 186 ? 8.21579   -74.36197 16.99632  0.000 234.46452 ? 186 SER B C   1 
ATOM   4074 O O   . SER B 2 186 ? 8.70971   -73.81688 16.00539  0.000 232.18523 ? 186 SER B O   1 
ATOM   4075 C CB  . SER B 2 186 ? 6.18329   -73.40968 18.10363  0.000 237.35661 ? 186 SER B CB  1 
ATOM   4076 O OG  . SER B 2 186 ? 5.80127   -72.63898 16.97663  0.000 235.81591 ? 186 SER B OG  1 
ATOM   4077 N N   . VAL B 2 187 ? 8.08425   -75.68342 17.10745  0.000 237.23766 ? 187 VAL B N   1 
ATOM   4078 C CA  . VAL B 2 187 ? 8.42845   -76.59865 16.02350  0.000 237.07299 ? 187 VAL B CA  1 
ATOM   4079 C C   . VAL B 2 187 ? 7.40203   -77.72506 16.00715  0.000 240.01507 ? 187 VAL B C   1 
ATOM   4080 O O   . VAL B 2 187 ? 7.22430   -78.42602 17.00999  0.000 241.53214 ? 187 VAL B O   1 
ATOM   4081 C CB  . VAL B 2 187 ? 9.85891   -77.15925 16.15241  0.000 235.85718 ? 187 VAL B CB  1 
ATOM   4082 C CG1 . VAL B 2 187 ? 10.10061  -77.75214 17.53471  0.000 236.97552 ? 187 VAL B CG1 1 
ATOM   4083 C CG2 . VAL B 2 187 ? 10.12644  -78.19154 15.06609  0.000 236.14390 ? 187 VAL B CG2 1 
ATOM   4084 N N   . THR B 2 188 ? 6.71022   -77.88531 14.88196  0.000 238.30558 ? 188 THR B N   1 
ATOM   4085 C CA  . THR B 2 188 ? 5.69924   -78.92843 14.74610  0.000 241.46976 ? 188 THR B CA  1 
ATOM   4086 C C   . THR B 2 188 ? 6.38735   -80.23127 14.35792  0.000 241.81713 ? 188 THR B C   1 
ATOM   4087 O O   . THR B 2 188 ? 6.93292   -80.35082 13.25605  0.000 240.88675 ? 188 THR B O   1 
ATOM   4088 C CB  . THR B 2 188 ? 4.64922   -78.53103 13.71236  0.000 242.72850 ? 188 THR B CB  1 
ATOM   4089 O OG1 . THR B 2 188 ? 4.02065   -77.30701 14.11333  0.000 242.26944 ? 188 THR B OG1 1 
ATOM   4090 C CG2 . THR B 2 188 ? 3.59099   -79.61700 13.58597  0.000 246.64024 ? 188 THR B CG2 1 
ATOM   4091 N N   . VAL B 2 189 ? 6.36816   -81.20502 15.26220  0.000 243.74944 ? 189 VAL B N   1 
ATOM   4092 C CA  . VAL B 2 189 ? 6.99043   -82.50349 15.01847  0.000 244.12118 ? 189 VAL B CA  1 
ATOM   4093 C C   . VAL B 2 189 ? 5.88808   -83.53978 14.82995  0.000 247.68361 ? 189 VAL B C   1 
ATOM   4094 O O   . VAL B 2 189 ? 4.76342   -83.33711 15.31169  0.000 249.90875 ? 189 VAL B O   1 
ATOM   4095 C CB  . VAL B 2 189 ? 7.94109   -82.88950 16.16406  0.000 242.79825 ? 189 VAL B CB  1 
ATOM   4096 C CG1 . VAL B 2 189 ? 8.94696   -81.77507 16.41537  0.000 239.93934 ? 189 VAL B CG1 1 
ATOM   4097 C CG2 . VAL B 2 189 ? 7.15845   -83.20579 17.42958  0.000 244.67805 ? 189 VAL B CG2 1 
ATOM   4098 N N   . PRO B 2 190 ? 6.14767   -84.64280 14.12699  0.000 247.20778 ? 190 PRO B N   1 
ATOM   4099 C CA  . PRO B 2 190 ? 5.11643   -85.67398 13.96871  0.000 250.94454 ? 190 PRO B CA  1 
ATOM   4100 C C   . PRO B 2 190 ? 4.71964   -86.28070 15.30692  0.000 252.23241 ? 190 PRO B C   1 
ATOM   4101 O O   . PRO B 2 190 ? 5.43829   -86.18756 16.30464  0.000 250.21490 ? 190 PRO B O   1 
ATOM   4102 C CB  . PRO B 2 190 ? 5.78673   -86.71351 13.06161  0.000 251.33374 ? 190 PRO B CB  1 
ATOM   4103 C CG  . PRO B 2 190 ? 6.84958   -85.95360 12.33860  0.000 248.23978 ? 190 PRO B CG  1 
ATOM   4104 C CD  . PRO B 2 190 ? 7.34513   -84.93317 13.31973  0.000 245.26007 ? 190 PRO B CD  1 
ATOM   4105 N N   . SER B 2 191 ? 3.54476   -86.91602 15.31294  1.000 251.39645 ? 191 SER B N   1 
ATOM   4106 C CA  . SER B 2 191 ? 3.01548   -87.48755 16.54715  1.000 253.22561 ? 191 SER B CA  1 
ATOM   4107 C C   . SER B 2 191 ? 3.89288   -88.61605 17.07342  1.000 252.08263 ? 191 SER B C   1 
ATOM   4108 O O   . SER B 2 191 ? 3.96874   -88.82583 18.28929  1.000 252.02139 ? 191 SER B O   1 
ATOM   4109 C CB  . SER B 2 191 ? 1.58907   -87.99029 16.32155  1.000 257.89709 ? 191 SER B CB  1 
ATOM   4110 O OG  . SER B 2 191 ? 0.74636   -86.94798 15.86233  1.000 259.00236 ? 191 SER B OG  1 
ATOM   4111 N N   . SER B 2 192 ? 4.56416   -89.34784 16.18281  1.000 257.96735 ? 192 SER B N   1 
ATOM   4112 C CA  . SER B 2 192 ? 5.35995   -90.49570 16.59927  1.000 257.04808 ? 192 SER B CA  1 
ATOM   4113 C C   . SER B 2 192 ? 6.70950   -90.10545 17.18829  1.000 253.09110 ? 192 SER B C   1 
ATOM   4114 O O   . SER B 2 192 ? 7.30878   -90.91051 17.90905  1.000 252.31922 ? 192 SER B O   1 
ATOM   4115 C CB  . SER B 2 192 ? 5.57911   -91.44124 15.41592  1.000 258.22128 ? 192 SER B CB  1 
ATOM   4116 O OG  . SER B 2 192 ? 6.41597   -90.84760 14.43819  1.000 256.03107 ? 192 SER B OG  1 
ATOM   4117 N N   . THR B 2 193 ? 7.19898   -88.89686 16.90597  1.000 255.34309 ? 193 THR B N   1 
ATOM   4118 C CA  . THR B 2 193 ? 8.53616   -88.50748 17.33824  1.000 252.04717 ? 193 THR B CA  1 
ATOM   4119 C C   . THR B 2 193 ? 8.59555   -88.07737 18.79935  1.000 251.58533 ? 193 THR B C   1 
ATOM   4120 O O   . THR B 2 193 ? 9.67378   -88.13225 19.40029  1.000 249.56214 ? 193 THR B O   1 
ATOM   4121 C CB  . THR B 2 193 ? 9.06863   -87.37970 16.45079  1.000 250.06727 ? 193 THR B CB  1 
ATOM   4122 O OG1 . THR B 2 193 ? 8.06352   -86.36894 16.30296  1.000 250.99069 ? 193 THR B OG1 1 
ATOM   4123 C CG2 . THR B 2 193 ? 9.45043   -87.91708 15.07898  1.000 250.47979 ? 193 THR B CG2 1 
ATOM   4124 N N   . TRP B 2 194 ? 7.47778   -87.65710 19.38202  1.000 251.33862 ? 194 TRP B N   1 
ATOM   4125 C CA  . TRP B 2 194 ? 7.42254   -87.22958 20.77174  1.000 251.58655 ? 194 TRP B CA  1 
ATOM   4126 C C   . TRP B 2 194 ? 6.11364   -87.71705 21.37522  1.000 255.33009 ? 194 TRP B C   1 
ATOM   4127 O O   . TRP B 2 194 ? 5.09160   -87.75808 20.67983  1.000 257.57788 ? 194 TRP B O   1 
ATOM   4128 C CB  . TRP B 2 194 ? 7.53044   -85.69939 20.89213  1.000 250.22383 ? 194 TRP B CB  1 
ATOM   4129 C CG  . TRP B 2 194 ? 7.82965   -85.21912 22.27825  1.000 250.21339 ? 194 TRP B CG  1 
ATOM   4130 C CD1 . TRP B 2 194 ? 9.02489   -85.29541 22.93222  1.000 248.41157 ? 194 TRP B CD1 1 
ATOM   4131 C CD2 . TRP B 2 194 ? 6.91395   -84.60031 23.18844  1.000 252.66793 ? 194 TRP B CD2 1 
ATOM   4132 N NE1 . TRP B 2 194 ? 8.91170   -84.75829 24.19104  1.000 249.56655 ? 194 TRP B NE1 1 
ATOM   4133 C CE2 . TRP B 2 194 ? 7.62499   -84.32476 24.37331  1.000 252.16011 ? 194 TRP B CE2 1 
ATOM   4134 C CE3 . TRP B 2 194 ? 5.56220   -84.25201 23.11645  1.000 255.52951 ? 194 TRP B CE3 1 
ATOM   4135 C CZ2 . TRP B 2 194 ? 7.03052   -83.71549 25.47512  1.000 254.44931 ? 194 TRP B CZ2 1 
ATOM   4136 C CZ3 . TRP B 2 194 ? 4.97417   -83.64765 24.21103  1.000 257.79286 ? 194 TRP B CZ3 1 
ATOM   4137 C CH2 . TRP B 2 194 ? 5.70763   -83.38443 25.37385  1.000 257.26928 ? 194 TRP B CH2 1 
ATOM   4138 N N   . PRO B 2 195 ? 6.10520   -88.09242 22.66935  1.000 252.54139 ? 195 PRO B N   1 
ATOM   4139 C CA  . PRO B 2 195 ? 7.17355   -88.05430 23.67881  1.000 250.59958 ? 195 PRO B CA  1 
ATOM   4140 C C   . PRO B 2 195 ? 8.17686   -89.20601 23.62340  1.000 248.90478 ? 195 PRO B C   1 
ATOM   4141 O O   . PRO B 2 195 ? 8.72691   -89.57437 24.66139  1.000 248.55892 ? 195 PRO B O   1 
ATOM   4142 C CB  . PRO B 2 195 ? 6.39581   -88.09991 24.99517  1.000 253.41885 ? 195 PRO B CB  1 
ATOM   4143 C CG  . PRO B 2 195 ? 5.18989   -88.89385 24.66905  1.000 256.54522 ? 195 PRO B CG  1 
ATOM   4144 C CD  . PRO B 2 195 ? 4.82364   -88.52458 23.25655  1.000 256.45452 ? 195 PRO B CD  1 
ATOM   4145 N N   . SER B 2 196 ? 8.42151   -89.75620 22.43579  1.000 255.74236 ? 196 SER B N   1 
ATOM   4146 C CA  . SER B 2 196 ? 9.40239   -90.82387 22.29085  1.000 254.14917 ? 196 SER B CA  1 
ATOM   4147 C C   . SER B 2 196 ? 10.82003  -90.27194 22.38206  1.000 250.97677 ? 196 SER B C   1 
ATOM   4148 O O   . SER B 2 196 ? 11.52800  -90.52198 23.36287  1.000 250.10325 ? 196 SER B O   1 
ATOM   4149 C CB  . SER B 2 196 ? 9.20618   -91.56062 20.96461  1.000 254.74063 ? 196 SER B CB  1 
ATOM   4150 O OG  . SER B 2 196 ? 9.60246   -90.75281 19.87082  1.000 252.70965 ? 196 SER B OG  1 
ATOM   4151 N N   . GLN B 2 197 ? 11.23924  -89.51745 21.36932  1.000 256.20375 ? 197 GLN B N   1 
ATOM   4152 C CA  . GLN B 2 197 ? 12.60182  -89.01130 21.32447  1.000 253.68689 ? 197 GLN B CA  1 
ATOM   4153 C C   . GLN B 2 197 ? 12.79094  -87.85662 22.30588  1.000 253.51237 ? 197 GLN B C   1 
ATOM   4154 O O   . GLN B 2 197 ? 11.83438  -87.22993 22.77063  1.000 255.08622 ? 197 GLN B O   1 
ATOM   4155 C CB  . GLN B 2 197 ? 12.96036  -88.55371 19.91022  1.000 252.36109 ? 197 GLN B CB  1 
ATOM   4156 C CG  . GLN B 2 197 ? 12.83853  -89.63534 18.85047  1.000 253.27904 ? 197 GLN B CG  1 
ATOM   4157 C CD  . GLN B 2 197 ? 13.43171  -89.21143 17.52103  1.000 252.19623 ? 197 GLN B CD  1 
ATOM   4158 O OE1 . GLN B 2 197 ? 14.59322  -88.80963 17.44697  1.000 250.23852 ? 197 GLN B OE1 1 
ATOM   4159 N NE2 . GLN B 2 197 ? 12.63317  -89.29223 16.46314  1.000 253.78709 ? 197 GLN B NE2 1 
ATOM   4160 N N   . THR B 2 198 ? 14.05627  -87.58142 22.61644  1.000 247.94324 ? 198 THR B N   1 
ATOM   4161 C CA  . THR B 2 198 ? 14.42497  -86.48436 23.50588  1.000 248.10871 ? 198 THR B CA  1 
ATOM   4162 C C   . THR B 2 198 ? 14.44642  -85.18728 22.70487  1.000 247.19857 ? 198 THR B C   1 
ATOM   4163 O O   . THR B 2 198 ? 15.26784  -85.02303 21.79694  1.000 245.46792 ? 198 THR B O   1 
ATOM   4164 C CB  . THR B 2 198 ? 15.78232  -86.75604 24.15071  1.000 247.12751 ? 198 THR B CB  1 
ATOM   4165 O OG1 . THR B 2 198 ? 15.65517  -87.80608 25.11842  1.000 248.44277 ? 198 THR B OG1 1 
ATOM   4166 C CG2 . THR B 2 198 ? 16.32358  -85.50273 24.82763  1.000 247.45516 ? 198 THR B CG2 1 
ATOM   4167 N N   . VAL B 2 199 ? 13.54382  -84.26793 23.03422  1.000 244.62674 ? 199 VAL B N   1 
ATOM   4168 C CA  . VAL B 2 199 ? 13.43486  -82.98690 22.34732  1.000 243.73282 ? 199 VAL B CA  1 
ATOM   4169 C C   . VAL B 2 199 ? 14.17287  -81.94106 23.17061  1.000 243.63983 ? 199 VAL B C   1 
ATOM   4170 O O   . VAL B 2 199 ? 13.81438  -81.67676 24.32462  1.000 245.34005 ? 199 VAL B O   1 
ATOM   4171 C CB  . VAL B 2 199 ? 11.96878  -82.58893 22.12263  1.000 245.01827 ? 199 VAL B CB  1 
ATOM   4172 C CG1 . VAL B 2 199 ? 11.88349  -81.18292 21.55595  1.000 243.74301 ? 199 VAL B CG1 1 
ATOM   4173 C CG2 . VAL B 2 199 ? 11.29864  -83.57620 21.18323  1.000 245.64166 ? 199 VAL B CG2 1 
ATOM   4174 N N   . THR B 2 200 ? 15.20155  -81.34487 22.57502  1.000 244.25487 ? 200 THR B N   1 
ATOM   4175 C CA  . THR B 2 200 ? 16.08696  -80.40708 23.24946  1.000 244.59685 ? 200 THR B CA  1 
ATOM   4176 C C   . THR B 2 200 ? 15.90390  -79.01233 22.66367  1.000 243.77053 ? 200 THR B C   1 
ATOM   4177 O O   . THR B 2 200 ? 15.86678  -78.84755 21.44028  1.000 242.11551 ? 200 THR B O   1 
ATOM   4178 C CB  . THR B 2 200 ? 17.54689  -80.85721 23.11126  1.000 243.87433 ? 200 THR B CB  1 
ATOM   4179 O OG1 . THR B 2 200 ? 17.79686  -81.96961 23.98225  1.000 244.81866 ? 200 THR B OG1 1 
ATOM   4180 C CG2 . THR B 2 200 ? 18.50412  -79.72065 23.43526  1.000 244.48633 ? 200 THR B CG2 1 
ATOM   4181 N N   . CYS B 2 201 ? 15.78861  -78.01050 23.53840  1.000 236.81505 ? 201 CYS B N   1 
ATOM   4182 C CA  . CYS B 2 201 ? 15.71013  -76.61008 23.13402  1.000 236.08454 ? 201 CYS B CA  1 
ATOM   4183 C C   . CYS B 2 201 ? 17.01300  -75.91919 23.52093  1.000 236.84714 ? 201 CYS B C   1 
ATOM   4184 O O   . CYS B 2 201 ? 17.29747  -75.74167 24.71041  1.000 239.35336 ? 201 CYS B O   1 
ATOM   4185 C CB  . CYS B 2 201 ? 14.51815  -75.90285 23.77650  1.000 237.05744 ? 201 CYS B CB  1 
ATOM   4186 S SG  . CYS B 2 201 ? 14.45583  -74.14028 23.35308  1.000 236.11398 ? 201 CYS B SG  1 
ATOM   4187 N N   . ASN B 2 202 ? 17.79241  -75.51836 22.51982  1.000 232.22201 ? 202 ASN B N   1 
ATOM   4188 C CA  . ASN B 2 202 ? 19.02828  -74.77882 22.73348  1.000 233.20994 ? 202 ASN B CA  1 
ATOM   4189 C C   . ASN B 2 202 ? 18.75339  -73.29380 22.52569  1.000 232.32385 ? 202 ASN B C   1 
ATOM   4190 O O   . ASN B 2 202 ? 18.25511  -72.89301 21.46801  1.000 229.82829 ? 202 ASN B O   1 
ATOM   4191 C CB  . ASN B 2 202 ? 20.12716  -75.25858 21.78227  1.000 232.30530 ? 202 ASN B CB  1 
ATOM   4192 C CG  . ASN B 2 202 ? 20.14951  -76.76648 21.62829  1.000 231.74750 ? 202 ASN B CG  1 
ATOM   4193 O OD1 . ASN B 2 202 ? 19.33450  -77.33879 20.90403  1.000 230.32263 ? 202 ASN B OD1 1 
ATOM   4194 N ND2 . ASN B 2 202 ? 21.09368  -77.41763 22.29859  1.000 233.00460 ? 202 ASN B ND2 1 
ATOM   4195 N N   . VAL B 2 203 ? 19.07460  -72.48192 23.53112  1.000 221.94545 ? 203 VAL B N   1 
ATOM   4196 C CA  . VAL B 2 203 ? 18.89226  -71.03539 23.47087  1.000 219.41795 ? 203 VAL B CA  1 
ATOM   4197 C C   . VAL B 2 203 ? 20.20188  -70.37430 23.87236  1.000 219.73293 ? 203 VAL B C   1 
ATOM   4198 O O   . VAL B 2 203 ? 20.81148  -70.75728 24.87693  1.000 223.61776 ? 203 VAL B O   1 
ATOM   4199 C CB  . VAL B 2 203 ? 17.74509  -70.55713 24.38249  1.000 218.33291 ? 203 VAL B CB  1 
ATOM   4200 C CG1 . VAL B 2 203 ? 17.55820  -69.04969 24.25881  1.000 215.84886 ? 203 VAL B CG1 1 
ATOM   4201 C CG2 . VAL B 2 203 ? 16.45424  -71.28183 24.04480  1.000 218.71152 ? 203 VAL B CG2 1 
ATOM   4202 N N   . ALA B 2 204 ? 20.63274  -69.38541 23.09171  1.000 217.11466 ? 204 ALA B N   1 
ATOM   4203 C CA  . ALA B 2 204 ? 21.86964  -68.67043 23.36776  1.000 224.99798 ? 204 ALA B CA  1 
ATOM   4204 C C   . ALA B 2 204 ? 21.67518  -67.18419 23.10950  1.000 228.99534 ? 204 ALA B C   1 
ATOM   4205 O O   . ALA B 2 204 ? 20.96487  -66.79336 22.17885  1.000 205.54180 ? 204 ALA B O   1 
ATOM   4206 C CB  . ALA B 2 204 ? 23.02933  -69.20458 22.51711  1.000 214.36705 ? 204 ALA B CB  1 
ATOM   4207 N N   . HIS B 2 205 ? 22.31312  -66.36121 23.94356  1.000 217.19045 ? 205 HIS B N   1 
ATOM   4208 C CA  . HIS B 2 205 ? 22.27249  -64.90302 23.83711  1.000 214.53273 ? 205 HIS B CA  1 
ATOM   4209 C C   . HIS B 2 205 ? 23.69973  -64.42052 23.61416  1.000 220.45359 ? 205 HIS B C   1 
ATOM   4210 O O   . HIS B 2 205 ? 24.44222  -64.18287 24.58036  1.000 225.72216 ? 205 HIS B O   1 
ATOM   4211 C CB  . HIS B 2 205 ? 21.65943  -64.28060 25.09069  1.000 216.90730 ? 205 HIS B CB  1 
ATOM   4212 C CG  . HIS B 2 205 ? 21.39824  -62.81065 24.98133  1.000 214.38662 ? 205 HIS B CG  1 
ATOM   4213 N ND1 . HIS B 2 205 ? 20.94127  -62.05921 26.04262  1.000 216.39451 ? 205 HIS B ND1 1 
ATOM   4214 C CD2 . HIS B 2 205 ? 21.52278  -61.95410 23.94019  1.000 210.48000 ? 205 HIS B CD2 1 
ATOM   4215 C CE1 . HIS B 2 205 ? 20.79898  -60.80264 25.66132  1.000 212.14957 ? 205 HIS B CE1 1 
ATOM   4216 N NE2 . HIS B 2 205 ? 21.14494  -60.71194 24.38986  1.000 207.96012 ? 205 HIS B NE2 1 
ATOM   4217 N N   . PRO B 2 206 ? 24.12933  -64.26849 22.35813  1.000 216.42119 ? 206 PRO B N   1 
ATOM   4218 C CA  . PRO B 2 206 ? 25.53241  -63.90126 22.09807  1.000 219.78894 ? 206 PRO B CA  1 
ATOM   4219 C C   . PRO B 2 206 ? 25.93440  -62.55361 22.67103  1.000 220.97707 ? 206 PRO B C   1 
ATOM   4220 O O   . PRO B 2 206 ? 27.13000  -62.32965 22.89912  1.000 223.96167 ? 206 PRO B O   1 
ATOM   4221 C CB  . PRO B 2 206 ? 25.61774  -63.90163 20.56444  1.000 216.26134 ? 206 PRO B CB  1 
ATOM   4222 C CG  . PRO B 2 206 ? 24.46731  -64.74335 20.11270  1.000 210.83963 ? 206 PRO B CG  1 
ATOM   4223 C CD  . PRO B 2 206 ? 23.37922  -64.50370 21.11394  1.000 207.29569 ? 206 PRO B CD  1 
ATOM   4224 N N   . ALA B 2 207 ? 24.98212  -61.64887 22.90733  1.000 216.07528 ? 207 ALA B N   1 
ATOM   4225 C CA  . ALA B 2 207 ? 25.32100  -60.35157 23.48344  1.000 216.34686 ? 207 ALA B CA  1 
ATOM   4226 C C   . ALA B 2 207 ? 25.85640  -60.50532 24.90183  1.000 223.48482 ? 207 ALA B C   1 
ATOM   4227 O O   . ALA B 2 207 ? 26.88236  -59.91479 25.25893  1.000 226.21303 ? 207 ALA B O   1 
ATOM   4228 C CB  . ALA B 2 207 ? 24.09943  -59.43257 23.46257  1.000 201.10805 ? 207 ALA B CB  1 
ATOM   4229 N N   . SER B 2 208 ? 25.17495  -61.30030 25.72476  1.000 213.14520 ? 208 SER B N   1 
ATOM   4230 C CA  . SER B 2 208 ? 25.58092  -61.53358 27.10373  1.000 218.09306 ? 208 SER B CA  1 
ATOM   4231 C C   . SER B 2 208 ? 26.36465  -62.82706 27.28306  1.000 223.46505 ? 208 SER B C   1 
ATOM   4232 O O   . SER B 2 208 ? 26.72507  -63.16228 28.41606  1.000 228.02272 ? 208 SER B O   1 
ATOM   4233 C CB  . SER B 2 208 ? 24.35357  -61.54180 28.02057  1.000 216.16154 ? 208 SER B CB  1 
ATOM   4234 O OG  . SER B 2 208 ? 23.41617  -62.52013 27.60766  1.000 214.29708 ? 208 SER B OG  1 
ATOM   4235 N N   . SER B 2 209 ? 26.62340  -63.56100 26.19920  1.000 218.15961 ? 209 SER B N   1 
ATOM   4236 C CA  . SER B 2 209 ? 27.46243  -64.76002 26.21636  1.000 221.26485 ? 209 SER B CA  1 
ATOM   4237 C C   . SER B 2 209 ? 26.89140  -65.83170 27.14876  1.000 222.09886 ? 209 SER B C   1 
ATOM   4238 O O   . SER B 2 209 ? 27.53286  -66.26868 28.10537  1.000 225.22904 ? 209 SER B O   1 
ATOM   4239 C CB  . SER B 2 209 ? 28.90463  -64.41031 26.60179  1.000 224.97910 ? 209 SER B CB  1 
ATOM   4240 O OG  . SER B 2 209 ? 29.42423  -63.38591 25.77324  1.000 224.47666 ? 209 SER B OG  1 
ATOM   4241 N N   . THR B 2 210 ? 25.66620  -66.25656 26.84807  1.000 229.49735 ? 210 THR B N   1 
ATOM   4242 C CA  . THR B 2 210 ? 25.02490  -67.34175 27.57491  1.000 230.81710 ? 210 THR B CA  1 
ATOM   4243 C C   . THR B 2 210 ? 24.49060  -68.36771 26.58503  1.000 225.52825 ? 210 THR B C   1 
ATOM   4244 O O   . THR B 2 210 ? 24.34550  -68.09463 25.39065  1.000 220.70583 ? 210 THR B O   1 
ATOM   4245 C CB  . THR B 2 210 ? 23.88743  -66.84081 28.47900  1.000 229.77965 ? 210 THR B CB  1 
ATOM   4246 O OG1 . THR B 2 210 ? 23.44371  -67.90813 29.32561  1.000 234.77558 ? 210 THR B OG1 1 
ATOM   4247 C CG2 . THR B 2 210 ? 22.71821  -66.36079 27.64844  1.000 226.57683 ? 210 THR B CG2 1 
ATOM   4248 N N   . LYS B 2 211 ? 24.19938  -69.56361 27.10397  1.000 233.59344 ? 211 LYS B N   1 
ATOM   4249 C CA  . LYS B 2 211 ? 23.74368  -70.67179 26.26577  1.000 230.55015 ? 211 LYS B CA  1 
ATOM   4250 C C   . LYS B 2 211 ? 23.04948  -71.68089 27.18164  1.000 232.28939 ? 211 LYS B C   1 
ATOM   4251 O O   . LYS B 2 211 ? 23.71492  -72.50989 27.80693  1.000 235.44856 ? 211 LYS B O   1 
ATOM   4252 C CB  . LYS B 2 211 ? 24.90443  -71.30216 25.51279  1.000 231.57597 ? 211 LYS B CB  1 
ATOM   4253 C CG  . LYS B 2 211 ? 24.53159  -72.50952 24.66984  1.000 228.87485 ? 211 LYS B CG  1 
ATOM   4254 C CD  . LYS B 2 211 ? 25.76792  -73.13621 24.04234  1.000 229.79336 ? 211 LYS B CD  1 
ATOM   4255 C CE  . LYS B 2 211 ? 25.41130  -74.36048 23.21500  1.000 230.06500 ? 211 LYS B CE  1 
ATOM   4256 N NZ  . LYS B 2 211 ? 26.61711  -74.98215 22.60102  1.000 231.66601 ? 211 LYS B NZ  1 
ATOM   4257 N N   . VAL B 2 212 ? 21.72575  -71.60144 27.24997  1.000 232.63492 ? 212 VAL B N   1 
ATOM   4258 C CA  . VAL B 2 212 ? 20.93012  -72.46469 28.11403  1.000 234.67260 ? 212 VAL B CA  1 
ATOM   4259 C C   . VAL B 2 212 ? 20.28876  -73.56125 27.27528  1.000 231.96731 ? 212 VAL B C   1 
ATOM   4260 O O   . VAL B 2 212 ? 19.87859  -73.33121 26.13160  1.000 228.68648 ? 212 VAL B O   1 
ATOM   4261 C CB  . VAL B 2 212 ? 19.86121  -71.65073 28.87334  1.000 234.70566 ? 212 VAL B CB  1 
ATOM   4262 C CG1 . VAL B 2 212 ? 19.27209  -72.46878 30.01452  1.000 237.28021 ? 212 VAL B CG1 1 
ATOM   4263 C CG2 . VAL B 2 212 ? 20.45348  -70.35006 29.39630  1.000 237.49403 ? 212 VAL B CG2 1 
ATOM   4264 N N   . ASP B 2 213 ? 20.20750  -74.76252 27.84294  1.000 243.26833 ? 213 ASP B N   1 
ATOM   4265 C CA  . ASP B 2 213 ? 19.60413  -75.91511 27.18187  1.000 240.55163 ? 213 ASP B CA  1 
ATOM   4266 C C   . ASP B 2 213 ? 18.45632  -76.43265 28.03559  1.000 241.37904 ? 213 ASP B C   1 
ATOM   4267 O O   . ASP B 2 213 ? 18.65091  -76.75115 29.21374  1.000 243.95713 ? 213 ASP B O   1 
ATOM   4268 C CB  . ASP B 2 213 ? 20.63333  -77.02300 26.94669  1.000 240.58118 ? 213 ASP B CB  1 
ATOM   4269 C CG  . ASP B 2 213 ? 21.24907  -76.96466 25.56234  1.000 238.22960 ? 213 ASP B CG  1 
ATOM   4270 O OD1 . ASP B 2 213 ? 21.21259  -75.88309 24.93784  1.000 236.85394 ? 213 ASP B OD1 1 
ATOM   4271 O OD2 . ASP B 2 213 ? 21.75937  -78.00493 25.09468  1.000 237.71521 ? 213 ASP B OD2 1 
ATOM   4272 N N   . LYS B 2 214 ? 17.27046  -76.53484 27.43825  1.000 237.81214 ? 214 LYS B N   1 
ATOM   4273 C CA  . LYS B 2 214 ? 16.08137  -77.00691 28.13553  1.000 238.74878 ? 214 LYS B CA  1 
ATOM   4274 C C   . LYS B 2 214 ? 15.44353  -78.13811 27.34441  1.000 236.92713 ? 214 LYS B C   1 
ATOM   4275 O O   . LYS B 2 214 ? 15.28219  -78.03352 26.12446  1.000 234.70603 ? 214 LYS B O   1 
ATOM   4276 C CB  . LYS B 2 214 ? 15.06847  -75.87437 28.34017  1.000 238.98501 ? 214 LYS B CB  1 
ATOM   4277 C CG  . LYS B 2 214 ? 15.57762  -74.71572 29.18099  1.000 241.11086 ? 214 LYS B CG  1 
ATOM   4278 C CD  . LYS B 2 214 ? 15.84343  -75.13539 30.61623  1.000 244.83707 ? 214 LYS B CD  1 
ATOM   4279 C CE  . LYS B 2 214 ? 16.24003  -73.94042 31.46729  1.000 247.45226 ? 214 LYS B CE  1 
ATOM   4280 N NZ  . LYS B 2 214 ? 16.55097  -74.33112 32.86913  1.000 251.58478 ? 214 LYS B NZ  1 
ATOM   4281 N N   . LYS B 2 215 ? 15.08815  -79.21339 28.03963  1.000 241.77665 ? 215 LYS B N   1 
ATOM   4282 C CA  . LYS B 2 215 ? 14.33650  -80.31260 27.45648  1.000 240.61386 ? 215 LYS B CA  1 
ATOM   4283 C C   . LYS B 2 215 ? 12.84034  -80.07912 27.67032  1.000 241.73201 ? 215 LYS B C   1 
ATOM   4284 O O   . LYS B 2 215 ? 12.42626  -79.24419 28.47706  1.000 243.48449 ? 215 LYS B O   1 
ATOM   4285 C CB  . LYS B 2 215 ? 14.78465  -81.64296 28.06916  1.000 241.34883 ? 215 LYS B CB  1 
ATOM   4286 C CG  . LYS B 2 215 ? 14.29745  -82.88957 27.34183  1.000 240.21000 ? 215 LYS B CG  1 
ATOM   4287 C CD  . LYS B 2 215 ? 14.71868  -84.15486 28.07098  1.000 240.83335 ? 215 LYS B CD  1 
ATOM   4288 C CE  . LYS B 2 215 ? 13.98981  -85.37314 27.52880  1.000 240.49595 ? 215 LYS B CE  1 
ATOM   4289 N NZ  . LYS B 2 215 ? 14.47881  -86.63394 28.14973  1.000 240.53471 ? 215 LYS B NZ  1 
ATOM   4290 N N   . ILE B 2 216 ? 12.02110  -80.82078 26.92904  1.000 236.80879 ? 216 ILE B N   1 
ATOM   4291 C CA  . ILE B 2 216 ? 10.56925  -80.68116 26.98178  1.000 238.44707 ? 216 ILE B CA  1 
ATOM   4292 C C   . ILE B 2 216 ? 9.98233   -82.00623 27.45057  1.000 240.26092 ? 216 ILE B C   1 
ATOM   4293 O O   . ILE B 2 216 ? 9.98317   -82.99423 26.70440  1.000 239.36990 ? 216 ILE B O   1 
ATOM   4294 C CB  . ILE B 2 216 ? 9.97463   -80.26401 25.62927  1.000 237.26011 ? 216 ILE B CB  1 
ATOM   4295 C CG1 . ILE B 2 216 ? 10.49155  -78.88390 25.20843  1.000 235.32683 ? 216 ILE B CG1 1 
ATOM   4296 C CG2 . ILE B 2 216 ? 8.45585   -80.25508 25.70230  1.000 239.92971 ? 216 ILE B CG2 1 
ATOM   4297 C CD1 . ILE B 2 216 ? 11.77610  -78.91186 24.40174  1.000 232.65003 ? 216 ILE B CD1 1 
ATOM   4298 N N   . VAL B 2 217 ? 9.48360   -82.02750 28.68342  0.000 239.48781 ? 217 VAL B N   1 
ATOM   4299 C CA  . VAL B 2 217 ? 8.78219   -83.17977 29.24681  0.000 241.69629 ? 217 VAL B CA  1 
ATOM   4300 C C   . VAL B 2 217 ? 7.59232   -82.66174 30.04684  0.000 245.25461 ? 217 VAL B C   1 
ATOM   4301 O O   . VAL B 2 217 ? 7.76674   -81.80241 30.92317  0.000 246.25215 ? 217 VAL B O   1 
ATOM   4302 C CB  . VAL B 2 217 ? 9.71124   -84.03740 30.12234  0.000 241.58294 ? 217 VAL B CB  1 
ATOM   4303 C CG1 . VAL B 2 217 ? 8.89747   -84.95999 31.01884  0.000 244.41232 ? 217 VAL B CG1 1 
ATOM   4304 C CG2 . VAL B 2 217 ? 10.66431  -84.84928 29.25803  0.000 238.74609 ? 217 VAL B CG2 1 
ATOM   4305 N N   . PRO B 2 218 ? 6.36759   -83.14496 29.78773  0.000 243.21747 ? 218 PRO B N   1 
ATOM   4306 C CA  . PRO B 2 218 ? 5.19083   -82.65773 30.50923  0.000 247.27697 ? 218 PRO B CA  1 
ATOM   4307 C C   . PRO B 2 218 ? 4.92704   -83.43330 31.79580  0.000 250.16729 ? 218 PRO B C   1 
ATOM   4308 O O   . PRO B 2 218 ? 3.77901   -83.47948 32.23714  0.000 254.05204 ? 218 PRO B O   1 
ATOM   4309 C CB  . PRO B 2 218 ? 4.05914   -82.87023 29.50197  0.000 248.88799 ? 218 PRO B CB  1 
ATOM   4310 C CG  . PRO B 2 218 ? 4.53826   -83.99870 28.60450  0.000 246.47794 ? 218 PRO B CG  1 
ATOM   4311 C CD  . PRO B 2 218 ? 6.01548   -84.22422 28.85151  0.000 243.01435 ? 218 PRO B CD  1 
ATOM   4312 N N   . GLN C 3 1   ? -5.38274  -24.69395 13.86135  1.000 218.96202 ? 1   GLN C N   1 
ATOM   4313 C CA  . GLN C 3 1   ? -5.13151  -25.92534 14.60049  1.000 213.97870 ? 1   GLN C CA  1 
ATOM   4314 C C   . GLN C 3 1   ? -6.20765  -26.96266 14.29505  1.000 216.88156 ? 1   GLN C C   1 
ATOM   4315 O O   . GLN C 3 1   ? -7.39218  -26.72812 14.53466  1.000 225.91397 ? 1   GLN C O   1 
ATOM   4316 C CB  . GLN C 3 1   ? -5.07026  -25.64713 16.10327  1.000 215.75691 ? 1   GLN C CB  1 
ATOM   4317 C CG  . GLN C 3 1   ? -4.58651  -26.82838 16.92122  1.000 210.10162 ? 1   GLN C CG  1 
ATOM   4318 C CD  . GLN C 3 1   ? -3.26141  -27.36919 16.42161  1.000 206.03413 ? 1   GLN C CD  1 
ATOM   4319 O OE1 . GLN C 3 1   ? -2.26832  -26.64483 16.34856  1.000 204.76496 ? 1   GLN C OE1 1 
ATOM   4320 N NE2 . GLN C 3 1   ? -3.24307  -28.64698 16.06255  1.000 205.22377 ? 1   GLN C NE2 1 
ATOM   4321 N N   . PHE C 3 2   ? -5.78943  -28.11178 13.77009  1.000 217.90903 ? 2   PHE C N   1 
ATOM   4322 C CA  . PHE C 3 2   ? -6.72759  -29.12968 13.31645  1.000 219.68321 ? 2   PHE C CA  1 
ATOM   4323 C C   . PHE C 3 2   ? -6.02510  -30.48029 13.29750  1.000 209.76408 ? 2   PHE C C   1 
ATOM   4324 O O   . PHE C 3 2   ? -4.80834  -30.57490 13.47473  1.000 202.95114 ? 2   PHE C O   1 
ATOM   4325 C CB  . PHE C 3 2   ? -7.29191  -28.78314 11.93495  1.000 221.45642 ? 2   PHE C CB  1 
ATOM   4326 C CG  . PHE C 3 2   ? -6.23795  -28.44455 10.91787  1.000 214.42958 ? 2   PHE C CG  1 
ATOM   4327 C CD1 . PHE C 3 2   ? -5.68489  -29.43073 10.11789  1.000 205.55092 ? 2   PHE C CD1 1 
ATOM   4328 C CD2 . PHE C 3 2   ? -5.79904  -27.13925 10.76321  1.000 215.26169 ? 2   PHE C CD2 1 
ATOM   4329 C CE1 . PHE C 3 2   ? -4.71563  -29.12193 9.18267   1.000 195.06990 ? 2   PHE C CE1 1 
ATOM   4330 C CE2 . PHE C 3 2   ? -4.82953  -26.82444 9.83054   1.000 209.19578 ? 2   PHE C CE2 1 
ATOM   4331 C CZ  . PHE C 3 2   ? -4.28774  -27.81703 9.03876   1.000 197.44457 ? 2   PHE C CZ  1 
ATOM   4332 N N   . VAL C 3 3   ? -6.81445  -31.52846 13.06995  1.000 213.83065 ? 3   VAL C N   1 
ATOM   4333 C CA  . VAL C 3 3   ? -6.33309  -32.90425 13.05585  1.000 205.95328 ? 3   VAL C CA  1 
ATOM   4334 C C   . VAL C 3 3   ? -6.60486  -33.50425 11.68309  1.000 200.15965 ? 3   VAL C C   1 
ATOM   4335 O O   . VAL C 3 3   ? -7.67545  -33.29148 11.10315  1.000 209.23573 ? 3   VAL C O   1 
ATOM   4336 C CB  . VAL C 3 3   ? -7.00016  -33.74815 14.16350  1.000 210.75020 ? 3   VAL C CB  1 
ATOM   4337 C CG1 . VAL C 3 3   ? -6.43379  -35.15994 14.17956  1.000 201.69173 ? 3   VAL C CG1 1 
ATOM   4338 C CG2 . VAL C 3 3   ? -6.82492  -33.08221 15.52125  1.000 215.38792 ? 3   VAL C CG2 1 
ATOM   4339 N N   . LEU C 3 4   ? -5.63082  -34.25099 11.16382  1.000 210.25919 ? 4   LEU C N   1 
ATOM   4340 C CA  . LEU C 3 4   ? -5.75749  -34.94109 9.88405   1.000 207.08114 ? 4   LEU C CA  1 
ATOM   4341 C C   . LEU C 3 4   ? -6.12847  -36.39475 10.15826  1.000 205.15693 ? 4   LEU C C   1 
ATOM   4342 O O   . LEU C 3 4   ? -5.31212  -37.16419 10.67591  1.000 199.40573 ? 4   LEU C O   1 
ATOM   4343 C CB  . LEU C 3 4   ? -4.46241  -34.84137 9.08136   1.000 197.73539 ? 4   LEU C CB  1 
ATOM   4344 C CG  . LEU C 3 4   ? -3.97422  -33.42205 8.78395   1.000 196.35960 ? 4   LEU C CG  1 
ATOM   4345 C CD1 . LEU C 3 4   ? -2.73461  -33.45055 7.90500   1.000 193.66080 ? 4   LEU C CD1 1 
ATOM   4346 C CD2 . LEU C 3 4   ? -5.07608  -32.59953 8.13464   1.000 202.30569 ? 4   LEU C CD2 1 
ATOM   4347 N N   . SER C 3 5   ? -7.35747  -36.76873 9.80739   1.000 207.20391 ? 5   SER C N   1 
ATOM   4348 C CA  . SER C 3 5   ? -7.89956  -38.08887 10.11199  1.000 208.22186 ? 5   SER C CA  1 
ATOM   4349 C C   . SER C 3 5   ? -7.72349  -38.99894 8.90081   1.000 205.67437 ? 5   SER C C   1 
ATOM   4350 O O   . SER C 3 5   ? -8.41854  -38.84338 7.89120   1.000 207.13871 ? 5   SER C O   1 
ATOM   4351 C CB  . SER C 3 5   ? -9.37060  -37.99000 10.51110  1.000 219.76799 ? 5   SER C CB  1 
ATOM   4352 O OG  . SER C 3 5   ? -9.53768  -37.16720 11.65282  1.000 224.44544 ? 5   SER C OG  1 
ATOM   4353 N N   . GLN C 3 6   ? -6.79266  -39.95338 9.00691   1.000 207.40760 ? 6   GLN C N   1 
ATOM   4354 C CA  . GLN C 3 6   ? -6.58839  -40.97928 7.99791   1.000 206.98447 ? 6   GLN C CA  1 
ATOM   4355 C C   . GLN C 3 6   ? -7.03141  -42.33735 8.52599   1.000 211.81945 ? 6   GLN C C   1 
ATOM   4356 O O   . GLN C 3 6   ? -6.81985  -42.64014 9.70584   1.000 213.49931 ? 6   GLN C O   1 
ATOM   4357 C CB  . GLN C 3 6   ? -5.11790  -41.07102 7.57109   1.000 202.96801 ? 6   GLN C CB  1 
ATOM   4358 C CG  . GLN C 3 6   ? -4.65540  -39.97753 6.62659   1.000 201.64196 ? 6   GLN C CG  1 
ATOM   4359 C CD  . GLN C 3 6   ? -3.28112  -40.26135 6.05180   1.000 199.76749 ? 6   GLN C CD  1 
ATOM   4360 O OE1 . GLN C 3 6   ? -2.81326  -41.39945 6.06601   1.000 199.92664 ? 6   GLN C OE1 1 
ATOM   4361 N NE2 . GLN C 3 6   ? -2.62548  -39.22598 5.54679   1.000 198.15324 ? 6   GLN C NE2 1 
ATOM   4362 N N   . PRO C 3 7   ? -7.64208  -43.17602 7.68372   1.000 202.21405 ? 7   PRO C N   1 
ATOM   4363 C CA  . PRO C 3 7   ? -7.99706  -44.53287 8.12399   1.000 204.00944 ? 7   PRO C CA  1 
ATOM   4364 C C   . PRO C 3 7   ? -6.76660  -45.37292 8.43321   1.000 202.23073 ? 7   PRO C C   1 
ATOM   4365 O O   . PRO C 3 7   ? -5.63438  -44.93097 8.21293   1.000 199.74739 ? 7   PRO C O   1 
ATOM   4366 C CB  . PRO C 3 7   ? -8.78909  -45.09419 6.93599   1.000 206.76983 ? 7   PRO C CB  1 
ATOM   4367 C CG  . PRO C 3 7   ? -8.35357  -44.27570 5.76544   1.000 205.64429 ? 7   PRO C CG  1 
ATOM   4368 C CD  . PRO C 3 7   ? -8.07771  -42.90616 6.30351   1.000 203.44317 ? 7   PRO C CD  1 
ATOM   4369 N N   . ASN C 3 8   ? -6.97199  -46.58982 8.93481   1.000 211.31860 ? 8   ASN C N   1 
ATOM   4370 C CA  . ASN C 3 8   ? -5.86511  -47.36722 9.48019   1.000 209.16113 ? 8   ASN C CA  1 
ATOM   4371 C C   . ASN C 3 8   ? -5.22171  -48.29993 8.45625   1.000 208.50006 ? 8   ASN C C   1 
ATOM   4372 O O   . ASN C 3 8   ? -3.99816  -48.28250 8.29146   1.000 206.39812 ? 8   ASN C O   1 
ATOM   4373 C CB  . ASN C 3 8   ? -6.34066  -48.15841 10.70166  1.000 212.46790 ? 8   ASN C CB  1 
ATOM   4374 C CG  . ASN C 3 8   ? -6.53735  -47.27690 11.91985  1.000 212.46333 ? 8   ASN C CG  1 
ATOM   4375 O OD1 . ASN C 3 8   ? -6.62081  -46.05359 11.80641  1.000 212.07380 ? 8   ASN C OD1 1 
ATOM   4376 N ND2 . ASN C 3 8   ? -6.60622  -47.89333 13.09356  1.000 213.91723 ? 8   ASN C ND2 1 
ATOM   4377 N N   . SER C 3 9   ? -6.01206  -49.12243 7.76829   1.000 205.05011 ? 9   SER C N   1 
ATOM   4378 C CA  . SER C 3 9   ? -5.44111  -50.09183 6.84266   1.000 205.84324 ? 9   SER C CA  1 
ATOM   4379 C C   . SER C 3 9   ? -6.39973  -50.34977 5.68981   1.000 208.92219 ? 9   SER C C   1 
ATOM   4380 O O   . SER C 3 9   ? -7.60816  -50.49105 5.89546   1.000 211.35002 ? 9   SER C O   1 
ATOM   4381 C CB  . SER C 3 9   ? -5.11111  -51.41111 7.55152   1.000 206.45952 ? 9   SER C CB  1 
ATOM   4382 O OG  . SER C 3 9   ? -6.28349  -52.03435 8.04635   1.000 209.15457 ? 9   SER C OG  1 
ATOM   4383 N N   . VAL C 3 10  ? -5.84639  -50.41805 4.47955   1.000 207.47999 ? 10  VAL C N   1 
ATOM   4384 C CA  . VAL C 3 10  ? -6.59954  -50.73488 3.27234   1.000 210.57650 ? 10  VAL C CA  1 
ATOM   4385 C C   . VAL C 3 10  ? -5.81134  -51.75638 2.46313   1.000 211.97814 ? 10  VAL C C   1 
ATOM   4386 O O   . VAL C 3 10  ? -4.57861  -51.69358 2.39630   1.000 210.01374 ? 10  VAL C O   1 
ATOM   4387 C CB  . VAL C 3 10  ? -6.89277  -49.47515 2.42713   1.000 210.15340 ? 10  VAL C CB  1 
ATOM   4388 C CG1 . VAL C 3 10  ? -7.87030  -48.56041 3.15164   1.000 210.08520 ? 10  VAL C CG1 1 
ATOM   4389 C CG2 . VAL C 3 10  ? -5.60463  -48.73113 2.10278   1.000 206.95339 ? 10  VAL C CG2 1 
ATOM   4390 N N   . SER C 3 11  ? -6.52333  -52.70491 1.85786   1.000 212.33827 ? 11  SER C N   1 
ATOM   4391 C CA  . SER C 3 11  ? -5.91788  -53.73278 1.02300   1.000 215.54952 ? 11  SER C CA  1 
ATOM   4392 C C   . SER C 3 11  ? -6.63148  -53.76802 -0.31918  1.000 219.11303 ? 11  SER C C   1 
ATOM   4393 O O   . SER C 3 11  ? -7.86287  -53.70323 -0.37752  1.000 220.93566 ? 11  SER C O   1 
ATOM   4394 C CB  . SER C 3 11  ? -5.98358  -55.11242 1.69049   1.000 220.71473 ? 11  SER C CB  1 
ATOM   4395 O OG  . SER C 3 11  ? -7.32295  -55.55552 1.81832   1.000 225.11107 ? 11  SER C OG  1 
ATOM   4396 N N   . THR C 3 12  ? -5.85647  -53.87122 -1.39589  1.000 222.94389 ? 12  THR C N   1 
ATOM   4397 C CA  . THR C 3 12  ? -6.39099  -53.79634 -2.74681  1.000 224.16880 ? 12  THR C CA  1 
ATOM   4398 C C   . THR C 3 12  ? -5.88151  -54.96387 -3.58106  1.000 228.75264 ? 12  THR C C   1 
ATOM   4399 O O   . THR C 3 12  ? -4.94821  -55.67631 -3.20118  1.000 230.83996 ? 12  THR C O   1 
ATOM   4400 C CB  . THR C 3 12  ? -6.01529  -52.47139 -3.42571  1.000 219.65279 ? 12  THR C CB  1 
ATOM   4401 O OG1 . THR C 3 12  ? -4.59022  -52.31855 -3.42117  1.000 217.77218 ? 12  THR C OG1 1 
ATOM   4402 C CG2 . THR C 3 12  ? -6.65189  -51.29507 -2.69955  1.000 216.28961 ? 12  THR C CG2 1 
ATOM   4403 N N   . ASN C 3 13  ? -6.51324  -55.14534 -4.73673  1.000 229.95470 ? 13  ASN C N   1 
ATOM   4404 C CA  . ASN C 3 13  ? -6.11372  -56.13466 -5.72392  1.000 234.23957 ? 13  ASN C CA  1 
ATOM   4405 C C   . ASN C 3 13  ? -5.46007  -55.43161 -6.90702  1.000 232.30153 ? 13  ASN C C   1 
ATOM   4406 O O   . ASN C 3 13  ? -5.78789  -54.28392 -7.22221  1.000 229.10618 ? 13  ASN C O   1 
ATOM   4407 C CB  . ASN C 3 13  ? -7.31801  -56.95730 -6.19150  1.000 239.93283 ? 13  ASN C CB  1 
ATOM   4408 C CG  . ASN C 3 13  ? -8.04028  -57.63357 -5.04172  1.000 241.45262 ? 13  ASN C CG  1 
ATOM   4409 O OD1 . ASN C 3 13  ? -7.42101  -58.29424 -4.20750  1.000 242.74201 ? 13  ASN C OD1 1 
ATOM   4410 N ND2 . ASN C 3 13  ? -9.35549  -57.45870 -4.98358  1.000 242.92331 ? 13  ASN C ND2 1 
ATOM   4411 N N   . LEU C 3 14  ? -4.52913  -56.13064 -7.55646  1.000 233.68967 ? 14  LEU C N   1 
ATOM   4412 C CA  . LEU C 3 14  ? -3.72871  -55.53034 -8.61933  1.000 232.59778 ? 14  LEU C CA  1 
ATOM   4413 C C   . LEU C 3 14  ? -4.61949  -55.00148 -9.73714  1.000 233.69636 ? 14  LEU C C   1 
ATOM   4414 O O   . LEU C 3 14  ? -5.33203  -55.76708 -10.39373 1.000 238.93490 ? 14  LEU C O   1 
ATOM   4415 C CB  . LEU C 3 14  ? -2.73182  -56.55461 -9.16451  1.000 236.92184 ? 14  LEU C CB  1 
ATOM   4416 C CG  . LEU C 3 14  ? -1.68841  -56.07207 -10.17779 1.000 236.00588 ? 14  LEU C CG  1 
ATOM   4417 C CD1 . LEU C 3 14  ? -0.36534  -56.78396 -9.94954  1.000 238.17474 ? 14  LEU C CD1 1 
ATOM   4418 C CD2 . LEU C 3 14  ? -2.16272  -56.29230 -11.60841 1.000 239.45606 ? 14  LEU C CD2 1 
ATOM   4419 N N   . GLY C 3 15  ? -4.57292  -53.69270 -9.95173  1.000 228.13458 ? 15  GLY C N   1 
ATOM   4420 C CA  . GLY C 3 15  ? -5.36257  -53.04947 -10.97380 1.000 228.97230 ? 15  GLY C CA  1 
ATOM   4421 C C   . GLY C 3 15  ? -6.63560  -52.38951 -10.49584 1.000 227.79820 ? 15  GLY C C   1 
ATOM   4422 O O   . GLY C 3 15  ? -7.58663  -52.28477 -11.27844 1.000 230.83795 ? 15  GLY C O   1 
ATOM   4423 N N   . SER C 3 16  ? -6.68879  -51.94502 -9.24536  1.000 227.74779 ? 16  SER C N   1 
ATOM   4424 C CA  . SER C 3 16  ? -7.87370  -51.31015 -8.69039  1.000 227.67904 ? 16  SER C CA  1 
ATOM   4425 C C   . SER C 3 16  ? -7.68451  -49.79856 -8.60846  1.000 224.10589 ? 16  SER C C   1 
ATOM   4426 O O   . SER C 3 16  ? -6.57817  -49.27109 -8.74294  1.000 221.16499 ? 16  SER C O   1 
ATOM   4427 C CB  . SER C 3 16  ? -8.19277  -51.88221 -7.30498  1.000 226.87553 ? 16  SER C CB  1 
ATOM   4428 O OG  . SER C 3 16  ? -8.42470  -53.27869 -7.36602  1.000 230.64536 ? 16  SER C OG  1 
ATOM   4429 N N   . THR C 3 17  ? -8.79624  -49.10088 -8.38877  1.000 226.29142 ? 17  THR C N   1 
ATOM   4430 C CA  . THR C 3 17  ? -8.80910  -47.65663 -8.18069  1.000 223.24214 ? 17  THR C CA  1 
ATOM   4431 C C   . THR C 3 17  ? -9.12162  -47.40490 -6.71126  1.000 220.98395 ? 17  THR C C   1 
ATOM   4432 O O   . THR C 3 17  ? -10.24605 -47.64792 -6.25971  1.000 223.12795 ? 17  THR C O   1 
ATOM   4433 C CB  . THR C 3 17  ? -9.83138  -46.97645 -9.08937  1.000 225.77322 ? 17  THR C CB  1 
ATOM   4434 O OG1 . THR C 3 17  ? -9.40328  -47.07996 -10.45339 1.000 227.53422 ? 17  THR C OG1 1 
ATOM   4435 C CG2 . THR C 3 17  ? -9.98428  -45.50752 -8.71824  1.000 222.84417 ? 17  THR C CG2 1 
ATOM   4436 N N   . VAL C 3 18  ? -8.12800  -46.92629 -5.96685  1.000 215.35284 ? 18  VAL C N   1 
ATOM   4437 C CA  . VAL C 3 18  ? -8.23623  -46.74161 -4.52421  1.000 213.12039 ? 18  VAL C CA  1 
ATOM   4438 C C   . VAL C 3 18  ? -8.15056  -45.25427 -4.20921  1.000 210.17624 ? 18  VAL C C   1 
ATOM   4439 O O   . VAL C 3 18  ? -7.29597  -44.54538 -4.75449  1.000 208.14116 ? 18  VAL C O   1 
ATOM   4440 C CB  . VAL C 3 18  ? -7.14701  -47.53206 -3.77099  1.000 211.14744 ? 18  VAL C CB  1 
ATOM   4441 C CG1 . VAL C 3 18  ? -5.76882  -47.24289 -4.34870  1.000 208.88772 ? 18  VAL C CG1 1 
ATOM   4442 C CG2 . VAL C 3 18  ? -7.18221  -47.21186 -2.28560  1.000 208.70130 ? 18  VAL C CG2 1 
ATOM   4443 N N   . LYS C 3 19  ? -9.04410  -44.78541 -3.34140  1.000 212.36996 ? 19  LYS C N   1 
ATOM   4444 C CA  . LYS C 3 19  ? -9.02530  -43.41997 -2.83582  1.000 209.79297 ? 19  LYS C CA  1 
ATOM   4445 C C   . LYS C 3 19  ? -8.65780  -43.43187 -1.35850  1.000 207.39992 ? 19  LYS C C   1 
ATOM   4446 O O   . LYS C 3 19  ? -9.17284  -44.24979 -0.58901  1.000 208.74388 ? 19  LYS C O   1 
ATOM   4447 C CB  . LYS C 3 19  ? -10.38207 -42.73567 -3.02701  1.000 212.02207 ? 19  LYS C CB  1 
ATOM   4448 C CG  . LYS C 3 19  ? -10.78287 -42.51753 -4.47709  1.000 214.35018 ? 19  LYS C CG  1 
ATOM   4449 C CD  . LYS C 3 19  ? -12.12689 -41.81070 -4.57029  1.000 216.58920 ? 19  LYS C CD  1 
ATOM   4450 C CE  . LYS C 3 19  ? -12.53804 -41.57382 -6.01386  1.000 219.05954 ? 19  LYS C CE  1 
ATOM   4451 N NZ  . LYS C 3 19  ? -13.86797 -40.91020 -6.10349  1.000 221.50219 ? 19  LYS C NZ  1 
ATOM   4452 N N   . LEU C 3 20  ? -7.76742  -42.52212 -0.96917  1.000 204.73166 ? 20  LEU C N   1 
ATOM   4453 C CA  . LEU C 3 20  ? -7.26405  -42.42869 0.39618   1.000 202.34209 ? 20  LEU C CA  1 
ATOM   4454 C C   . LEU C 3 20  ? -7.60281  -41.05036 0.94411   1.000 201.02385 ? 20  LEU C C   1 
ATOM   4455 O O   . LEU C 3 20  ? -7.16691  -40.03598 0.39039   1.000 199.55651 ? 20  LEU C O   1 
ATOM   4456 C CB  . LEU C 3 20  ? -5.75407  -42.67131 0.43757   1.000 199.73362 ? 20  LEU C CB  1 
ATOM   4457 C CG  . LEU C 3 20  ? -5.25780  -43.91533 -0.30219  1.000 201.04968 ? 20  LEU C CG  1 
ATOM   4458 C CD1 . LEU C 3 20  ? -3.81910  -43.72412 -0.75076  1.000 198.79063 ? 20  LEU C CD1 1 
ATOM   4459 C CD2 . LEU C 3 20  ? -5.38818  -45.15409 0.57025   1.000 201.98989 ? 20  LEU C CD2 1 
ATOM   4460 N N   . SER C 3 21  ? -8.37078  -41.01456 2.02707   1.000 207.41748 ? 21  SER C N   1 
ATOM   4461 C CA  . SER C 3 21  ? -8.85551  -39.75966 2.57703   1.000 206.84488 ? 21  SER C CA  1 
ATOM   4462 C C   . SER C 3 21  ? -7.87061  -39.17861 3.59049   1.000 203.75408 ? 21  SER C C   1 
ATOM   4463 O O   . SER C 3 21  ? -6.90929  -39.82302 4.01687   1.000 202.19611 ? 21  SER C O   1 
ATOM   4464 C CB  . SER C 3 21  ? -10.22746 -39.95510 3.22438   1.000 209.58431 ? 21  SER C CB  1 
ATOM   4465 O OG  . SER C 3 21  ? -10.71722 -38.74030 3.76601   1.000 209.34021 ? 21  SER C OG  1 
ATOM   4466 N N   . CYS C 3 22  ? -8.13360  -37.93002 3.97335   1.000 209.93433 ? 22  CYS C N   1 
ATOM   4467 C CA  . CYS C 3 22  ? -7.34660  -37.20316 4.96179   1.000 203.50582 ? 22  CYS C CA  1 
ATOM   4468 C C   . CYS C 3 22  ? -8.21818  -36.09587 5.54263   1.000 215.12983 ? 22  CYS C C   1 
ATOM   4469 O O   . CYS C 3 22  ? -8.08792  -34.92837 5.16049   1.000 218.06183 ? 22  CYS C O   1 
ATOM   4470 C CB  . CYS C 3 22  ? -6.07302  -36.63565 4.32716   1.000 200.94740 ? 22  CYS C CB  1 
ATOM   4471 S SG  . CYS C 3 22  ? -5.00952  -35.65798 5.42125   1.000 198.14226 ? 22  CYS C SG  1 
ATOM   4472 N N   . LYS C 3 23  ? -9.11410  -36.45400 6.46062   1.000 201.87680 ? 23  LYS C N   1 
ATOM   4473 C CA  . LYS C 3 23  ? -10.19302 -35.56113 6.87004   1.000 209.62488 ? 23  LYS C CA  1 
ATOM   4474 C C   . LYS C 3 23  ? -9.69749  -34.55021 7.89789   1.000 210.12959 ? 23  LYS C C   1 
ATOM   4475 O O   . LYS C 3 23  ? -9.28653  -34.92404 9.00191   1.000 209.41299 ? 23  LYS C O   1 
ATOM   4476 C CB  . LYS C 3 23  ? -11.36165 -36.36884 7.43011   1.000 214.67848 ? 23  LYS C CB  1 
ATOM   4477 C CG  . LYS C 3 23  ? -12.63640 -35.56366 7.61392   1.000 221.05823 ? 23  LYS C CG  1 
ATOM   4478 C CD  . LYS C 3 23  ? -13.83276 -36.47092 7.84370   1.000 226.03224 ? 23  LYS C CD  1 
ATOM   4479 C CE  . LYS C 3 23  ? -15.12612 -35.67353 7.87305   1.000 232.44167 ? 23  LYS C CE  1 
ATOM   4480 N NZ  . LYS C 3 23  ? -16.32323 -36.55229 7.97697   1.000 237.20454 ? 23  LYS C NZ  1 
ATOM   4481 N N   . ARG C 3 24  ? -9.74799  -33.27138 7.53451   1.000 210.15073 ? 24  ARG C N   1 
ATOM   4482 C CA  . ARG C 3 24  ? -9.41884  -32.19552 8.45740   1.000 212.22702 ? 24  ARG C CA  1 
ATOM   4483 C C   . ARG C 3 24  ? -10.57868 -31.95579 9.41609   1.000 219.78431 ? 24  ARG C C   1 
ATOM   4484 O O   . ARG C 3 24  ? -11.74649 -31.97164 9.01645   1.000 223.71163 ? 24  ARG C O   1 
ATOM   4485 C CB  . ARG C 3 24  ? -9.09608  -30.91734 7.68246   1.000 211.30168 ? 24  ARG C CB  1 
ATOM   4486 C CG  . ARG C 3 24  ? -8.82312  -29.70123 8.54731   1.000 214.53988 ? 24  ARG C CG  1 
ATOM   4487 C CD  . ARG C 3 24  ? -8.49483  -28.48821 7.69174   1.000 213.14334 ? 24  ARG C CD  1 
ATOM   4488 N NE  . ARG C 3 24  ? -8.16764  -27.31717 8.49614   1.000 215.98341 ? 24  ARG C NE  1 
ATOM   4489 C CZ  . ARG C 3 24  ? -7.79192  -26.14815 7.99576   1.000 215.83557 ? 24  ARG C CZ  1 
ATOM   4490 N NH1 . ARG C 3 24  ? -7.68355  -25.95767 6.69110   1.000 217.42902 ? 24  ARG C NH1 1 
ATOM   4491 N NH2 . ARG C 3 24  ? -7.51491  -25.14582 8.82491   1.000 214.45759 ? 24  ARG C NH2 1 
ATOM   4492 N N   . SER C 3 25  ? -10.25033 -31.73474 10.69032  1.000 209.85812 ? 25  SER C N   1 
ATOM   4493 C CA  . SER C 3 25  ? -11.28209 -31.58091 11.71174  1.000 217.78237 ? 25  SER C CA  1 
ATOM   4494 C C   . SER C 3 25  ? -11.90934 -30.19058 11.67115  1.000 223.23603 ? 25  SER C C   1 
ATOM   4495 O O   . SER C 3 25  ? -13.12415 -30.05107 11.49348  1.000 228.17040 ? 25  SER C O   1 
ATOM   4496 C CB  . SER C 3 25  ? -10.69663 -31.86730 13.09772  1.000 218.71324 ? 25  SER C CB  1 
ATOM   4497 O OG  . SER C 3 25  ? -9.69851  -30.92109 13.43816  1.000 217.03117 ? 25  SER C OG  1 
ATOM   4498 N N   . THR C 3 26  ? -11.09650 -29.15010 11.84080  1.000 222.01593 ? 26  THR C N   1 
ATOM   4499 C CA  . THR C 3 26  ? -11.58006 -27.77909 11.90242  1.000 227.25408 ? 26  THR C CA  1 
ATOM   4500 C C   . THR C 3 26  ? -10.92753 -26.93993 10.81211  1.000 222.95589 ? 26  THR C C   1 
ATOM   4501 O O   . THR C 3 26  ? -9.78773  -27.19096 10.40991  1.000 216.72074 ? 26  THR C O   1 
ATOM   4502 C CB  . THR C 3 26  ? -11.29697 -27.14632 13.27257  1.000 232.25245 ? 26  THR C CB  1 
ATOM   4503 O OG1 . THR C 3 26  ? -9.88559  -26.95458 13.43060  1.000 227.87123 ? 26  THR C OG1 1 
ATOM   4504 C CG2 . THR C 3 26  ? -11.80700 -28.04368 14.39099  1.000 236.19098 ? 26  THR C CG2 1 
ATOM   4505 N N   . GLY C 3 27  ? -11.66072 -25.93294 10.34285  1.000 244.80469 ? 27  GLY C N   1 
ATOM   4506 C CA  . GLY C 3 27  ? -11.15555 -25.04157 9.31697   1.000 241.20373 ? 27  GLY C CA  1 
ATOM   4507 C C   . GLY C 3 27  ? -11.33530 -25.58439 7.91480   1.000 228.66972 ? 27  GLY C C   1 
ATOM   4508 O O   . GLY C 3 27  ? -11.34299 -26.80175 7.71058   1.000 211.97842 ? 27  GLY C O   1 
ATOM   4509 N N   . ASN C 3 28  ? -11.48080 -24.69280 6.93800   1.000 250.59625 ? 28  ASN C N   1 
ATOM   4510 C CA  . ASN C 3 28  ? -11.67437 -25.11940 5.55823   1.000 245.59056 ? 28  ASN C CA  1 
ATOM   4511 C C   . ASN C 3 28  ? -10.36181 -25.64851 4.98985   1.000 219.10057 ? 28  ASN C C   1 
ATOM   4512 O O   . ASN C 3 28  ? -9.33854  -24.95708 5.01778   1.000 213.46294 ? 28  ASN C O   1 
ATOM   4513 C CB  . ASN C 3 28  ? -12.21118 -23.96511 4.71415   1.000 254.08735 ? 28  ASN C CB  1 
ATOM   4514 C CG  . ASN C 3 28  ? -11.34604 -22.72262 4.79838   1.000 253.70733 ? 28  ASN C CG  1 
ATOM   4515 O OD1 . ASN C 3 28  ? -10.59479 -22.53679 5.75502   1.000 253.56120 ? 28  ASN C OD1 1 
ATOM   4516 N ND2 . ASN C 3 28  ? -11.45293 -21.85994 3.79385   1.000 253.56889 ? 28  ASN C ND2 1 
ATOM   4517 N N   . ILE C 3 29  ? -10.39226 -26.88256 4.47916   1.000 229.46732 ? 29  ILE C N   1 
ATOM   4518 C CA  . ILE C 3 29  ? -9.19134  -27.50412 3.93351   1.000 222.90177 ? 29  ILE C CA  1 
ATOM   4519 C C   . ILE C 3 29  ? -8.70777  -26.79075 2.67669   1.000 220.03988 ? 29  ILE C C   1 
ATOM   4520 O O   . ILE C 3 29  ? -7.53766  -26.92402 2.30022   1.000 215.43593 ? 29  ILE C O   1 
ATOM   4521 C CB  . ILE C 3 29  ? -9.45044  -28.99885 3.65728   1.000 221.18161 ? 29  ILE C CB  1 
ATOM   4522 C CG1 . ILE C 3 29  ? -8.13960  -29.74006 3.37730   1.000 215.20933 ? 29  ILE C CG1 1 
ATOM   4523 C CG2 . ILE C 3 29  ? -10.42725 -29.16689 2.50078   1.000 222.42673 ? 29  ILE C CG2 1 
ATOM   4524 C CD1 . ILE C 3 29  ? -7.13212  -29.65016 4.50556   1.000 212.90753 ? 29  ILE C CD1 1 
ATOM   4525 N N   . GLY C 3 30  ? -9.57358  -26.01357 2.02750   1.000 223.74261 ? 30  GLY C N   1 
ATOM   4526 C CA  . GLY C 3 30  ? -9.21102  -25.31116 0.81239   1.000 221.60109 ? 30  GLY C CA  1 
ATOM   4527 C C   . GLY C 3 30  ? -8.37218  -24.06778 1.02983   1.000 221.05919 ? 30  GLY C C   1 
ATOM   4528 O O   . GLY C 3 30  ? -8.24747  -23.23230 0.12875   1.000 220.27599 ? 30  GLY C O   1 
ATOM   4529 N N   . SER C 3 31  ? -7.78852  -23.93244 2.22058   1.000 216.58194 ? 31  SER C N   1 
ATOM   4530 C CA  . SER C 3 31  ? -6.90867  -22.81694 2.53499   1.000 216.18570 ? 31  SER C CA  1 
ATOM   4531 C C   . SER C 3 31  ? -5.52430  -23.25667 2.99014   1.000 211.50592 ? 31  SER C C   1 
ATOM   4532 O O   . SER C 3 31  ? -4.67171  -22.39723 3.24197   1.000 210.71248 ? 31  SER C O   1 
ATOM   4533 C CB  . SER C 3 31  ? -7.54099  -21.92426 3.61227   1.000 222.33880 ? 31  SER C CB  1 
ATOM   4534 O OG  . SER C 3 31  ? -8.74439  -21.33788 3.14761   1.000 226.79283 ? 31  SER C OG  1 
ATOM   4535 N N   . ASN C 3 32  ? -5.27321  -24.55995 3.10434   1.000 208.83160 ? 32  ASN C N   1 
ATOM   4536 C CA  . ASN C 3 32  ? -3.97304  -25.08004 3.51176   1.000 204.46820 ? 32  ASN C CA  1 
ATOM   4537 C C   . ASN C 3 32  ? -3.54138  -26.15823 2.52930   1.000 199.26323 ? 32  ASN C C   1 
ATOM   4538 O O   . ASN C 3 32  ? -4.27049  -27.13283 2.31621   1.000 196.52225 ? 32  ASN C O   1 
ATOM   4539 C CB  . ASN C 3 32  ? -4.02356  -25.63763 4.93745   1.000 205.74532 ? 32  ASN C CB  1 
ATOM   4540 C CG  . ASN C 3 32  ? -4.46415  -24.60100 5.95144   1.000 210.93684 ? 32  ASN C CG  1 
ATOM   4541 O OD1 . ASN C 3 32  ? -5.25254  -24.88998 6.85134   1.000 213.26580 ? 32  ASN C OD1 1 
ATOM   4542 N ND2 . ASN C 3 32  ? -3.96119  -23.38104 5.80487   1.000 213.39947 ? 32  ASN C ND2 1 
ATOM   4543 N N   . TYR C 3 33  ? -2.36367  -25.97745 1.93082   1.000 202.83091 ? 33  TYR C N   1 
ATOM   4544 C CA  . TYR C 3 33  ? -1.81681  -26.97107 1.01445   1.000 187.52172 ? 33  TYR C CA  1 
ATOM   4545 C C   . TYR C 3 33  ? -1.64875  -28.31219 1.71582   1.000 186.02328 ? 33  TYR C C   1 
ATOM   4546 O O   . TYR C 3 33  ? -1.05445  -28.39060 2.79400   1.000 185.04496 ? 33  TYR C O   1 
ATOM   4547 C CB  . TYR C 3 33  ? -0.46311  -26.50784 0.47253   1.000 184.28691 ? 33  TYR C CB  1 
ATOM   4548 C CG  . TYR C 3 33  ? -0.51196  -25.35473 -0.50357  1.000 199.51009 ? 33  TYR C CG  1 
ATOM   4549 C CD1 . TYR C 3 33  ? -1.53255  -25.24630 -1.43730  1.000 201.88829 ? 33  TYR C CD1 1 
ATOM   4550 C CD2 . TYR C 3 33  ? 0.47681   -24.38004 -0.49828  1.000 198.16079 ? 33  TYR C CD2 1 
ATOM   4551 C CE1 . TYR C 3 33  ? -1.57213  -24.19238 -2.33340  1.000 202.91550 ? 33  TYR C CE1 1 
ATOM   4552 C CE2 . TYR C 3 33  ? 0.44666   -23.32552 -1.38824  1.000 200.36424 ? 33  TYR C CE2 1 
ATOM   4553 C CZ  . TYR C 3 33  ? -0.57882  -23.23568 -2.30339  1.000 202.16532 ? 33  TYR C CZ  1 
ATOM   4554 O OH  . TYR C 3 33  ? -0.60709  -22.18354 -3.18926  1.000 203.30907 ? 33  TYR C OH  1 
ATOM   4555 N N   . VAL C 3 34  ? -2.16822  -29.36879 1.09898   1.000 185.30103 ? 34  VAL C N   1 
ATOM   4556 C CA  . VAL C 3 34  ? -1.95067  -30.73098 1.56994   1.000 185.36079 ? 34  VAL C CA  1 
ATOM   4557 C C   . VAL C 3 34  ? -0.95308  -31.40027 0.63606   1.000 184.61771 ? 34  VAL C C   1 
ATOM   4558 O O   . VAL C 3 34  ? -0.93631  -31.14929 -0.57483  1.000 185.02572 ? 34  VAL C O   1 
ATOM   4559 C CB  . VAL C 3 34  ? -3.26845  -31.53201 1.65204   1.000 187.64625 ? 34  VAL C CB  1 
ATOM   4560 C CG1 . VAL C 3 34  ? -3.07229  -32.79919 2.47583   1.000 187.66447 ? 34  VAL C CG1 1 
ATOM   4561 C CG2 . VAL C 3 34  ? -4.37900  -30.67522 2.23952   1.000 188.87991 ? 34  VAL C CG2 1 
ATOM   4562 N N   . SER C 3 35  ? -0.10302  -32.25359 1.20357   1.000 179.84150 ? 35  SER C N   1 
ATOM   4563 C CA  . SER C 3 35  ? 0.96286   -32.91446 0.45946   1.000 179.22098 ? 35  SER C CA  1 
ATOM   4564 C C   . SER C 3 35  ? 0.95894   -34.39615 0.79936   1.000 179.93700 ? 35  SER C C   1 
ATOM   4565 O O   . SER C 3 35  ? 1.11321   -34.76674 1.96757   1.000 179.39172 ? 35  SER C O   1 
ATOM   4566 C CB  . SER C 3 35  ? 2.32307   -32.28696 0.77756   1.000 177.19812 ? 35  SER C CB  1 
ATOM   4567 O OG  . SER C 3 35  ? 2.40173   -31.90692 2.14062   1.000 176.39367 ? 35  SER C OG  1 
ATOM   4568 N N   . TRP C 3 36  ? 0.78872   -35.23839 -0.21715  1.000 180.88881 ? 36  TRP C N   1 
ATOM   4569 C CA  . TRP C 3 36  ? 0.69257   -36.68058 -0.03218  1.000 181.98457 ? 36  TRP C CA  1 
ATOM   4570 C C   . TRP C 3 36  ? 2.05506   -37.32483 -0.25800  1.000 181.07942 ? 36  TRP C C   1 
ATOM   4571 O O   . TRP C 3 36  ? 2.63376   -37.20600 -1.34372  1.000 181.19923 ? 36  TRP C O   1 
ATOM   4572 C CB  . TRP C 3 36  ? -0.35466  -37.28695 -0.96504  1.000 184.52609 ? 36  TRP C CB  1 
ATOM   4573 C CG  . TRP C 3 36  ? -1.74867  -37.17437 -0.43438  1.000 185.94949 ? 36  TRP C CG  1 
ATOM   4574 C CD1 . TRP C 3 36  ? -2.66757  -36.21219 -0.73632  1.000 186.72069 ? 36  TRP C CD1 1 
ATOM   4575 C CD2 . TRP C 3 36  ? -2.38159  -38.05464 0.50190   1.000 186.96775 ? 36  TRP C CD2 1 
ATOM   4576 N NE1 . TRP C 3 36  ? -3.83514  -36.44115 -0.04885  1.000 188.26093 ? 36  TRP C NE1 1 
ATOM   4577 C CE2 . TRP C 3 36  ? -3.68492  -37.56646 0.71845   1.000 188.43460 ? 36  TRP C CE2 1 
ATOM   4578 C CE3 . TRP C 3 36  ? -1.97336  -39.21040 1.17547   1.000 186.91194 ? 36  TRP C CE3 1 
ATOM   4579 C CZ2 . TRP C 3 36  ? -4.58278  -38.19330 1.57970   1.000 189.89617 ? 36  TRP C CZ2 1 
ATOM   4580 C CZ3 . TRP C 3 36  ? -2.86550  -39.83014 2.03182   1.000 188.24250 ? 36  TRP C CZ3 1 
ATOM   4581 C CH2 . TRP C 3 36  ? -4.15487  -39.32030 2.22646   1.000 189.74271 ? 36  TRP C CH2 1 
ATOM   4582 N N   . TYR C 3 37  ? 2.55495   -38.00987 0.76622   1.000 180.83438 ? 37  TYR C N   1 
ATOM   4583 C CA  . TYR C 3 37  ? 3.84340   -38.68180 0.72800   1.000 180.11435 ? 37  TYR C CA  1 
ATOM   4584 C C   . TYR C 3 37  ? 3.65108   -40.19001 0.81389   1.000 181.60885 ? 37  TYR C C   1 
ATOM   4585 O O   . TYR C 3 37  ? 2.72040   -40.67771 1.46080   1.000 182.53545 ? 37  TYR C O   1 
ATOM   4586 C CB  . TYR C 3 37  ? 4.74040   -38.21589 1.87790   1.000 178.10542 ? 37  TYR C CB  1 
ATOM   4587 C CG  . TYR C 3 37  ? 4.95107   -36.72298 1.93110   1.000 176.77957 ? 37  TYR C CG  1 
ATOM   4588 C CD1 . TYR C 3 37  ? 5.97895   -36.12077 1.21899   1.000 175.93505 ? 37  TYR C CD1 1 
ATOM   4589 C CD2 . TYR C 3 37  ? 4.12534   -35.91604 2.69979   1.000 176.58950 ? 37  TYR C CD2 1 
ATOM   4590 C CE1 . TYR C 3 37  ? 6.17454   -34.75647 1.26897   1.000 174.87420 ? 37  TYR C CE1 1 
ATOM   4591 C CE2 . TYR C 3 37  ? 4.31312   -34.55359 2.75536   1.000 175.59682 ? 37  TYR C CE2 1 
ATOM   4592 C CZ  . TYR C 3 37  ? 5.33785   -33.97974 2.03935   1.000 174.70810 ? 37  TYR C CZ  1 
ATOM   4593 O OH  . TYR C 3 37  ? 5.52356   -32.62246 2.09763   1.000 173.86364 ? 37  TYR C OH  1 
ATOM   4594 N N   . GLN C 3 38  ? 4.54686   -40.92656 0.16116   1.000 182.75099 ? 38  GLN C N   1 
ATOM   4595 C CA  . GLN C 3 38  ? 4.53428   -42.38611 0.17273   1.000 184.29578 ? 38  GLN C CA  1 
ATOM   4596 C C   . GLN C 3 38  ? 5.72923   -42.87200 0.98298   1.000 183.03185 ? 38  GLN C C   1 
ATOM   4597 O O   . GLN C 3 38  ? 6.88009   -42.68686 0.57295   1.000 182.30994 ? 38  GLN C O   1 
ATOM   4598 C CB  . GLN C 3 38  ? 4.57226   -42.94950 -1.24645  1.000 186.32665 ? 38  GLN C CB  1 
ATOM   4599 C CG  . GLN C 3 38  ? 4.74550   -44.46156 -1.30387  1.000 188.09858 ? 38  GLN C CG  1 
ATOM   4600 C CD  . GLN C 3 38  ? 4.76134   -44.99702 -2.72177  1.000 191.99115 ? 38  GLN C CD  1 
ATOM   4601 O OE1 . GLN C 3 38  ? 4.65646   -44.23890 -3.68533  1.000 195.18497 ? 38  GLN C OE1 1 
ATOM   4602 N NE2 . GLN C 3 38  ? 4.89226   -46.31160 -2.85608  1.000 196.15238 ? 38  GLN C NE2 1 
ATOM   4603 N N   . HIS C 3 39  ? 5.45816   -43.49395 2.12677   1.000 185.92309 ? 39  HIS C N   1 
ATOM   4604 C CA  . HIS C 3 39  ? 6.49742   -44.05047 2.98306   1.000 189.89662 ? 39  HIS C CA  1 
ATOM   4605 C C   . HIS C 3 39  ? 6.47412   -45.56803 2.86786   1.000 195.84522 ? 39  HIS C C   1 
ATOM   4606 O O   . HIS C 3 39  ? 5.47527   -46.20661 3.21743   1.000 197.13488 ? 39  HIS C O   1 
ATOM   4607 C CB  . HIS C 3 39  ? 6.31044   -43.62302 4.43825   1.000 187.84756 ? 39  HIS C CB  1 
ATOM   4608 C CG  . HIS C 3 39  ? 7.42275   -44.06205 5.33889   1.000 192.21716 ? 39  HIS C CG  1 
ATOM   4609 N ND1 . HIS C 3 39  ? 8.69450   -44.32222 4.87538   1.000 194.86537 ? 39  HIS C ND1 1 
ATOM   4610 C CD2 . HIS C 3 39  ? 7.45401   -44.29361 6.67252   1.000 192.69615 ? 39  HIS C CD2 1 
ATOM   4611 C CE1 . HIS C 3 39  ? 9.46245   -44.69049 5.88511   1.000 197.16608 ? 39  HIS C CE1 1 
ATOM   4612 N NE2 . HIS C 3 39  ? 8.73396   -44.68180 6.98685   1.000 195.99798 ? 39  HIS C NE2 1 
ATOM   4613 N N   . HIS C 3 40  ? 7.56864   -46.13701 2.37538   1.000 198.12428 ? 40  HIS C N   1 
ATOM   4614 C CA  . HIS C 3 40  ? 7.73539   -47.57928 2.29239   1.000 205.45285 ? 40  HIS C CA  1 
ATOM   4615 C C   . HIS C 3 40  ? 8.63886   -48.04285 3.42670   1.000 210.42964 ? 40  HIS C C   1 
ATOM   4616 O O   . HIS C 3 40  ? 9.59981   -47.35606 3.78665   1.000 210.07568 ? 40  HIS C O   1 
ATOM   4617 C CB  . HIS C 3 40  ? 8.32915   -47.98395 0.94136   1.000 211.10198 ? 40  HIS C CB  1 
ATOM   4618 C CG  . HIS C 3 40  ? 8.06524   -49.40888 0.56517   1.000 217.77042 ? 40  HIS C CG  1 
ATOM   4619 N ND1 . HIS C 3 40  ? 8.65061   -50.47282 1.21698   1.000 224.31991 ? 40  HIS C ND1 1 
ATOM   4620 C CD2 . HIS C 3 40  ? 7.28318   -49.94471 -0.40183  1.000 220.07039 ? 40  HIS C CD2 1 
ATOM   4621 C CE1 . HIS C 3 40  ? 8.23722   -51.60260 0.67097   1.000 228.58177 ? 40  HIS C CE1 1 
ATOM   4622 N NE2 . HIS C 3 40  ? 7.40723   -51.31001 -0.31396  1.000 226.11251 ? 40  HIS C NE2 1 
ATOM   4623 N N   . GLU C 3 41  ? 8.32103   -49.20501 3.99293   1.000 214.82876 ? 41  GLU C N   1 
ATOM   4624 C CA  . GLU C 3 41  ? 9.08616   -49.71139 5.12401   1.000 218.61007 ? 41  GLU C CA  1 
ATOM   4625 C C   . GLU C 3 41  ? 10.52448  -49.99897 4.71099   1.000 225.21461 ? 41  GLU C C   1 
ATOM   4626 O O   . GLU C 3 41  ? 10.78756  -50.48792 3.60887   1.000 229.51212 ? 41  GLU C O   1 
ATOM   4627 C CB  . GLU C 3 41  ? 8.43474   -50.97583 5.68531   1.000 223.42925 ? 41  GLU C CB  1 
ATOM   4628 C CG  . GLU C 3 41  ? 8.99801   -51.40555 7.02980   1.000 226.05051 ? 41  GLU C CG  1 
ATOM   4629 C CD  . GLU C 3 41  ? 8.77348   -50.36432 8.10995   1.000 218.85856 ? 41  GLU C CD  1 
ATOM   4630 O OE1 . GLU C 3 41  ? 7.59914   -50.05582 8.40495   1.000 219.20380 ? 41  GLU C OE1 1 
ATOM   4631 O OE2 . GLU C 3 41  ? 9.77109   -49.84553 8.65467   1.000 214.23854 ? 41  GLU C OE2 1 
ATOM   4632 N N   . GLY C 3 42  ? 11.45923  -49.68576 5.60458   1.000 215.75283 ? 42  GLY C N   1 
ATOM   4633 C CA  . GLY C 3 42  ? 12.86540  -49.87908 5.30790   1.000 223.78553 ? 42  GLY C CA  1 
ATOM   4634 C C   . GLY C 3 42  ? 13.41092  -48.94167 4.25546   1.000 222.60254 ? 42  GLY C C   1 
ATOM   4635 O O   . GLY C 3 42  ? 14.40471  -49.26806 3.59934   1.000 228.79586 ? 42  GLY C O   1 
ATOM   4636 N N   . ARG C 3 43  ? 12.78262  -47.78269 4.07244   1.000 218.90196 ? 43  ARG C N   1 
ATOM   4637 C CA  . ARG C 3 43  ? 13.21870  -46.80595 3.08552   1.000 216.52211 ? 43  ARG C CA  1 
ATOM   4638 C C   . ARG C 3 43  ? 12.89868  -45.41090 3.60670   1.000 208.10130 ? 43  ARG C C   1 
ATOM   4639 O O   . ARG C 3 43  ? 12.34579  -45.24361 4.69736   1.000 202.87683 ? 43  ARG C O   1 
ATOM   4640 C CB  . ARG C 3 43  ? 12.55929  -47.06152 1.72464   1.000 216.46299 ? 43  ARG C CB  1 
ATOM   4641 C CG  . ARG C 3 43  ? 13.34508  -48.00087 0.82363   1.000 226.32572 ? 43  ARG C CG  1 
ATOM   4642 C CD  . ARG C 3 43  ? 12.55740  -49.25210 0.46114   1.000 228.63706 ? 43  ARG C CD  1 
ATOM   4643 N NE  . ARG C 3 43  ? 11.52469  -48.99646 -0.53620  1.000 225.20274 ? 43  ARG C NE  1 
ATOM   4644 C CZ  . ARG C 3 43  ? 10.94341  -49.93899 -1.26618  1.000 228.13221 ? 43  ARG C CZ  1 
ATOM   4645 N NH1 . ARG C 3 43  ? 11.28027  -51.21278 -1.14517  1.000 234.63671 ? 43  ARG C NH1 1 
ATOM   4646 N NH2 . ARG C 3 43  ? 10.00595  -49.59454 -2.14452  1.000 224.99336 ? 43  ARG C NH2 1 
ATOM   4647 N N   . SER C 3 44  ? 13.25974  -44.40147 2.81630   1.000 199.20091 ? 44  SER C N   1 
ATOM   4648 C CA  . SER C 3 44  ? 12.90591  -43.04476 3.19350   1.000 190.61118 ? 44  SER C CA  1 
ATOM   4649 C C   . SER C 3 44  ? 11.61892  -42.62085 2.49674   1.000 184.81095 ? 44  SER C C   1 
ATOM   4650 O O   . SER C 3 44  ? 11.35103  -43.04057 1.36667   1.000 189.20034 ? 44  SER C O   1 
ATOM   4651 C CB  . SER C 3 44  ? 14.02535  -42.06604 2.82920   1.000 192.05880 ? 44  SER C CB  1 
ATOM   4652 O OG  . SER C 3 44  ? 14.14265  -41.91996 1.42564   1.000 194.59667 ? 44  SER C OG  1 
ATOM   4653 N N   . PRO C 3 45  ? 10.79866  -41.80028 3.15122   1.000 179.21369 ? 45  PRO C N   1 
ATOM   4654 C CA  . PRO C 3 45  ? 9.53466   -41.38128 2.53421   1.000 179.83719 ? 45  PRO C CA  1 
ATOM   4655 C C   . PRO C 3 45  ? 9.76991   -40.56869 1.26901   1.000 179.94547 ? 45  PRO C C   1 
ATOM   4656 O O   . PRO C 3 45  ? 10.68414  -39.74490 1.19491   1.000 178.87716 ? 45  PRO C O   1 
ATOM   4657 C CB  . PRO C 3 45  ? 8.86764   -40.53935 3.62850   1.000 178.71574 ? 45  PRO C CB  1 
ATOM   4658 C CG  . PRO C 3 45  ? 9.50958   -40.99129 4.90297   1.000 178.00313 ? 45  PRO C CG  1 
ATOM   4659 C CD  . PRO C 3 45  ? 10.92311  -41.32174 4.53794   1.000 177.85283 ? 45  PRO C CD  1 
ATOM   4660 N N   . THR C 3 46  ? 8.93460   -40.81695 0.26680   1.000 183.29361 ? 46  THR C N   1 
ATOM   4661 C CA  . THR C 3 46  ? 8.95584   -40.09283 -0.99495  1.000 183.71070 ? 46  THR C CA  1 
ATOM   4662 C C   . THR C 3 46  ? 7.77674   -39.12456 -1.04048  1.000 183.49329 ? 46  THR C C   1 
ATOM   4663 O O   . THR C 3 46  ? 7.01498   -38.99439 -0.08033  1.000 183.05244 ? 46  THR C O   1 
ATOM   4664 C CB  . THR C 3 46  ? 8.92166   -41.06516 -2.17538  1.000 187.34316 ? 46  THR C CB  1 
ATOM   4665 O OG1 . THR C 3 46  ? 7.62016   -41.65653 -2.27074  1.000 188.70524 ? 46  THR C OG1 1 
ATOM   4666 C CG2 . THR C 3 46  ? 9.95528   -42.16509 -1.98402  1.000 194.47577 ? 46  THR C CG2 1 
ATOM   4667 N N   . THR C 3 47  ? 7.62301   -38.44215 -2.17417  1.000 181.17022 ? 47  THR C N   1 
ATOM   4668 C CA  . THR C 3 47  ? 6.58036   -37.43485 -2.34191  1.000 181.08866 ? 47  THR C CA  1 
ATOM   4669 C C   . THR C 3 47  ? 5.77870   -37.74682 -3.59608  1.000 183.20094 ? 47  THR C C   1 
ATOM   4670 O O   . THR C 3 47  ? 6.34664   -37.84936 -4.68827  1.000 184.03473 ? 47  THR C O   1 
ATOM   4671 C CB  . THR C 3 47  ? 7.17875   -36.02795 -2.42630  1.000 179.52606 ? 47  THR C CB  1 
ATOM   4672 O OG1 . THR C 3 47  ? 8.01759   -35.79619 -1.28785  1.000 177.88737 ? 47  THR C OG1 1 
ATOM   4673 C CG2 . THR C 3 47  ? 6.07406   -34.98413 -2.45295  1.000 179.48304 ? 47  THR C CG2 1 
ATOM   4674 N N   . MET C 3 48  ? 4.46363   -37.88672 -3.43987  1.000 190.33003 ? 48  MET C N   1 
ATOM   4675 C CA  . MET C 3 48  ? 3.56373   -38.21206 -4.54095  1.000 192.67350 ? 48  MET C CA  1 
ATOM   4676 C C   . MET C 3 48  ? 2.68953   -37.04842 -4.98004  1.000 192.82144 ? 48  MET C C   1 
ATOM   4677 O O   . MET C 3 48  ? 2.48627   -36.85969 -6.18066  1.000 194.18643 ? 48  MET C O   1 
ATOM   4678 C CB  . MET C 3 48  ? 2.66379   -39.39284 -4.15642  1.000 194.45554 ? 48  MET C CB  1 
ATOM   4679 C CG  . MET C 3 48  ? 3.40425   -40.69769 -3.89812  1.000 194.89836 ? 48  MET C CG  1 
ATOM   4680 S SD  . MET C 3 48  ? 4.17333   -41.38971 -5.37612  1.000 197.33936 ? 48  MET C SD  1 
ATOM   4681 C CE  . MET C 3 48  ? 5.89923   -41.01949 -5.07403  1.000 198.21617 ? 48  MET C CE  1 
ATOM   4682 N N   . ILE C 3 49  ? 2.15380   -36.26801 -4.04277  1.000 191.54793 ? 49  ILE C N   1 
ATOM   4683 C CA  . ILE C 3 49  ? 1.25566   -35.16137 -4.35186  1.000 191.84059 ? 49  ILE C CA  1 
ATOM   4684 C C   . ILE C 3 49  ? 1.67344   -33.94576 -3.53591  1.000 189.60674 ? 49  ILE C C   1 
ATOM   4685 O O   . ILE C 3 49  ? 2.03033   -34.06829 -2.35901  1.000 188.36178 ? 49  ILE C O   1 
ATOM   4686 C CB  . ILE C 3 49  ? -0.21887  -35.52648 -4.06766  1.000 193.71038 ? 49  ILE C CB  1 
ATOM   4687 C CG1 . ILE C 3 49  ? -0.65628  -36.72142 -4.91690  1.000 196.28838 ? 49  ILE C CG1 1 
ATOM   4688 C CG2 . ILE C 3 49  ? -1.13422  -34.34001 -4.32729  1.000 194.11409 ? 49  ILE C CG2 1 
ATOM   4689 C CD1 . ILE C 3 49  ? -0.71496  -36.43249 -6.40000  1.000 199.20428 ? 49  ILE C CD1 1 
ATOM   4690 N N   . TYR C 3 50  ? 1.63687   -32.77336 -4.16702  1.000 194.83942 ? 50  TYR C N   1 
ATOM   4691 C CA  . TYR C 3 50  ? 1.90180   -31.50969 -3.49602  1.000 195.78309 ? 50  TYR C CA  1 
ATOM   4692 C C   . TYR C 3 50  ? 0.96071   -30.45484 -4.05841  1.000 202.42234 ? 50  TYR C C   1 
ATOM   4693 O O   . TYR C 3 50  ? 0.42384   -30.60286 -5.15912  1.000 207.06025 ? 50  TYR C O   1 
ATOM   4694 C CB  . TYR C 3 50  ? 3.35761   -31.06057 -3.67402  1.000 195.30861 ? 50  TYR C CB  1 
ATOM   4695 C CG  . TYR C 3 50  ? 3.63749   -30.47600 -5.03832  1.000 199.22495 ? 50  TYR C CG  1 
ATOM   4696 C CD1 . TYR C 3 50  ? 3.87493   -31.29876 -6.12994  1.000 201.85241 ? 50  TYR C CD1 1 
ATOM   4697 C CD2 . TYR C 3 50  ? 3.65959   -29.10066 -5.23578  1.000 205.03021 ? 50  TYR C CD2 1 
ATOM   4698 C CE1 . TYR C 3 50  ? 4.12520   -30.77079 -7.37976  1.000 208.43409 ? 50  TYR C CE1 1 
ATOM   4699 C CE2 . TYR C 3 50  ? 3.90788   -28.56319 -6.48166  1.000 209.13573 ? 50  TYR C CE2 1 
ATOM   4700 C CZ  . TYR C 3 50  ? 4.14182   -29.40259 -7.55001  1.000 209.72830 ? 50  TYR C CZ  1 
ATOM   4701 O OH  . TYR C 3 50  ? 4.39205   -28.87160 -8.79404  1.000 212.11100 ? 50  TYR C OH  1 
ATOM   4702 N N   . ARG C 3 51  ? 0.78972   -29.37418 -3.29753  1.000 196.21281 ? 51  ARG C N   1 
ATOM   4703 C CA  . ARG C 3 51  ? -0.11389  -28.27836 -3.65317  1.000 202.38976 ? 51  ARG C CA  1 
ATOM   4704 C C   . ARG C 3 51  ? -1.45181  -28.81468 -4.15731  1.000 205.45532 ? 51  ARG C C   1 
ATOM   4705 O O   . ARG C 3 51  ? -1.90679  -28.49756 -5.25925  1.000 207.19301 ? 51  ARG C O   1 
ATOM   4706 C CB  . ARG C 3 51  ? 0.52615   -27.33983 -4.67778  1.000 203.12298 ? 51  ARG C CB  1 
ATOM   4707 C CG  . ARG C 3 51  ? 1.52443   -26.35573 -4.07975  1.000 202.60593 ? 51  ARG C CG  1 
ATOM   4708 C CD  . ARG C 3 51  ? 1.56410   -25.04709 -4.86228  1.000 204.81814 ? 51  ARG C CD  1 
ATOM   4709 N NE  . ARG C 3 51  ? 2.84273   -24.83315 -5.53032  1.000 203.81513 ? 51  ARG C NE  1 
ATOM   4710 C CZ  . ARG C 3 51  ? 3.05809   -25.03662 -6.82295  1.000 204.41783 ? 51  ARG C CZ  1 
ATOM   4711 N NH1 . ARG C 3 51  ? 2.09352   -25.45161 -7.62780  1.000 205.23997 ? 51  ARG C NH1 1 
ATOM   4712 N NH2 . ARG C 3 51  ? 4.27127   -24.81524 -7.32131  1.000 205.36933 ? 51  ARG C NH2 1 
ATOM   4713 N N   . ASP C 3 52  ? -2.05536  -29.67725 -3.33428  1.000 202.66350 ? 52  ASP C N   1 
ATOM   4714 C CA  . ASP C 3 52  ? -3.39162  -30.23163 -3.53079  1.000 205.31515 ? 52  ASP C CA  1 
ATOM   4715 C C   . ASP C 3 52  ? -3.42345  -31.32521 -4.59452  1.000 203.17631 ? 52  ASP C C   1 
ATOM   4716 O O   . ASP C 3 52  ? -3.79995  -32.46160 -4.29631  1.000 202.51094 ? 52  ASP C O   1 
ATOM   4717 C CB  . ASP C 3 52  ? -4.39573  -29.12665 -3.87863  1.000 210.97403 ? 52  ASP C CB  1 
ATOM   4718 C CG  . ASP C 3 52  ? -4.48217  -28.06557 -2.80159  1.000 212.12671 ? 52  ASP C CG  1 
ATOM   4719 O OD1 . ASP C 3 52  ? -4.92201  -28.38996 -1.67917  1.000 213.48778 ? 52  ASP C OD1 1 
ATOM   4720 O OD2 . ASP C 3 52  ? -4.09386  -26.91010 -3.07504  1.000 211.93724 ? 52  ASP C OD2 1 
ATOM   4721 N N   . ASP C 3 53  ? -3.03633  -31.01513 -5.83129  1.000 203.73340 ? 53  ASP C N   1 
ATOM   4722 C CA  . ASP C 3 53  ? -3.21382  -31.98975 -6.90167  1.000 202.84688 ? 53  ASP C CA  1 
ATOM   4723 C C   . ASP C 3 53  ? -2.01664  -32.17747 -7.82374  1.000 201.50818 ? 53  ASP C C   1 
ATOM   4724 O O   . ASP C 3 53  ? -1.95504  -33.21545 -8.49450  1.000 201.83847 ? 53  ASP C O   1 
ATOM   4725 C CB  . ASP C 3 53  ? -4.44057  -31.63145 -7.75310  1.000 206.94025 ? 53  ASP C CB  1 
ATOM   4726 C CG  . ASP C 3 53  ? -4.40566  -30.20120 -8.24379  1.000 209.26050 ? 53  ASP C CG  1 
ATOM   4727 O OD1 . ASP C 3 53  ? -3.35740  -29.53797 -8.07896  1.000 207.80272 ? 53  ASP C OD1 1 
ATOM   4728 O OD2 . ASP C 3 53  ? -5.42737  -29.73780 -8.79059  1.000 213.06329 ? 53  ASP C OD2 1 
ATOM   4729 N N   . GLN C 3 54  ? -1.07299  -31.24287 -7.90762  1.000 201.71917 ? 54  GLN C N   1 
ATOM   4730 C CA  . GLN C 3 54  ? 0.06652   -31.43125 -8.79637  1.000 200.95860 ? 54  GLN C CA  1 
ATOM   4731 C C   . GLN C 3 54  ? 1.00820   -32.49707 -8.24475  1.000 199.20761 ? 54  GLN C C   1 
ATOM   4732 O O   . GLN C 3 54  ? 1.18860   -32.62786 -7.03054  1.000 197.77657 ? 54  GLN C O   1 
ATOM   4733 C CB  . GLN C 3 54  ? 0.81169   -30.11571 -8.99960  1.000 201.23884 ? 54  GLN C CB  1 
ATOM   4734 C CG  . GLN C 3 54  ? 0.01052   -29.06023 -9.74275  1.000 203.75730 ? 54  GLN C CG  1 
ATOM   4735 C CD  . GLN C 3 54  ? 0.86670   -27.91517 -10.24551 1.000 204.82271 ? 54  GLN C CD  1 
ATOM   4736 O OE1 . GLN C 3 54  ? 1.97308   -27.68728 -9.75661  1.000 204.59323 ? 54  GLN C OE1 1 
ATOM   4737 N NE2 . GLN C 3 54  ? 0.35886   -27.19152 -11.23674 1.000 206.72682 ? 54  GLN C NE2 1 
ATOM   4738 N N   . ARG C 3 55  ? 1.60717   -33.27206 -9.15130  1.000 199.97225 ? 55  ARG C N   1 
ATOM   4739 C CA  . ARG C 3 55  ? 2.48851   -34.35358 -8.74388  1.000 199.25638 ? 55  ARG C CA  1 
ATOM   4740 C C   . ARG C 3 55  ? 3.88608   -34.16517 -9.32590  1.000 200.33550 ? 55  ARG C C   1 
ATOM   4741 O O   . ARG C 3 55  ? 4.03925   -33.63834 -10.43343 1.000 202.68801 ? 55  ARG C O   1 
ATOM   4742 C CB  . ARG C 3 55  ? 1.93320   -35.71903 -9.17383  1.000 200.78360 ? 55  ARG C CB  1 
ATOM   4743 C CG  . ARG C 3 55  ? 1.89175   -35.95082 -10.67323 1.000 203.34351 ? 55  ARG C CG  1 
ATOM   4744 C CD  . ARG C 3 55  ? 1.23210   -37.27887 -11.00355 1.000 205.42072 ? 55  ARG C CD  1 
ATOM   4745 N NE  . ARG C 3 55  ? 1.33187   -37.59824 -12.42239 1.000 207.99049 ? 55  ARG C NE  1 
ATOM   4746 C CZ  . ARG C 3 55  ? 0.50142   -37.14615 -13.35177 1.000 209.89688 ? 55  ARG C CZ  1 
ATOM   4747 N NH1 . ARG C 3 55  ? -0.50162  -36.33853 -13.04866 1.000 209.54321 ? 55  ARG C NH1 1 
ATOM   4748 N NH2 . ARG C 3 55  ? 0.68195   -37.51342 -14.61711 1.000 212.42166 ? 55  ARG C NH2 1 
ATOM   4749 N N   . PRO C 3 56  ? 4.92291   -34.57957 -8.59986  1.000 204.22262 ? 56  PRO C N   1 
ATOM   4750 C CA  . PRO C 3 56  ? 6.29296   -34.35932 -9.07431  1.000 206.73812 ? 56  PRO C CA  1 
ATOM   4751 C C   . PRO C 3 56  ? 6.61375   -35.18673 -10.30928 1.000 211.00857 ? 56  PRO C C   1 
ATOM   4752 O O   . PRO C 3 56  ? 5.97897   -36.20198 -10.60364 1.000 211.54380 ? 56  PRO C O   1 
ATOM   4753 C CB  . PRO C 3 56  ? 7.15987   -34.79371 -7.88549  1.000 205.02279 ? 56  PRO C CB  1 
ATOM   4754 C CG  . PRO C 3 56  ? 6.24820   -34.74758 -6.70340  1.000 197.44620 ? 56  PRO C CG  1 
ATOM   4755 C CD  . PRO C 3 56  ? 4.89625   -35.11334 -7.22826  1.000 199.45499 ? 56  PRO C CD  1 
ATOM   4756 N N   . ASP C 3 57  ? 7.62551   -34.72197 -11.03910 1.000 222.70390 ? 57  ASP C N   1 
ATOM   4757 C CA  . ASP C 3 57  ? 8.14778   -35.46690 -12.17603 1.000 226.96459 ? 57  ASP C CA  1 
ATOM   4758 C C   . ASP C 3 57  ? 8.73738   -36.78703 -11.70016 1.000 228.19736 ? 57  ASP C C   1 
ATOM   4759 O O   . ASP C 3 57  ? 9.65621   -36.80671 -10.87597 1.000 228.36211 ? 57  ASP C O   1 
ATOM   4760 C CB  . ASP C 3 57  ? 9.20334   -34.63554 -12.90144 1.000 230.81932 ? 57  ASP C CB  1 
ATOM   4761 C CG  . ASP C 3 57  ? 8.67562   -33.28432 -13.34668 1.000 230.25411 ? 57  ASP C CG  1 
ATOM   4762 O OD1 . ASP C 3 57  ? 7.91553   -33.23555 -14.33732 1.000 231.55449 ? 57  ASP C OD1 1 
ATOM   4763 O OD2 . ASP C 3 57  ? 9.00986   -32.27115 -12.69596 1.000 228.78746 ? 57  ASP C OD2 1 
ATOM   4764 N N   . GLY C 3 58  ? 8.20688   -37.89028 -12.21901 1.000 218.60822 ? 58  GLY C N   1 
ATOM   4765 C CA  . GLY C 3 58  ? 8.55664   -39.21256 -11.74260 1.000 219.95143 ? 58  GLY C CA  1 
ATOM   4766 C C   . GLY C 3 58  ? 7.45719   -39.89713 -10.96081 1.000 216.69978 ? 58  GLY C C   1 
ATOM   4767 O O   . GLY C 3 58  ? 7.68430   -40.99366 -10.43717 1.000 217.55676 ? 58  GLY C O   1 
ATOM   4768 N N   . VAL C 3 59  ? 6.28538   -39.28433 -10.85616 1.000 213.90399 ? 59  VAL C N   1 
ATOM   4769 C CA  . VAL C 3 59  ? 5.10642   -39.87028 -10.22947 1.000 210.91643 ? 59  VAL C CA  1 
ATOM   4770 C C   . VAL C 3 59  ? 4.09985   -40.16942 -11.33437 1.000 212.85547 ? 59  VAL C C   1 
ATOM   4771 O O   . VAL C 3 59  ? 3.62061   -39.23786 -11.99275 1.000 213.34928 ? 59  VAL C O   1 
ATOM   4772 C CB  . VAL C 3 59  ? 4.50321   -38.94017 -9.16844  1.000 206.46323 ? 59  VAL C CB  1 
ATOM   4773 C CG1 . VAL C 3 59  ? 3.23832   -39.54546 -8.59612  1.000 204.75405 ? 59  VAL C CG1 1 
ATOM   4774 C CG2 . VAL C 3 59  ? 5.52208   -38.66700 -8.06526  1.000 204.38106 ? 59  VAL C CG2 1 
ATOM   4775 N N   . PRO C 3 60  ? 3.76438   -41.43393 -11.58409 1.000 210.93067 ? 60  PRO C N   1 
ATOM   4776 C CA  . PRO C 3 60  ? 2.85107   -41.75090 -12.68520 1.000 214.32914 ? 60  PRO C CA  1 
ATOM   4777 C C   . PRO C 3 60  ? 1.47648   -41.13054 -12.48263 1.000 214.46892 ? 60  PRO C C   1 
ATOM   4778 O O   . PRO C 3 60  ? 1.08174   -40.76052 -11.37498 1.000 212.41252 ? 60  PRO C O   1 
ATOM   4779 C CB  . PRO C 3 60  ? 2.77986   -43.28314 -12.65847 1.000 216.90087 ? 60  PRO C CB  1 
ATOM   4780 C CG  . PRO C 3 60  ? 4.02824   -43.71067 -11.95401 1.000 215.04520 ? 60  PRO C CG  1 
ATOM   4781 C CD  . PRO C 3 60  ? 4.29366   -42.64418 -10.93498 1.000 211.18971 ? 60  PRO C CD  1 
ATOM   4782 N N   . ASP C 3 61  ? 0.73722   -41.02579 -13.59261 1.000 217.41804 ? 61  ASP C N   1 
ATOM   4783 C CA  . ASP C 3 61  ? -0.61178  -40.46790 -13.55406 1.000 218.15788 ? 61  ASP C CA  1 
ATOM   4784 C C   . ASP C 3 61  ? -1.54739  -41.28192 -12.67017 1.000 219.12962 ? 61  ASP C C   1 
ATOM   4785 O O   . ASP C 3 61  ? -2.61270  -40.78351 -12.28950 1.000 219.20805 ? 61  ASP C O   1 
ATOM   4786 C CB  . ASP C 3 61  ? -1.17518  -40.37248 -14.97523 1.000 221.46086 ? 61  ASP C CB  1 
ATOM   4787 C CG  . ASP C 3 61  ? -2.57894  -39.79651 -15.01148 1.000 222.58995 ? 61  ASP C CG  1 
ATOM   4788 O OD1 . ASP C 3 61  ? -2.75756  -38.63431 -14.59030 1.000 220.21139 ? 61  ASP C OD1 1 
ATOM   4789 O OD2 . ASP C 3 61  ? -3.50302  -40.50763 -15.45950 1.000 226.06633 ? 61  ASP C OD2 1 
ATOM   4790 N N   . ARG C 3 62  ? -1.16671  -42.51727 -12.33227 1.000 213.01802 ? 62  ARG C N   1 
ATOM   4791 C CA  . ARG C 3 62  ? -1.97907  -43.34486 -11.44680 1.000 213.94605 ? 62  ARG C CA  1 
ATOM   4792 C C   . ARG C 3 62  ? -2.28521  -42.62359 -10.14070 1.000 210.93377 ? 62  ARG C C   1 
ATOM   4793 O O   . ARG C 3 62  ? -3.39476  -42.73113 -9.60735  1.000 211.92631 ? 62  ARG C O   1 
ATOM   4794 C CB  . ARG C 3 62  ? -1.25599  -44.66501 -11.17773 1.000 214.67488 ? 62  ARG C CB  1 
ATOM   4795 C CG  . ARG C 3 62  ? -0.51918  -45.20447 -12.39763 1.000 216.94933 ? 62  ARG C CG  1 
ATOM   4796 C CD  . ARG C 3 62  ? -0.21573  -46.69416 -12.29262 1.000 219.10808 ? 62  ARG C CD  1 
ATOM   4797 N NE  . ARG C 3 62  ? 0.88795   -46.99282 -11.38745 1.000 216.44714 ? 62  ARG C NE  1 
ATOM   4798 C CZ  . ARG C 3 62  ? 0.74086   -47.43619 -10.14653 1.000 215.05341 ? 62  ARG C CZ  1 
ATOM   4799 N NH1 . ARG C 3 62  ? -0.45691  -47.62636 -9.61810  1.000 215.97811 ? 62  ARG C NH1 1 
ATOM   4800 N NH2 . ARG C 3 62  ? 1.82272   -47.70061 -9.41933  1.000 212.86178 ? 62  ARG C NH2 1 
ATOM   4801 N N   . PHE C 3 63  ? -1.31776  -41.87119 -9.62121  1.000 208.50059 ? 63  PHE C N   1 
ATOM   4802 C CA  . PHE C 3 63  ? -1.48842  -41.11704 -8.38775  1.000 205.71235 ? 63  PHE C CA  1 
ATOM   4803 C C   . PHE C 3 63  ? -2.14055  -39.77159 -8.69399  1.000 205.23208 ? 63  PHE C C   1 
ATOM   4804 O O   . PHE C 3 63  ? -1.70094  -39.05726 -9.59959  1.000 204.96160 ? 63  PHE C O   1 
ATOM   4805 C CB  . PHE C 3 63  ? -0.13761  -40.91138 -7.69980  1.000 202.57471 ? 63  PHE C CB  1 
ATOM   4806 C CG  . PHE C 3 63  ? 0.63743   -42.18190 -7.49606  1.000 203.07494 ? 63  PHE C CG  1 
ATOM   4807 C CD1 . PHE C 3 63  ? 1.48013   -42.66126 -8.48494  1.000 204.27233 ? 63  PHE C CD1 1 
ATOM   4808 C CD2 . PHE C 3 63  ? 0.51938   -42.89913 -6.31809  1.000 202.53786 ? 63  PHE C CD2 1 
ATOM   4809 C CE1 . PHE C 3 63  ? 2.19005   -43.83230 -8.30399  1.000 204.96087 ? 63  PHE C CE1 1 
ATOM   4810 C CE2 . PHE C 3 63  ? 1.22769   -44.07122 -6.13023  1.000 203.09676 ? 63  PHE C CE2 1 
ATOM   4811 C CZ  . PHE C 3 63  ? 2.06421   -44.53802 -7.12451  1.000 204.32588 ? 63  PHE C CZ  1 
ATOM   4812 N N   . SER C 3 64  ? -3.18269  -39.42364 -7.93825  1.000 208.79847 ? 64  SER C N   1 
ATOM   4813 C CA  . SER C 3 64  ? -3.93460  -38.20215 -8.19503  1.000 208.76940 ? 64  SER C CA  1 
ATOM   4814 C C   . SER C 3 64  ? -4.48074  -37.65549 -6.88279  1.000 207.30721 ? 64  SER C C   1 
ATOM   4815 O O   . SER C 3 64  ? -4.71844  -38.40947 -5.93801  1.000 207.45304 ? 64  SER C O   1 
ATOM   4816 C CB  . SER C 3 64  ? -5.08345  -38.46032 -9.17818  1.000 212.38527 ? 64  SER C CB  1 
ATOM   4817 O OG  . SER C 3 64  ? -4.61999  -39.07630 -10.36932 1.000 214.21282 ? 64  SER C OG  1 
ATOM   4818 N N   . GLY C 3 65  ? -4.68860  -36.33603 -6.83781  1.000 213.00289 ? 65  GLY C N   1 
ATOM   4819 C CA  . GLY C 3 65  ? -5.24199  -35.68785 -5.66209  1.000 211.95119 ? 65  GLY C CA  1 
ATOM   4820 C C   . GLY C 3 65  ? -6.60475  -35.06917 -5.91880  1.000 214.02451 ? 65  GLY C C   1 
ATOM   4821 O O   . GLY C 3 65  ? -7.00406  -34.90514 -7.06974  1.000 215.84080 ? 65  GLY C O   1 
ATOM   4822 N N   . SER C 3 66  ? -7.31546  -34.72779 -4.84362  1.000 209.09996 ? 66  SER C N   1 
ATOM   4823 C CA  . SER C 3 66  ? -8.66419  -34.18985 -4.97331  1.000 211.73178 ? 66  SER C CA  1 
ATOM   4824 C C   . SER C 3 66  ? -9.15435  -33.56982 -3.66941  1.000 214.57744 ? 66  SER C C   1 
ATOM   4825 O O   . SER C 3 66  ? -9.25760  -34.25614 -2.64717  1.000 214.46215 ? 66  SER C O   1 
ATOM   4826 C CB  . SER C 3 66  ? -9.62514  -35.28788 -5.42901  1.000 214.84358 ? 66  SER C CB  1 
ATOM   4827 O OG  . SER C 3 66  ? -9.25164  -36.54633 -4.89811  1.000 214.82221 ? 66  SER C OG  1 
ATOM   4828 N N   . ILE C 3 67  ? -9.46567  -32.27574 -3.69872  1.000 218.71477 ? 67  ILE C N   1 
ATOM   4829 C CA  . ILE C 3 67  ? -9.99393  -31.55748 -2.54332  1.000 221.24376 ? 67  ILE C CA  1 
ATOM   4830 C C   . ILE C 3 67  ? -11.50805 -31.48700 -2.67039  1.000 225.90816 ? 67  ILE C C   1 
ATOM   4831 O O   . ILE C 3 67  ? -12.03295 -31.04501 -3.70008  1.000 227.26659 ? 67  ILE C O   1 
ATOM   4832 C CB  . ILE C 3 67  ? -9.38496  -30.14847 -2.42973  1.000 220.47426 ? 67  ILE C CB  1 
ATOM   4833 C CG1 . ILE C 3 67  ? -7.94774  -30.22293 -1.91125  1.000 216.43965 ? 67  ILE C CG1 1 
ATOM   4834 C CG2 . ILE C 3 67  ? -10.23701 -29.26067 -1.52819  1.000 224.41893 ? 67  ILE C CG2 1 
ATOM   4835 C CD1 . ILE C 3 67  ? -7.84507  -30.58615 -0.44647  1.000 216.48438 ? 67  ILE C CD1 1 
ATOM   4836 N N   . ASP C 3 68  ? -12.21094 -31.92896 -1.62909  1.000 207.41382 ? 68  ASP C N   1 
ATOM   4837 C CA  . ASP C 3 68  ? -13.67047 -31.91352 -1.58407  1.000 235.75056 ? 68  ASP C CA  1 
ATOM   4838 C C   . ASP C 3 68  ? -14.10866 -30.96318 -0.47522  1.000 241.70679 ? 68  ASP C C   1 
ATOM   4839 O O   . ASP C 3 68  ? -13.97805 -31.28755 0.71069   1.000 238.23507 ? 68  ASP C O   1 
ATOM   4840 C CB  . ASP C 3 68  ? -14.22123 -33.32228 -1.35376  1.000 235.08675 ? 68  ASP C CB  1 
ATOM   4841 C CG  . ASP C 3 68  ? -15.73748 -33.35643 -1.29795  1.000 245.77250 ? 68  ASP C CG  1 
ATOM   4842 O OD1 . ASP C 3 68  ? -16.38202 -32.44385 -1.85757  1.000 248.85037 ? 68  ASP C OD1 1 
ATOM   4843 O OD2 . ASP C 3 68  ? -16.28376 -34.29854 -0.68585  1.000 247.67876 ? 68  ASP C OD2 1 
ATOM   4844 N N   . ARG C 3 69  ? -14.62457 -29.79073 -0.86144  1.000 237.75660 ? 69  ARG C N   1 
ATOM   4845 C CA  . ARG C 3 69  ? -15.13332 -28.82718 0.11042   1.000 242.73639 ? 69  ARG C CA  1 
ATOM   4846 C C   . ARG C 3 69  ? -16.31124 -29.37163 0.91370   1.000 247.91862 ? 69  ARG C C   1 
ATOM   4847 O O   . ARG C 3 69  ? -16.50657 -28.95204 2.05936   1.000 251.19764 ? 69  ARG C O   1 
ATOM   4848 C CB  . ARG C 3 69  ? -15.51722 -27.52672 -0.61445  1.000 244.36987 ? 69  ARG C CB  1 
ATOM   4849 C CG  . ARG C 3 69  ? -16.31956 -26.52082 0.21300   1.000 249.82273 ? 69  ARG C CG  1 
ATOM   4850 C CD  . ARG C 3 69  ? -15.54793 -25.98965 1.41890   1.000 250.20752 ? 69  ARG C CD  1 
ATOM   4851 N NE  . ARG C 3 69  ? -14.53657 -25.00253 1.05859   1.000 247.39050 ? 69  ARG C NE  1 
ATOM   4852 C CZ  . ARG C 3 69  ? -13.23478 -25.15155 1.26302   1.000 243.04574 ? 69  ARG C CZ  1 
ATOM   4853 N NH1 . ARG C 3 69  ? -12.74428 -26.24049 1.83226   1.000 237.28191 ? 69  ARG C NH1 1 
ATOM   4854 N NH2 . ARG C 3 69  ? -12.40494 -24.17951 0.89499   1.000 240.95867 ? 69  ARG C NH2 1 
ATOM   4855 N N   . SER C 3 70  ? -17.08259 -30.30898 0.35692   1.000 235.47992 ? 70  SER C N   1 
ATOM   4856 C CA  . SER C 3 70  ? -18.23596 -30.83787 1.07857   1.000 240.33295 ? 70  SER C CA  1 
ATOM   4857 C C   . SER C 3 70  ? -17.80855 -31.61647 2.31766   1.000 240.20929 ? 70  SER C C   1 
ATOM   4858 O O   . SER C 3 70  ? -18.26873 -31.32789 3.42675   1.000 244.27278 ? 70  SER C O   1 
ATOM   4859 C CB  . SER C 3 70  ? -19.07598 -31.71673 0.15338   1.000 241.25601 ? 70  SER C CB  1 
ATOM   4860 O OG  . SER C 3 70  ? -19.57182 -30.97874 -0.95025  1.000 241.77290 ? 70  SER C OG  1 
ATOM   4861 N N   . SER C 3 71  ? -16.94844 -32.62144 2.14935   1.000 236.04636 ? 71  SER C N   1 
ATOM   4862 C CA  . SER C 3 71  ? -16.51070 -33.45945 3.25990   1.000 235.60425 ? 71  SER C CA  1 
ATOM   4863 C C   . SER C 3 71  ? -15.25051 -32.93973 3.94068   1.000 232.48082 ? 71  SER C C   1 
ATOM   4864 O O   . SER C 3 71  ? -14.77230 -33.57522 4.88672   1.000 231.36545 ? 71  SER C O   1 
ATOM   4865 C CB  . SER C 3 71  ? -16.27870 -34.89681 2.78039   1.000 232.91291 ? 71  SER C CB  1 
ATOM   4866 O OG  . SER C 3 71  ? -15.21672 -34.96527 1.84410   1.000 227.56908 ? 71  SER C OG  1 
ATOM   4867 N N   . ASN C 3 72  ? -14.70898 -31.81008 3.48209   1.000 231.05391 ? 72  ASN C N   1 
ATOM   4868 C CA  . ASN C 3 72  ? -13.52249 -31.18832 4.07359   1.000 228.28755 ? 72  ASN C CA  1 
ATOM   4869 C C   . ASN C 3 72  ? -12.37197 -32.18788 4.18058   1.000 222.87263 ? 72  ASN C C   1 
ATOM   4870 O O   . ASN C 3 72  ? -11.79434 -32.40256 5.24877   1.000 222.26612 ? 72  ASN C O   1 
ATOM   4871 C CB  . ASN C 3 72  ? -13.84715 -30.57865 5.44005   1.000 233.04894 ? 72  ASN C CB  1 
ATOM   4872 C CG  . ASN C 3 72  ? -12.81685 -29.55625 5.88348   1.000 231.51094 ? 72  ASN C CG  1 
ATOM   4873 O OD1 . ASN C 3 72  ? -12.42195 -28.68182 5.11241   1.000 229.76575 ? 72  ASN C OD1 1 
ATOM   4874 N ND2 . ASN C 3 72  ? -12.36983 -29.66743 7.12951   1.000 232.38374 ? 72  ASN C ND2 1 
ATOM   4875 N N   . SER C 3 73  ? -12.03938 -32.80869 3.05153   1.000 222.18000 ? 73  SER C N   1 
ATOM   4876 C CA  . SER C 3 73  ? -11.01392 -33.84045 3.03772   1.000 217.43453 ? 73  SER C CA  1 
ATOM   4877 C C   . SER C 3 73  ? -10.35471 -33.90301 1.66982   1.000 213.59884 ? 73  SER C C   1 
ATOM   4878 O O   . SER C 3 73  ? -11.02540 -33.77505 0.64160   1.000 215.05948 ? 73  SER C O   1 
ATOM   4879 C CB  . SER C 3 73  ? -11.60119 -35.21063 3.39224   1.000 218.91248 ? 73  SER C CB  1 
ATOM   4880 O OG  . SER C 3 73  ? -10.63888 -36.23628 3.22019   1.000 214.55023 ? 73  SER C OG  1 
ATOM   4881 N N   . ALA C 3 74  ? -9.04019  -34.09946 1.67031   1.000 218.22604 ? 74  ALA C N   1 
ATOM   4882 C CA  . ALA C 3 74  ? -8.31903  -34.40977 0.44875   1.000 214.64719 ? 74  ALA C CA  1 
ATOM   4883 C C   . ALA C 3 74  ? -8.38581  -35.90848 0.17994   1.000 211.74343 ? 74  ALA C C   1 
ATOM   4884 O O   . ALA C 3 74  ? -8.68000  -36.71081 1.06939   1.000 210.05201 ? 74  ALA C O   1 
ATOM   4885 C CB  . ALA C 3 74  ? -6.86316  -33.95135 0.54398   1.000 210.17007 ? 74  ALA C CB  1 
ATOM   4886 N N   . LEU C 3 75  ? -8.11045  -36.28528 -1.06633  1.000 200.06821 ? 75  LEU C N   1 
ATOM   4887 C CA  . LEU C 3 75  ? -8.21006  -37.68077 -1.47752  1.000 201.87136 ? 75  LEU C CA  1 
ATOM   4888 C C   . LEU C 3 75  ? -7.09796  -38.01044 -2.45962  1.000 200.87580 ? 75  LEU C C   1 
ATOM   4889 O O   . LEU C 3 75  ? -7.02994  -37.42665 -3.54542  1.000 201.16490 ? 75  LEU C O   1 
ATOM   4890 C CB  . LEU C 3 75  ? -9.58137  -37.97312 -2.09309  1.000 205.51617 ? 75  LEU C CB  1 
ATOM   4891 C CG  . LEU C 3 75  ? -10.66875 -38.37307 -1.09470  1.000 207.43971 ? 75  LEU C CG  1 
ATOM   4892 C CD1 . LEU C 3 75  ? -12.05165 -38.09065 -1.65527  1.000 210.77436 ? 75  LEU C CD1 1 
ATOM   4893 C CD2 . LEU C 3 75  ? -10.53067 -39.84346 -0.73265  1.000 208.35949 ? 75  LEU C CD2 1 
ATOM   4894 N N   . LEU C 3 76  ? -6.23399  -38.94602 -2.07463  1.000 197.92448 ? 76  LEU C N   1 
ATOM   4895 C CA  . LEU C 3 76  ? -5.20292  -39.47323 -2.95801  1.000 197.50553 ? 76  LEU C CA  1 
ATOM   4896 C C   . LEU C 3 76  ? -5.75956  -40.69034 -3.68653  1.000 200.69646 ? 76  LEU C C   1 
ATOM   4897 O O   . LEU C 3 76  ? -6.09266  -41.69896 -3.05470  1.000 201.84592 ? 76  LEU C O   1 
ATOM   4898 C CB  . LEU C 3 76  ? -3.94746  -39.84060 -2.16814  1.000 194.99523 ? 76  LEU C CB  1 
ATOM   4899 C CG  . LEU C 3 76  ? -2.84876  -40.58502 -2.93067  1.000 194.86315 ? 76  LEU C CG  1 
ATOM   4900 C CD1 . LEU C 3 76  ? -2.37888  -39.78080 -4.13059  1.000 194.51950 ? 76  LEU C CD1 1 
ATOM   4901 C CD2 . LEU C 3 76  ? -1.68134  -40.90781 -2.01162  1.000 192.52367 ? 76  LEU C CD2 1 
ATOM   4902 N N   . THR C 3 77  ? -5.86504  -40.59383 -5.00836  1.000 205.35802 ? 77  THR C N   1 
ATOM   4903 C CA  . THR C 3 77  ? -6.44270  -41.64633 -5.83443  1.000 208.85417 ? 77  THR C CA  1 
ATOM   4904 C C   . THR C 3 77  ? -5.32656  -42.33805 -6.60516  1.000 208.85112 ? 77  THR C C   1 
ATOM   4905 O O   . THR C 3 77  ? -4.58866  -41.68666 -7.35207  1.000 207.70082 ? 77  THR C O   1 
ATOM   4906 C CB  . THR C 3 77  ? -7.48813  -41.07788 -6.79448  1.000 211.34477 ? 77  THR C CB  1 
ATOM   4907 O OG1 . THR C 3 77  ? -8.34112  -40.16757 -6.08888  1.000 210.88201 ? 77  THR C OG1 1 
ATOM   4908 C CG2 . THR C 3 77  ? -8.33459  -42.19743 -7.38171  1.000 215.45356 ? 77  THR C CG2 1 
ATOM   4909 N N   . ILE C 3 78  ? -5.20634  -43.65071 -6.42288  1.000 206.55515 ? 78  ILE C N   1 
ATOM   4910 C CA  . ILE C 3 78  ? -4.17953  -44.45502 -7.07667  1.000 207.00223 ? 78  ILE C CA  1 
ATOM   4911 C C   . ILE C 3 78  ? -4.88449  -45.48720 -7.94586  1.000 211.26077 ? 78  ILE C C   1 
ATOM   4912 O O   . ILE C 3 78  ? -5.51301  -46.42013 -7.42957  1.000 213.10462 ? 78  ILE C O   1 
ATOM   4913 C CB  . ILE C 3 78  ? -3.24351  -45.13084 -6.06620  1.000 205.00056 ? 78  ILE C CB  1 
ATOM   4914 C CG1 . ILE C 3 78  ? -2.60763  -44.08578 -5.14725  1.000 201.10099 ? 78  ILE C CG1 1 
ATOM   4915 C CG2 . ILE C 3 78  ? -2.16862  -45.93069 -6.78942  1.000 205.71798 ? 78  ILE C CG2 1 
ATOM   4916 C CD1 . ILE C 3 78  ? -1.70798  -44.67434 -4.08334  1.000 199.15896 ? 78  ILE C CD1 1 
ATOM   4917 N N   . ASP C 3 79  ? -4.78051  -45.32539 -9.26080  1.000 211.88030 ? 79  ASP C N   1 
ATOM   4918 C CA  . ASP C 3 79  ? -5.39126  -46.24627 -10.20687 1.000 216.26617 ? 79  ASP C CA  1 
ATOM   4919 C C   . ASP C 3 79  ? -4.39036  -47.31672 -10.61986 1.000 217.28067 ? 79  ASP C C   1 
ATOM   4920 O O   . ASP C 3 79  ? -3.17690  -47.09387 -10.60428 1.000 214.83384 ? 79  ASP C O   1 
ATOM   4921 C CB  . ASP C 3 79  ? -5.88507  -45.49750 -11.44521 1.000 218.10068 ? 79  ASP C CB  1 
ATOM   4922 C CG  . ASP C 3 79  ? -6.51542  -44.16315 -11.10600 1.000 216.25245 ? 79  ASP C CG  1 
ATOM   4923 O OD1 . ASP C 3 79  ? -7.42914  -44.13199 -10.25579 1.000 216.43005 ? 79  ASP C OD1 1 
ATOM   4924 O OD2 . ASP C 3 79  ? -6.08590  -43.14174 -11.68214 1.000 214.74405 ? 79  ASP C OD2 1 
ATOM   4925 N N   . ASN C 3 80  ? -4.91406  -48.48290 -10.99529 1.000 220.80130 ? 80  ASN C N   1 
ATOM   4926 C CA  . ASN C 3 80  ? -4.10206  -49.60538 -11.46481 1.000 222.62188 ? 80  ASN C CA  1 
ATOM   4927 C C   . ASN C 3 80  ? -2.99106  -49.92139 -10.46191 1.000 219.39249 ? 80  ASN C C   1 
ATOM   4928 O O   . ASN C 3 80  ? -1.79830  -49.79079 -10.74531 1.000 217.86545 ? 80  ASN C O   1 
ATOM   4929 C CB  . ASN C 3 80  ? -3.53508  -49.31504 -12.85698 1.000 224.03273 ? 80  ASN C CB  1 
ATOM   4930 C CG  . ASN C 3 80  ? -2.82526  -50.50943 -13.46375 1.000 226.79465 ? 80  ASN C CG  1 
ATOM   4931 O OD1 . ASN C 3 80  ? -3.11391  -51.65686 -13.12364 1.000 229.01577 ? 80  ASN C OD1 1 
ATOM   4932 N ND2 . ASN C 3 80  ? -1.88719  -50.24447 -14.36497 1.000 226.84411 ? 80  ASN C ND2 1 
ATOM   4933 N N   . VAL C 3 81  ? -3.41518  -50.32550 -9.26167  1.000 224.22870 ? 81  VAL C N   1 
ATOM   4934 C CA  . VAL C 3 81  ? -2.47994  -50.55601 -8.16527  1.000 222.99623 ? 81  VAL C CA  1 
ATOM   4935 C C   . VAL C 3 81  ? -1.48323  -51.63306 -8.56587  1.000 227.54896 ? 81  VAL C C   1 
ATOM   4936 O O   . VAL C 3 81  ? -1.86386  -52.74528 -8.95298  1.000 232.39728 ? 81  VAL C O   1 
ATOM   4937 C CB  . VAL C 3 81  ? -3.23335  -50.93687 -6.88549  1.000 222.71229 ? 81  VAL C CB  1 
ATOM   4938 C CG1 . VAL C 3 81  ? -2.25202  -51.25618 -5.76631  1.000 221.94427 ? 81  VAL C CG1 1 
ATOM   4939 C CG2 . VAL C 3 81  ? -4.17323  -49.81535 -6.47230  1.000 219.63918 ? 81  VAL C CG2 1 
ATOM   4940 N N   . GLN C 3 82  ? -0.19890  -51.30616 -8.47533  1.000 223.72451 ? 82  GLN C N   1 
ATOM   4941 C CA  . GLN C 3 82  ? 0.86732   -52.21301 -8.86743  1.000 227.87393 ? 82  GLN C CA  1 
ATOM   4942 C C   . GLN C 3 82  ? 1.44844   -52.90851 -7.63890  1.000 228.96291 ? 82  GLN C C   1 
ATOM   4943 O O   . GLN C 3 82  ? 1.07701   -52.63107 -6.49496  1.000 225.68077 ? 82  GLN C O   1 
ATOM   4944 C CB  . GLN C 3 82  ? 1.94126   -51.46296 -9.65506  1.000 227.25466 ? 82  GLN C CB  1 
ATOM   4945 C CG  . GLN C 3 82  ? 1.49663   -51.07921 -11.05501 1.000 228.08178 ? 82  GLN C CG  1 
ATOM   4946 C CD  . GLN C 3 82  ? 0.88041   -52.25002 -11.79866 1.000 233.53457 ? 82  GLN C CD  1 
ATOM   4947 O OE1 . GLN C 3 82  ? 1.49130   -53.31041 -11.92182 1.000 236.94631 ? 82  GLN C OE1 1 
ATOM   4948 N NE2 . GLN C 3 82  ? -0.34608  -52.07077 -12.27696 1.000 233.00541 ? 82  GLN C NE2 1 
ATOM   4949 N N   . THR C 3 83  ? 2.38153   -53.82773 -7.89282  1.000 228.32027 ? 83  THR C N   1 
ATOM   4950 C CA  . THR C 3 83  ? 2.91261   -54.67197 -6.82681  1.000 230.57283 ? 83  THR C CA  1 
ATOM   4951 C C   . THR C 3 83  ? 3.65115   -53.85206 -5.77553  1.000 227.15694 ? 83  THR C C   1 
ATOM   4952 O O   . THR C 3 83  ? 3.52413   -54.11252 -4.57356  1.000 226.40993 ? 83  THR C O   1 
ATOM   4953 C CB  . THR C 3 83  ? 3.83607   -55.73633 -7.41879  1.000 235.48509 ? 83  THR C CB  1 
ATOM   4954 O OG1 . THR C 3 83  ? 3.19616   -56.35311 -8.54268  1.000 238.13071 ? 83  THR C OG1 1 
ATOM   4955 C CG2 . THR C 3 83  ? 4.15690   -56.80479 -6.38120  1.000 238.77451 ? 83  THR C CG2 1 
ATOM   4956 N N   . GLU C 3 84  ? 4.42450   -52.85476 -6.20639  1.000 233.68443 ? 84  GLU C N   1 
ATOM   4957 C CA  . GLU C 3 84  ? 5.23820   -52.07546 -5.28229  1.000 229.87823 ? 84  GLU C CA  1 
ATOM   4958 C C   . GLU C 3 84  ? 4.43714   -51.04203 -4.50035  1.000 223.11777 ? 84  GLU C C   1 
ATOM   4959 O O   . GLU C 3 84  ? 4.99814   -50.39997 -3.60585  1.000 220.01923 ? 84  GLU C O   1 
ATOM   4960 C CB  . GLU C 3 84  ? 6.37130   -51.37301 -6.03695  1.000 230.44500 ? 84  GLU C CB  1 
ATOM   4961 C CG  . GLU C 3 84  ? 5.95682   -50.08933 -6.74144  1.000 225.58885 ? 84  GLU C CG  1 
ATOM   4962 C CD  . GLU C 3 84  ? 5.06735   -50.33688 -7.94208  1.000 226.74169 ? 84  GLU C CD  1 
ATOM   4963 O OE1 . GLU C 3 84  ? 5.16606   -51.42757 -8.54233  1.000 232.60498 ? 84  GLU C OE1 1 
ATOM   4964 O OE2 . GLU C 3 84  ? 4.26772   -49.44059 -8.28411  1.000 223.08254 ? 84  GLU C OE2 1 
ATOM   4965 N N   . ASP C 3 85  ? 3.15009   -50.86679 -4.80430  1.000 217.53323 ? 85  ASP C N   1 
ATOM   4966 C CA  . ASP C 3 85  ? 2.33917   -49.87307 -4.10755  1.000 212.04464 ? 85  ASP C CA  1 
ATOM   4967 C C   . ASP C 3 85  ? 1.99022   -50.27311 -2.67949  1.000 211.15433 ? 85  ASP C C   1 
ATOM   4968 O O   . ASP C 3 85  ? 1.27299   -49.52224 -2.00853  1.000 209.45919 ? 85  ASP C O   1 
ATOM   4969 C CB  . ASP C 3 85  ? 1.05625   -49.59582 -4.89340  1.000 214.17876 ? 85  ASP C CB  1 
ATOM   4970 C CG  . ASP C 3 85  ? 1.28936   -48.68905 -6.08422  1.000 214.24990 ? 85  ASP C CG  1 
ATOM   4971 O OD1 . ASP C 3 85  ? 2.40738   -48.14584 -6.20603  1.000 212.19708 ? 85  ASP C OD1 1 
ATOM   4972 O OD2 . ASP C 3 85  ? 0.35684   -48.51926 -6.89753  1.000 216.49869 ? 85  ASP C OD2 1 
ATOM   4973 N N   . GLU C 3 86  ? 2.46693   -51.41864 -2.19587  1.000 215.11670 ? 86  GLU C N   1 
ATOM   4974 C CA  . GLU C 3 86  ? 2.23337   -51.80059 -0.81012  1.000 215.70518 ? 86  GLU C CA  1 
ATOM   4975 C C   . GLU C 3 86  ? 3.12664   -50.97772 0.10872   1.000 210.33364 ? 86  GLU C C   1 
ATOM   4976 O O   . GLU C 3 86  ? 4.26746   -51.36129 0.38767   1.000 213.28049 ? 86  GLU C O   1 
ATOM   4977 C CB  . GLU C 3 86  ? 2.47636   -53.29835 -0.61390  1.000 222.83513 ? 86  GLU C CB  1 
ATOM   4978 C CG  . GLU C 3 86  ? 2.06804   -53.81865 0.75496   1.000 223.83741 ? 86  GLU C CG  1 
ATOM   4979 C CD  . GLU C 3 86  ? 1.87690   -55.32374 0.77596   1.000 230.89027 ? 86  GLU C CD  1 
ATOM   4980 O OE1 . GLU C 3 86  ? 1.74125   -55.92144 -0.31256  1.000 234.42548 ? 86  GLU C OE1 1 
ATOM   4981 O OE2 . GLU C 3 86  ? 1.85814   -55.90804 1.88061   1.000 233.36354 ? 86  GLU C OE2 1 
ATOM   4982 N N   . ALA C 3 87  ? 2.61694   -49.83987 0.57184   1.000 216.65794 ? 87  ALA C N   1 
ATOM   4983 C CA  . ALA C 3 87  ? 3.38366   -48.93845 1.41934   1.000 210.66524 ? 87  ALA C CA  1 
ATOM   4984 C C   . ALA C 3 87  ? 2.41276   -48.06144 2.19610   1.000 205.81734 ? 87  ALA C C   1 
ATOM   4985 O O   . ALA C 3 87  ? 1.20054   -48.09044 1.97140   1.000 206.45954 ? 87  ALA C O   1 
ATOM   4986 C CB  . ALA C 3 87  ? 4.35452   -48.08820 0.59391   1.000 208.65845 ? 87  ALA C CB  1 
ATOM   4987 N N   . ALA C 3 88  ? 2.96546   -47.27710 3.11687   1.000 201.45848 ? 88  ALA C N   1 
ATOM   4988 C CA  . ALA C 3 88  ? 2.18243   -46.33319 3.89947   1.000 195.79636 ? 88  ALA C CA  1 
ATOM   4989 C C   . ALA C 3 88  ? 2.15254   -44.97989 3.20319   1.000 193.22883 ? 88  ALA C C   1 
ATOM   4990 O O   . ALA C 3 88  ? 3.16293   -44.52431 2.66022   1.000 192.04266 ? 88  ALA C O   1 
ATOM   4991 C CB  . ALA C 3 88  ? 2.75906   -46.18667 5.30818   1.000 196.02553 ? 88  ALA C CB  1 
ATOM   4992 N N   . TYR C 3 89  ? 0.98643   -44.34097 3.22183   1.000 186.44711 ? 89  TYR C N   1 
ATOM   4993 C CA  . TYR C 3 89  ? 0.78672   -43.05335 2.57638   1.000 185.81587 ? 89  TYR C CA  1 
ATOM   4994 C C   . TYR C 3 89  ? 0.36386   -42.01883 3.61170   1.000 184.57509 ? 89  TYR C C   1 
ATOM   4995 O O   . TYR C 3 89  ? -0.34861  -42.33093 4.57072   1.000 185.21655 ? 89  TYR C O   1 
ATOM   4996 C CB  . TYR C 3 89  ? -0.25147  -43.16060 1.45171   1.000 188.21275 ? 89  TYR C CB  1 
ATOM   4997 C CG  . TYR C 3 89  ? 0.20930   -44.02398 0.29391   1.000 189.67294 ? 89  TYR C CG  1 
ATOM   4998 C CD1 . TYR C 3 89  ? 0.06577   -45.40596 0.32906   1.000 191.55496 ? 89  TYR C CD1 1 
ATOM   4999 C CD2 . TYR C 3 89  ? 0.79435   -43.45648 -0.83095  1.000 189.37331 ? 89  TYR C CD2 1 
ATOM   5000 C CE1 . TYR C 3 89  ? 0.48944   -46.19703 -0.72478  1.000 193.20921 ? 89  TYR C CE1 1 
ATOM   5001 C CE2 . TYR C 3 89  ? 1.21992   -44.23982 -1.89003  1.000 191.00606 ? 89  TYR C CE2 1 
ATOM   5002 C CZ  . TYR C 3 89  ? 1.06517   -45.60887 -1.83125  1.000 192.97402 ? 89  TYR C CZ  1 
ATOM   5003 O OH  . TYR C 3 89  ? 1.48696   -46.39272 -2.88143  1.000 194.91086 ? 89  TYR C OH  1 
ATOM   5004 N N   . PHE C 3 90  ? 0.81518   -40.78066 3.41071   1.000 181.91083 ? 90  PHE C N   1 
ATOM   5005 C CA  . PHE C 3 90  ? 0.69191   -39.73165 4.41486   1.000 180.62266 ? 90  PHE C CA  1 
ATOM   5006 C C   . PHE C 3 90  ? 0.27734   -38.41799 3.76858   1.000 180.46666 ? 90  PHE C C   1 
ATOM   5007 O O   . PHE C 3 90  ? 0.58910   -38.15862 2.60602   1.000 180.48942 ? 90  PHE C O   1 
ATOM   5008 C CB  . PHE C 3 90  ? 2.01406   -39.52294 5.16367   1.000 178.52082 ? 90  PHE C CB  1 
ATOM   5009 C CG  . PHE C 3 90  ? 2.14014   -40.33401 6.41752   1.000 178.45339 ? 90  PHE C CG  1 
ATOM   5010 C CD1 . PHE C 3 90  ? 1.53140   -39.91418 7.58790   1.000 178.48626 ? 90  PHE C CD1 1 
ATOM   5011 C CD2 . PHE C 3 90  ? 2.87873   -41.50557 6.43311   1.000 178.51503 ? 90  PHE C CD2 1 
ATOM   5012 C CE1 . PHE C 3 90  ? 1.64913   -40.65020 8.74924   1.000 178.53490 ? 90  PHE C CE1 1 
ATOM   5013 C CE2 . PHE C 3 90  ? 2.99982   -42.24783 7.59200   1.000 178.49524 ? 90  PHE C CE2 1 
ATOM   5014 C CZ  . PHE C 3 90  ? 2.38504   -41.81868 8.75194   1.000 178.47386 ? 90  PHE C CZ  1 
ATOM   5015 N N   . CYS C 3 91  ? -0.40922  -37.58172 4.54574   1.000 186.99223 ? 91  CYS C N   1 
ATOM   5016 C CA  . CYS C 3 91  ? -0.78397  -36.23417 4.14039   1.000 186.79842 ? 91  CYS C CA  1 
ATOM   5017 C C   . CYS C 3 91  ? -0.18997  -35.22422 5.11545   1.000 185.13610 ? 91  CYS C C   1 
ATOM   5018 O O   . CYS C 3 91  ? 0.08367   -35.54002 6.27620   1.000 184.67787 ? 91  CYS C O   1 
ATOM   5019 C CB  . CYS C 3 91  ? -2.31230  -36.06498 4.06538   1.000 188.91412 ? 91  CYS C CB  1 
ATOM   5020 S SG  . CYS C 3 91  ? -3.25770  -36.68903 5.48655   1.000 190.28954 ? 91  CYS C SG  1 
ATOM   5021 N N   . HIS C 3 92  ? 0.00631   -33.99736 4.63476   1.000 191.55974 ? 92  HIS C N   1 
ATOM   5022 C CA  . HIS C 3 92  ? 0.69298   -32.97614 5.42051   1.000 190.13271 ? 92  HIS C CA  1 
ATOM   5023 C C   . HIS C 3 92  ? 0.21583   -31.59455 4.99877   1.000 190.32342 ? 92  HIS C C   1 
ATOM   5024 O O   . HIS C 3 92  ? 0.41129   -31.19365 3.84757   1.000 190.20766 ? 92  HIS C O   1 
ATOM   5025 C CB  . HIS C 3 92  ? 2.21050   -33.09699 5.25492   1.000 188.44146 ? 92  HIS C CB  1 
ATOM   5026 C CG  . HIS C 3 92  ? 2.96219   -31.86701 5.65418   1.000 187.20549 ? 92  HIS C CG  1 
ATOM   5027 N ND1 . HIS C 3 92  ? 3.67998   -31.10961 4.75404   1.000 186.38257 ? 92  HIS C ND1 1 
ATOM   5028 C CD2 . HIS C 3 92  ? 3.10582   -31.25990 6.85569   1.000 186.88997 ? 92  HIS C CD2 1 
ATOM   5029 C CE1 . HIS C 3 92  ? 4.23535   -30.08985 5.38424   1.000 185.59648 ? 92  HIS C CE1 1 
ATOM   5030 N NE2 . HIS C 3 92  ? 3.90216   -30.15748 6.66063   1.000 185.93349 ? 92  HIS C NE2 1 
ATOM   5031 N N   . SER C 3 93  ? -0.39767  -30.86897 5.93125   1.000 185.33875 ? 93  SER C N   1 
ATOM   5032 C CA  . SER C 3 93  ? -0.83045  -29.49419 5.72168   1.000 185.65060 ? 93  SER C CA  1 
ATOM   5033 C C   . SER C 3 93  ? -0.07501  -28.57753 6.67548   1.000 184.65076 ? 93  SER C C   1 
ATOM   5034 O O   . SER C 3 93  ? 0.10953   -28.90927 7.85084   1.000 184.63937 ? 93  SER C O   1 
ATOM   5035 C CB  . SER C 3 93  ? -2.34048  -29.34670 5.94186   1.000 187.76114 ? 93  SER C CB  1 
ATOM   5036 O OG  . SER C 3 93  ? -3.06966  -30.31798 5.21008   1.000 189.03211 ? 93  SER C OG  1 
ATOM   5037 N N   . TYR C 3 94  ? 0.35807   -27.42459 6.17074   1.000 180.44952 ? 94  TYR C N   1 
ATOM   5038 C CA  . TYR C 3 94  ? 1.14621   -26.47816 6.94616   1.000 179.69889 ? 94  TYR C CA  1 
ATOM   5039 C C   . TYR C 3 94  ? 0.43279   -25.13523 7.03298   1.000 181.27874 ? 94  TYR C C   1 
ATOM   5040 O O   . TYR C 3 94  ? -0.21570  -24.70507 6.07450   1.000 182.82086 ? 94  TYR C O   1 
ATOM   5041 C CB  . TYR C 3 94  ? 2.53954   -26.27851 6.33728   1.000 178.05243 ? 94  TYR C CB  1 
ATOM   5042 C CG  . TYR C 3 94  ? 3.28221   -25.11167 6.94323   1.000 177.60782 ? 94  TYR C CG  1 
ATOM   5043 C CD1 . TYR C 3 94  ? 3.77192   -25.17864 8.23875   1.000 177.57970 ? 94  TYR C CD1 1 
ATOM   5044 C CD2 . TYR C 3 94  ? 3.47767   -23.93705 6.22866   1.000 177.43134 ? 94  TYR C CD2 1 
ATOM   5045 C CE1 . TYR C 3 94  ? 4.43981   -24.11405 8.80409   1.000 179.88032 ? 94  TYR C CE1 1 
ATOM   5046 C CE2 . TYR C 3 94  ? 4.14916   -22.86519 6.78670   1.000 184.05553 ? 94  TYR C CE2 1 
ATOM   5047 C CZ  . TYR C 3 94  ? 4.62916   -22.96062 8.07580   1.000 185.41348 ? 94  TYR C CZ  1 
ATOM   5048 O OH  . TYR C 3 94  ? 5.29864   -21.90009 8.64252   1.000 186.70491 ? 94  TYR C OH  1 
ATOM   5049 N N   . SER C 3 95  ? 0.57011   -24.47059 8.18049   1.000 181.12261 ? 95  SER C N   1 
ATOM   5050 C CA  . SER C 3 95  ? -0.03172  -23.15638 8.38037   1.000 188.59567 ? 95  SER C CA  1 
ATOM   5051 C C   . SER C 3 95  ? 0.63315   -22.47452 9.56476   1.000 189.40221 ? 95  SER C C   1 
ATOM   5052 O O   . SER C 3 95  ? 0.63223   -23.02398 10.67106  1.000 188.78210 ? 95  SER C O   1 
ATOM   5053 C CB  . SER C 3 95  ? -1.53840  -23.27579 8.61224   1.000 195.27729 ? 95  SER C CB  1 
ATOM   5054 O OG  . SER C 3 95  ? -1.81053  -23.95829 9.82242   1.000 196.29031 ? 95  SER C OG  1 
ATOM   5055 N N   . THR C 3 96  ? 1.19848   -21.28715 9.32850   1.000 184.92684 ? 96  THR C N   1 
ATOM   5056 C CA  . THR C 3 96  ? 1.66324   -20.37625 10.37813  1.000 187.02722 ? 96  THR C CA  1 
ATOM   5057 C C   . THR C 3 96  ? 2.52885   -21.08149 11.42420  1.000 182.52959 ? 96  THR C C   1 
ATOM   5058 O O   . THR C 3 96  ? 2.29769   -20.98051 12.63178  1.000 185.03811 ? 96  THR C O   1 
ATOM   5059 C CB  . THR C 3 96  ? 0.48133   -19.66667 11.04428  1.000 195.41926 ? 96  THR C CB  1 
ATOM   5060 O OG1 . THR C 3 96  ? -0.33621  -20.62572 11.72790  1.000 196.83555 ? 96  THR C OG1 1 
ATOM   5061 C CG2 . THR C 3 96  ? -0.35957  -18.94499 10.00307  1.000 200.36053 ? 96  THR C CG2 1 
ATOM   5062 N N   . GLY C 3 97  ? 3.54733   -21.79449 10.94969  1.000 184.93109 ? 97  GLY C N   1 
ATOM   5063 C CA  . GLY C 3 97  ? 4.47357   -22.45819 11.84567  1.000 179.67972 ? 97  GLY C CA  1 
ATOM   5064 C C   . GLY C 3 97  ? 3.97607   -23.74768 12.45719  1.000 177.92106 ? 97  GLY C C   1 
ATOM   5065 O O   . GLY C 3 97  ? 4.51547   -24.18099 13.47904  1.000 178.03142 ? 97  GLY C O   1 
ATOM   5066 N N   . MET C 3 98  ? 2.96523   -24.38058 11.86520  1.000 188.02154 ? 98  MET C N   1 
ATOM   5067 C CA  . MET C 3 98  ? 2.41829   -25.63528 12.37078  1.000 185.13952 ? 98  MET C CA  1 
ATOM   5068 C C   . MET C 3 98  ? 2.39891   -26.64439 11.23190  1.000 182.09787 ? 98  MET C C   1 
ATOM   5069 O O   . MET C 3 98  ? 1.65467   -26.47475 10.26160  1.000 182.44474 ? 98  MET C O   1 
ATOM   5070 C CB  . MET C 3 98  ? 1.01572   -25.43598 12.94882  1.000 194.79302 ? 98  MET C CB  1 
ATOM   5071 C CG  . MET C 3 98  ? 0.52268   -26.58725 13.81415  1.000 194.86875 ? 98  MET C CG  1 
ATOM   5072 S SD  . MET C 3 98  ? 1.58155   -26.89208 15.24323  1.000 191.10233 ? 98  MET C SD  1 
ATOM   5073 C CE  . MET C 3 98  ? 2.34129   -28.44864 14.78460  1.000 183.96734 ? 98  MET C CE  1 
ATOM   5074 N N   . TYR C 3 99  ? 3.21459   -27.69122 11.35184  1.000 179.02755 ? 99  TYR C N   1 
ATOM   5075 C CA  . TYR C 3 99  ? 3.30199   -28.75696 10.35505  1.000 178.31906 ? 99  TYR C CA  1 
ATOM   5076 C C   . TYR C 3 99  ? 2.49349   -29.94286 10.87189  1.000 179.25511 ? 99  TYR C C   1 
ATOM   5077 O O   . TYR C 3 99  ? 2.96221   -30.70231 11.72300  1.000 179.06083 ? 99  TYR C O   1 
ATOM   5078 C CB  . TYR C 3 99  ? 4.75321   -29.15256 10.09992  1.000 176.84011 ? 99  TYR C CB  1 
ATOM   5079 C CG  . TYR C 3 99  ? 5.64179   -28.06669 9.52522   1.000 176.01578 ? 99  TYR C CG  1 
ATOM   5080 C CD1 . TYR C 3 99  ? 6.11538   -27.03141 10.32144  1.000 176.15884 ? 99  TYR C CD1 1 
ATOM   5081 C CD2 . TYR C 3 99  ? 6.03370   -28.09718 8.19297   1.000 175.30578 ? 99  TYR C CD2 1 
ATOM   5082 C CE1 . TYR C 3 99  ? 6.94161   -26.04971 9.80439   1.000 175.58037 ? 99  TYR C CE1 1 
ATOM   5083 C CE2 . TYR C 3 99  ? 6.85603   -27.11803 7.66577   1.000 174.67627 ? 99  TYR C CE2 1 
ATOM   5084 C CZ  . TYR C 3 99  ? 7.30527   -26.09617 8.47521   1.000 174.79301 ? 99  TYR C CZ  1 
ATOM   5085 O OH  . TYR C 3 99  ? 8.12460   -25.12103 7.95428   1.000 180.10791 ? 99  TYR C OH  1 
ATOM   5086 N N   . ILE C 3 100 ? 1.27962   -30.10840 10.35160  1.000 186.26204 ? 100 ILE C N   1 
ATOM   5087 C CA  . ILE C 3 100 ? 0.36476   -31.15204 10.80491  1.000 187.53201 ? 100 ILE C CA  1 
ATOM   5088 C C   . ILE C 3 100 ? 0.40815   -32.31668 9.82529   1.000 187.30362 ? 100 ILE C C   1 
ATOM   5089 O O   . ILE C 3 100 ? 0.44933   -32.11745 8.60430   1.000 187.01135 ? 100 ILE C O   1 
ATOM   5090 C CB  . ILE C 3 100 ? -1.06716  -30.60320 10.95608  1.000 192.59005 ? 100 ILE C CB  1 
ATOM   5091 C CG1 . ILE C 3 100 ? -1.05539  -29.31439 11.78158  1.000 200.84576 ? 100 ILE C CG1 1 
ATOM   5092 C CG2 . ILE C 3 100 ? -1.97136  -31.63804 11.60842  1.000 194.29059 ? 100 ILE C CG2 1 
ATOM   5093 C CD1 . ILE C 3 100 ? -2.42545  -28.72140 12.01647  1.000 208.71447 ? 100 ILE C CD1 1 
ATOM   5094 N N   . PHE C 3 101 ? 0.39466   -33.53594 10.35874  1.000 187.62778 ? 101 PHE C N   1 
ATOM   5095 C CA  . PHE C 3 101 ? 0.47880   -34.75586 9.56826   1.000 187.69143 ? 101 PHE C CA  1 
ATOM   5096 C C   . PHE C 3 101 ? -0.74890  -35.62921 9.80075   1.000 189.60150 ? 101 PHE C C   1 
ATOM   5097 O O   . PHE C 3 101 ? -1.56209  -35.38115 10.69489  1.000 195.00210 ? 101 PHE C O   1 
ATOM   5098 C CB  . PHE C 3 101 ? 1.75336   -35.54119 9.90253   1.000 186.40682 ? 101 PHE C CB  1 
ATOM   5099 C CG  . PHE C 3 101 ? 2.96628   -35.07690 9.15143   1.000 184.88050 ? 101 PHE C CG  1 
ATOM   5100 C CD1 . PHE C 3 101 ? 3.70185   -33.99069 9.59524   1.000 183.87982 ? 101 PHE C CD1 1 
ATOM   5101 C CD2 . PHE C 3 101 ? 3.37283   -35.73107 8.00066   1.000 184.71068 ? 101 PHE C CD2 1 
ATOM   5102 C CE1 . PHE C 3 101 ? 4.81916   -33.56443 8.90289   1.000 182.67812 ? 101 PHE C CE1 1 
ATOM   5103 C CE2 . PHE C 3 101 ? 4.48848   -35.31063 7.30466   1.000 183.53535 ? 101 PHE C CE2 1 
ATOM   5104 C CZ  . PHE C 3 101 ? 5.21307   -34.22611 7.75634   1.000 182.48681 ? 101 PHE C CZ  1 
ATOM   5105 N N   . GLY C 3 102 ? -0.86710  -36.67358 8.97852   1.000 197.14787 ? 102 GLY C N   1 
ATOM   5106 C CA  . GLY C 3 102 ? -1.98029  -37.59309 9.04428   1.000 199.16789 ? 102 GLY C CA  1 
ATOM   5107 C C   . GLY C 3 102 ? -1.65892  -38.85052 9.83457   1.000 199.27268 ? 102 GLY C C   1 
ATOM   5108 O O   . GLY C 3 102 ? -0.65615  -38.94403 10.54525  1.000 197.85830 ? 102 GLY C O   1 
ATOM   5109 N N   . GLY C 3 103 ? -2.54011  -39.83935 9.69368   1.000 197.87789 ? 103 GLY C N   1 
ATOM   5110 C CA  . GLY C 3 103 ? -2.43002  -41.07463 10.44566  1.000 198.37326 ? 103 GLY C CA  1 
ATOM   5111 C C   . GLY C 3 103 ? -1.53943  -42.12126 9.80830   1.000 197.81616 ? 103 GLY C C   1 
ATOM   5112 O O   . GLY C 3 103 ? -0.90926  -42.91702 10.51126  1.000 197.32969 ? 103 GLY C O   1 
ATOM   5113 N N   . GLY C 3 104 ? -1.48062  -42.13633 8.47938   1.000 197.18396 ? 104 GLY C N   1 
ATOM   5114 C CA  . GLY C 3 104 ? -0.66667  -43.10684 7.77507   1.000 197.03787 ? 104 GLY C CA  1 
ATOM   5115 C C   . GLY C 3 104 ? -1.40823  -44.38631 7.45356   1.000 199.38399 ? 104 GLY C C   1 
ATOM   5116 O O   . GLY C 3 104 ? -1.25708  -45.39338 8.15149   1.000 199.79164 ? 104 GLY C O   1 
ATOM   5117 N N   . THR C 3 105 ? -2.21397  -44.35783 6.39584   1.000 193.60956 ? 105 THR C N   1 
ATOM   5118 C CA  . THR C 3 105 ? -2.98094  -45.52617 5.98491   1.000 196.26056 ? 105 THR C CA  1 
ATOM   5119 C C   . THR C 3 105 ? -2.06318  -46.50710 5.26501   1.000 196.38911 ? 105 THR C C   1 
ATOM   5120 O O   . THR C 3 105 ? -1.40496  -46.14538 4.28349   1.000 195.71220 ? 105 THR C O   1 
ATOM   5121 C CB  . THR C 3 105 ? -4.14188  -45.11020 5.08513   1.000 198.32062 ? 105 THR C CB  1 
ATOM   5122 O OG1 . THR C 3 105 ? -4.92260  -44.10659 5.74638   1.000 198.21431 ? 105 THR C OG1 1 
ATOM   5123 C CG2 . THR C 3 105 ? -5.02630  -46.30479 4.77449   1.000 201.44501 ? 105 THR C CG2 1 
ATOM   5124 N N   . LYS C 3 106 ? -2.01836  -47.74474 5.75172   1.000 205.87144 ? 106 LYS C N   1 
ATOM   5125 C CA  . LYS C 3 106 ? -1.14067  -48.77015 5.19769   1.000 207.14692 ? 106 LYS C CA  1 
ATOM   5126 C C   . LYS C 3 106 ? -1.86597  -49.47364 4.05493   1.000 210.27990 ? 106 LYS C C   1 
ATOM   5127 O O   . LYS C 3 106 ? -2.83025  -50.21211 4.28123   1.000 215.40923 ? 106 LYS C O   1 
ATOM   5128 C CB  . LYS C 3 106 ? -0.71719  -49.75673 6.28404   1.000 209.86168 ? 106 LYS C CB  1 
ATOM   5129 C CG  . LYS C 3 106 ? 0.41535   -50.69066 5.87845   1.000 212.69094 ? 106 LYS C CG  1 
ATOM   5130 C CD  . LYS C 3 106 ? -0.10958  -51.99342 5.29650   1.000 221.64286 ? 106 LYS C CD  1 
ATOM   5131 C CE  . LYS C 3 106 ? 0.97621   -52.73731 4.53755   1.000 224.54948 ? 106 LYS C CE  1 
ATOM   5132 N NZ  . LYS C 3 106 ? 0.46795   -54.01060 3.95467   1.000 230.54122 ? 106 LYS C NZ  1 
ATOM   5133 N N   . LEU C 3 107 ? -1.39714  -49.24913 2.82977   1.000 209.30868 ? 107 LEU C N   1 
ATOM   5134 C CA  . LEU C 3 107 ? -1.97796  -49.86749 1.64573   1.000 214.47308 ? 107 LEU C CA  1 
ATOM   5135 C C   . LEU C 3 107 ? -1.34194  -51.23191 1.41198   1.000 220.43901 ? 107 LEU C C   1 
ATOM   5136 O O   . LEU C 3 107 ? -0.11402  -51.34951 1.35467   1.000 221.06541 ? 107 LEU C O   1 
ATOM   5137 C CB  . LEU C 3 107 ? -1.78203  -48.97080 0.42204   1.000 210.12315 ? 107 LEU C CB  1 
ATOM   5138 C CG  . LEU C 3 107 ? -2.22697  -49.52093 -0.93452  1.000 214.28212 ? 107 LEU C CG  1 
ATOM   5139 C CD1 . LEU C 3 107 ? -3.69638  -49.90584 -0.90513  1.000 218.01453 ? 107 LEU C CD1 1 
ATOM   5140 C CD2 . LEU C 3 107 ? -1.96127  -48.50288 -2.03243  1.000 211.77682 ? 107 LEU C CD2 1 
ATOM   5141 N N   . THR C 3 108 ? -2.17799  -52.25741 1.27780   1.000 212.14626 ? 108 THR C N   1 
ATOM   5142 C CA  . THR C 3 108 ? -1.72290  -53.62788 1.08560   1.000 217.56325 ? 108 THR C CA  1 
ATOM   5143 C C   . THR C 3 108 ? -2.04168  -54.07731 -0.33352  1.000 219.51731 ? 108 THR C C   1 
ATOM   5144 O O   . THR C 3 108 ? -3.15160  -53.85049 -0.82687  1.000 221.06501 ? 108 THR C O   1 
ATOM   5145 C CB  . THR C 3 108 ? -2.38029  -54.57291 2.09505   1.000 221.22281 ? 108 THR C CB  1 
ATOM   5146 O OG1 . THR C 3 108 ? -2.26559  -54.02444 3.41407   1.000 218.14049 ? 108 THR C OG1 1 
ATOM   5147 C CG2 . THR C 3 108 ? -1.71007  -55.93920 2.06282   1.000 227.61219 ? 108 THR C CG2 1 
ATOM   5148 N N   . VAL C 3 109 ? -1.06916  -54.70838 -0.98401  1.000 218.25642 ? 109 VAL C N   1 
ATOM   5149 C CA  . VAL C 3 109 ? -1.24574  -55.27786 -2.31466  1.000 221.73501 ? 109 VAL C CA  1 
ATOM   5150 C C   . VAL C 3 109 ? -1.39464  -56.78467 -2.16200  1.000 228.09083 ? 109 VAL C C   1 
ATOM   5151 O O   . VAL C 3 109 ? -0.46873  -57.46563 -1.70446  1.000 231.85239 ? 109 VAL C O   1 
ATOM   5152 C CB  . VAL C 3 109 ? -0.07091  -54.92554 -3.23970  1.000 220.90054 ? 109 VAL C CB  1 
ATOM   5153 C CG1 . VAL C 3 109 ? -0.21043  -55.64880 -4.57017  1.000 224.92589 ? 109 VAL C CG1 1 
ATOM   5154 C CG2 . VAL C 3 109 ? 0.00079   -53.42109 -3.45134  1.000 218.22802 ? 109 VAL C CG2 1 
ATOM   5155 N N   . LEU C 3 110 ? -2.55783  -57.30760 -2.54595  1.000 224.81791 ? 110 LEU C N   1 
ATOM   5156 C CA  . LEU C 3 110 ? -2.88172  -58.71961 -2.34518  1.000 233.09307 ? 110 LEU C CA  1 
ATOM   5157 C C   . LEU C 3 110 ? -2.48201  -59.50640 -3.58672  1.000 251.29992 ? 110 LEU C C   1 
ATOM   5158 O O   . LEU C 3 110 ? -3.26673  -59.68365 -4.51967  1.000 258.52768 ? 110 LEU C O   1 
ATOM   5159 C CB  . LEU C 3 110 ? -4.36151  -58.88898 -2.02519  1.000 235.49466 ? 110 LEU C CB  1 
ATOM   5160 C CG  . LEU C 3 110 ? -4.81731  -58.31511 -0.68287  1.000 230.00209 ? 110 LEU C CG  1 
ATOM   5161 C CD1 . LEU C 3 110 ? -6.31496  -58.49609 -0.49685  1.000 220.94516 ? 110 LEU C CD1 1 
ATOM   5162 C CD2 . LEU C 3 110 ? -4.05043  -58.96827 0.45479   1.000 228.69236 ? 110 LEU C CD2 1 
ATOM   5163 N N   . GLY C 3 111 ? -1.24063  -59.98571 -3.59552  1.000 247.01236 ? 111 GLY C N   1 
ATOM   5164 C CA  . GLY C 3 111 ? -0.78972  -60.90099 -4.62471  1.000 250.54676 ? 111 GLY C CA  1 
ATOM   5165 C C   . GLY C 3 111 ? -1.07424  -62.33424 -4.22839  1.000 253.62270 ? 111 GLY C C   1 
ATOM   5166 O O   . GLY C 3 111 ? -1.19259  -63.22109 -5.07951  1.000 257.84542 ? 111 GLY C O   1 
ATOM   5167 N N   . GLN C 3 112 ? -1.18424  -62.56306 -2.92390  1.000 267.10301 ? 112 GLN C N   1 
ATOM   5168 C CA  . GLN C 3 112 ? -1.55408  -63.83510 -2.32751  1.000 275.37826 ? 112 GLN C CA  1 
ATOM   5169 C C   . GLN C 3 112 ? -3.05471  -63.87731 -2.06922  1.000 274.27453 ? 112 GLN C C   1 
ATOM   5170 O O   . GLN C 3 112 ? -3.70569  -62.83391 -1.95780  1.000 262.23873 ? 112 GLN C O   1 
ATOM   5171 C CB  . GLN C 3 112 ? -0.78656  -64.03980 -1.02172  1.000 272.98056 ? 112 GLN C CB  1 
ATOM   5172 C CG  . GLN C 3 112 ? 0.72541   -64.07989 -1.18652  1.000 247.04177 ? 112 GLN C CG  1 
ATOM   5173 C CD  . GLN C 3 112 ? 1.19651   -65.30220 -1.94971  1.000 246.69686 ? 112 GLN C CD  1 
ATOM   5174 O OE1 . GLN C 3 112 ? 0.62206   -66.38382 -1.82687  1.000 243.00367 ? 112 GLN C OE1 1 
ATOM   5175 N NE2 . GLN C 3 112 ? 2.24474   -65.13461 -2.74798  1.000 247.97877 ? 112 GLN C NE2 1 
ATOM   5176 N N   . PRO C 3 113 ? -3.64312  -65.06687 -1.97996  1.000 253.15548 ? 113 PRO C N   1 
ATOM   5177 C CA  . PRO C 3 113 ? -5.08291  -65.16554 -1.72271  1.000 253.92642 ? 113 PRO C CA  1 
ATOM   5178 C C   . PRO C 3 113 ? -5.40661  -64.96003 -0.24736  1.000 253.22091 ? 113 PRO C C   1 
ATOM   5179 O O   . PRO C 3 113 ? -4.52759  -64.90594 0.61386   1.000 253.03061 ? 113 PRO C O   1 
ATOM   5180 C CB  . PRO C 3 113 ? -5.42076  -66.59021 -2.17023  1.000 260.31167 ? 113 PRO C CB  1 
ATOM   5181 C CG  . PRO C 3 113 ? -4.16386  -67.34854 -1.93333  1.000 263.10980 ? 113 PRO C CG  1 
ATOM   5182 C CD  . PRO C 3 113 ? -3.03740  -66.38911 -2.22528  1.000 259.00673 ? 113 PRO C CD  1 
ATOM   5183 N N   . LYS C 3 114 ? -6.70624  -64.84618 0.02825   1.000 247.84576 ? 114 LYS C N   1 
ATOM   5184 C CA  . LYS C 3 114 ? -7.17349  -64.68217 1.39887   1.000 247.41841 ? 114 LYS C CA  1 
ATOM   5185 C C   . LYS C 3 114 ? -6.74880  -65.86787 2.25740   1.000 252.58234 ? 114 LYS C C   1 
ATOM   5186 O O   . LYS C 3 114 ? -6.63986  -67.00234 1.78363   1.000 257.72548 ? 114 LYS C O   1 
ATOM   5187 C CB  . LYS C 3 114 ? -8.69567  -64.53144 1.43553   1.000 247.56948 ? 114 LYS C CB  1 
ATOM   5188 C CG  . LYS C 3 114 ? -9.19895  -63.13122 1.11910   1.000 241.80851 ? 114 LYS C CG  1 
ATOM   5189 C CD  . LYS C 3 114 ? -10.68783 -63.00736 1.41334   1.000 242.29180 ? 114 LYS C CD  1 
ATOM   5190 C CE  . LYS C 3 114 ? -11.17399 -61.57595 1.25411   1.000 236.25609 ? 114 LYS C CE  1 
ATOM   5191 N NZ  . LYS C 3 114 ? -12.61518 -61.44107 1.60279   1.000 237.18643 ? 114 LYS C NZ  1 
ATOM   5192 N N   . SER C 3 115 ? -6.51198  -65.59497 3.53877   1.000 242.95253 ? 115 SER C N   1 
ATOM   5193 C CA  . SER C 3 115 ? -5.99219  -66.60674 4.44810   1.000 247.69510 ? 115 SER C CA  1 
ATOM   5194 C C   . SER C 3 115 ? -6.40121  -66.27525 5.87425   1.000 246.24674 ? 115 SER C C   1 
ATOM   5195 O O   . SER C 3 115 ? -6.17772  -65.15496 6.34160   1.000 241.28235 ? 115 SER C O   1 
ATOM   5196 C CB  . SER C 3 115 ? -4.46627  -66.69896 4.34526   1.000 248.16731 ? 115 SER C CB  1 
ATOM   5197 O OG  . SER C 3 115 ? -3.93789  -67.53759 5.35700   1.000 252.05937 ? 115 SER C OG  1 
ATOM   5198 N N   . THR C 3 116 ? -7.00235  -67.26439 6.56665   1.000 238.25602 ? 116 THR C N   1 
ATOM   5199 C CA  . THR C 3 116 ? -7.34509  -67.17530 7.97747   1.000 236.74060 ? 116 THR C CA  1 
ATOM   5200 C C   . THR C 3 116 ? -6.16618  -67.62193 8.83906   1.000 237.62890 ? 116 THR C C   1 
ATOM   5201 O O   . THR C 3 116 ? -5.35242  -68.44675 8.41025   1.000 242.00738 ? 116 THR C O   1 
ATOM   5202 C CB  . THR C 3 116 ? -8.56725  -68.03884 8.28787   1.000 240.92313 ? 116 THR C CB  1 
ATOM   5203 O OG1 . THR C 3 116 ? -8.42467  -69.32074 7.66327   1.000 245.71287 ? 116 THR C OG1 1 
ATOM   5204 C CG2 . THR C 3 116 ? -9.83821  -67.36724 7.78439   1.000 242.98995 ? 116 THR C CG2 1 
ATOM   5205 N N   . PRO C 3 117 ? -6.03988  -67.08983 10.05383  1.000 241.26890 ? 117 PRO C N   1 
ATOM   5206 C CA  . PRO C 3 117 ? -4.87872  -67.42430 10.88539  1.000 242.64423 ? 117 PRO C CA  1 
ATOM   5207 C C   . PRO C 3 117 ? -5.04340  -68.75461 11.60445  1.000 248.26621 ? 117 PRO C C   1 
ATOM   5208 O O   . PRO C 3 117 ? -6.13514  -69.11650 12.05062  1.000 248.68352 ? 117 PRO C O   1 
ATOM   5209 C CB  . PRO C 3 117 ? -4.82367  -66.26325 11.88371  1.000 235.00870 ? 117 PRO C CB  1 
ATOM   5210 C CG  . PRO C 3 117 ? -6.24536  -65.85086 12.03306  1.000 231.40454 ? 117 PRO C CG  1 
ATOM   5211 C CD  . PRO C 3 117 ? -6.89600  -66.07027 10.68779  1.000 235.22875 ? 117 PRO C CD  1 
ATOM   5212 N N   . THR C 3 118 ? -3.93364  -69.48039 11.71963  1.000 236.22554 ? 118 THR C N   1 
ATOM   5213 C CA  . THR C 3 118 ? -3.87743  -70.73191 12.46466  1.000 241.03996 ? 118 THR C CA  1 
ATOM   5214 C C   . THR C 3 118 ? -3.33358  -70.44443 13.85921  1.000 238.38431 ? 118 THR C C   1 
ATOM   5215 O O   . THR C 3 118 ? -2.20660  -69.95763 14.00137  1.000 236.95373 ? 118 THR C O   1 
ATOM   5216 C CB  . THR C 3 118 ? -3.00318  -71.75950 11.74583  1.000 246.69885 ? 118 THR C CB  1 
ATOM   5217 O OG1 . THR C 3 118 ? -3.58116  -72.07340 10.47246  1.000 248.65478 ? 118 THR C OG1 1 
ATOM   5218 C CG2 . THR C 3 118 ? -2.88523  -73.03106 12.57209  1.000 251.53363 ? 118 THR C CG2 1 
ATOM   5219 N N   . LEU C 3 119 ? -4.12960  -70.74484 14.87944  1.000 232.97434 ? 119 LEU C N   1 
ATOM   5220 C CA  . LEU C 3 119 ? -3.79880  -70.40777 16.25571  1.000 230.29801 ? 119 LEU C CA  1 
ATOM   5221 C C   . LEU C 3 119 ? -3.16921  -71.59449 16.97890  1.000 230.94695 ? 119 LEU C C   1 
ATOM   5222 O O   . LEU C 3 119 ? -3.32823  -72.75341 16.58741  1.000 234.08914 ? 119 LEU C O   1 
ATOM   5223 C CB  . LEU C 3 119 ? -5.04380  -69.93155 17.01153  1.000 231.02749 ? 119 LEU C CB  1 
ATOM   5224 C CG  . LEU C 3 119 ? -5.45796  -68.46537 16.83683  1.000 229.09520 ? 119 LEU C CG  1 
ATOM   5225 C CD1 . LEU C 3 119 ? -5.94195  -68.16620 15.42199  1.000 230.66688 ? 119 LEU C CD1 1 
ATOM   5226 C CD2 . LEU C 3 119 ? -6.52086  -68.09002 17.85630  1.000 229.77491 ? 119 LEU C CD2 1 
ATOM   5227 N N   . THR C 3 120 ? -2.44471  -71.28057 18.05271  1.000 235.78111 ? 120 THR C N   1 
ATOM   5228 C CA  . THR C 3 120 ? -1.73995  -72.28159 18.84502  1.000 239.01297 ? 120 THR C CA  1 
ATOM   5229 C C   . THR C 3 120 ? -1.54666  -71.72861 20.24892  1.000 233.91270 ? 120 THR C C   1 
ATOM   5230 O O   . THR C 3 120 ? -1.07238  -70.59995 20.40840  1.000 229.42631 ? 120 THR C O   1 
ATOM   5231 C CB  . THR C 3 120 ? -0.38706  -72.63600 18.21365  1.000 242.98552 ? 120 THR C CB  1 
ATOM   5232 O OG1 . THR C 3 120 ? -0.59865  -73.25918 16.94031  1.000 247.96936 ? 120 THR C OG1 1 
ATOM   5233 C CG2 . THR C 3 120 ? 0.39608   -73.58075 19.11257  1.000 245.90854 ? 120 THR C CG2 1 
ATOM   5234 N N   . MET C 3 121 ? -1.90995  -72.51785 21.25748  1.000 247.84723 ? 121 MET C N   1 
ATOM   5235 C CA  . MET C 3 121 ? -1.90736  -72.06714 22.64096  1.000 243.30053 ? 121 MET C CA  1 
ATOM   5236 C C   . MET C 3 121 ? -0.90823  -72.86334 23.47090  1.000 245.40940 ? 121 MET C C   1 
ATOM   5237 O O   . MET C 3 121 ? -0.63272  -74.03422 23.19135  1.000 250.59361 ? 121 MET C O   1 
ATOM   5238 C CB  . MET C 3 121 ? -3.30496  -72.18342 23.25799  1.000 241.61506 ? 121 MET C CB  1 
ATOM   5239 C CG  . MET C 3 121 ? -4.32185  -71.22124 22.66754  1.000 238.48350 ? 121 MET C CG  1 
ATOM   5240 S SD  . MET C 3 121 ? -3.81048  -69.50061 22.83857  1.000 232.13759 ? 121 MET C SD  1 
ATOM   5241 C CE  . MET C 3 121 ? -3.60595  -69.38449 24.61442  1.000 229.37582 ? 121 MET C CE  1 
ATOM   5242 N N   . PHE C 3 122 ? -0.37580  -72.21040 24.50937  1.000 235.51180 ? 122 PHE C N   1 
ATOM   5243 C CA  . PHE C 3 122 ? 0.62810   -72.79251 25.39266  1.000 236.64708 ? 122 PHE C CA  1 
ATOM   5244 C C   . PHE C 3 122 ? 0.39718   -72.31361 26.82317  1.000 231.95036 ? 122 PHE C C   1 
ATOM   5245 O O   . PHE C 3 122 ? 0.26786   -71.09699 27.05370  1.000 227.23655 ? 122 PHE C O   1 
ATOM   5246 C CB  . PHE C 3 122 ? 2.04031   -72.42295 24.93174  1.000 237.33490 ? 122 PHE C CB  1 
ATOM   5247 C CG  . PHE C 3 122 ? 2.63449   -73.39408 23.95395  1.000 243.86788 ? 122 PHE C CG  1 
ATOM   5248 C CD1 . PHE C 3 122 ? 2.59124   -74.75643 24.19768  1.000 248.69824 ? 122 PHE C CD1 1 
ATOM   5249 C CD2 . PHE C 3 122 ? 3.23550   -72.94485 22.79002  1.000 245.43395 ? 122 PHE C CD2 1 
ATOM   5250 C CE1 . PHE C 3 122 ? 3.14101   -75.65192 23.30113  1.000 255.22754 ? 122 PHE C CE1 1 
ATOM   5251 C CE2 . PHE C 3 122 ? 3.78489   -73.83576 21.88862  1.000 252.02698 ? 122 PHE C CE2 1 
ATOM   5252 C CZ  . PHE C 3 122 ? 3.73764   -75.19074 22.14488  1.000 257.00723 ? 122 PHE C CZ  1 
ATOM   5253 N N   . PRO C 3 123 ? 0.33847   -73.22163 27.79361  1.000 236.54674 ? 123 PRO C N   1 
ATOM   5254 C CA  . PRO C 3 123 ? 0.16905   -72.81340 29.19142  1.000 232.65433 ? 123 PRO C CA  1 
ATOM   5255 C C   . PRO C 3 123 ? 1.51391   -72.60053 29.86392  1.000 231.42641 ? 123 PRO C C   1 
ATOM   5256 O O   . PRO C 3 123 ? 2.55206   -73.02778 29.33628  1.000 234.26606 ? 123 PRO C O   1 
ATOM   5257 C CB  . PRO C 3 123 ? -0.58239  -74.00211 29.80500  1.000 235.03494 ? 123 PRO C CB  1 
ATOM   5258 C CG  . PRO C 3 123 ? -0.06911  -75.17424 29.03483  1.000 240.32180 ? 123 PRO C CG  1 
ATOM   5259 C CD  . PRO C 3 123 ? 0.23372   -74.68313 27.63163  1.000 241.94490 ? 123 PRO C CD  1 
ATOM   5260 N N   . PRO C 3 124 ? 1.54117   -71.94364 31.02734  1.000 234.03838 ? 124 PRO C N   1 
ATOM   5261 C CA  . PRO C 3 124 ? 2.82136   -71.69527 31.70347  1.000 232.75648 ? 124 PRO C CA  1 
ATOM   5262 C C   . PRO C 3 124 ? 3.54804   -72.98537 32.05655  1.000 236.45509 ? 124 PRO C C   1 
ATOM   5263 O O   . PRO C 3 124 ? 2.93573   -74.02322 32.31740  1.000 238.91835 ? 124 PRO C O   1 
ATOM   5264 C CB  . PRO C 3 124 ? 2.41214   -70.92554 32.96479  1.000 228.93495 ? 124 PRO C CB  1 
ATOM   5265 C CG  . PRO C 3 124 ? 1.11909   -70.28322 32.60579  1.000 227.42263 ? 124 PRO C CG  1 
ATOM   5266 C CD  . PRO C 3 124 ? 0.42363   -71.26394 31.70619  1.000 231.05384 ? 124 PRO C CD  1 
ATOM   5267 N N   . SER C 3 125 ? 4.87908   -72.90177 32.06575  1.000 235.85407 ? 125 SER C N   1 
ATOM   5268 C CA  . SER C 3 125 ? 5.74327   -74.03298 32.35796  1.000 239.33201 ? 125 SER C CA  1 
ATOM   5269 C C   . SER C 3 125 ? 5.82517   -74.27536 33.86490  1.000 237.36825 ? 125 SER C C   1 
ATOM   5270 O O   . SER C 3 125 ? 5.64637   -73.34761 34.65833  1.000 233.59142 ? 125 SER C O   1 
ATOM   5271 C CB  . SER C 3 125 ? 7.14045   -73.78612 31.79907  1.000 240.73431 ? 125 SER C CB  1 
ATOM   5272 O OG  . SER C 3 125 ? 7.09762   -73.56624 30.40000  1.000 242.85877 ? 125 SER C OG  1 
ATOM   5273 N N   . PRO C 3 126 ? 6.09355   -75.51940 34.28208  1.000 240.25864 ? 126 PRO C N   1 
ATOM   5274 C CA  . PRO C 3 126 ? 6.17028   -75.80100 35.72745  1.000 238.44097 ? 126 PRO C CA  1 
ATOM   5275 C C   . PRO C 3 126 ? 7.21072   -74.96696 36.45551  1.000 235.71557 ? 126 PRO C C   1 
ATOM   5276 O O   . PRO C 3 126 ? 6.97454   -74.55483 37.59831  1.000 233.09851 ? 126 PRO C O   1 
ATOM   5277 C CB  . PRO C 3 126 ? 6.50988   -77.29898 35.77163  1.000 241.98570 ? 126 PRO C CB  1 
ATOM   5278 C CG  . PRO C 3 126 ? 6.02484   -77.83813 34.47256  1.000 245.70068 ? 126 PRO C CG  1 
ATOM   5279 C CD  . PRO C 3 126 ? 6.23622   -76.74158 33.47184  1.000 245.22154 ? 126 PRO C CD  1 
ATOM   5280 N N   . GLU C 3 127 ? 8.35521   -74.70168 35.82158  1.000 242.45491 ? 127 GLU C N   1 
ATOM   5281 C CA  . GLU C 3 127 ? 9.41155   -73.93406 36.47369  1.000 240.23736 ? 127 GLU C CA  1 
ATOM   5282 C C   . GLU C 3 127 ? 8.97520   -72.50397 36.76587  1.000 235.92664 ? 127 GLU C C   1 
ATOM   5283 O O   . GLU C 3 127 ? 9.36475   -71.93821 37.79338  1.000 233.34520 ? 127 GLU C O   1 
ATOM   5284 C CB  . GLU C 3 127 ? 10.67365  -73.93743 35.60798  1.000 242.68360 ? 127 GLU C CB  1 
ATOM   5285 C CG  . GLU C 3 127 ? 11.14980  -75.32215 35.18451  1.000 247.56829 ? 127 GLU C CG  1 
ATOM   5286 C CD  . GLU C 3 127 ? 10.38211  -75.86021 33.99363  1.000 250.87430 ? 127 GLU C CD  1 
ATOM   5287 O OE1 . GLU C 3 127 ? 9.68303   -75.06388 33.33203  1.000 249.49526 ? 127 GLU C OE1 1 
ATOM   5288 O OE2 . GLU C 3 127 ? 10.47163  -77.07542 33.72340  1.000 254.75751 ? 127 GLU C OE2 1 
ATOM   5289 N N   . GLU C 3 128 ? 8.16891   -71.90591 35.88447  1.000 242.21134 ? 128 GLU C N   1 
ATOM   5290 C CA  . GLU C 3 128 ? 7.64215   -70.57538 36.16204  1.000 238.14504 ? 128 GLU C CA  1 
ATOM   5291 C C   . GLU C 3 128 ? 6.64405   -70.60247 37.31029  1.000 236.87622 ? 128 GLU C C   1 
ATOM   5292 O O   . GLU C 3 128 ? 6.52672   -69.61843 38.04831  1.000 233.89695 ? 128 GLU C O   1 
ATOM   5293 C CB  . GLU C 3 128 ? 6.99092   -69.99271 34.90868  1.000 237.59639 ? 128 GLU C CB  1 
ATOM   5294 C CG  . GLU C 3 128 ? 6.64335   -68.51384 35.02603  1.000 233.38516 ? 128 GLU C CG  1 
ATOM   5295 C CD  . GLU C 3 128 ? 5.66560   -68.05859 33.96277  1.000 232.64450 ? 128 GLU C CD  1 
ATOM   5296 O OE1 . GLU C 3 128 ? 4.99001   -68.92310 33.36527  1.000 235.42674 ? 128 GLU C OE1 1 
ATOM   5297 O OE2 . GLU C 3 128 ? 5.57062   -66.83600 33.72691  1.000 229.04053 ? 128 GLU C OE2 1 
ATOM   5298 N N   . LEU C 3 129 ? 5.91342   -71.70992 37.47028  1.000 237.37914 ? 129 LEU C N   1 
ATOM   5299 C CA  . LEU C 3 129 ? 4.98929   -71.83101 38.59224  1.000 236.87918 ? 129 LEU C CA  1 
ATOM   5300 C C   . LEU C 3 129 ? 5.72769   -71.81918 39.92328  1.000 236.12434 ? 129 LEU C C   1 
ATOM   5301 O O   . LEU C 3 129 ? 5.19299   -71.33117 40.92567  1.000 234.99809 ? 129 LEU C O   1 
ATOM   5302 C CB  . LEU C 3 129 ? 4.16384   -73.11154 38.45979  1.000 239.73369 ? 129 LEU C CB  1 
ATOM   5303 C CG  . LEU C 3 129 ? 3.60557   -73.45991 37.07767  1.000 241.66773 ? 129 LEU C CG  1 
ATOM   5304 C CD1 . LEU C 3 129 ? 2.82826   -74.76781 37.12720  1.000 244.44814 ? 129 LEU C CD1 1 
ATOM   5305 C CD2 . LEU C 3 129 ? 2.74190   -72.33518 36.52386  1.000 239.34629 ? 129 LEU C CD2 1 
ATOM   5306 N N   . GLN C 3 130 ? 6.95318   -72.35109 39.95327  1.000 240.78640 ? 130 GLN C N   1 
ATOM   5307 C CA  . GLN C 3 130 ? 7.73962   -72.33445 41.18201  1.000 240.09533 ? 130 GLN C CA  1 
ATOM   5308 C C   . GLN C 3 130 ? 8.07848   -70.91222 41.60826  1.000 236.94085 ? 130 GLN C C   1 
ATOM   5309 O O   . GLN C 3 130 ? 8.19286   -70.63317 42.80714  1.000 235.98038 ? 130 GLN C O   1 
ATOM   5310 C CB  . GLN C 3 130 ? 9.02499   -73.14412 40.99743  1.000 241.99075 ? 130 GLN C CB  1 
ATOM   5311 C CG  . GLN C 3 130 ? 8.89080   -74.36310 40.09352  1.000 245.17785 ? 130 GLN C CG  1 
ATOM   5312 C CD  . GLN C 3 130 ? 8.08720   -75.48684 40.72006  1.000 246.48028 ? 130 GLN C CD  1 
ATOM   5313 O OE1 . GLN C 3 130 ? 8.16632   -75.72653 41.92463  1.000 247.35480 ? 130 GLN C OE1 1 
ATOM   5314 N NE2 . GLN C 3 130 ? 7.30853   -76.18509 39.90053  1.000 246.65974 ? 130 GLN C NE2 1 
ATOM   5315 N N   . GLU C 3 131 ? 8.23947   -70.00434 40.64738  1.000 243.27340 ? 131 GLU C N   1 
ATOM   5316 C CA  . GLU C 3 131 ? 8.62691   -68.62547 40.91305  1.000 240.05879 ? 131 GLU C CA  1 
ATOM   5317 C C   . GLU C 3 131 ? 7.44430   -67.71753 41.21583  1.000 238.25169 ? 131 GLU C C   1 
ATOM   5318 O O   . GLU C 3 131 ? 7.63436   -66.50301 41.34420  1.000 235.60823 ? 131 GLU C O   1 
ATOM   5319 C CB  . GLU C 3 131 ? 9.40618   -68.05599 39.72650  1.000 239.19702 ? 131 GLU C CB  1 
ATOM   5320 C CG  . GLU C 3 131 ? 10.84766  -68.51576 39.63654  1.000 240.67414 ? 131 GLU C CG  1 
ATOM   5321 C CD  . GLU C 3 131 ? 11.62477  -67.75799 38.57879  1.000 239.80404 ? 131 GLU C CD  1 
ATOM   5322 O OE1 . GLU C 3 131 ? 11.01269  -67.35910 37.56533  1.000 239.18432 ? 131 GLU C OE1 1 
ATOM   5323 O OE2 . GLU C 3 131 ? 12.84200  -67.54889 38.76595  1.000 239.83538 ? 131 GLU C OE2 1 
ATOM   5324 N N   . ASN C 3 132 ? 6.23700   -68.27292 41.32380  1.000 241.87359 ? 132 ASN C N   1 
ATOM   5325 C CA  . ASN C 3 132 ? 5.01856   -67.50249 41.56761  1.000 241.01100 ? 132 ASN C CA  1 
ATOM   5326 C C   . ASN C 3 132 ? 4.77915   -66.48428 40.44936  1.000 238.79575 ? 132 ASN C C   1 
ATOM   5327 O O   . ASN C 3 132 ? 4.70380   -65.27453 40.67295  1.000 236.47608 ? 132 ASN C O   1 
ATOM   5328 C CB  . ASN C 3 132 ? 5.05993   -66.82365 42.94156  1.000 240.19829 ? 132 ASN C CB  1 
ATOM   5329 C CG  . ASN C 3 132 ? 5.04754   -67.81979 44.08221  1.000 242.53817 ? 132 ASN C CG  1 
ATOM   5330 O OD1 . ASN C 3 132 ? 4.42186   -68.87628 43.99114  1.000 244.88517 ? 132 ASN C OD1 1 
ATOM   5331 N ND2 . ASN C 3 132 ? 5.74124   -67.48906 45.16511  1.000 241.90348 ? 132 ASN C ND2 1 
ATOM   5332 N N   . LYS C 3 133 ? 4.65303   -67.00577 39.23018  1.000 236.57664 ? 133 LYS C N   1 
ATOM   5333 C CA  . LYS C 3 133 ? 4.44787   -66.18299 38.04553  1.000 234.55072 ? 133 LYS C CA  1 
ATOM   5334 C C   . LYS C 3 133 ? 3.82705   -67.04784 36.95695  1.000 236.94384 ? 133 LYS C C   1 
ATOM   5335 O O   . LYS C 3 133 ? 4.01789   -68.26649 36.93390  1.000 239.91146 ? 133 LYS C O   1 
ATOM   5336 C CB  . LYS C 3 133 ? 5.76781   -65.56394 37.56361  1.000 232.68504 ? 133 LYS C CB  1 
ATOM   5337 C CG  . LYS C 3 133 ? 5.64064   -64.59174 36.39654  1.000 229.75915 ? 133 LYS C CG  1 
ATOM   5338 C CD  . LYS C 3 133 ? 4.81185   -63.37286 36.77053  1.000 228.53682 ? 133 LYS C CD  1 
ATOM   5339 C CE  . LYS C 3 133 ? 4.63257   -62.43598 35.58508  1.000 225.79903 ? 133 LYS C CE  1 
ATOM   5340 N NZ  . LYS C 3 133 ? 5.93061   -61.89595 35.09897  1.000 224.11342 ? 133 LYS C NZ  1 
ATOM   5341 N N   . ALA C 3 134 ? 3.07500   -66.40776 36.06263  1.000 233.15757 ? 134 ALA C N   1 
ATOM   5342 C CA  . ALA C 3 134 ? 2.45386   -67.10813 34.94812  1.000 234.92659 ? 134 ALA C CA  1 
ATOM   5343 C C   . ALA C 3 134 ? 2.37208   -66.17369 33.74947  1.000 232.54705 ? 134 ALA C C   1 
ATOM   5344 O O   . ALA C 3 134 ? 2.26678   -64.95343 33.90107  1.000 228.60167 ? 134 ALA C O   1 
ATOM   5345 C CB  . ALA C 3 134 ? 1.06100   -67.63279 35.31665  1.000 235.16959 ? 134 ALA C CB  1 
ATOM   5346 N N   . THR C 3 135 ? 2.43095   -66.76002 32.55416  1.000 227.70702 ? 135 THR C N   1 
ATOM   5347 C CA  . THR C 3 135 ? 2.35546   -65.99552 31.31487  1.000 226.01039 ? 135 THR C CA  1 
ATOM   5348 C C   . THR C 3 135 ? 1.81495   -66.88959 30.20779  1.000 229.26629 ? 135 THR C C   1 
ATOM   5349 O O   . THR C 3 135 ? 2.34857   -67.97824 29.97643  1.000 233.43194 ? 135 THR C O   1 
ATOM   5350 C CB  . THR C 3 135 ? 3.72674   -65.42981 30.91862  1.000 224.91602 ? 135 THR C CB  1 
ATOM   5351 O OG1 . THR C 3 135 ? 4.20838   -64.56308 31.95324  1.000 221.64038 ? 135 THR C OG1 1 
ATOM   5352 C CG2 . THR C 3 135 ? 3.62667   -64.64030 29.61881  1.000 223.26158 ? 135 THR C CG2 1 
ATOM   5353 N N   . LEU C 3 136 ? 0.76660   -66.42995 29.52819  1.000 219.60334 ? 136 LEU C N   1 
ATOM   5354 C CA  . LEU C 3 136 ? 0.14554   -67.17878 28.44473  1.000 221.33363 ? 136 LEU C CA  1 
ATOM   5355 C C   . LEU C 3 136 ? 0.68649   -66.73139 27.09080  1.000 219.84429 ? 136 LEU C C   1 
ATOM   5356 O O   . LEU C 3 136 ? 1.16660   -65.60800 26.92371  1.000 217.64426 ? 136 LEU C O   1 
ATOM   5357 C CB  . LEU C 3 136 ? -1.37811  -67.02883 28.47381  1.000 223.55563 ? 136 LEU C CB  1 
ATOM   5358 C CG  . LEU C 3 136 ? -2.12491  -68.00638 29.38213  1.000 226.24541 ? 136 LEU C CG  1 
ATOM   5359 C CD1 . LEU C 3 136 ? -3.60417  -68.02040 29.03963  1.000 228.86952 ? 136 LEU C CD1 1 
ATOM   5360 C CD2 . LEU C 3 136 ? -1.53374  -69.40133 29.26553  1.000 227.17523 ? 136 LEU C CD2 1 
ATOM   5361 N N   . VAL C 3 137 ? 0.59459   -67.63563 26.11618  1.000 223.19786 ? 137 VAL C N   1 
ATOM   5362 C CA  . VAL C 3 137 ? 1.18917   -67.45431 24.79656  1.000 222.25181 ? 137 VAL C CA  1 
ATOM   5363 C C   . VAL C 3 137 ? 0.13595   -67.75370 23.73789  1.000 224.50074 ? 137 VAL C C   1 
ATOM   5364 O O   . VAL C 3 137 ? -0.47129  -68.83011 23.74846  1.000 227.15896 ? 137 VAL C O   1 
ATOM   5365 C CB  . VAL C 3 137 ? 2.41947   -68.36265 24.60136  1.000 221.99517 ? 137 VAL C CB  1 
ATOM   5366 C CG1 . VAL C 3 137 ? 3.00459   -68.17891 23.20969  1.000 221.35278 ? 137 VAL C CG1 1 
ATOM   5367 C CG2 . VAL C 3 137 ? 3.46646   -68.08647 25.67247  1.000 220.02672 ? 137 VAL C CG2 1 
ATOM   5368 N N   . CYS C 3 138 ? -0.07665  -66.80719 22.82484  1.000 221.56631 ? 138 CYS C N   1 
ATOM   5369 C CA  . CYS C 3 138 ? -0.96923  -66.98998 21.68491  1.000 228.39732 ? 138 CYS C CA  1 
ATOM   5370 C C   . CYS C 3 138 ? -0.13843  -66.88101 20.41352  1.000 231.95621 ? 138 CYS C C   1 
ATOM   5371 O O   . CYS C 3 138 ? 0.51536   -65.85802 20.18194  1.000 222.57886 ? 138 CYS C O   1 
ATOM   5372 C CB  . CYS C 3 138 ? -2.10550  -65.96001 21.69747  1.000 221.30549 ? 138 CYS C CB  1 
ATOM   5373 S SG  . CYS C 3 138 ? -3.46888  -66.28647 20.53766  1.000 223.11635 ? 138 CYS C SG  1 
ATOM   5374 N N   . LEU C 3 139 ? -0.15363  -67.93680 19.60132  1.000 225.15002 ? 139 LEU C N   1 
ATOM   5375 C CA  . LEU C 3 139 ? 0.67117   -68.03083 18.39712  1.000 227.61829 ? 139 LEU C CA  1 
ATOM   5376 C C   . LEU C 3 139 ? -0.22652  -67.90055 17.16996  1.000 229.15272 ? 139 LEU C C   1 
ATOM   5377 O O   . LEU C 3 139 ? -0.95176  -68.83477 16.81697  1.000 234.56112 ? 139 LEU C O   1 
ATOM   5378 C CB  . LEU C 3 139 ? 1.45068   -69.34313 18.37445  1.000 235.29428 ? 139 LEU C CB  1 
ATOM   5379 C CG  . LEU C 3 139 ? 2.52740   -69.53387 19.44451  1.000 235.29127 ? 139 LEU C CG  1 
ATOM   5380 C CD1 . LEU C 3 139 ? 3.24862   -70.85918 19.24820  1.000 242.69852 ? 139 LEU C CD1 1 
ATOM   5381 C CD2 . LEU C 3 139 ? 3.51306   -68.37722 19.42606  1.000 229.89404 ? 139 LEU C CD2 1 
ATOM   5382 N N   . ILE C 3 140 ? -0.16411  -66.74410 16.51693  1.000 234.41622 ? 140 ILE C N   1 
ATOM   5383 C CA  . ILE C 3 140 ? -0.93179  -66.46925 15.30765  1.000 234.19924 ? 140 ILE C CA  1 
ATOM   5384 C C   . ILE C 3 140 ? 0.01295   -66.59289 14.11927  1.000 238.24557 ? 140 ILE C C   1 
ATOM   5385 O O   . ILE C 3 140 ? 0.99836   -65.85217 14.02112  1.000 236.95186 ? 140 ILE C O   1 
ATOM   5386 C CB  . ILE C 3 140 ? -1.58119  -65.07701 15.36010  1.000 220.91409 ? 140 ILE C CB  1 
ATOM   5387 C CG1 . ILE C 3 140 ? -2.23260  -64.83409 16.72396  1.000 208.83541 ? 140 ILE C CG1 1 
ATOM   5388 C CG2 . ILE C 3 140 ? -2.61541  -64.93049 14.26632  1.000 228.23159 ? 140 ILE C CG2 1 
ATOM   5389 C CD1 . ILE C 3 140 ? -1.41515  -63.95450 17.64900  1.000 201.89551 ? 140 ILE C CD1 1 
ATOM   5390 N N   . SER C 3 141 ? -0.27949  -67.52186 13.21204  1.000 236.97722 ? 141 SER C N   1 
ATOM   5391 C CA  . SER C 3 141 ? 0.64062   -67.85069 12.13432  1.000 240.53222 ? 141 SER C CA  1 
ATOM   5392 C C   . SER C 3 141 ? -0.09278  -67.95383 10.80319  1.000 241.11443 ? 141 SER C C   1 
ATOM   5393 O O   . SER C 3 141 ? -1.31232  -68.13464 10.75077  1.000 240.76013 ? 141 SER C O   1 
ATOM   5394 C CB  . SER C 3 141 ? 1.38345   -69.16308 12.42544  1.000 246.77315 ? 141 SER C CB  1 
ATOM   5395 O OG  . SER C 3 141 ? 0.48164   -70.18001 12.82752  1.000 250.15453 ? 141 SER C OG  1 
ATOM   5396 N N   . ASN C 3 142 ? 0.69090   -67.83867 9.73117   1.000 250.99722 ? 142 ASN C N   1 
ATOM   5397 C CA  . ASN C 3 142 ? 0.26108   -68.00773 8.33827   1.000 251.43304 ? 142 ASN C CA  1 
ATOM   5398 C C   . ASN C 3 142 ? -1.09209  -67.34920 8.06265   1.000 247.61290 ? 142 ASN C C   1 
ATOM   5399 O O   . ASN C 3 142 ? -2.06909  -67.99213 7.67763   1.000 249.79971 ? 142 ASN C O   1 
ATOM   5400 C CB  . ASN C 3 142 ? 0.24728   -69.48718 7.93951   1.000 257.68179 ? 142 ASN C CB  1 
ATOM   5401 C CG  . ASN C 3 142 ? -0.58830  -70.34624 8.87075   1.000 261.03871 ? 142 ASN C CG  1 
ATOM   5402 O OD1 . ASN C 3 142 ? -0.06205  -70.98715 9.78066   1.000 264.02303 ? 142 ASN C OD1 1 
ATOM   5403 N ND2 . ASN C 3 142 ? -1.89734  -70.36174 8.64821   1.000 260.49607 ? 142 ASN C ND2 1 
ATOM   5404 N N   . PHE C 3 143 ? -1.12516  -66.03244 8.25062   1.000 251.80653 ? 143 PHE C N   1 
ATOM   5405 C CA  . PHE C 3 143 ? -2.29033  -65.22453 7.92598   1.000 247.52885 ? 143 PHE C CA  1 
ATOM   5406 C C   . PHE C 3 143 ? -1.89078  -64.09817 6.98221   1.000 242.38355 ? 143 PHE C C   1 
ATOM   5407 O O   . PHE C 3 143 ? -0.76819  -63.58666 7.03893   1.000 240.66703 ? 143 PHE C O   1 
ATOM   5408 C CB  . PHE C 3 143 ? -2.94829  -64.64613 9.18798   1.000 244.00881 ? 143 PHE C CB  1 
ATOM   5409 C CG  . PHE C 3 143 ? -2.02504  -63.81414 10.03329  1.000 239.36166 ? 143 PHE C CG  1 
ATOM   5410 C CD1 . PHE C 3 143 ? -1.26639  -64.39928 11.03192  1.000 242.07975 ? 143 PHE C CD1 1 
ATOM   5411 C CD2 . PHE C 3 143 ? -1.92623  -62.44543 9.83913   1.000 231.89380 ? 143 PHE C CD2 1 
ATOM   5412 C CE1 . PHE C 3 143 ? -0.42305  -63.63849 11.81588  1.000 238.26456 ? 143 PHE C CE1 1 
ATOM   5413 C CE2 . PHE C 3 143 ? -1.08109  -61.67933 10.61964  1.000 227.04559 ? 143 PHE C CE2 1 
ATOM   5414 C CZ  . PHE C 3 143 ? -0.32795  -62.27747 11.60870  1.000 230.05075 ? 143 PHE C CZ  1 
ATOM   5415 N N   . SER C 3 144 ? -2.82519  -63.71765 6.11086   1.000 234.31808 ? 144 SER C N   1 
ATOM   5416 C CA  . SER C 3 144 ? -2.59839  -62.66979 5.12307   1.000 233.12475 ? 144 SER C CA  1 
ATOM   5417 C C   . SER C 3 144 ? -3.92708  -62.19025 4.55036   1.000 235.23411 ? 144 SER C C   1 
ATOM   5418 O O   . SER C 3 144 ? -4.78264  -63.01395 4.20198   1.000 239.05218 ? 144 SER C O   1 
ATOM   5419 C CB  . SER C 3 144 ? -1.68990  -63.17390 4.00110   1.000 234.36208 ? 144 SER C CB  1 
ATOM   5420 O OG  . SER C 3 144 ? -1.58838  -62.22156 2.95767   1.000 233.75928 ? 144 SER C OG  1 
ATOM   5421 N N   . PRO C 3 145 ? -4.14384  -60.86953 4.43131   1.000 242.79312 ? 145 PRO C N   1 
ATOM   5422 C CA  . PRO C 3 145 ? -3.21622  -59.80751 4.84059   1.000 237.56353 ? 145 PRO C CA  1 
ATOM   5423 C C   . PRO C 3 145 ? -3.19055  -59.57665 6.35140   1.000 231.77057 ? 145 PRO C C   1 
ATOM   5424 O O   . PRO C 3 145 ? -3.79901  -60.33864 7.10298   1.000 231.27488 ? 145 PRO C O   1 
ATOM   5425 C CB  . PRO C 3 145 ? -3.75662  -58.57513 4.11241   1.000 230.97388 ? 145 PRO C CB  1 
ATOM   5426 C CG  . PRO C 3 145 ? -5.20578  -58.84413 3.96327   1.000 232.55611 ? 145 PRO C CG  1 
ATOM   5427 C CD  . PRO C 3 145 ? -5.33085  -60.32675 3.74805   1.000 240.58035 ? 145 PRO C CD  1 
ATOM   5428 N N   . SER C 3 146 ? -2.49614  -58.52242 6.78277   1.000 227.24242 ? 146 SER C N   1 
ATOM   5429 C CA  . SER C 3 146 ? -2.19577  -58.29610 8.19131   1.000 224.82955 ? 146 SER C CA  1 
ATOM   5430 C C   . SER C 3 146 ? -3.13413  -57.28649 8.84698   1.000 220.27840 ? 146 SER C C   1 
ATOM   5431 O O   . SER C 3 146 ? -2.75698  -56.64071 9.83084   1.000 216.69385 ? 146 SER C O   1 
ATOM   5432 C CB  . SER C 3 146 ? -0.74281  -57.84997 8.34899   1.000 225.85476 ? 146 SER C CB  1 
ATOM   5433 O OG  . SER C 3 146 ? -0.43949  -56.77858 7.47374   1.000 222.94822 ? 146 SER C OG  1 
ATOM   5434 N N   . GLY C 3 147 ? -4.35033  -57.13798 8.33003   1.000 218.22557 ? 147 GLY C N   1 
ATOM   5435 C CA  . GLY C 3 147 ? -5.33655  -56.30661 8.99251   1.000 218.11236 ? 147 GLY C CA  1 
ATOM   5436 C C   . GLY C 3 147 ? -5.98798  -57.04145 10.14648  1.000 219.56216 ? 147 GLY C C   1 
ATOM   5437 O O   . GLY C 3 147 ? -7.17443  -57.37796 10.08674  1.000 222.51790 ? 147 GLY C O   1 
ATOM   5438 N N   . VAL C 3 148 ? -5.22243  -57.29225 11.20535  1.000 221.69037 ? 148 VAL C N   1 
ATOM   5439 C CA  . VAL C 3 148 ? -5.64470  -58.17919 12.27899  1.000 221.27866 ? 148 VAL C CA  1 
ATOM   5440 C C   . VAL C 3 148 ? -5.82128  -57.39093 13.57228  1.000 210.72889 ? 148 VAL C C   1 
ATOM   5441 O O   . VAL C 3 148 ? -5.31939  -56.27472 13.73423  1.000 208.03792 ? 148 VAL C O   1 
ATOM   5442 C CB  . VAL C 3 148 ? -4.64861  -59.33923 12.48010  1.000 227.81614 ? 148 VAL C CB  1 
ATOM   5443 C CG1 . VAL C 3 148 ? -4.57610  -60.19471 11.22663  1.000 231.72557 ? 148 VAL C CG1 1 
ATOM   5444 C CG2 . VAL C 3 148 ? -3.27480  -58.80126 12.84302  1.000 228.85928 ? 148 VAL C CG2 1 
ATOM   5445 N N   . THR C 3 149 ? -6.54825  -58.00028 14.50797  1.000 217.48672 ? 149 THR C N   1 
ATOM   5446 C CA  . THR C 3 149 ? -6.82654  -57.41022 15.81049  1.000 218.12922 ? 149 THR C CA  1 
ATOM   5447 C C   . THR C 3 149 ? -6.92498  -58.53396 16.83141  1.000 219.61459 ? 149 THR C C   1 
ATOM   5448 O O   . THR C 3 149 ? -7.62035  -59.52561 16.59276  1.000 225.86275 ? 149 THR C O   1 
ATOM   5449 C CB  . THR C 3 149 ? -8.12365  -56.58956 15.77986  1.000 223.52253 ? 149 THR C CB  1 
ATOM   5450 O OG1 . THR C 3 149 ? -7.90327  -55.36853 15.06488  1.000 219.92586 ? 149 THR C OG1 1 
ATOM   5451 C CG2 . THR C 3 149 ? -8.60115  -56.27511 17.18879  1.000 224.65348 ? 149 THR C CG2 1 
ATOM   5452 N N   . VAL C 3 150 ? -6.23164  -58.37959 17.95432  1.000 212.32334 ? 150 VAL C N   1 
ATOM   5453 C CA  . VAL C 3 150 ? -6.13320  -59.42714 18.95593  1.000 216.45528 ? 150 VAL C CA  1 
ATOM   5454 C C   . VAL C 3 150 ? -7.04299  -59.10273 20.13423  1.000 221.25230 ? 150 VAL C C   1 
ATOM   5455 O O   . VAL C 3 150 ? -7.52326  -57.98261 20.29039  1.000 219.99364 ? 150 VAL C O   1 
ATOM   5456 C CB  . VAL C 3 150 ? -4.67419  -59.62904 19.42409  1.000 211.77701 ? 150 VAL C CB  1 
ATOM   5457 C CG1 . VAL C 3 150 ? -3.78711  -59.98758 18.24075  1.000 206.35983 ? 150 VAL C CG1 1 
ATOM   5458 C CG2 . VAL C 3 150 ? -4.17290  -58.37511 20.11371  1.000 207.38572 ? 150 VAL C CG2 1 
ATOM   5459 N N   . ALA C 3 151 ? -7.28520  -60.10721 20.97793  1.000 214.22826 ? 151 ALA C N   1 
ATOM   5460 C CA  . ALA C 3 151 ? -8.10275  -59.92747 22.17690  1.000 215.65810 ? 151 ALA C CA  1 
ATOM   5461 C C   . ALA C 3 151 ? -7.85517  -61.10080 23.11716  1.000 217.50602 ? 151 ALA C C   1 
ATOM   5462 O O   . ALA C 3 151 ? -8.23542  -62.23348 22.80496  1.000 221.32418 ? 151 ALA C O   1 
ATOM   5463 C CB  . ALA C 3 151 ? -9.57613  -59.81472 21.81224  1.000 218.84074 ? 151 ALA C CB  1 
ATOM   5464 N N   . TRP C 3 152 ? -7.23271  -60.82573 24.26134  1.000 217.33199 ? 152 TRP C N   1 
ATOM   5465 C CA  . TRP C 3 152 ? -7.06237  -61.81668 25.31706  1.000 221.67573 ? 152 TRP C CA  1 
ATOM   5466 C C   . TRP C 3 152 ? -8.29221  -61.81515 26.21582  1.000 226.07384 ? 152 TRP C C   1 
ATOM   5467 O O   . TRP C 3 152 ? -8.78009  -60.74949 26.60649  1.000 224.80613 ? 152 TRP C O   1 
ATOM   5468 C CB  . TRP C 3 152 ? -5.81153  -61.52445 26.14660  1.000 219.79447 ? 152 TRP C CB  1 
ATOM   5469 C CG  . TRP C 3 152 ? -4.53743  -62.06010 25.56955  1.000 219.25341 ? 152 TRP C CG  1 
ATOM   5470 C CD1 . TRP C 3 152 ? -3.57767  -61.35525 24.90457  1.000 216.47430 ? 152 TRP C CD1 1 
ATOM   5471 C CD2 . TRP C 3 152 ? -4.07752  -63.41579 25.61900  1.000 223.28098 ? 152 TRP C CD2 1 
ATOM   5472 N NE1 . TRP C 3 152 ? -2.54970  -62.18789 24.53382  1.000 219.07676 ? 152 TRP C NE1 1 
ATOM   5473 C CE2 . TRP C 3 152 ? -2.83315  -63.45870 24.96028  1.000 224.19157 ? 152 TRP C CE2 1 
ATOM   5474 C CE3 . TRP C 3 152 ? -4.59877  -64.59773 26.15391  1.000 227.22682 ? 152 TRP C CE3 1 
ATOM   5475 C CZ2 . TRP C 3 152 ? -2.10103  -64.63534 24.82555  1.000 228.88976 ? 152 TRP C CZ2 1 
ATOM   5476 C CZ3 . TRP C 3 152 ? -3.87227  -65.76542 26.01564  1.000 231.33230 ? 152 TRP C CZ3 1 
ATOM   5477 C CH2 . TRP C 3 152 ? -2.63787  -65.77621 25.35539  1.000 230.97217 ? 152 TRP C CH2 1 
ATOM   5478 N N   . LYS C 3 153 ? -8.79261  -63.00619 26.54051  1.000 228.31948 ? 153 LYS C N   1 
ATOM   5479 C CA  . LYS C 3 153 ? -9.99949  -63.13286 27.34372  1.000 231.80627 ? 153 LYS C CA  1 
ATOM   5480 C C   . LYS C 3 153 ? -9.79656  -64.19782 28.41217  1.000 234.22751 ? 153 LYS C C   1 
ATOM   5481 O O   . LYS C 3 153 ? -9.07944  -65.18036 28.20526  1.000 234.81432 ? 153 LYS C O   1 
ATOM   5482 C CB  . LYS C 3 153 ? -11.22283 -63.48034 26.48004  1.000 234.65782 ? 153 LYS C CB  1 
ATOM   5483 C CG  . LYS C 3 153 ? -11.17178 -62.93021 25.05893  1.000 232.56284 ? 153 LYS C CG  1 
ATOM   5484 C CD  . LYS C 3 153 ? -12.55772 -62.84367 24.44508  1.000 235.43616 ? 153 LYS C CD  1 
ATOM   5485 C CE  . LYS C 3 153 ? -13.21479 -64.20809 24.34490  1.000 239.79912 ? 153 LYS C CE  1 
ATOM   5486 N NZ  . LYS C 3 153 ? -12.83687 -64.93384 23.10163  1.000 240.84624 ? 153 LYS C NZ  1 
ATOM   5487 N N   . ALA C 3 154 ? -10.44250 -63.99170 29.55993  1.000 236.41583 ? 154 ALA C N   1 
ATOM   5488 C CA  . ALA C 3 154 ? -10.34732 -64.89752 30.70153  1.000 239.16045 ? 154 ALA C CA  1 
ATOM   5489 C C   . ALA C 3 154 ? -11.74563 -65.12488 31.26023  1.000 244.06124 ? 154 ALA C C   1 
ATOM   5490 O O   . ALA C 3 154 ? -12.34533 -64.20595 31.82860  1.000 246.98231 ? 154 ALA C O   1 
ATOM   5491 C CB  . ALA C 3 154 ? -9.41549  -64.33605 31.77601  1.000 237.61405 ? 154 ALA C CB  1 
ATOM   5492 N N   . ASN C 3 155 ? -12.25637 -66.34916 31.10019  1.000 243.06027 ? 155 ASN C N   1 
ATOM   5493 C CA  . ASN C 3 155 ? -13.59013 -66.73058 31.57433  1.000 247.88354 ? 155 ASN C CA  1 
ATOM   5494 C C   . ASN C 3 155 ? -14.67195 -65.82955 30.98349  1.000 250.54697 ? 155 ASN C C   1 
ATOM   5495 O O   . ASN C 3 155 ? -15.65746 -65.49390 31.64358  1.000 255.49789 ? 155 ASN C O   1 
ATOM   5496 C CB  . ASN C 3 155 ? -13.66088 -66.73574 33.10401  1.000 250.64533 ? 155 ASN C CB  1 
ATOM   5497 C CG  . ASN C 3 155 ? -13.82463 -68.13290 33.67557  1.000 252.80460 ? 155 ASN C CG  1 
ATOM   5498 O OD1 . ASN C 3 155 ? -14.88932 -68.74069 33.56444  1.000 256.85417 ? 155 ASN C OD1 1 
ATOM   5499 N ND2 . ASN C 3 155 ? -12.77015 -68.64636 34.29585  1.000 250.29953 ? 155 ASN C ND2 1 
ATOM   5500 N N   . GLY C 3 156 ? -14.48953 -65.43922 29.72316  1.000 249.34364 ? 156 GLY C N   1 
ATOM   5501 C CA  . GLY C 3 156 ? -15.41893 -64.58038 29.02989  1.000 251.19178 ? 156 GLY C CA  1 
ATOM   5502 C C   . GLY C 3 156 ? -15.16130 -63.09810 29.21190  1.000 249.63278 ? 156 GLY C C   1 
ATOM   5503 O O   . GLY C 3 156 ? -15.46152 -62.31108 28.30845  1.000 248.44546 ? 156 GLY C O   1 
ATOM   5504 N N   . THR C 3 157 ? -14.61295 -62.69969 30.35326  1.000 254.61669 ? 157 THR C N   1 
ATOM   5505 C CA  . THR C 3 157 ? -14.31506 -61.29218 30.59056  1.000 253.50270 ? 157 THR C CA  1 
ATOM   5506 C C   . THR C 3 157 ? -13.02740 -60.90582 29.87110  1.000 246.78740 ? 157 THR C C   1 
ATOM   5507 O O   . THR C 3 157 ? -12.04028 -61.64506 29.94066  1.000 244.04725 ? 157 THR C O   1 
ATOM   5508 C CB  . THR C 3 157 ? -14.17898 -61.01055 32.08376  1.000 256.44496 ? 157 THR C CB  1 
ATOM   5509 O OG1 . THR C 3 157 ? -13.11845 -61.80675 32.62708  1.000 253.53302 ? 157 THR C OG1 1 
ATOM   5510 C CG2 . THR C 3 157 ? -15.47543 -61.33966 32.80763  1.000 264.09442 ? 157 THR C CG2 1 
ATOM   5511 N N   . PRO C 3 158 ? -12.99817 -59.76992 29.17310  1.000 242.98375 ? 158 PRO C N   1 
ATOM   5512 C CA  . PRO C 3 158 ? -11.78205 -59.35023 28.46249  1.000 236.38881 ? 158 PRO C CA  1 
ATOM   5513 C C   . PRO C 3 158 ? -10.75633 -58.77628 29.42751  1.000 233.91274 ? 158 PRO C C   1 
ATOM   5514 O O   . PRO C 3 158 ? -10.93227 -57.67909 29.96650  1.000 235.43762 ? 158 PRO C O   1 
ATOM   5515 C CB  . PRO C 3 158 ? -12.30269 -58.28729 27.48072  1.000 235.68307 ? 158 PRO C CB  1 
ATOM   5516 C CG  . PRO C 3 158 ? -13.81072 -58.37023 27.53585  1.000 242.35589 ? 158 PRO C CG  1 
ATOM   5517 C CD  . PRO C 3 158 ? -14.12985 -58.87269 28.89947  1.000 246.82652 ? 158 PRO C CD  1 
ATOM   5518 N N   . ILE C 3 159 ? -9.67478  -59.52375 29.64986  1.000 236.88396 ? 159 ILE C N   1 
ATOM   5519 C CA  . ILE C 3 159 ? -8.58533  -59.03245 30.48456  1.000 234.03652 ? 159 ILE C CA  1 
ATOM   5520 C C   . ILE C 3 159 ? -7.83812  -57.93809 29.73444  1.000 229.50836 ? 159 ILE C C   1 
ATOM   5521 O O   . ILE C 3 159 ? -7.41301  -58.12493 28.58664  1.000 226.54840 ? 159 ILE C O   1 
ATOM   5522 C CB  . ILE C 3 159 ? -7.65323  -60.18452 30.89197  1.000 232.99666 ? 159 ILE C CB  1 
ATOM   5523 C CG1 . ILE C 3 159 ? -6.36247  -59.64201 31.51215  1.000 230.03618 ? 159 ILE C CG1 1 
ATOM   5524 C CG2 . ILE C 3 159 ? -7.36138  -61.09618 29.70524  1.000 231.58887 ? 159 ILE C CG2 1 
ATOM   5525 C CD1 . ILE C 3 159 ? -6.57013  -58.92270 32.82797  1.000 232.75165 ? 159 ILE C CD1 1 
ATOM   5526 N N   . THR C 3 160 ? -7.68149  -56.78267 30.37878  1.000 235.62912 ? 160 THR C N   1 
ATOM   5527 C CA  . THR C 3 160 ? -7.14328  -55.59442 29.72769  1.000 231.51517 ? 160 THR C CA  1 
ATOM   5528 C C   . THR C 3 160 ? -5.64821  -55.41210 29.96058  1.000 227.35732 ? 160 THR C C   1 
ATOM   5529 O O   . THR C 3 160 ? -4.88439  -55.27765 29.00020  1.000 223.11282 ? 160 THR C O   1 
ATOM   5530 C CB  . THR C 3 160 ? -7.89644  -54.34831 30.20924  1.000 235.31227 ? 160 THR C CB  1 
ATOM   5531 O OG1 . THR C 3 160 ? -9.30597  -54.60603 30.19602  1.000 241.14945 ? 160 THR C OG1 1 
ATOM   5532 C CG2 . THR C 3 160 ? -7.59840  -53.16576 29.30101  1.000 231.56375 ? 160 THR C CG2 1 
ATOM   5533 N N   . GLN C 3 161 ? -5.21380  -55.40249 31.21565  1.000 232.67259 ? 161 GLN C N   1 
ATOM   5534 C CA  . GLN C 3 161 ? -3.82836  -55.10468 31.54102  1.000 229.38057 ? 161 GLN C CA  1 
ATOM   5535 C C   . GLN C 3 161 ? -2.97811  -56.37124 31.52032  1.000 228.38399 ? 161 GLN C C   1 
ATOM   5536 O O   . GLN C 3 161 ? -3.48333  -57.49428 31.58860  1.000 231.11709 ? 161 GLN C O   1 
ATOM   5537 C CB  . GLN C 3 161 ? -3.73147  -54.42884 32.90966  1.000 233.02006 ? 161 GLN C CB  1 
ATOM   5538 C CG  . GLN C 3 161 ? -4.85939  -53.44801 33.20500  1.000 236.52841 ? 161 GLN C CG  1 
ATOM   5539 C CD  . GLN C 3 161 ? -4.95356  -52.32113 32.19117  1.000 233.74497 ? 161 GLN C CD  1 
ATOM   5540 O OE1 . GLN C 3 161 ? -3.96569  -51.95262 31.55475  1.000 228.97573 ? 161 GLN C OE1 1 
ATOM   5541 N NE2 . GLN C 3 161 ? -6.15055  -51.76684 32.03767  1.000 237.39094 ? 161 GLN C NE2 1 
ATOM   5542 N N   . GLY C 3 162 ? -1.66765  -56.17137 31.42716  1.000 220.15972 ? 162 GLY C N   1 
ATOM   5543 C CA  . GLY C 3 162 ? -0.73654  -57.28446 31.36521  1.000 220.35226 ? 162 GLY C CA  1 
ATOM   5544 C C   . GLY C 3 162 ? -0.75305  -58.02403 30.04533  1.000 219.96384 ? 162 GLY C C   1 
ATOM   5545 O O   . GLY C 3 162 ? -0.66948  -59.25831 30.03079  1.000 223.12934 ? 162 GLY C O   1 
ATOM   5546 N N   . VAL C 3 163 ? -0.85794  -57.29943 28.93369  1.000 221.15662 ? 163 VAL C N   1 
ATOM   5547 C CA  . VAL C 3 163 ? -0.94079  -57.89263 27.60362  1.000 220.15116 ? 163 VAL C CA  1 
ATOM   5548 C C   . VAL C 3 163 ? -0.01292  -57.12775 26.66964  1.000 217.09415 ? 163 VAL C C   1 
ATOM   5549 O O   . VAL C 3 163 ? 0.03163   -55.89323 26.69473  1.000 213.99347 ? 163 VAL C O   1 
ATOM   5550 C CB  . VAL C 3 163 ? -2.39127  -57.88663 27.07202  1.000 218.63849 ? 163 VAL C CB  1 
ATOM   5551 C CG1 . VAL C 3 163 ? -2.42350  -58.15219 25.57400  1.000 209.24080 ? 163 VAL C CG1 1 
ATOM   5552 C CG2 . VAL C 3 163 ? -3.23155  -58.91730 27.81058  1.000 222.89169 ? 163 VAL C CG2 1 
ATOM   5553 N N   . ASP C 3 164 ? 0.73491   -57.86565 25.85003  1.000 215.67824 ? 164 ASP C N   1 
ATOM   5554 C CA  . ASP C 3 164 ? 1.63851   -57.28126 24.86780  1.000 212.10602 ? 164 ASP C CA  1 
ATOM   5555 C C   . ASP C 3 164 ? 1.51899   -58.06359 23.57004  1.000 212.47630 ? 164 ASP C C   1 
ATOM   5556 O O   . ASP C 3 164 ? 1.55167   -59.29732 23.58404  1.000 218.65466 ? 164 ASP C O   1 
ATOM   5557 C CB  . ASP C 3 164 ? 3.08317   -57.29165 25.37660  1.000 219.98902 ? 164 ASP C CB  1 
ATOM   5558 C CG  . ASP C 3 164 ? 3.25659   -56.46841 26.63581  1.000 219.78616 ? 164 ASP C CG  1 
ATOM   5559 O OD1 . ASP C 3 164 ? 2.99819   -55.24748 26.58617  1.000 215.69086 ? 164 ASP C OD1 1 
ATOM   5560 O OD2 . ASP C 3 164 ? 3.62692   -57.04507 27.67967  1.000 223.74973 ? 164 ASP C OD2 1 
ATOM   5561 N N   . THR C 3 165 ? 1.37948   -57.34842 22.45489  1.000 208.21947 ? 165 THR C N   1 
ATOM   5562 C CA  . THR C 3 165 ? 1.10269   -57.96066 21.16027  1.000 208.06805 ? 165 THR C CA  1 
ATOM   5563 C C   . THR C 3 165 ? 2.06865   -57.41324 20.12157  1.000 206.73532 ? 165 THR C C   1 
ATOM   5564 O O   . THR C 3 165 ? 2.16199   -56.19517 19.93730  1.000 204.23856 ? 165 THR C O   1 
ATOM   5565 C CB  . THR C 3 165 ? -0.34408  -57.70213 20.72853  1.000 204.46625 ? 165 THR C CB  1 
ATOM   5566 O OG1 . THR C 3 165 ? -1.24072  -58.30578 21.66958  1.000 209.61045 ? 165 THR C OG1 1 
ATOM   5567 C CG2 . THR C 3 165 ? -0.60054  -58.27830 19.34254  1.000 203.91839 ? 165 THR C CG2 1 
ATOM   5568 N N   . SER C 3 166 ? 2.77461   -58.31143 19.44141  1.000 201.31784 ? 166 SER C N   1 
ATOM   5569 C CA  . SER C 3 166 ? 3.67540   -57.91932 18.37003  1.000 205.89896 ? 166 SER C CA  1 
ATOM   5570 C C   . SER C 3 166 ? 2.90500   -57.71543 17.07108  1.000 202.80220 ? 166 SER C C   1 
ATOM   5571 O O   . SER C 3 166 ? 1.92726   -58.41283 16.78532  1.000 203.82742 ? 166 SER C O   1 
ATOM   5572 C CB  . SER C 3 166 ? 4.76366   -58.97469 18.17053  1.000 224.11720 ? 166 SER C CB  1 
ATOM   5573 O OG  . SER C 3 166 ? 4.19717   -60.25121 17.92919  1.000 236.22088 ? 166 SER C OG  1 
ATOM   5574 N N   . ASN C 3 167 ? 3.35606   -56.74309 16.28372  1.000 211.66248 ? 167 ASN C N   1 
ATOM   5575 C CA  . ASN C 3 167 ? 2.72691   -56.47411 15.00308  1.000 209.90759 ? 167 ASN C CA  1 
ATOM   5576 C C   . ASN C 3 167 ? 3.06879   -57.58089 14.00489  1.000 220.71340 ? 167 ASN C C   1 
ATOM   5577 O O   . ASN C 3 167 ? 4.10922   -58.23385 14.12378  1.000 237.73366 ? 167 ASN C O   1 
ATOM   5578 C CB  . ASN C 3 167 ? 3.17460   -55.11882 14.46221  1.000 214.85864 ? 167 ASN C CB  1 
ATOM   5579 C CG  . ASN C 3 167 ? 2.74251   -53.96702 15.34933  1.000 208.77552 ? 167 ASN C CG  1 
ATOM   5580 O OD1 . ASN C 3 167 ? 1.85040   -54.11287 16.18558  1.000 203.33119 ? 167 ASN C OD1 1 
ATOM   5581 N ND2 . ASN C 3 167 ? 3.37039   -52.81149 15.16671  1.000 204.65773 ? 167 ASN C ND2 1 
ATOM   5582 N N   . PRO C 3 168 ? 2.20078   -57.81868 13.01993  1.000 209.36273 ? 168 PRO C N   1 
ATOM   5583 C CA  . PRO C 3 168 ? 2.43452   -58.91870 12.07084  1.000 226.11828 ? 168 PRO C CA  1 
ATOM   5584 C C   . PRO C 3 168 ? 3.73676   -58.73695 11.30931  1.000 234.44881 ? 168 PRO C C   1 
ATOM   5585 O O   . PRO C 3 168 ? 3.90876   -57.78248 10.54715  1.000 229.45704 ? 168 PRO C O   1 
ATOM   5586 C CB  . PRO C 3 168 ? 1.21993   -58.84548 11.14042  1.000 228.85242 ? 168 PRO C CB  1 
ATOM   5587 C CG  . PRO C 3 168 ? 0.17149   -58.17531 11.94517  1.000 208.61152 ? 168 PRO C CG  1 
ATOM   5588 C CD  . PRO C 3 168 ? 0.88897   -57.18344 12.80920  1.000 201.33841 ? 168 PRO C CD  1 
ATOM   5589 N N   . THR C 3 169 ? 4.65921   -59.66625 11.52466  1.000 221.21341 ? 169 THR C N   1 
ATOM   5590 C CA  . THR C 3 169 ? 5.94846   -59.65487 10.85426  1.000 225.71702 ? 169 THR C CA  1 
ATOM   5591 C C   . THR C 3 169 ? 5.94835   -60.65071 9.70341   1.000 230.58015 ? 169 THR C C   1 
ATOM   5592 O O   . THR C 3 169 ? 5.06366   -61.49790 9.57314   1.000 232.92673 ? 169 THR C O   1 
ATOM   5593 C CB  . THR C 3 169 ? 7.07761   -59.97801 11.83999  1.000 229.74415 ? 169 THR C CB  1 
ATOM   5594 O OG1 . THR C 3 169 ? 8.33899   -59.81250 11.18259  1.000 231.66558 ? 169 THR C OG1 1 
ATOM   5595 C CG2 . THR C 3 169 ? 6.96580   -61.41198 12.34131  1.000 235.87601 ? 169 THR C CG2 1 
ATOM   5596 N N   . LYS C 3 170 ? 6.96275   -60.54522 8.85784   1.000 234.71956 ? 170 LYS C N   1 
ATOM   5597 C CA  . LYS C 3 170 ? 7.14383   -61.47141 7.74243   1.000 238.23471 ? 170 LYS C CA  1 
ATOM   5598 C C   . LYS C 3 170 ? 8.17329   -62.54141 8.08516   1.000 244.91894 ? 170 LYS C C   1 
ATOM   5599 O O   . LYS C 3 170 ? 9.36128   -62.23954 8.23391   1.000 245.97176 ? 170 LYS C O   1 
ATOM   5600 C CB  . LYS C 3 170 ? 7.57342   -60.71113 6.49286   1.000 234.28474 ? 170 LYS C CB  1 
ATOM   5601 C CG  . LYS C 3 170 ? 6.41813   -60.15856 5.68044   1.000 228.93398 ? 170 LYS C CG  1 
ATOM   5602 C CD  . LYS C 3 170 ? 6.88988   -59.72048 4.30724   1.000 226.25353 ? 170 LYS C CD  1 
ATOM   5603 C CE  . LYS C 3 170 ? 5.77193   -59.07691 3.50198   1.000 220.97783 ? 170 LYS C CE  1 
ATOM   5604 N NZ  . LYS C 3 170 ? 6.23651   -58.63217 2.15558   1.000 218.84772 ? 170 LYS C NZ  1 
ATOM   5605 N N   . GLU C 3 171 ? 7.72212   -63.77937 8.20779   1.000 234.33719 ? 171 GLU C N   1 
ATOM   5606 C CA  . GLU C 3 171 ? 8.57089   -64.97262 8.33935   1.000 240.91252 ? 171 GLU C CA  1 
ATOM   5607 C C   . GLU C 3 171 ? 8.19552   -66.09196 7.37207   1.000 244.22434 ? 171 GLU C C   1 
ATOM   5608 O O   . GLU C 3 171 ? 9.09478   -66.79369 6.91416   1.000 248.16895 ? 171 GLU C O   1 
ATOM   5609 C CB  . GLU C 3 171 ? 8.49408   -65.54459 9.76415   1.000 243.63362 ? 171 GLU C CB  1 
ATOM   5610 C CG  . GLU C 3 171 ? 9.31100   -66.79828 9.95672   1.000 250.29665 ? 171 GLU C CG  1 
ATOM   5611 C CD  . GLU C 3 171 ? 10.79174  -66.51209 10.04451  1.000 251.73320 ? 171 GLU C CD  1 
ATOM   5612 O OE1 . GLU C 3 171 ? 11.19948  -65.32627 10.12655  1.000 247.88683 ? 171 GLU C OE1 1 
ATOM   5613 O OE2 . GLU C 3 171 ? 11.55628  -67.48919 10.05460  1.000 256.73261 ? 171 GLU C OE2 1 
ATOM   5614 N N   . ASP C 3 172 ? 6.91906   -66.24302 6.97196   1.000 254.18766 ? 172 ASP C N   1 
ATOM   5615 C CA  . ASP C 3 172 ? 6.44746   -67.20223 5.96415   1.000 256.96100 ? 172 ASP C CA  1 
ATOM   5616 C C   . ASP C 3 172 ? 6.04368   -66.43887 4.69900   1.000 252.14429 ? 172 ASP C C   1 
ATOM   5617 O O   . ASP C 3 172 ? 6.25895   -65.22948 4.58844   1.000 246.86066 ? 172 ASP C O   1 
ATOM   5618 C CB  . ASP C 3 172 ? 5.27088   -68.04189 6.49648   1.000 260.12309 ? 172 ASP C CB  1 
ATOM   5619 C CG  . ASP C 3 172 ? 5.62330   -68.79862 7.75061   1.000 261.76246 ? 172 ASP C CG  1 
ATOM   5620 O OD1 . ASP C 3 172 ? 6.82824   -69.05456 7.90617   1.000 258.83255 ? 172 ASP C OD1 1 
ATOM   5621 O OD2 . ASP C 3 172 ? 4.74037   -69.09615 8.59211   1.000 265.68778 ? 172 ASP C OD2 1 
ATOM   5622 N N   . ASN C 3 173 ? 5.49182   -67.16135 3.71591   1.000 258.97990 ? 173 ASN C N   1 
ATOM   5623 C CA  . ASN C 3 173 ? 4.84571   -66.49865 2.57863   1.000 254.74099 ? 173 ASN C CA  1 
ATOM   5624 C C   . ASN C 3 173 ? 3.70647   -65.57493 3.01864   1.000 250.17169 ? 173 ASN C C   1 
ATOM   5625 O O   . ASN C 3 173 ? 3.29760   -64.68520 2.25914   1.000 245.54527 ? 173 ASN C O   1 
ATOM   5626 C CB  . ASN C 3 173 ? 4.31230   -67.54722 1.59719   1.000 258.42375 ? 173 ASN C CB  1 
ATOM   5627 C CG  . ASN C 3 173 ? 3.54561   -68.64616 2.29747   1.000 263.24725 ? 173 ASN C CG  1 
ATOM   5628 O OD1 . ASN C 3 173 ? 2.47927   -68.40261 2.85469   1.000 262.13250 ? 173 ASN C OD1 1 
ATOM   5629 N ND2 . ASN C 3 173 ? 4.10456   -69.85309 2.31234   1.000 268.57737 ? 173 ASN C ND2 1 
ATOM   5630 N N   . LYS C 3 174 ? 3.18820   -65.77017 4.22818   1.000 247.74076 ? 174 LYS C N   1 
ATOM   5631 C CA  . LYS C 3 174 ? 2.18306   -64.90896 4.83588   1.000 243.82592 ? 174 LYS C CA  1 
ATOM   5632 C C   . LYS C 3 174 ? 2.68572   -64.44222 6.19882   1.000 242.94922 ? 174 LYS C C   1 
ATOM   5633 O O   . LYS C 3 174 ? 3.70966   -64.91242 6.70033   1.000 246.28509 ? 174 LYS C O   1 
ATOM   5634 C CB  . LYS C 3 174 ? 0.83598   -65.63549 4.95850   1.000 246.60011 ? 174 LYS C CB  1 
ATOM   5635 C CG  . LYS C 3 174 ? 0.31098   -66.13278 3.62017   1.000 247.37302 ? 174 LYS C CG  1 
ATOM   5636 C CD  . LYS C 3 174 ? -0.74710  -67.20859 3.77597   1.000 252.24691 ? 174 LYS C CD  1 
ATOM   5637 C CE  . LYS C 3 174 ? -1.21637  -67.70883 2.41626   1.000 253.45952 ? 174 LYS C CE  1 
ATOM   5638 N NZ  . LYS C 3 174 ? -1.83943  -66.62652 1.60528   1.000 248.35965 ? 174 LYS C NZ  1 
ATOM   5639 N N   . TYR C 3 175 ? 1.95992   -63.50123 6.80077   1.000 244.40641 ? 175 TYR C N   1 
ATOM   5640 C CA  . TYR C 3 175 ? 2.44264   -62.82969 8.00180   1.000 242.32420 ? 175 TYR C CA  1 
ATOM   5641 C C   . TYR C 3 175 ? 2.41671   -63.77303 9.20738   1.000 246.75949 ? 175 TYR C C   1 
ATOM   5642 O O   . TYR C 3 175 ? 1.95925   -64.91755 9.13655   1.000 250.95570 ? 175 TYR C O   1 
ATOM   5643 C CB  . TYR C 3 175 ? 1.61518   -61.57730 8.28096   1.000 235.26983 ? 175 TYR C CB  1 
ATOM   5644 C CG  . TYR C 3 175 ? 1.56514   -60.59991 7.12995   1.000 230.15537 ? 175 TYR C CG  1 
ATOM   5645 C CD1 . TYR C 3 175 ? 2.63758   -59.76063 6.85786   1.000 227.07076 ? 175 TYR C CD1 1 
ATOM   5646 C CD2 . TYR C 3 175 ? 0.44133   -60.51055 6.32003   1.000 228.41692 ? 175 TYR C CD2 1 
ATOM   5647 C CE1 . TYR C 3 175 ? 2.59388   -58.86287 5.80753   1.000 222.10060 ? 175 TYR C CE1 1 
ATOM   5648 C CE2 . TYR C 3 175 ? 0.38783   -59.61547 5.26829   1.000 223.66102 ? 175 TYR C CE2 1 
ATOM   5649 C CZ  . TYR C 3 175 ? 1.46668   -58.79433 5.01682   1.000 220.35704 ? 175 TYR C CZ  1 
ATOM   5650 O OH  . TYR C 3 175 ? 1.41886   -57.90167 3.97102   1.000 215.72339 ? 175 TYR C OH  1 
ATOM   5651 N N   . MET C 3 176 ? 2.92116   -63.27075 10.33474  1.000 232.91487 ? 176 MET C N   1 
ATOM   5652 C CA  . MET C 3 176 ? 2.98472   -64.02782 11.57748  1.000 235.95370 ? 176 MET C CA  1 
ATOM   5653 C C   . MET C 3 176 ? 3.09201   -63.04400 12.73592  1.000 229.54104 ? 176 MET C C   1 
ATOM   5654 O O   . MET C 3 176 ? 3.74594   -62.00567 12.61057  1.000 226.65869 ? 176 MET C O   1 
ATOM   5655 C CB  . MET C 3 176 ? 4.17366   -64.99559 11.57724  1.000 241.70449 ? 176 MET C CB  1 
ATOM   5656 C CG  . MET C 3 176 ? 4.16276   -66.00384 12.70906  1.000 245.29343 ? 176 MET C CG  1 
ATOM   5657 S SD  . MET C 3 176 ? 5.69172   -66.95249 12.78426  1.000 251.19698 ? 176 MET C SD  1 
ATOM   5658 C CE  . MET C 3 176 ? 6.88365   -65.62879 12.95660  1.000 247.03882 ? 176 MET C CE  1 
ATOM   5659 N N   . ALA C 3 177 ? 2.44760   -63.37210 13.85523  1.000 233.22932 ? 177 ALA C N   1 
ATOM   5660 C CA  . ALA C 3 177 ? 2.43196   -62.47867 15.00704  1.000 218.10510 ? 177 ALA C CA  1 
ATOM   5661 C C   . ALA C 3 177 ? 2.21253   -63.29039 16.27629  1.000 219.39199 ? 177 ALA C C   1 
ATOM   5662 O O   . ALA C 3 177 ? 1.80566   -64.45359 16.22904  1.000 225.98423 ? 177 ALA C O   1 
ATOM   5663 C CB  . ALA C 3 177 ? 1.35375   -61.39932 14.86288  1.000 206.46556 ? 177 ALA C CB  1 
ATOM   5664 N N   . SER C 3 178 ? 2.48116   -62.65428 17.41679  1.000 209.18354 ? 178 SER C N   1 
ATOM   5665 C CA  . SER C 3 178 ? 2.38179   -63.31972 18.70872  1.000 209.68805 ? 178 SER C CA  1 
ATOM   5666 C C   . SER C 3 178 ? 1.97547   -62.31248 19.77615  1.000 208.30990 ? 178 SER C C   1 
ATOM   5667 O O   . SER C 3 178 ? 2.23834   -61.11323 19.65129  1.000 206.34685 ? 178 SER C O   1 
ATOM   5668 C CB  . SER C 3 178 ? 3.70423   -63.99600 19.09117  1.000 208.92362 ? 178 SER C CB  1 
ATOM   5669 O OG  . SER C 3 178 ? 4.78946   -63.09080 18.98541  1.000 206.39141 ? 178 SER C OG  1 
ATOM   5670 N N   . SER C 3 179 ? 1.33361   -62.81636 20.83163  1.000 208.63597 ? 179 SER C N   1 
ATOM   5671 C CA  . SER C 3 179 ? 0.84335   -61.98628 21.92396  1.000 206.73219 ? 179 SER C CA  1 
ATOM   5672 C C   . SER C 3 179 ? 1.04332   -62.71817 23.24564  1.000 213.47408 ? 179 SER C C   1 
ATOM   5673 O O   . SER C 3 179 ? 1.07846   -63.95047 23.28877  1.000 221.30433 ? 179 SER C O   1 
ATOM   5674 C CB  . SER C 3 179 ? -0.63774  -61.62443 21.73304  1.000 202.96963 ? 179 SER C CB  1 
ATOM   5675 O OG  . SER C 3 179 ? -1.06436  -60.67363 22.69348  1.000 202.03407 ? 179 SER C OG  1 
ATOM   5676 N N   . PHE C 3 180 ? 1.16499   -61.94762 24.32793  1.000 208.03349 ? 180 PHE C N   1 
ATOM   5677 C CA  . PHE C 3 180 ? 1.50349   -62.48905 25.63658  1.000 208.27812 ? 180 PHE C CA  1 
ATOM   5678 C C   . PHE C 3 180 ? 0.58517   -61.91205 26.70711  1.000 209.06267 ? 180 PHE C C   1 
ATOM   5679 O O   . PHE C 3 180 ? -0.01710  -60.85038 26.53234  1.000 208.76452 ? 180 PHE C O   1 
ATOM   5680 C CB  . PHE C 3 180 ? 2.97006   -62.20450 25.99171  1.000 206.06770 ? 180 PHE C CB  1 
ATOM   5681 C CG  . PHE C 3 180 ? 3.95289   -62.94279 25.12764  1.000 205.69525 ? 180 PHE C CG  1 
ATOM   5682 C CD1 . PHE C 3 180 ? 3.83191   -64.30786 24.92990  1.000 217.21017 ? 180 PHE C CD1 1 
ATOM   5683 C CD2 . PHE C 3 180 ? 4.98716   -62.27089 24.50130  1.000 203.72678 ? 180 PHE C CD2 1 
ATOM   5684 C CE1 . PHE C 3 180 ? 4.73192   -64.99017 24.13158  1.000 223.02842 ? 180 PHE C CE1 1 
ATOM   5685 C CE2 . PHE C 3 180 ? 5.88923   -62.94561 23.70059  1.000 205.90294 ? 180 PHE C CE2 1 
ATOM   5686 C CZ  . PHE C 3 180 ? 5.76182   -64.30735 23.51541  1.000 221.44365 ? 180 PHE C CZ  1 
ATOM   5687 N N   . LEU C 3 181 ? 0.49799   -62.62422 27.83129  1.000 218.22769 ? 181 LEU C N   1 
ATOM   5688 C CA  . LEU C 3 181 ? -0.39351  -62.24702 28.92634  1.000 217.42156 ? 181 LEU C CA  1 
ATOM   5689 C C   . LEU C 3 181 ? 0.25644   -62.65291 30.24280  1.000 219.53938 ? 181 LEU C C   1 
ATOM   5690 O O   . LEU C 3 181 ? 0.32698   -63.84400 30.55217  1.000 222.92926 ? 181 LEU C O   1 
ATOM   5691 C CB  . LEU C 3 181 ? -1.76257  -62.90802 28.76390  1.000 220.88041 ? 181 LEU C CB  1 
ATOM   5692 C CG  . LEU C 3 181 ? -2.67190  -62.95159 29.99417  1.000 222.25584 ? 181 LEU C CG  1 
ATOM   5693 C CD1 . LEU C 3 181 ? -3.15894  -61.56166 30.36816  1.000 219.48534 ? 181 LEU C CD1 1 
ATOM   5694 C CD2 . LEU C 3 181 ? -3.84314  -63.90159 29.77910  1.000 225.90002 ? 181 LEU C CD2 1 
ATOM   5695 N N   . HIS C 3 182 ? 0.72051   -61.67121 31.01543  1.000 227.84180 ? 182 HIS C N   1 
ATOM   5696 C CA  . HIS C 3 182 ? 1.34112   -61.93826 32.30761  1.000 228.72165 ? 182 HIS C CA  1 
ATOM   5697 C C   . HIS C 3 182 ? 0.28135   -62.21056 33.37011  1.000 230.54622 ? 182 HIS C C   1 
ATOM   5698 O O   . HIS C 3 182 ? -0.83008  -61.67459 33.32147  1.000 230.45744 ? 182 HIS C O   1 
ATOM   5699 C CB  . HIS C 3 182 ? 2.21039   -60.75794 32.73731  1.000 225.59537 ? 182 HIS C CB  1 
ATOM   5700 C CG  . HIS C 3 182 ? 3.02350   -60.17260 31.62726  1.000 223.81334 ? 182 HIS C CG  1 
ATOM   5701 N ND1 . HIS C 3 182 ? 3.27909   -58.82229 31.52522  1.000 222.75225 ? 182 HIS C ND1 1 
ATOM   5702 C CD2 . HIS C 3 182 ? 3.63618   -60.75301 30.56889  1.000 223.67129 ? 182 HIS C CD2 1 
ATOM   5703 C CE1 . HIS C 3 182 ? 4.01476   -58.59619 30.45155  1.000 221.60458 ? 182 HIS C CE1 1 
ATOM   5704 N NE2 . HIS C 3 182 ? 4.24475   -59.75107 29.85334  1.000 221.76321 ? 182 HIS C NE2 1 
ATOM   5705 N N   . LEU C 3 183 ? 0.64134   -63.04245 34.34817  1.000 225.40897 ? 183 LEU C N   1 
ATOM   5706 C CA  . LEU C 3 183 ? -0.30942  -63.48175 35.36239  1.000 228.47211 ? 183 LEU C CA  1 
ATOM   5707 C C   . LEU C 3 183 ? 0.40782   -63.75161 36.67951  1.000 229.21717 ? 183 LEU C C   1 
ATOM   5708 O O   . LEU C 3 183 ? 1.63634   -63.84368 36.73954  1.000 228.95724 ? 183 LEU C O   1 
ATOM   5709 C CB  . LEU C 3 183 ? -1.05524  -64.74404 34.91548  1.000 232.26509 ? 183 LEU C CB  1 
ATOM   5710 C CG  . LEU C 3 183 ? -1.96090  -64.68106 33.68376  1.000 231.87422 ? 183 LEU C CG  1 
ATOM   5711 C CD1 . LEU C 3 183 ? -2.33947  -66.08268 33.20823  1.000 234.76094 ? 183 LEU C CD1 1 
ATOM   5712 C CD2 . LEU C 3 183 ? -3.20507  -63.85882 33.96451  1.000 233.71917 ? 183 LEU C CD2 1 
ATOM   5713 N N   . THR C 3 184 ? -0.38603  -63.89595 37.73689  1.000 231.73968 ? 184 THR C N   1 
ATOM   5714 C CA  . THR C 3 184 ? 0.08675   -64.33572 39.04059  1.000 234.65772 ? 184 THR C CA  1 
ATOM   5715 C C   . THR C 3 184 ? -0.05787  -65.85314 39.14825  1.000 237.50076 ? 184 THR C C   1 
ATOM   5716 O O   . THR C 3 184 ? -0.85057  -66.47272 38.43564  1.000 238.30503 ? 184 THR C O   1 
ATOM   5717 C CB  . THR C 3 184 ? -0.69838  -63.64143 40.15868  1.000 236.61926 ? 184 THR C CB  1 
ATOM   5718 O OG1 . THR C 3 184 ? -0.84550  -62.25032 39.84829  1.000 234.43504 ? 184 THR C OG1 1 
ATOM   5719 C CG2 . THR C 3 184 ? 0.00835   -63.77482 41.50120  1.000 237.35595 ? 184 THR C CG2 1 
ATOM   5720 N N   . SER C 3 185 ? 0.74001   -66.45246 40.03748  1.000 237.92361 ? 185 SER C N   1 
ATOM   5721 C CA  . SER C 3 185 ? 0.67875   -67.89909 40.23353  1.000 240.92133 ? 185 SER C CA  1 
ATOM   5722 C C   . SER C 3 185 ? -0.70847  -68.33931 40.67795  1.000 243.95492 ? 185 SER C C   1 
ATOM   5723 O O   . SER C 3 185 ? -1.30595  -69.24399 40.08687  1.000 245.06607 ? 185 SER C O   1 
ATOM   5724 C CB  . SER C 3 185 ? 1.71781   -68.34159 41.26049  1.000 241.99893 ? 185 SER C CB  1 
ATOM   5725 O OG  . SER C 3 185 ? 1.56153   -67.64905 42.48767  1.000 242.00074 ? 185 SER C OG  1 
ATOM   5726 N N   . ASP C 3 186 ? -1.22798  -67.72430 41.73742  1.000 240.07367 ? 186 ASP C N   1 
ATOM   5727 C CA  . ASP C 3 186 ? -2.54028  -68.11582 42.23152  1.000 243.59443 ? 186 ASP C CA  1 
ATOM   5728 C C   . ASP C 3 186 ? -3.65116  -67.58264 41.33749  1.000 243.97795 ? 186 ASP C C   1 
ATOM   5729 O O   . ASP C 3 186 ? -4.75483  -68.14383 41.30940  1.000 246.79737 ? 186 ASP C O   1 
ATOM   5730 C CB  . ASP C 3 186 ? -2.72111  -67.63921 43.67116  1.000 245.26503 ? 186 ASP C CB  1 
ATOM   5731 C CG  . ASP C 3 186 ? -4.03914  -68.08253 44.27271  1.000 249.63330 ? 186 ASP C CG  1 
ATOM   5732 O OD1 . ASP C 3 186 ? -4.26293  -69.30859 44.41250  1.000 251.19930 ? 186 ASP C OD1 1 
ATOM   5733 O OD2 . ASP C 3 186 ? -4.84819  -67.20128 44.62415  1.000 251.72403 ? 186 ASP C OD2 1 
ATOM   5734 N N   . GLN C 3 187 ? -3.37627  -66.51454 40.59226  1.000 244.25580 ? 187 GLN C N   1 
ATOM   5735 C CA  . GLN C 3 187 ? -4.39583  -65.91134 39.74447  1.000 244.55940 ? 187 GLN C CA  1 
ATOM   5736 C C   . GLN C 3 187 ? -4.65304  -66.72493 38.48116  1.000 242.61419 ? 187 GLN C C   1 
ATOM   5737 O O   . GLN C 3 187 ? -5.74570  -66.63280 37.90975  1.000 243.81770 ? 187 GLN C O   1 
ATOM   5738 C CB  . GLN C 3 187 ? -3.98870  -64.48318 39.38027  1.000 241.24679 ? 187 GLN C CB  1 
ATOM   5739 C CG  . GLN C 3 187 ? -5.08807  -63.64359 38.76249  1.000 242.08155 ? 187 GLN C CG  1 
ATOM   5740 C CD  . GLN C 3 187 ? -4.60265  -62.26628 38.34764  1.000 238.70845 ? 187 GLN C CD  1 
ATOM   5741 O OE1 . GLN C 3 187 ? -3.67667  -61.71972 38.94409  1.000 236.75789 ? 187 GLN C OE1 1 
ATOM   5742 N NE2 . GLN C 3 187 ? -5.21607  -61.70606 37.30919  1.000 237.94863 ? 187 GLN C NE2 1 
ATOM   5743 N N   . TRP C 3 188 ? -3.68269  -67.52753 38.03971  1.000 240.22974 ? 188 TRP C N   1 
ATOM   5744 C CA  . TRP C 3 188 ? -3.90794  -68.37861 36.87649  1.000 240.83960 ? 188 TRP C CA  1 
ATOM   5745 C C   . TRP C 3 188 ? -4.84109  -69.53188 37.22245  1.000 245.11757 ? 188 TRP C C   1 
ATOM   5746 O O   . TRP C 3 188 ? -5.86925  -69.73391 36.56657  1.000 246.75028 ? 188 TRP C O   1 
ATOM   5747 C CB  . TRP C 3 188 ? -2.57868  -68.90311 36.32875  1.000 240.31413 ? 188 TRP C CB  1 
ATOM   5748 C CG  . TRP C 3 188 ? -2.75319  -69.80304 35.13932  1.000 242.28469 ? 188 TRP C CG  1 
ATOM   5749 C CD1 . TRP C 3 188 ? -3.03486  -69.42366 33.85906  1.000 241.44341 ? 188 TRP C CD1 1 
ATOM   5750 C CD2 . TRP C 3 188 ? -2.66134  -71.23324 35.12157  1.000 245.83509 ? 188 TRP C CD2 1 
ATOM   5751 N NE1 . TRP C 3 188 ? -3.12302  -70.52765 33.04597  1.000 244.43992 ? 188 TRP C NE1 1 
ATOM   5752 C CE2 . TRP C 3 188 ? -2.89709  -71.65092 33.79687  1.000 247.37297 ? 188 TRP C CE2 1 
ATOM   5753 C CE3 . TRP C 3 188 ? -2.39901  -72.19981 36.09558  1.000 248.54243 ? 188 TRP C CE3 1 
ATOM   5754 C CZ2 . TRP C 3 188 ? -2.88013  -72.99321 33.42301  1.000 251.63546 ? 188 TRP C CZ2 1 
ATOM   5755 C CZ3 . TRP C 3 188 ? -2.38461  -73.53215 35.72326  1.000 251.29766 ? 188 TRP C CZ3 1 
ATOM   5756 C CH2 . TRP C 3 188 ? -2.62022  -73.91585 34.39839  1.000 252.97247 ? 188 TRP C CH2 1 
ATOM   5757 N N   . ARG C 3 189 ? -4.50201  -70.29741 38.26254  1.000 245.43697 ? 189 ARG C N   1 
ATOM   5758 C CA  . ARG C 3 189 ? -5.37391  -71.37026 38.72577  1.000 248.92022 ? 189 ARG C CA  1 
ATOM   5759 C C   . ARG C 3 189 ? -6.67405  -70.85243 39.32605  1.000 251.01860 ? 189 ARG C C   1 
ATOM   5760 O O   . ARG C 3 189 ? -7.56400  -71.65816 39.61874  1.000 253.54556 ? 189 ARG C O   1 
ATOM   5761 C CB  . ARG C 3 189 ? -4.63746  -72.24261 39.74674  1.000 248.83120 ? 189 ARG C CB  1 
ATOM   5762 C CG  . ARG C 3 189 ? -3.56903  -73.12863 39.12671  1.000 248.09908 ? 189 ARG C CG  1 
ATOM   5763 C CD  . ARG C 3 189 ? -2.78740  -73.92647 40.15715  1.000 249.50372 ? 189 ARG C CD  1 
ATOM   5764 N NE  . ARG C 3 189 ? -1.80437  -74.79286 39.51602  1.000 249.73881 ? 189 ARG C NE  1 
ATOM   5765 C CZ  . ARG C 3 189 ? -0.93219  -75.55235 40.16473  1.000 250.02025 ? 189 ARG C CZ  1 
ATOM   5766 N NH1 . ARG C 3 189 ? -0.88412  -75.57557 41.48649  1.000 251.09041 ? 189 ARG C NH1 1 
ATOM   5767 N NH2 . ARG C 3 189 ? -0.08569  -76.30673 39.46925  1.000 249.58654 ? 189 ARG C NH2 1 
ATOM   5768 N N   . SER C 3 190 ? -6.80183  -69.53702 39.51407  1.000 251.70062 ? 190 SER C N   1 
ATOM   5769 C CA  . SER C 3 190 ? -8.04471  -68.96971 40.02534  1.000 254.93720 ? 190 SER C CA  1 
ATOM   5770 C C   . SER C 3 190 ? -9.19278  -69.19210 39.04753  1.000 256.12621 ? 190 SER C C   1 
ATOM   5771 O O   . SER C 3 190 ? -10.26291 -69.68093 39.42822  1.000 259.71073 ? 190 SER C O   1 
ATOM   5772 C CB  . SER C 3 190 ? -7.85760  -67.47909 40.30715  1.000 253.93016 ? 190 SER C CB  1 
ATOM   5773 O OG  . SER C 3 190 ? -9.10815  -66.83026 40.45365  1.000 257.20622 ? 190 SER C OG  1 
ATOM   5774 N N   . HIS C 3 191 ? -8.98670  -68.83908 37.78202  1.000 253.46840 ? 191 HIS C N   1 
ATOM   5775 C CA  . HIS C 3 191 ? -9.99198  -68.98754 36.74382  1.000 254.33047 ? 191 HIS C CA  1 
ATOM   5776 C C   . HIS C 3 191 ? -9.63826  -70.16571 35.84509  1.000 253.58031 ? 191 HIS C C   1 
ATOM   5777 O O   . HIS C 3 191 ? -8.46324  -70.45113 35.60185  1.000 250.19216 ? 191 HIS C O   1 
ATOM   5778 C CB  . HIS C 3 191 ? -10.11348 -67.70655 35.91251  1.000 252.32032 ? 191 HIS C CB  1 
ATOM   5779 C CG  . HIS C 3 191 ? -10.30254 -66.47123 36.73682  1.000 253.33105 ? 191 HIS C CG  1 
ATOM   5780 N ND1 . HIS C 3 191 ? -9.31422  -65.52380 36.89511  1.000 250.22330 ? 191 HIS C ND1 1 
ATOM   5781 C CD2 . HIS C 3 191 ? -11.36224 -66.03286 37.45707  1.000 257.71576 ? 191 HIS C CD2 1 
ATOM   5782 C CE1 . HIS C 3 191 ? -9.75861  -64.55208 37.67192  1.000 252.60692 ? 191 HIS C CE1 1 
ATOM   5783 N NE2 . HIS C 3 191 ? -10.99849 -64.83692 38.02708  1.000 257.60253 ? 191 HIS C NE2 1 
ATOM   5784 N N   . ASN C 3 192 ? -10.66641 -70.85552 35.35381  1.000 253.77084 ? 192 ASN C N   1 
ATOM   5785 C CA  . ASN C 3 192 ? -10.48583 -72.05505 34.54513  1.000 254.21698 ? 192 ASN C CA  1 
ATOM   5786 C C   . ASN C 3 192 ? -10.95261 -71.86059 33.10548  1.000 252.57725 ? 192 ASN C C   1 
ATOM   5787 O O   . ASN C 3 192 ? -11.48885 -72.78038 32.48271  1.000 255.22103 ? 192 ASN C O   1 
ATOM   5788 C CB  . ASN C 3 192 ? -11.19146 -73.25154 35.17753  1.000 257.19888 ? 192 ASN C CB  1 
ATOM   5789 C CG  . ASN C 3 192 ? -12.65377 -72.98169 35.48086  1.000 259.65034 ? 192 ASN C CG  1 
ATOM   5790 O OD1 . ASN C 3 192 ? -13.25264 -72.04784 34.94671  1.000 259.86369 ? 192 ASN C OD1 1 
ATOM   5791 N ND2 . ASN C 3 192 ? -13.23826 -73.80648 36.34131  1.000 261.75827 ? 192 ASN C ND2 1 
ATOM   5792 N N   . SER C 3 193 ? -10.74173 -70.66853 32.55359  1.000 249.16801 ? 193 SER C N   1 
ATOM   5793 C CA  . SER C 3 193 ? -11.12771 -70.39689 31.17218  1.000 248.35671 ? 193 SER C CA  1 
ATOM   5794 C C   . SER C 3 193 ? -10.31098 -69.22662 30.65007  1.000 244.40182 ? 193 SER C C   1 
ATOM   5795 O O   . SER C 3 193 ? -10.42496 -68.11073 31.16626  1.000 243.04955 ? 193 SER C O   1 
ATOM   5796 C CB  . SER C 3 193 ? -12.62323 -70.10430 31.07380  1.000 250.35797 ? 193 SER C CB  1 
ATOM   5797 O OG  . SER C 3 193 ? -12.96732 -69.64839 29.77810  1.000 249.32418 ? 193 SER C OG  1 
ATOM   5798 N N   . PHE C 3 194 ? -9.48367  -69.48434 29.63879  1.000 249.31101 ? 194 PHE C N   1 
ATOM   5799 C CA  . PHE C 3 194 ? -8.69724  -68.46390 28.96044  1.000 245.38030 ? 194 PHE C CA  1 
ATOM   5800 C C   . PHE C 3 194 ? -8.82142  -68.67136 27.45887  1.000 245.74332 ? 194 PHE C C   1 
ATOM   5801 O O   . PHE C 3 194 ? -8.75265  -69.80611 26.97739  1.000 249.04930 ? 194 PHE C O   1 
ATOM   5802 C CB  . PHE C 3 194 ? -7.21994  -68.52036 29.36688  1.000 243.91181 ? 194 PHE C CB  1 
ATOM   5803 C CG  . PHE C 3 194 ? -6.99953  -68.72117 30.83719  1.000 244.33288 ? 194 PHE C CG  1 
ATOM   5804 C CD1 . PHE C 3 194 ? -6.92818  -67.63751 31.69566  1.000 242.02127 ? 194 PHE C CD1 1 
ATOM   5805 C CD2 . PHE C 3 194 ? -6.85648  -69.99588 31.36020  1.000 247.65943 ? 194 PHE C CD2 1 
ATOM   5806 C CE1 . PHE C 3 194 ? -6.72330  -67.82134 33.04804  1.000 243.33744 ? 194 PHE C CE1 1 
ATOM   5807 C CE2 . PHE C 3 194 ? -6.65230  -70.18605 32.71104  1.000 248.52611 ? 194 PHE C CE2 1 
ATOM   5808 C CZ  . PHE C 3 194 ? -6.58451  -69.09701 33.55570  1.000 246.54863 ? 194 PHE C CZ  1 
ATOM   5809 N N   . THR C 3 195 ? -9.00079  -67.57765 26.71724  1.000 235.36075 ? 195 THR C N   1 
ATOM   5810 C CA  . THR C 3 195 ? -9.26064  -67.65898 25.28552  1.000 236.60470 ? 195 THR C CA  1 
ATOM   5811 C C   . THR C 3 195 ? -8.54069  -66.53394 24.55150  1.000 232.37903 ? 195 THR C C   1 
ATOM   5812 O O   . THR C 3 195 ? -8.28964  -65.46403 25.11265  1.000 227.75079 ? 195 THR C O   1 
ATOM   5813 C CB  . THR C 3 195 ? -10.76794 -67.59961 24.98082  1.000 238.59892 ? 195 THR C CB  1 
ATOM   5814 O OG1 . THR C 3 195 ? -11.33594 -66.43215 25.58275  1.000 236.74415 ? 195 THR C OG1 1 
ATOM   5815 C CG2 . THR C 3 195 ? -11.48293 -68.83039 25.52458  1.000 242.75027 ? 195 THR C CG2 1 
ATOM   5816 N N   . CYS C 3 196 ? -8.21687  -66.78909 23.28220  1.000 230.68750 ? 196 CYS C N   1 
ATOM   5817 C CA  . CYS C 3 196 ? -7.51094  -65.84026 22.42248  1.000 226.29262 ? 196 CYS C CA  1 
ATOM   5818 C C   . CYS C 3 196 ? -8.26892  -65.74545 21.10368  1.000 227.64711 ? 196 CYS C C   1 
ATOM   5819 O O   . CYS C 3 196 ? -8.20924  -66.66908 20.28562  1.000 231.73694 ? 196 CYS C O   1 
ATOM   5820 C CB  . CYS C 3 196 ? -6.05877  -66.27953 22.19268  1.000 228.51136 ? 196 CYS C CB  1 
ATOM   5821 S SG  . CYS C 3 196 ? -5.03381  -65.15352 21.18986  1.000 225.50166 ? 196 CYS C SG  1 
ATOM   5822 N N   . GLN C 3 197 ? -8.98744  -64.64298 20.89715  1.000 228.13868 ? 197 GLN C N   1 
ATOM   5823 C CA  . GLN C 3 197 ? -9.75413  -64.42537 19.67620  1.000 229.80217 ? 197 GLN C CA  1 
ATOM   5824 C C   . GLN C 3 197 ? -9.07048  -63.36338 18.82408  1.000 224.45826 ? 197 GLN C C   1 
ATOM   5825 O O   . GLN C 3 197 ? -8.68104  -62.30554 19.33169  1.000 219.26558 ? 197 GLN C O   1 
ATOM   5826 C CB  . GLN C 3 197 ? -11.20188 -64.02321 19.98607  1.000 231.89734 ? 197 GLN C CB  1 
ATOM   5827 C CG  . GLN C 3 197 ? -11.36593 -62.74283 20.78909  1.000 228.58680 ? 197 GLN C CG  1 
ATOM   5828 C CD  . GLN C 3 197 ? -12.81257 -62.29287 20.88076  1.000 231.44192 ? 197 GLN C CD  1 
ATOM   5829 O OE1 . GLN C 3 197 ? -13.73454 -63.08545 20.68809  1.000 236.96706 ? 197 GLN C OE1 1 
ATOM   5830 N NE2 . GLN C 3 197 ? -13.01762 -61.01251 21.17036  1.000 230.52688 ? 197 GLN C NE2 1 
ATOM   5831 N N   . VAL C 3 198 ? -8.91596  -63.65483 17.53409  1.000 226.18454 ? 198 VAL C N   1 
ATOM   5832 C CA  . VAL C 3 198 ? -8.23455  -62.77284 16.59138  1.000 223.24382 ? 198 VAL C CA  1 
ATOM   5833 C C   . VAL C 3 198 ? -9.24540  -62.33024 15.54339  1.000 225.39253 ? 198 VAL C C   1 
ATOM   5834 O O   . VAL C 3 198 ? -9.78791  -63.16356 14.80745  1.000 231.24556 ? 198 VAL C O   1 
ATOM   5835 C CB  . VAL C 3 198 ? -7.03249  -63.46260 15.92686  1.000 226.50152 ? 198 VAL C CB  1 
ATOM   5836 C CG1 . VAL C 3 198 ? -6.05109  -62.42697 15.39196  1.000 218.82206 ? 198 VAL C CG1 1 
ATOM   5837 C CG2 . VAL C 3 198 ? -6.35088  -64.41346 16.89971  1.000 230.95952 ? 198 VAL C CG2 1 
ATOM   5838 N N   . THR C 3 199 ? -9.49117  -61.02431 15.46864  1.000 230.47336 ? 199 THR C N   1 
ATOM   5839 C CA  . THR C 3 199 ? -10.41564 -60.46032 14.48544  1.000 232.95719 ? 199 THR C CA  1 
ATOM   5840 C C   . THR C 3 199 ? -9.64979  -60.24887 13.18484  1.000 228.61750 ? 199 THR C C   1 
ATOM   5841 O O   . THR C 3 199 ? -8.94596  -59.24987 13.01810  1.000 224.63143 ? 199 THR C O   1 
ATOM   5842 C CB  . THR C 3 199 ? -11.02589 -59.16001 14.99645  1.000 232.02540 ? 199 THR C CB  1 
ATOM   5843 O OG1 . THR C 3 199 ? -11.73552 -59.41220 16.21585  1.000 233.61287 ? 199 THR C OG1 1 
ATOM   5844 C CG2 . THR C 3 199 ? -11.98784 -58.58217 13.96852  1.000 233.68732 ? 199 THR C CG2 1 
ATOM   5845 N N   . HIS C 3 200 ? -9.78396  -61.19633 12.26035  1.000 227.00209 ? 200 HIS C N   1 
ATOM   5846 C CA  . HIS C 3 200 ? -9.07374  -61.17623 10.98378  1.000 230.67064 ? 200 HIS C CA  1 
ATOM   5847 C C   . HIS C 3 200 ? -10.07995 -60.83320 9.88772   1.000 234.47781 ? 200 HIS C C   1 
ATOM   5848 O O   . HIS C 3 200 ? -10.64445 -61.71278 9.23558   1.000 238.86936 ? 200 HIS C O   1 
ATOM   5849 C CB  . HIS C 3 200 ? -8.38594  -62.52983 10.72872  1.000 232.82967 ? 200 HIS C CB  1 
ATOM   5850 C CG  . HIS C 3 200 ? -7.40404  -62.51200 9.59775   1.000 240.24420 ? 200 HIS C CG  1 
ATOM   5851 N ND1 . HIS C 3 200 ? -7.72049  -62.04292 8.34092   1.000 239.39519 ? 200 HIS C ND1 1 
ATOM   5852 C CD2 . HIS C 3 200 ? -6.11442  -62.92001 9.53232   1.000 242.59480 ? 200 HIS C CD2 1 
ATOM   5853 C CE1 . HIS C 3 200 ? -6.66628  -62.15486 7.55269   1.000 241.13956 ? 200 HIS C CE1 1 
ATOM   5854 N NE2 . HIS C 3 200 ? -5.67873  -62.68547 8.25090   1.000 244.53345 ? 200 HIS C NE2 1 
ATOM   5855 N N   . GLU C 3 201 ? -10.30487 -59.53107 9.69426   1.000 243.50952 ? 201 GLU C N   1 
ATOM   5856 C CA  . GLU C 3 201 ? -11.18603 -59.01799 8.64216   1.000 244.61657 ? 201 GLU C CA  1 
ATOM   5857 C C   . GLU C 3 201 ? -12.62150 -59.51226 8.80320   1.000 248.55384 ? 201 GLU C C   1 
ATOM   5858 O O   . GLU C 3 201 ? -13.34880 -59.66887 7.81931   1.000 250.26383 ? 201 GLU C O   1 
ATOM   5859 C CB  . GLU C 3 201 ? -10.65544 -59.37609 7.25023   1.000 246.82865 ? 201 GLU C CB  1 
ATOM   5860 C CG  . GLU C 3 201 ? -9.25445  -58.86588 6.96813   1.000 244.51999 ? 201 GLU C CG  1 
ATOM   5861 C CD  . GLU C 3 201 ? -8.68017  -59.42711 5.68294   1.000 246.86003 ? 201 GLU C CD  1 
ATOM   5862 O OE1 . GLU C 3 201 ? -8.62031  -60.66760 5.54664   1.000 252.64796 ? 201 GLU C OE1 1 
ATOM   5863 O OE2 . GLU C 3 201 ? -8.29746  -58.62665 4.80481   1.000 243.21985 ? 201 GLU C OE2 1 
ATOM   5864 N N   . GLY C 3 202 ? -13.04282 -59.75734 10.04081  1.000 233.39133 ? 202 GLY C N   1 
ATOM   5865 C CA  . GLY C 3 202 ? -14.38349 -60.24334 10.29790  1.000 237.55864 ? 202 GLY C CA  1 
ATOM   5866 C C   . GLY C 3 202 ? -14.39707 -61.61671 10.93237  1.000 239.51592 ? 202 GLY C C   1 
ATOM   5867 O O   . GLY C 3 202 ? -15.22910 -61.90145 11.79853  1.000 241.55489 ? 202 GLY C O   1 
ATOM   5868 N N   . ASN C 3 203 ? -13.47823 -62.47871 10.50605  1.000 241.20638 ? 203 ASN C N   1 
ATOM   5869 C CA  . ASN C 3 203 ? -13.35782 -63.81779 11.07162  1.000 245.91699 ? 203 ASN C CA  1 
ATOM   5870 C C   . ASN C 3 203 ? -12.67202 -63.72121 12.42790  1.000 244.04800 ? 203 ASN C C   1 
ATOM   5871 O O   . ASN C 3 203 ? -11.49586 -63.35432 12.51146  1.000 241.97461 ? 203 ASN C O   1 
ATOM   5872 C CB  . ASN C 3 203 ? -12.57678 -64.72874 10.13010  1.000 249.82801 ? 203 ASN C CB  1 
ATOM   5873 C CG  . ASN C 3 203 ? -13.27823 -64.93298 8.80401   1.000 252.35756 ? 203 ASN C CG  1 
ATOM   5874 O OD1 . ASN C 3 203 ? -14.50330 -65.03716 8.74677   1.000 253.57500 ? 203 ASN C OD1 1 
ATOM   5875 N ND2 . ASN C 3 203 ? -12.50335 -64.99081 7.72744   1.000 253.41563 ? 203 ASN C ND2 1 
ATOM   5876 N N   . THR C 3 204 ? -13.40332 -64.04547 13.49393  1.000 242.28364 ? 204 THR C N   1 
ATOM   5877 C CA  . THR C 3 204 ? -12.85282 -64.02348 14.84776  1.000 239.47903 ? 204 THR C CA  1 
ATOM   5878 C C   . THR C 3 204 ? -12.52194 -65.45567 15.26174  1.000 243.04561 ? 204 THR C C   1 
ATOM   5879 O O   . THR C 3 204 ? -13.24826 -66.10242 16.01634  1.000 245.58775 ? 204 THR C O   1 
ATOM   5880 C CB  . THR C 3 204 ? -13.82634 -63.36061 15.81899  1.000 238.47490 ? 204 THR C CB  1 
ATOM   5881 O OG1 . THR C 3 204 ? -15.05655 -64.09561 15.84664  1.000 243.76114 ? 204 THR C OG1 1 
ATOM   5882 C CG2 . THR C 3 204 ? -14.10510 -61.92644 15.39379  1.000 233.72831 ? 204 THR C CG2 1 
ATOM   5883 N N   . VAL C 3 205 ? -11.39482 -65.95301 14.74586  1.000 232.22429 ? 205 VAL C N   1 
ATOM   5884 C CA  . VAL C 3 205 ? -10.91077 -67.27540 15.12482  1.000 237.09923 ? 205 VAL C CA  1 
ATOM   5885 C C   . VAL C 3 205 ? -10.47763 -67.25310 16.58676  1.000 234.95341 ? 205 VAL C C   1 
ATOM   5886 O O   . VAL C 3 205 ? -9.98688  -66.23777 17.09711  1.000 230.78045 ? 205 VAL C O   1 
ATOM   5887 C CB  . VAL C 3 205 ? -9.75659  -67.70880 14.20207  1.000 240.58434 ? 205 VAL C CB  1 
ATOM   5888 C CG1 . VAL C 3 205 ? -9.49386  -69.20044 14.33271  1.000 248.85522 ? 205 VAL C CG1 1 
ATOM   5889 C CG2 . VAL C 3 205 ? -10.06305 -67.33574 12.75694  1.000 241.92572 ? 205 VAL C CG2 1 
ATOM   5890 N N   . GLU C 3 206 ? -10.65405 -68.38199 17.27253  1.000 229.83149 ? 206 GLU C N   1 
ATOM   5891 C CA  . GLU C 3 206 ? -10.49619 -68.40423 18.71968  1.000 228.11404 ? 206 GLU C CA  1 
ATOM   5892 C C   . GLU C 3 206 ? -10.07204 -69.79102 19.19047  1.000 233.11341 ? 206 GLU C C   1 
ATOM   5893 O O   . GLU C 3 206 ? -10.50068 -70.80539 18.63347  1.000 238.50780 ? 206 GLU C O   1 
ATOM   5894 C CB  . GLU C 3 206 ? -11.80422 -67.96725 19.39589  1.000 228.66319 ? 206 GLU C CB  1 
ATOM   5895 C CG  . GLU C 3 206 ? -11.78001 -67.95923 20.91199  1.000 227.81028 ? 206 GLU C CG  1 
ATOM   5896 C CD  . GLU C 3 206 ? -12.17311 -69.29708 21.50036  1.000 230.94478 ? 206 GLU C CD  1 
ATOM   5897 O OE1 . GLU C 3 206 ? -13.01349 -69.98983 20.88972  1.000 235.43477 ? 206 GLU C OE1 1 
ATOM   5898 O OE2 . GLU C 3 206 ? -11.63342 -69.66261 22.56239  1.000 229.75580 ? 206 GLU C OE2 1 
ATOM   5899 N N   . LYS C 3 207 ? -9.22488  -69.81854 20.22269  1.000 232.52551 ? 207 LYS C N   1 
ATOM   5900 C CA  . LYS C 3 207 ? -8.77818  -71.04950 20.86433  1.000 237.74804 ? 207 LYS C CA  1 
ATOM   5901 C C   . LYS C 3 207 ? -8.74808  -70.84152 22.37438  1.000 234.86175 ? 207 LYS C C   1 
ATOM   5902 O O   . LYS C 3 207 ? -8.86868  -69.71754 22.86669  1.000 229.51267 ? 207 LYS C O   1 
ATOM   5903 C CB  . LYS C 3 207 ? -7.40022  -71.48848 20.35733  1.000 242.62008 ? 207 LYS C CB  1 
ATOM   5904 C CG  . LYS C 3 207 ? -7.42543  -72.22525 19.03206  1.000 248.60061 ? 207 LYS C CG  1 
ATOM   5905 C CD  . LYS C 3 207 ? -6.14514  -73.01900 18.84885  1.000 252.78276 ? 207 LYS C CD  1 
ATOM   5906 C CE  . LYS C 3 207 ? -5.91615  -73.94800 20.03144  1.000 254.23436 ? 207 LYS C CE  1 
ATOM   5907 N NZ  . LYS C 3 207 ? -4.56404  -74.56943 20.01076  1.000 257.38492 ? 207 LYS C NZ  1 
ATOM   5908 N N   . THR C 3 208 ? -8.56518  -71.93516 23.11748  1.000 250.60495 ? 208 THR C N   1 
ATOM   5909 C CA  . THR C 3 208 ? -8.73943  -71.89116 24.56469  1.000 248.43266 ? 208 THR C CA  1 
ATOM   5910 C C   . THR C 3 208 ? -7.80306  -72.87355 25.25961  1.000 251.44636 ? 208 THR C C   1 
ATOM   5911 O O   . THR C 3 208 ? -7.24627  -73.78213 24.63779  1.000 256.42846 ? 208 THR C O   1 
ATOM   5912 C CB  . THR C 3 208 ? -10.18977 -72.20004 24.95486  1.000 231.86975 ? 208 THR C CB  1 
ATOM   5913 O OG1 . THR C 3 208 ? -10.32580 -72.15026 26.38030  1.000 231.96337 ? 208 THR C OG1 1 
ATOM   5914 C CG2 . THR C 3 208 ? -10.58907 -73.58292 24.45792  1.000 242.58382 ? 208 THR C CG2 1 
ATOM   5915 N N   . VAL C 3 209 ? -7.64931  -72.67670 26.57575  1.000 254.27573 ? 209 VAL C N   1 
ATOM   5916 C CA  . VAL C 3 209 ? -6.87071  -73.54940 27.45272  1.000 256.02168 ? 209 VAL C CA  1 
ATOM   5917 C C   . VAL C 3 209 ? -7.57835  -73.64031 28.80138  1.000 254.64417 ? 209 VAL C C   1 
ATOM   5918 O O   . VAL C 3 209 ? -8.54199  -72.92154 29.07239  1.000 252.17166 ? 209 VAL C O   1 
ATOM   5919 C CB  . VAL C 3 209 ? -5.42054  -73.05544 27.64937  1.000 230.26533 ? 209 VAL C CB  1 
ATOM   5920 C CG1 . VAL C 3 209 ? -4.58981  -73.31289 26.40520  1.000 231.18287 ? 209 VAL C CG1 1 
ATOM   5921 C CG2 . VAL C 3 209 ? -5.40659  -71.57737 28.01235  1.000 221.61224 ? 209 VAL C CG2 1 
ATOM   5922 N N   . SER C 3 210 ? -7.07711  -74.53458 29.66246  1.000 249.50316 ? 210 SER C N   1 
ATOM   5923 C CA  . SER C 3 210 ? -7.68270  -74.74950 30.97597  1.000 248.70083 ? 210 SER C CA  1 
ATOM   5924 C C   . SER C 3 210 ? -6.65462  -75.22477 31.99401  1.000 248.75470 ? 210 SER C C   1 
ATOM   5925 O O   . SER C 3 210 ? -5.74070  -75.98183 31.63537  1.000 250.98954 ? 210 SER C O   1 
ATOM   5926 C CB  . SER C 3 210 ? -8.82744  -75.76482 30.89730  1.000 252.28524 ? 210 SER C CB  1 
ATOM   5927 O OG  . SER C 3 210 ? -8.34155  -77.05900 30.58784  1.000 256.13900 ? 210 SER C OG  1 
ATOM   5928 N N   . PRO C 3 211 ? -6.77571  -74.80261 33.25592  1.000 250.04030 ? 211 PRO C N   1 
ATOM   5929 C CA  . PRO C 3 211 ? -5.82700  -75.25901 34.28542  1.000 249.87472 ? 211 PRO C CA  1 
ATOM   5930 C C   . PRO C 3 211 ? -5.86527  -76.75347 34.54931  1.000 253.54137 ? 211 PRO C C   1 
ATOM   5931 O O   . PRO C 3 211 ? -4.86999  -77.30129 35.03909  1.000 253.90776 ? 211 PRO C O   1 
ATOM   5932 C CB  . PRO C 3 211 ? -6.25201  -74.46497 35.52882  1.000 247.14046 ? 211 PRO C CB  1 
ATOM   5933 C CG  . PRO C 3 211 ? -6.92753  -73.25767 34.99021  1.000 245.20808 ? 211 PRO C CG  1 
ATOM   5934 C CD  . PRO C 3 211 ? -7.62661  -73.70627 33.73948  1.000 247.16135 ? 211 PRO C CD  1 
ATOM   5935 N N   . THR C 3 212 ? -6.97352  -77.43058 34.26219  1.000 246.28731 ? 212 THR C N   1 
ATOM   5936 C CA  . THR C 3 212 ? -7.03840  -78.88298 34.41057  1.000 249.07830 ? 212 THR C CA  1 
ATOM   5937 C C   . THR C 3 212 ? -6.40585  -79.50753 33.17404  1.000 251.75128 ? 212 THR C C   1 
ATOM   5938 O O   . THR C 3 212 ? -7.06278  -79.68967 32.14704  1.000 253.73831 ? 212 THR C O   1 
ATOM   5939 C CB  . THR C 3 212 ? -8.47589  -79.34967 34.60460  1.000 243.71886 ? 212 THR C CB  1 
ATOM   5940 O OG1 . THR C 3 212 ? -9.30406  -78.80808 33.56851  1.000 242.41757 ? 212 THR C OG1 1 
ATOM   5941 C CG2 . THR C 3 212 ? -9.00100  -78.89682 35.96149  1.000 243.47992 ? 212 THR C CG2 1 
ATOM   5942 N N   . GLU C 3 213 ? -5.11916  -79.83161 33.27309  1.000 255.35129 ? 213 GLU C N   1 
ATOM   5943 C CA  . GLU C 3 213 ? -4.33105  -80.32817 32.15819  1.000 259.79615 ? 213 GLU C CA  1 
ATOM   5944 C C   . GLU C 3 213 ? -3.69726  -81.66120 32.53329  1.000 265.09177 ? 213 GLU C C   1 
ATOM   5945 O O   . GLU C 3 213 ? -3.68084  -82.06301 33.69981  1.000 263.41446 ? 213 GLU C O   1 
ATOM   5946 C CB  . GLU C 3 213 ? -3.24822  -79.31610 31.76141  1.000 257.56820 ? 213 GLU C CB  1 
ATOM   5947 C CG  . GLU C 3 213 ? -2.33693  -78.93089 32.91857  1.000 254.62967 ? 213 GLU C CG  1 
ATOM   5948 C CD  . GLU C 3 213 ? -1.38757  -77.80200 32.57503  1.000 251.96680 ? 213 GLU C CD  1 
ATOM   5949 O OE1 . GLU C 3 213 ? -1.36977  -77.37152 31.40353  1.000 253.37133 ? 213 GLU C OE1 1 
ATOM   5950 O OE2 . GLU C 3 213 ? -0.65990  -77.34288 33.48073  1.000 248.87665 ? 213 GLU C OE2 1 
ATOM   5951 N N   . CYS C 3 214 ? -3.16638  -82.34945 31.52489  1.000 253.20764 ? 214 CYS C N   1 
ATOM   5952 C CA  . CYS C 3 214 ? -2.46267  -83.60071 31.76633  1.000 256.69778 ? 214 CYS C CA  1 
ATOM   5953 C C   . CYS C 3 214 ? -1.12973  -83.32738 32.45248  1.000 254.65686 ? 214 CYS C C   1 
ATOM   5954 O O   . CYS C 3 214 ? -0.38097  -82.43051 32.05203  1.000 254.08509 ? 214 CYS C O   1 
ATOM   5955 C CB  . CYS C 3 214 ? -2.24299  -84.35244 30.45411  1.000 262.83957 ? 214 CYS C CB  1 
ATOM   5956 S SG  . CYS C 3 214 ? -3.75481  -84.99677 29.69834  1.000 266.22249 ? 214 CYS C SG  1 
ATOM   5957 N N   . VAL C 3 215 ? -0.83433  -84.10603 33.49130  1.000 257.35647 ? 215 VAL C N   1 
ATOM   5958 C CA  . VAL C 3 215 ? 0.37581   -83.93302 34.28112  1.000 255.26464 ? 215 VAL C CA  1 
ATOM   5959 C C   . VAL C 3 215 ? 1.17480   -85.23004 34.25807  1.000 258.96420 ? 215 VAL C C   1 
ATOM   5960 O O   . VAL C 3 215 ? 0.66846   -86.29720 33.90059  1.000 262.60751 ? 215 VAL C O   1 
ATOM   5961 C CB  . VAL C 3 215 ? 0.06778   -83.50771 35.73226  1.000 250.33858 ? 215 VAL C CB  1 
ATOM   5962 C CG1 . VAL C 3 215 ? -0.69883  -82.19626 35.75277  1.000 247.22814 ? 215 VAL C CG1 1 
ATOM   5963 C CG2 . VAL C 3 215 ? -0.71190  -84.59944 36.46110  1.000 250.72481 ? 215 VAL C CG2 1 
ATOM   5964 N N   . ALA C 3 216 ? 2.44137   -85.12073 34.65609  1.000 243.43802 ? 216 ALA C N   1 
ATOM   5965 C CA  . ALA C 3 216 ? 3.35163   -86.26233 34.74858  1.000 246.52350 ? 216 ALA C CA  1 
ATOM   5966 C C   . ALA C 3 216 ? 3.43078   -87.04232 33.43754  1.000 252.97897 ? 216 ALA C C   1 
ATOM   5967 O O   . ALA C 3 216 ? 3.45877   -86.45393 32.35589  1.000 255.06008 ? 216 ALA C O   1 
ATOM   5968 C CB  . ALA C 3 216 ? 2.93180   -87.18173 35.88859  1.000 244.96192 ? 216 ALA C CB  1 
ATOM   5969 N N   . GLU D 4 20  ? 6.26952   36.31607  18.68817  1.000 232.62005 ? 1   GLU D N   1 
ATOM   5970 C CA  . GLU D 4 20  ? 6.32579   36.25222  20.14395  1.000 226.66844 ? 1   GLU D CA  1 
ATOM   5971 C C   . GLU D 4 20  ? 6.23948   34.82035  20.65703  1.000 214.28658 ? 1   GLU D C   1 
ATOM   5972 O O   . GLU D 4 20  ? 5.51641   33.99330  20.10173  1.000 211.83300 ? 1   GLU D O   1 
ATOM   5973 C CB  . GLU D 4 20  ? 5.19831   37.08128  20.76417  1.000 224.60767 ? 1   GLU D CB  1 
ATOM   5974 C CG  . GLU D 4 20  ? 5.50557   38.55999  20.91311  1.000 230.61536 ? 1   GLU D CG  1 
ATOM   5975 C CD  . GLU D 4 20  ? 4.45516   39.28802  21.73021  1.000 224.79146 ? 1   GLU D CD  1 
ATOM   5976 O OE1 . GLU D 4 20  ? 3.29525   38.82471  21.75939  1.000 220.12234 ? 1   GLU D OE1 1 
ATOM   5977 O OE2 . GLU D 4 20  ? 4.79133   40.31872  22.35016  1.000 223.86976 ? 1   GLU D OE2 1 
ATOM   5978 N N   . VAL D 4 21  ? 6.98619   34.53607  21.72491  1.000 215.33959 ? 2   VAL D N   1 
ATOM   5979 C CA  . VAL D 4 21  ? 6.84569   33.26429  22.42006  1.000 204.44523 ? 2   VAL D CA  1 
ATOM   5980 C C   . VAL D 4 21  ? 5.49035   33.22576  23.11115  1.000 196.24956 ? 2   VAL D C   1 
ATOM   5981 O O   . VAL D 4 21  ? 5.04237   34.22173  23.69620  1.000 196.67026 ? 2   VAL D O   1 
ATOM   5982 C CB  . VAL D 4 21  ? 7.99376   33.07299  23.42588  1.000 197.78004 ? 2   VAL D CB  1 
ATOM   5983 C CG1 . VAL D 4 21  ? 7.92603   31.69274  24.06383  1.000 189.79965 ? 2   VAL D CG1 1 
ATOM   5984 C CG2 . VAL D 4 21  ? 9.33751   33.29291  22.74575  1.000 207.18569 ? 2   VAL D CG2 1 
ATOM   5985 N N   . MET D 4 22  ? 4.82117   32.07691  23.04144  1.000 214.37480 ? 3   MET D N   1 
ATOM   5986 C CA  . MET D 4 22  ? 3.46978   31.96414  23.58395  1.000 206.72193 ? 3   MET D CA  1 
ATOM   5987 C C   . MET D 4 22  ? 3.25562   30.54278  24.08477  1.000 186.68113 ? 3   MET D C   1 
ATOM   5988 O O   . MET D 4 22  ? 3.22124   29.60058  23.28724  1.000 185.34485 ? 3   MET D O   1 
ATOM   5989 C CB  . MET D 4 22  ? 2.42985   32.33551  22.53110  1.000 215.10021 ? 3   MET D CB  1 
ATOM   5990 C CG  . MET D 4 22  ? 1.08033   32.72599  23.10525  1.000 211.41187 ? 3   MET D CG  1 
ATOM   5991 S SD  . MET D 4 22  ? -0.22928  32.68365  21.86901  1.000 213.52250 ? 3   MET D SD  1 
ATOM   5992 C CE  . MET D 4 22  ? -0.27567  30.93144  21.50024  1.000 203.95454 ? 3   MET D CE  1 
ATOM   5993 N N   . LEU D 4 23  ? 3.10423   30.39560  25.39898  1.000 190.62708 ? 4   LEU D N   1 
ATOM   5994 C CA  . LEU D 4 23  ? 2.79781   29.11853  26.04007  1.000 180.58045 ? 4   LEU D CA  1 
ATOM   5995 C C   . LEU D 4 23  ? 1.40088   29.23452  26.64250  1.000 176.18253 ? 4   LEU D C   1 
ATOM   5996 O O   . LEU D 4 23  ? 1.22670   29.82166  27.71419  1.000 173.50096 ? 4   LEU D O   1 
ATOM   5997 C CB  . LEU D 4 23  ? 3.83290   28.77722  27.10893  1.000 175.62861 ? 4   LEU D CB  1 
ATOM   5998 C CG  . LEU D 4 23  ? 5.31117   28.74650  26.71731  1.000 180.58269 ? 4   LEU D CG  1 
ATOM   5999 C CD1 . LEU D 4 23  ? 6.18215   28.79428  27.96264  1.000 176.06603 ? 4   LEU D CD1 1 
ATOM   6000 C CD2 . LEU D 4 23  ? 5.62780   27.50980  25.89259  1.000 181.71481 ? 4   LEU D CD2 1 
ATOM   6001 N N   . VAL D 4 24  ? 0.40770   28.67860  25.95633  1.000 184.56750 ? 5   VAL D N   1 
ATOM   6002 C CA  . VAL D 4 24  ? -0.98084  28.73983  26.39970  1.000 181.45619 ? 5   VAL D CA  1 
ATOM   6003 C C   . VAL D 4 24  ? -1.34888  27.38352  26.99367  1.000 173.40043 ? 5   VAL D C   1 
ATOM   6004 O O   . VAL D 4 24  ? -1.38953  26.36970  26.28777  1.000 171.92607 ? 5   VAL D O   1 
ATOM   6005 C CB  . VAL D 4 24  ? -1.92596  29.14241  25.25758  1.000 187.41106 ? 5   VAL D CB  1 
ATOM   6006 C CG1 . VAL D 4 24  ? -1.84920  30.64341  25.01871  1.000 194.99647 ? 5   VAL D CG1 1 
ATOM   6007 C CG2 . VAL D 4 24  ? -1.58563  28.39608  23.97799  1.000 190.36371 ? 5   VAL D CG2 1 
ATOM   6008 N N   . GLU D 4 25  ? -1.60910  27.36082  28.29839  1.000 182.58919 ? 6   GLU D N   1 
ATOM   6009 C CA  . GLU D 4 25  ? -1.95943  26.13559  28.99982  1.000 176.34347 ? 6   GLU D CA  1 
ATOM   6010 C C   . GLU D 4 25  ? -3.46274  25.87846  28.92919  1.000 175.85112 ? 6   GLU D C   1 
ATOM   6011 O O   . GLU D 4 25  ? -4.23972  26.69535  28.43031  1.000 179.41886 ? 6   GLU D O   1 
ATOM   6012 C CB  . GLU D 4 25  ? -1.50819  26.19882  30.45828  1.000 171.53730 ? 6   GLU D CB  1 
ATOM   6013 C CG  . GLU D 4 25  ? -0.00908  26.16994  30.65421  1.000 173.47632 ? 6   GLU D CG  1 
ATOM   6014 C CD  . GLU D 4 25  ? 0.60304   27.55284  30.69123  1.000 176.02748 ? 6   GLU D CD  1 
ATOM   6015 O OE1 . GLU D 4 25  ? -0.11162  28.53577  30.40149  1.000 178.49295 ? 6   GLU D OE1 1 
ATOM   6016 O OE2 . GLU D 4 25  ? 1.80067   27.65463  31.02125  1.000 176.15072 ? 6   GLU D OE2 1 
ATOM   6017 N N   . SER D 4 26  ? -3.86884  24.72336  29.45276  1.000 184.12926 ? 7   SER D N   1 
ATOM   6018 C CA  . SER D 4 26  ? -5.26606  24.30875  29.43103  1.000 184.01958 ? 7   SER D CA  1 
ATOM   6019 C C   . SER D 4 26  ? -5.44226  23.11274  30.35566  1.000 179.75676 ? 7   SER D C   1 
ATOM   6020 O O   . SER D 4 26  ? -4.49146  22.37601  30.63301  1.000 177.13053 ? 7   SER D O   1 
ATOM   6021 C CB  . SER D 4 26  ? -5.72538  23.95610  28.01145  1.000 187.63592 ? 7   SER D CB  1 
ATOM   6022 O OG  . SER D 4 26  ? -7.06387  23.49273  28.00764  1.000 187.39986 ? 7   SER D OG  1 
ATOM   6023 N N   . GLY D 4 27  ? -6.67404  22.93340  30.83226  1.000 183.38834 ? 8   GLY D N   1 
ATOM   6024 C CA  . GLY D 4 27  ? -7.03287  21.73795  31.57268  1.000 181.69018 ? 8   GLY D CA  1 
ATOM   6025 C C   . GLY D 4 27  ? -7.30894  21.92690  33.05167  1.000 181.28007 ? 8   GLY D C   1 
ATOM   6026 O O   . GLY D 4 27  ? -6.89190  21.10205  33.86900  1.000 181.20225 ? 8   GLY D O   1 
ATOM   6027 N N   . GLY D 4 28  ? -8.02528  22.98815  33.41479  1.000 204.15676 ? 9   GLY D N   1 
ATOM   6028 C CA  . GLY D 4 28  ? -8.33846  23.26743  34.80661  1.000 204.22317 ? 9   GLY D CA  1 
ATOM   6029 C C   . GLY D 4 28  ? -9.75463  22.84506  35.15278  1.000 210.67319 ? 9   GLY D C   1 
ATOM   6030 O O   . GLY D 4 28  ? -10.71058 23.21902  34.46894  1.000 215.13260 ? 9   GLY D O   1 
ATOM   6031 N N   . ASP D 4 29  ? -9.87614  22.06786  36.22818  1.000 219.34055 ? 10  ASP D N   1 
ATOM   6032 C CA  . ASP D 4 29  ? -11.16912 21.57987  36.69669  1.000 221.44402 ? 10  ASP D CA  1 
ATOM   6033 C C   . ASP D 4 29  ? -10.97713 20.95009  38.07157  1.000 221.51300 ? 10  ASP D C   1 
ATOM   6034 O O   . ASP D 4 29  ? -9.85062  20.76816  38.54085  1.000 219.29011 ? 10  ASP D O   1 
ATOM   6035 C CB  . ASP D 4 29  ? -11.78213 20.58088  35.70957  1.000 221.84441 ? 10  ASP D CB  1 
ATOM   6036 C CG  . ASP D 4 29  ? -13.28750 20.47470  35.84604  1.000 221.54192 ? 10  ASP D CG  1 
ATOM   6037 O OD1 . ASP D 4 29  ? -13.75654 19.86180  36.82791  1.000 221.50014 ? 10  ASP D OD1 1 
ATOM   6038 O OD2 . ASP D 4 29  ? -14.00127 21.02058  34.97795  1.000 220.91310 ? 10  ASP D OD2 1 
ATOM   6039 N N   . LEU D 4 30  ? -12.09763 20.62250  38.71351  1.000 213.77945 ? 11  LEU D N   1 
ATOM   6040 C CA  . LEU D 4 30  ? -12.09083 20.02457  40.04242  1.000 214.56878 ? 11  LEU D CA  1 
ATOM   6041 C C   . LEU D 4 30  ? -12.07327 18.50462  39.94058  1.000 215.19877 ? 11  LEU D C   1 
ATOM   6042 O O   . LEU D 4 30  ? -12.67506 17.92387  39.03289  1.000 214.98038 ? 11  LEU D O   1 
ATOM   6043 C CB  . LEU D 4 30  ? -13.31377 20.47749  40.84279  1.000 215.70754 ? 11  LEU D CB  1 
ATOM   6044 C CG  . LEU D 4 30  ? -13.44888 19.93425  42.26804  1.000 217.48767 ? 11  LEU D CG  1 
ATOM   6045 C CD1 . LEU D 4 30  ? -12.77781 20.85625  43.27402  1.000 217.38604 ? 11  LEU D CD1 1 
ATOM   6046 C CD2 . LEU D 4 30  ? -14.90694 19.70673  42.62358  1.000 219.38552 ? 11  LEU D CD2 1 
ATOM   6047 N N   . VAL D 4 31  ? -11.38257 17.86297  40.88077  1.000 212.98692 ? 12  VAL D N   1 
ATOM   6048 C CA  . VAL D 4 31  ? -11.26233 16.40984  40.90919  1.000 214.60550 ? 12  VAL D CA  1 
ATOM   6049 C C   . VAL D 4 31  ? -11.46903 15.91763  42.33512  1.000 217.87836 ? 12  VAL D C   1 
ATOM   6050 O O   . VAL D 4 31  ? -10.96948 16.51827  43.29254  1.000 218.33734 ? 12  VAL D O   1 
ATOM   6051 C CB  . VAL D 4 31  ? -9.89618  15.94047  40.36544  1.000 213.81898 ? 12  VAL D CB  1 
ATOM   6052 C CG1 . VAL D 4 31  ? -9.83680  16.10409  38.85425  1.000 212.04816 ? 12  VAL D CG1 1 
ATOM   6053 C CG2 . VAL D 4 31  ? -8.76881  16.71480  41.02900  1.000 212.91624 ? 12  VAL D CG2 1 
ATOM   6054 N N   . LYS D 4 32  ? -12.21636 14.82735  42.47276  1.000 205.70700 ? 13  LYS D N   1 
ATOM   6055 C CA  . LYS D 4 32  ? -12.31358 14.15075  43.75608  1.000 210.06449 ? 13  LYS D CA  1 
ATOM   6056 C C   . LYS D 4 32  ? -10.96133 13.53677  44.11419  1.000 211.31109 ? 13  LYS D C   1 
ATOM   6057 O O   . LYS D 4 32  ? -10.24519 13.05979  43.22793  1.000 209.97644 ? 13  LYS D O   1 
ATOM   6058 C CB  . LYS D 4 32  ? -13.38665 13.06241  43.70470  1.000 213.87781 ? 13  LYS D CB  1 
ATOM   6059 C CG  . LYS D 4 32  ? -14.71835 13.44015  44.33637  1.000 214.97195 ? 13  LYS D CG  1 
ATOM   6060 C CD  . LYS D 4 32  ? -14.62932 13.38343  45.85132  1.000 219.22163 ? 13  LYS D CD  1 
ATOM   6061 C CE  . LYS D 4 32  ? -15.86651 12.75048  46.46983  1.000 223.59227 ? 13  LYS D CE  1 
ATOM   6062 N NZ  . LYS D 4 32  ? -17.08916 13.57841  46.28092  1.000 220.65197 ? 13  LYS D NZ  1 
ATOM   6063 N N   . PRO D 4 33  ? -10.57608 13.54412  45.39980  1.000 212.12081 ? 14  PRO D N   1 
ATOM   6064 C CA  . PRO D 4 33  ? -9.28719  12.95087  45.78866  1.000 213.55896 ? 14  PRO D CA  1 
ATOM   6065 C C   . PRO D 4 33  ? -9.15196  11.49755  45.36026  1.000 216.64375 ? 14  PRO D C   1 
ATOM   6066 O O   . PRO D 4 33  ? -9.81539  10.60951  45.90518  1.000 222.27176 ? 14  PRO D O   1 
ATOM   6067 C CB  . PRO D 4 33  ? -9.27815  13.09176  47.31878  1.000 217.49538 ? 14  PRO D CB  1 
ATOM   6068 C CG  . PRO D 4 33  ? -10.69971 13.38783  47.70367  1.000 219.31571 ? 14  PRO D CG  1 
ATOM   6069 C CD  . PRO D 4 33  ? -11.27369 14.14065  46.54922  1.000 214.20932 ? 14  PRO D CD  1 
ATOM   6070 N N   . GLY D 4 34  ? -8.29094  11.25415  44.37439  1.000 211.48271 ? 15  GLY D N   1 
ATOM   6071 C CA  . GLY D 4 34  ? -8.09445  9.92522   43.83048  1.000 214.17056 ? 15  GLY D CA  1 
ATOM   6072 C C   . GLY D 4 34  ? -8.22064  9.89151   42.32093  1.000 210.52259 ? 15  GLY D C   1 
ATOM   6073 O O   . GLY D 4 34  ? -7.84171  8.90709   41.67880  1.000 211.84306 ? 15  GLY D O   1 
ATOM   6074 N N   . GLY D 4 35  ? -8.74486  10.96967  41.74338  1.000 209.02341 ? 16  GLY D N   1 
ATOM   6075 C CA  . GLY D 4 35  ? -8.98226  11.04330  40.31762  1.000 206.28852 ? 16  GLY D CA  1 
ATOM   6076 C C   . GLY D 4 35  ? -7.72019  11.32423  39.52159  1.000 203.75916 ? 16  GLY D C   1 
ATOM   6077 O O   . GLY D 4 35  ? -6.59559  11.27046  40.02227  1.000 204.15441 ? 16  GLY D O   1 
ATOM   6078 N N   . SER D 4 36  ? -7.92784  11.63670  38.24230  1.000 206.46389 ? 17  SER D N   1 
ATOM   6079 C CA  . SER D 4 36  ? -6.83385  11.87551  37.31159  1.000 204.60144 ? 17  SER D CA  1 
ATOM   6080 C C   . SER D 4 36  ? -7.21340  12.98864  36.34403  1.000 201.75546 ? 17  SER D C   1 
ATOM   6081 O O   . SER D 4 36  ? -8.39291  13.28057  36.13348  1.000 201.45212 ? 17  SER D O   1 
ATOM   6082 C CB  . SER D 4 36  ? -6.46578  10.60114  36.53868  1.000 206.42334 ? 17  SER D CB  1 
ATOM   6083 O OG  . SER D 4 36  ? -7.60789  10.02807  35.92446  1.000 207.50495 ? 17  SER D OG  1 
ATOM   6084 N N   . LEU D 4 37  ? -6.19222  13.60024  35.74322  1.000 199.45392 ? 18  LEU D N   1 
ATOM   6085 C CA  . LEU D 4 37  ? -6.39118  14.73584  34.85152  1.000 195.57521 ? 18  LEU D CA  1 
ATOM   6086 C C   . LEU D 4 37  ? -5.14585  14.93246  33.99760  1.000 194.03359 ? 18  LEU D C   1 
ATOM   6087 O O   . LEU D 4 37  ? -4.02536  14.66135  34.43803  1.000 194.02480 ? 18  LEU D O   1 
ATOM   6088 C CB  . LEU D 4 37  ? -6.70375  16.01217  35.64282  1.000 194.93988 ? 18  LEU D CB  1 
ATOM   6089 C CG  . LEU D 4 37  ? -6.83043  17.32838  34.87201  1.000 193.85272 ? 18  LEU D CG  1 
ATOM   6090 C CD1 . LEU D 4 37  ? -7.98105  17.26976  33.87857  1.000 194.46550 ? 18  LEU D CD1 1 
ATOM   6091 C CD2 . LEU D 4 37  ? -6.99916  18.49670  35.82981  1.000 194.07390 ? 18  LEU D CD2 1 
ATOM   6092 N N   . LYS D 4 38  ? -5.35727  15.40710  32.77205  1.000 189.72680 ? 19  LYS D N   1 
ATOM   6093 C CA  . LYS D 4 38  ? -4.27906  15.72689  31.84636  1.000 183.01112 ? 19  LYS D CA  1 
ATOM   6094 C C   . LYS D 4 38  ? -4.37071  17.19635  31.46027  1.000 182.76692 ? 19  LYS D C   1 
ATOM   6095 O O   . LYS D 4 38  ? -5.44431  17.67768  31.08640  1.000 183.54212 ? 19  LYS D O   1 
ATOM   6096 C CB  . LYS D 4 38  ? -4.33838  14.83944  30.59922  1.000 184.39053 ? 19  LYS D CB  1 
ATOM   6097 C CG  . LYS D 4 38  ? -5.74475  14.55098  30.09822  1.000 180.98929 ? 19  LYS D CG  1 
ATOM   6098 C CD  . LYS D 4 38  ? -5.72115  13.52583  28.97378  1.000 182.87378 ? 19  LYS D CD  1 
ATOM   6099 C CE  . LYS D 4 38  ? -7.07318  12.84771  28.81301  1.000 186.60247 ? 19  LYS D CE  1 
ATOM   6100 N NZ  . LYS D 4 38  ? -7.02880  11.75110  27.80654  1.000 191.62697 ? 19  LYS D NZ  1 
ATOM   6101 N N   . VAL D 4 39  ? -3.24921  17.90516  31.55654  1.000 172.41060 ? 20  VAL D N   1 
ATOM   6102 C CA  . VAL D 4 39  ? -3.17779  19.32691  31.24574  1.000 172.55970 ? 20  VAL D CA  1 
ATOM   6103 C C   . VAL D 4 39  ? -2.21462  19.52117  30.08598  1.000 173.56727 ? 20  VAL D C   1 
ATOM   6104 O O   . VAL D 4 39  ? -1.11046  18.96668  30.09019  1.000 173.21431 ? 20  VAL D O   1 
ATOM   6105 C CB  . VAL D 4 39  ? -2.74266  20.15462  32.46761  1.000 172.53584 ? 20  VAL D CB  1 
ATOM   6106 C CG1 . VAL D 4 39  ? -3.89756  20.31185  33.42917  1.000 172.98003 ? 20  VAL D CG1 1 
ATOM   6107 C CG2 . VAL D 4 39  ? -1.56474  19.49919  33.16857  1.000 171.31935 ? 20  VAL D CG2 1 
ATOM   6108 N N   . SER D 4 40  ? -2.62959  20.30942  29.09796  1.000 163.39669 ? 21  SER D N   1 
ATOM   6109 C CA  . SER D 4 40  ? -1.81480  20.55995  27.92008  1.000 165.71777 ? 21  SER D CA  1 
ATOM   6110 C C   . SER D 4 40  ? -1.16240  21.93864  28.00847  1.000 168.88853 ? 21  SER D C   1 
ATOM   6111 O O   . SER D 4 40  ? -1.38644  22.71182  28.94762  1.000 169.22580 ? 21  SER D O   1 
ATOM   6112 C CB  . SER D 4 40  ? -2.65387  20.42823  26.64746  1.000 167.21636 ? 21  SER D CB  1 
ATOM   6113 O OG  . SER D 4 40  ? -3.52856  21.53136  26.49647  1.000 169.93612 ? 21  SER D OG  1 
ATOM   6114 N N   . CYS D 4 41  ? -0.33464  22.24139  27.00610  1.000 159.10829 ? 22  CYS D N   1 
ATOM   6115 C CA  . CYS D 4 41  ? 0.38794   23.51343  26.94850  1.000 162.30557 ? 22  CYS D CA  1 
ATOM   6116 C C   . CYS D 4 41  ? 0.81439   23.74231  25.49242  1.000 165.35502 ? 22  CYS D C   1 
ATOM   6117 O O   . CYS D 4 41  ? 1.89447   23.31441  25.08956  1.000 166.90095 ? 22  CYS D O   1 
ATOM   6118 C CB  . CYS D 4 41  ? 1.58978   23.51119  27.87935  1.000 162.99334 ? 22  CYS D CB  1 
ATOM   6119 S SG  . CYS D 4 41  ? 2.60331   25.00482  27.83993  1.000 167.31938 ? 22  CYS D SG  1 
ATOM   6120 N N   . ALA D 4 42  ? -0.03640  24.42166  24.72317  1.000 160.92379 ? 23  ALA D N   1 
ATOM   6121 C CA  . ALA D 4 42  ? 0.21198   24.61676  23.29423  1.000 165.02795 ? 23  ALA D CA  1 
ATOM   6122 C C   . ALA D 4 42  ? 1.32138   25.64181  23.10139  1.000 171.84490 ? 23  ALA D C   1 
ATOM   6123 O O   . ALA D 4 42  ? 1.08592   26.85040  23.15777  1.000 176.96395 ? 23  ALA D O   1 
ATOM   6124 C CB  . ALA D 4 42  ? -1.06671  25.05423  22.58943  1.000 167.47319 ? 23  ALA D CB  1 
ATOM   6125 N N   . ALA D 4 43  ? 2.53582   25.16018  22.85949  1.000 165.98895 ? 24  ALA D N   1 
ATOM   6126 C CA  . ALA D 4 43  ? 3.66255   26.04150  22.60628  1.000 173.08854 ? 24  ALA D CA  1 
ATOM   6127 C C   . ALA D 4 43  ? 3.61332   26.56167  21.17561  1.000 181.97229 ? 24  ALA D C   1 
ATOM   6128 O O   . ALA D 4 43  ? 3.28737   25.82364  20.24220  1.000 181.51605 ? 24  ALA D O   1 
ATOM   6129 C CB  . ALA D 4 43  ? 4.97656   25.30520  22.85995  1.000 171.31587 ? 24  ALA D CB  1 
ATOM   6130 N N   . SER D 4 44  ? 3.93024   27.84356  21.00626  1.000 179.07804 ? 25  SER D N   1 
ATOM   6131 C CA  . SER D 4 44  ? 3.84355   28.47548  19.69873  1.000 188.90563 ? 25  SER D CA  1 
ATOM   6132 C C   . SER D 4 44  ? 4.89930   29.56347  19.58423  1.000 202.83110 ? 25  SER D C   1 
ATOM   6133 O O   . SER D 4 44  ? 5.19008   30.26386  20.55807  1.000 205.94216 ? 25  SER D O   1 
ATOM   6134 C CB  . SER D 4 44  ? 2.45123   29.07226  19.46210  1.000 192.48017 ? 25  SER D CB  1 
ATOM   6135 O OG  . SER D 4 44  ? 1.44195   28.07931  19.53201  1.000 199.58869 ? 25  SER D OG  1 
ATOM   6136 N N   . GLY D 4 45  ? 5.46330   29.69867  18.38725  1.000 188.14833 ? 26  GLY D N   1 
ATOM   6137 C CA  . GLY D 4 45  ? 6.36717   30.79133  18.09913  1.000 206.90260 ? 26  GLY D CA  1 
ATOM   6138 C C   . GLY D 4 45  ? 7.83301   30.52207  18.34223  1.000 207.49159 ? 26  GLY D C   1 
ATOM   6139 O O   . GLY D 4 45  ? 8.59046   31.47152  18.57442  1.000 212.66335 ? 26  GLY D O   1 
ATOM   6140 N N   . PHE D 4 46  ? 8.26361   29.26377  18.29163  1.000 210.77591 ? 27  PHE D N   1 
ATOM   6141 C CA  . PHE D 4 46  ? 9.66869   28.91939  18.48075  1.000 209.16035 ? 27  PHE D CA  1 
ATOM   6142 C C   . PHE D 4 46  ? 9.86399   27.46182  18.08578  1.000 197.10769 ? 27  PHE D C   1 
ATOM   6143 O O   . PHE D 4 46  ? 8.90069   26.71523  17.89326  1.000 192.19246 ? 27  PHE D O   1 
ATOM   6144 C CB  . PHE D 4 46  ? 10.12599  29.16296  19.92326  1.000 200.30869 ? 27  PHE D CB  1 
ATOM   6145 C CG  . PHE D 4 46  ? 9.43546   28.29629  20.93773  1.000 186.85396 ? 27  PHE D CG  1 
ATOM   6146 C CD1 . PHE D 4 46  ? 8.17539   28.62212  21.40978  1.000 183.35898 ? 27  PHE D CD1 1 
ATOM   6147 C CD2 . PHE D 4 46  ? 10.05405  27.16129  21.42901  1.000 179.95558 ? 27  PHE D CD2 1 
ATOM   6148 C CE1 . PHE D 4 46  ? 7.54513   27.82470  22.34672  1.000 174.00737 ? 27  PHE D CE1 1 
ATOM   6149 C CE2 . PHE D 4 46  ? 9.43244   26.36235  22.36632  1.000 173.80700 ? 27  PHE D CE2 1 
ATOM   6150 C CZ  . PHE D 4 46  ? 8.17696   26.69375  22.82595  1.000 171.19476 ? 27  PHE D CZ  1 
ATOM   6151 N N   . THR D 4 47  ? 11.12988  27.06730  17.96650  1.000 194.75753 ? 28  THR D N   1 
ATOM   6152 C CA  . THR D 4 47  ? 11.49021  25.69365  17.62014  1.000 185.52984 ? 28  THR D CA  1 
ATOM   6153 C C   . THR D 4 47  ? 11.26244  24.82141  18.84895  1.000 178.51392 ? 28  THR D C   1 
ATOM   6154 O O   . THR D 4 47  ? 12.10269  24.76415  19.74915  1.000 178.09473 ? 28  THR D O   1 
ATOM   6155 C CB  . THR D 4 47  ? 12.93696  25.62188  17.14408  1.000 199.33476 ? 28  THR D CB  1 
ATOM   6156 O OG1 . THR D 4 47  ? 13.21459  26.73664  16.28693  1.000 210.60842 ? 28  THR D OG1 1 
ATOM   6157 C CG2 . THR D 4 47  ? 13.18130  24.33255  16.37418  1.000 190.42107 ? 28  THR D CG2 1 
ATOM   6158 N N   . PHE D 4 48  ? 10.11895  24.13174  18.88395  1.000 187.66471 ? 29  PHE D N   1 
ATOM   6159 C CA  . PHE D 4 48  ? 9.71640   23.40971  20.08830  1.000 177.71064 ? 29  PHE D CA  1 
ATOM   6160 C C   . PHE D 4 48  ? 10.69437  22.28958  20.42456  1.000 175.61582 ? 29  PHE D C   1 
ATOM   6161 O O   . PHE D 4 48  ? 11.11957  22.14873  21.57691  1.000 174.68259 ? 29  PHE D O   1 
ATOM   6162 C CB  . PHE D 4 48  ? 8.30155   22.85844  19.91780  1.000 171.59884 ? 29  PHE D CB  1 
ATOM   6163 C CG  . PHE D 4 48  ? 7.80997   22.08063  21.10203  1.000 166.88777 ? 29  PHE D CG  1 
ATOM   6164 C CD1 . PHE D 4 48  ? 7.75333   22.66631  22.35509  1.000 166.23620 ? 29  PHE D CD1 1 
ATOM   6165 C CD2 . PHE D 4 48  ? 7.39644   20.76716  20.96190  1.000 163.20039 ? 29  PHE D CD2 1 
ATOM   6166 C CE1 . PHE D 4 48  ? 7.29857   21.95475  23.44777  1.000 162.13690 ? 29  PHE D CE1 1 
ATOM   6167 C CE2 . PHE D 4 48  ? 6.93786   20.05040  22.05040  1.000 159.51543 ? 29  PHE D CE2 1 
ATOM   6168 C CZ  . PHE D 4 48  ? 6.88968   20.64493  23.29546  1.000 159.01603 ? 29  PHE D CZ  1 
ATOM   6169 N N   . SER D 4 49  ? 11.06559  21.48038  19.43009  1.000 174.97712 ? 30  SER D N   1 
ATOM   6170 C CA  . SER D 4 49  ? 11.98893  20.37750  19.67316  1.000 174.64506 ? 30  SER D CA  1 
ATOM   6171 C C   . SER D 4 49  ? 13.39298  20.84729  20.03169  1.000 179.35041 ? 30  SER D C   1 
ATOM   6172 O O   . SER D 4 49  ? 14.19178  20.03840  20.51625  1.000 179.44680 ? 30  SER D O   1 
ATOM   6173 C CB  . SER D 4 49  ? 12.04960  19.46170  18.44930  1.000 173.08160 ? 30  SER D CB  1 
ATOM   6174 O OG  . SER D 4 49  ? 12.51804  20.16285  17.31139  1.000 175.14998 ? 30  SER D OG  1 
ATOM   6175 N N   . ASN D 4 50  ? 13.71071  22.12404  19.81140  1.000 176.32463 ? 31  ASN D N   1 
ATOM   6176 C CA  . ASN D 4 50  ? 15.03003  22.64616  20.14189  1.000 177.75115 ? 31  ASN D CA  1 
ATOM   6177 C C   . ASN D 4 50  ? 15.20648  22.91725  21.62991  1.000 177.50293 ? 31  ASN D C   1 
ATOM   6178 O O   . ASN D 4 50  ? 16.34489  22.92944  22.10961  1.000 178.74943 ? 31  ASN D O   1 
ATOM   6179 C CB  . ASN D 4 50  ? 15.29812  23.93410  19.35936  1.000 184.23969 ? 31  ASN D CB  1 
ATOM   6180 C CG  . ASN D 4 50  ? 16.32438  23.74832  18.25969  1.000 194.24477 ? 31  ASN D CG  1 
ATOM   6181 O OD1 . ASN D 4 50  ? 16.80037  22.63942  18.01820  1.000 189.39959 ? 31  ASN D OD1 1 
ATOM   6182 N ND2 . ASN D 4 50  ? 16.66786  24.83796  17.58235  1.000 201.00996 ? 31  ASN D ND2 1 
ATOM   6183 N N   . TYR D 4 51  ? 14.11940  23.13308  22.36812  1.000 173.32530 ? 32  TYR D N   1 
ATOM   6184 C CA  . TYR D 4 51  ? 14.19593  23.51264  23.77159  1.000 172.14452 ? 32  TYR D CA  1 
ATOM   6185 C C   . TYR D 4 51  ? 13.36286  22.55876  24.61557  1.000 168.03761 ? 32  TYR D C   1 
ATOM   6186 O O   . TYR D 4 51  ? 12.26810  22.15415  24.21258  1.000 165.33193 ? 32  TYR D O   1 
ATOM   6187 C CB  . TYR D 4 51  ? 13.71619  24.95641  23.97690  1.000 172.67732 ? 32  TYR D CB  1 
ATOM   6188 C CG  . TYR D 4 51  ? 14.12713  25.89985  22.86616  1.000 176.11219 ? 32  TYR D CG  1 
ATOM   6189 C CD1 . TYR D 4 51  ? 15.45968  26.19882  22.64071  1.000 178.57856 ? 32  TYR D CD1 1 
ATOM   6190 C CD2 . TYR D 4 51  ? 13.18073  26.49292  22.04719  1.000 176.83712 ? 32  TYR D CD2 1 
ATOM   6191 C CE1 . TYR D 4 51  ? 15.84250  27.05979  21.62777  1.000 189.45199 ? 32  TYR D CE1 1 
ATOM   6192 C CE2 . TYR D 4 51  ? 13.54987  27.35623  21.03003  1.000 180.18607 ? 32  TYR D CE2 1 
ATOM   6193 C CZ  . TYR D 4 51  ? 14.88308  27.63678  20.82566  1.000 193.29995 ? 32  TYR D CZ  1 
ATOM   6194 O OH  . TYR D 4 51  ? 15.25887  28.49462  19.81681  1.000 202.92103 ? 32  TYR D OH  1 
ATOM   6195 N N   . ALA D 4 52  ? 13.88582  22.20589  25.78736  1.000 161.53395 ? 33  ALA D N   1 
ATOM   6196 C CA  . ALA D 4 52  ? 13.20072  21.29385  26.69033  1.000 160.17437 ? 33  ALA D CA  1 
ATOM   6197 C C   . ALA D 4 52  ? 12.18555  22.04573  27.54781  1.000 158.35624 ? 33  ALA D C   1 
ATOM   6198 O O   . ALA D 4 52  ? 12.25310  23.26631  27.71001  1.000 158.41120 ? 33  ALA D O   1 
ATOM   6199 C CB  . ALA D 4 52  ? 14.20606  20.55961  27.57841  1.000 161.39640 ? 33  ALA D CB  1 
ATOM   6200 N N   . MET D 4 53  ? 11.24123  21.29490  28.10883  1.000 162.43147 ? 34  MET D N   1 
ATOM   6201 C CA  . MET D 4 53  ? 10.09718  21.86142  28.80865  1.000 159.29308 ? 34  MET D CA  1 
ATOM   6202 C C   . MET D 4 53  ? 10.04890  21.37760  30.25401  1.000 157.31631 ? 34  MET D C   1 
ATOM   6203 O O   . MET D 4 53  ? 10.77776  20.46728  30.65784  1.000 158.20531 ? 34  MET D O   1 
ATOM   6204 C CB  . MET D 4 53  ? 8.79206   21.50765  28.08701  1.000 156.50185 ? 34  MET D CB  1 
ATOM   6205 C CG  . MET D 4 53  ? 8.71334   22.03642  26.66724  1.000 158.75232 ? 34  MET D CG  1 
ATOM   6206 S SD  . MET D 4 53  ? 8.93040   23.82362  26.59452  1.000 161.97744 ? 34  MET D SD  1 
ATOM   6207 C CE  . MET D 4 53  ? 7.59395   24.36550  27.65639  1.000 158.17926 ? 34  MET D CE  1 
ATOM   6208 N N   . SER D 4 54  ? 9.16179   21.99866  31.03226  1.000 166.67393 ? 35  SER D N   1 
ATOM   6209 C CA  . SER D 4 54  ? 9.04779   21.70400  32.45454  1.000 165.17371 ? 35  SER D CA  1 
ATOM   6210 C C   . SER D 4 54  ? 7.73825   22.26902  32.98989  1.000 162.07406 ? 35  SER D C   1 
ATOM   6211 O O   . SER D 4 54  ? 7.13031   23.15814  32.38779  1.000 161.78455 ? 35  SER D O   1 
ATOM   6212 C CB  . SER D 4 54  ? 10.23673  22.27393  33.23662  1.000 168.00580 ? 35  SER D CB  1 
ATOM   6213 O OG  . SER D 4 54  ? 10.13077  21.98253  34.61910  1.000 166.94491 ? 35  SER D OG  1 
ATOM   6214 N N   . TRP D 4 55  ? 7.31428   21.73482  34.13623  1.000 173.87165 ? 36  TRP D N   1 
ATOM   6215 C CA  . TRP D 4 55  ? 6.12944   22.19453  34.85029  1.000 171.17257 ? 36  TRP D CA  1 
ATOM   6216 C C   . TRP D 4 55  ? 6.50743   22.60442  36.26771  1.000 171.44929 ? 36  TRP D C   1 
ATOM   6217 O O   . TRP D 4 55  ? 7.38180   21.99084  36.88754  1.000 173.12055 ? 36  TRP D O   1 
ATOM   6218 C CB  . TRP D 4 55  ? 5.04386   21.10729  34.92183  1.000 168.90092 ? 36  TRP D CB  1 
ATOM   6219 C CG  . TRP D 4 55  ? 4.33668   20.80635  33.63219  1.000 167.97576 ? 36  TRP D CG  1 
ATOM   6220 C CD1 . TRP D 4 55  ? 4.64319   19.81876  32.74396  1.000 168.45328 ? 36  TRP D CD1 1 
ATOM   6221 C CD2 . TRP D 4 55  ? 3.18449   21.47799  33.10237  1.000 166.48315 ? 36  TRP D CD2 1 
ATOM   6222 N NE1 . TRP D 4 55  ? 3.76293   19.83859  31.68985  1.000 167.21441 ? 36  TRP D NE1 1 
ATOM   6223 C CE2 . TRP D 4 55  ? 2.85893   20.84924  31.88433  1.000 166.15702 ? 36  TRP D CE2 1 
ATOM   6224 C CE3 . TRP D 4 55  ? 2.40178   22.55240  33.53623  1.000 165.53275 ? 36  TRP D CE3 1 
ATOM   6225 C CZ2 . TRP D 4 55  ? 1.78619   21.25977  31.09461  1.000 165.13451 ? 36  TRP D CZ2 1 
ATOM   6226 C CZ3 . TRP D 4 55  ? 1.33690   22.95892  32.75056  1.000 164.71064 ? 36  TRP D CZ3 1 
ATOM   6227 C CH2 . TRP D 4 55  ? 1.03942   22.31382  31.54375  1.000 164.59835 ? 36  TRP D CH2 1 
ATOM   6228 N N   . VAL D 4 56  ? 5.83819   23.63885  36.77974  1.000 168.98787 ? 37  VAL D N   1 
ATOM   6229 C CA  . VAL D 4 56  ? 5.97059   24.06527  38.16932  1.000 168.96819 ? 37  VAL D CA  1 
ATOM   6230 C C   . VAL D 4 56  ? 4.60504   24.52525  38.66216  1.000 166.92713 ? 37  VAL D C   1 
ATOM   6231 O O   . VAL D 4 56  ? 3.81534   25.10122  37.90793  1.000 166.12467 ? 37  VAL D O   1 
ATOM   6232 C CB  . VAL D 4 56  ? 7.01479   25.19225  38.35232  1.000 171.49309 ? 37  VAL D CB  1 
ATOM   6233 C CG1 . VAL D 4 56  ? 8.42946   24.63709  38.29238  1.000 174.79888 ? 37  VAL D CG1 1 
ATOM   6234 C CG2 . VAL D 4 56  ? 6.81497   26.28475  37.31207  1.000 171.71875 ? 37  VAL D CG2 1 
ATOM   6235 N N   . ARG D 4 57  ? 4.32706   24.27157  39.93935  1.000 182.54497 ? 38  ARG D N   1 
ATOM   6236 C CA  . ARG D 4 57  ? 3.04951   24.63322  40.53451  1.000 180.69169 ? 38  ARG D CA  1 
ATOM   6237 C C   . ARG D 4 57  ? 3.25287   25.60880  41.68516  1.000 181.91179 ? 38  ARG D C   1 
ATOM   6238 O O   . ARG D 4 57  ? 4.24970   25.54165  42.41246  1.000 184.17116 ? 38  ARG D O   1 
ATOM   6239 C CB  . ARG D 4 57  ? 2.28177   23.39752  41.03046  1.000 180.07307 ? 38  ARG D CB  1 
ATOM   6240 C CG  . ARG D 4 57  ? 2.91267   22.66354  42.20602  1.000 182.22278 ? 38  ARG D CG  1 
ATOM   6241 C CD  . ARG D 4 57  ? 2.02846   21.49927  42.63266  1.000 182.55001 ? 38  ARG D CD  1 
ATOM   6242 N NE  . ARG D 4 57  ? 2.65422   20.65426  43.64229  1.000 186.28712 ? 38  ARG D NE  1 
ATOM   6243 C CZ  . ARG D 4 57  ? 2.14581   19.50781  44.07302  1.000 188.75197 ? 38  ARG D CZ  1 
ATOM   6244 N NH1 . ARG D 4 57  ? 1.00393   19.03739  43.59885  1.000 187.39990 ? 38  ARG D NH1 1 
ATOM   6245 N NH2 . ARG D 4 57  ? 2.80060   18.81443  45.00005  1.000 198.92557 ? 38  ARG D NH2 1 
ATOM   6246 N N   . GLN D 4 58  ? 2.29122   26.51637  41.84013  1.000 188.07374 ? 39  GLN D N   1 
ATOM   6247 C CA  . GLN D 4 58  ? 2.30217   27.53209  42.88823  1.000 189.61746 ? 39  GLN D CA  1 
ATOM   6248 C C   . GLN D 4 58  ? 1.09812   27.29499  43.79071  1.000 189.56470 ? 39  GLN D C   1 
ATOM   6249 O O   . GLN D 4 58  ? -0.04692  27.49155  43.36959  1.000 188.48662 ? 39  GLN D O   1 
ATOM   6250 C CB  . GLN D 4 58  ? 2.27754   28.93791  42.28931  1.000 190.18467 ? 39  GLN D CB  1 
ATOM   6251 C CG  . GLN D 4 58  ? 2.44634   30.05381  43.30470  1.000 192.70413 ? 39  GLN D CG  1 
ATOM   6252 C CD  . GLN D 4 58  ? 2.47010   31.42925  42.66275  1.000 194.32656 ? 39  GLN D CD  1 
ATOM   6253 O OE1 . GLN D 4 58  ? 2.11336   32.42691  43.29059  1.000 194.70992 ? 39  GLN D OE1 1 
ATOM   6254 N NE2 . GLN D 4 58  ? 2.89693   31.48895  41.40668  1.000 196.24567 ? 39  GLN D NE2 1 
ATOM   6255 N N   . THR D 4 59  ? 1.36096   26.86750  45.02793  1.000 182.83194 ? 40  THR D N   1 
ATOM   6256 C CA  . THR D 4 59  ? 0.30396   26.59674  45.98985  1.000 184.57085 ? 40  THR D CA  1 
ATOM   6257 C C   . THR D 4 59  ? -0.52214  27.85941  46.24272  1.000 184.79447 ? 40  THR D C   1 
ATOM   6258 O O   . THR D 4 59  ? -0.08597  28.96836  45.92226  1.000 184.51119 ? 40  THR D O   1 
ATOM   6259 C CB  . THR D 4 59  ? 0.91170   26.08876  47.29855  1.000 187.62967 ? 40  THR D CB  1 
ATOM   6260 O OG1 . THR D 4 59  ? 1.64853   27.14466  47.92753  1.000 189.48322 ? 40  THR D OG1 1 
ATOM   6261 C CG2 . THR D 4 59  ? 1.84212   24.91690  47.03304  1.000 188.67224 ? 40  THR D CG2 1 
ATOM   6262 N N   . PRO D 4 60  ? -1.72739  27.71852  46.81175  1.000 178.72003 ? 41  PRO D N   1 
ATOM   6263 C CA  . PRO D 4 60  ? -2.51527  28.92161  47.13457  1.000 178.06845 ? 41  PRO D CA  1 
ATOM   6264 C C   . PRO D 4 60  ? -1.78663  29.88183  48.05540  1.000 180.11502 ? 41  PRO D C   1 
ATOM   6265 O O   . PRO D 4 60  ? -2.07429  31.08576  48.03793  1.000 180.39261 ? 41  PRO D O   1 
ATOM   6266 C CB  . PRO D 4 60  ? -3.77929  28.34979  47.79457  1.000 179.56455 ? 41  PRO D CB  1 
ATOM   6267 C CG  . PRO D 4 60  ? -3.39718  26.97240  48.23476  1.000 181.02742 ? 41  PRO D CG  1 
ATOM   6268 C CD  . PRO D 4 60  ? -2.44652  26.48831  47.18698  1.000 178.79834 ? 41  PRO D CD  1 
ATOM   6269 N N   . GLU D 4 61  ? -0.84113  29.38512  48.85155  1.000 182.06218 ? 42  GLU D N   1 
ATOM   6270 C CA  . GLU D 4 61  ? 0.03574   30.18082  49.70434  1.000 184.72814 ? 42  GLU D CA  1 
ATOM   6271 C C   . GLU D 4 61  ? 1.12069   30.90879  48.92149  1.000 185.35402 ? 42  GLU D C   1 
ATOM   6272 O O   . GLU D 4 61  ? 2.02697   31.46728  49.55707  1.000 188.03075 ? 42  GLU D O   1 
ATOM   6273 C CB  . GLU D 4 61  ? 0.68100   29.28372  50.76150  1.000 188.85949 ? 42  GLU D CB  1 
ATOM   6274 C CG  . GLU D 4 61  ? -0.29672  28.39860  51.51638  1.000 189.86764 ? 42  GLU D CG  1 
ATOM   6275 C CD  . GLU D 4 61  ? 0.12167   26.93995  51.51703  1.000 191.78025 ? 42  GLU D CD  1 
ATOM   6276 O OE1 . GLU D 4 61  ? 0.08205   26.30690  50.44105  1.000 190.12843 ? 42  GLU D OE1 1 
ATOM   6277 O OE2 . GLU D 4 61  ? 0.50078   26.42885  52.59156  1.000 195.93009 ? 42  GLU D OE2 1 
ATOM   6278 N N   . LYS D 4 62  ? 1.04007   30.89145  47.58970  1.000 193.74300 ? 43  LYS D N   1 
ATOM   6279 C CA  . LYS D 4 62  ? 2.02585   31.50062  46.69817  1.000 194.52106 ? 43  LYS D CA  1 
ATOM   6280 C C   . LYS D 4 62  ? 3.40007   30.84630  46.81486  1.000 196.69391 ? 43  LYS D C   1 
ATOM   6281 O O   . LYS D 4 62  ? 4.41701   31.47059  46.49514  1.000 199.66647 ? 43  LYS D O   1 
ATOM   6282 C CB  . LYS D 4 62  ? 2.13519   33.01277  46.93348  1.000 197.44418 ? 43  LYS D CB  1 
ATOM   6283 C CG  . LYS D 4 62  ? 0.84749   33.77718  46.66557  1.000 196.30465 ? 43  LYS D CG  1 
ATOM   6284 C CD  . LYS D 4 62  ? 1.01767   34.76280  45.52081  1.000 197.77573 ? 43  LYS D CD  1 
ATOM   6285 C CE  . LYS D 4 62  ? 2.09704   35.78678  45.83205  1.000 202.14952 ? 43  LYS D CE  1 
ATOM   6286 N NZ  . LYS D 4 62  ? 2.27597   36.76119  44.72067  1.000 206.60585 ? 43  LYS D NZ  1 
ATOM   6287 N N   . ARG D 4 63  ? 3.45249   29.59361  47.26368  1.000 189.20218 ? 44  ARG D N   1 
ATOM   6288 C CA  . ARG D 4 63  ? 4.70141   28.84637  47.33313  1.000 191.83517 ? 44  ARG D CA  1 
ATOM   6289 C C   . ARG D 4 63  ? 4.91474   28.08356  46.03288  1.000 189.86085 ? 44  ARG D C   1 
ATOM   6290 O O   . ARG D 4 63  ? 4.02014   27.36783  45.57197  1.000 186.29096 ? 44  ARG D O   1 
ATOM   6291 C CB  . ARG D 4 63  ? 4.69643   27.87127  48.51045  1.000 194.02607 ? 44  ARG D CB  1 
ATOM   6292 C CG  . ARG D 4 63  ? 4.70965   28.51704  49.88225  1.000 199.89283 ? 44  ARG D CG  1 
ATOM   6293 C CD  . ARG D 4 63  ? 4.80249   27.44685  50.95665  1.000 203.16373 ? 44  ARG D CD  1 
ATOM   6294 N NE  . ARG D 4 63  ? 4.81585   28.00085  52.30447  1.000 207.12660 ? 44  ARG D NE  1 
ATOM   6295 C CZ  . ARG D 4 63  ? 4.90935   27.27212  53.40830  1.000 211.46300 ? 44  ARG D CZ  1 
ATOM   6296 N NH1 . ARG D 4 63  ? 5.00246   25.95313  53.35972  1.000 212.31136 ? 44  ARG D NH1 1 
ATOM   6297 N NH2 . ARG D 4 63  ? 4.90957   27.88146  54.59032  1.000 214.27153 ? 44  ARG D NH2 1 
ATOM   6298 N N   . LEU D 4 64  ? 6.10264   28.22799  45.45448  1.000 186.75337 ? 45  LEU D N   1 
ATOM   6299 C CA  . LEU D 4 64  ? 6.43245   27.57897  44.19455  1.000 184.68808 ? 45  LEU D CA  1 
ATOM   6300 C C   . LEU D 4 64  ? 7.08685   26.22587  44.44041  1.000 186.56092 ? 45  LEU D C   1 
ATOM   6301 O O   . LEU D 4 64  ? 7.93007   26.07941  45.33009  1.000 191.45110 ? 45  LEU D O   1 
ATOM   6302 C CB  . LEU D 4 64  ? 7.35939   28.46698  43.36331  1.000 187.39072 ? 45  LEU D CB  1 
ATOM   6303 C CG  . LEU D 4 64  ? 6.71963   29.73587  42.79764  1.000 185.87343 ? 45  LEU D CG  1 
ATOM   6304 C CD1 . LEU D 4 64  ? 7.77911   30.75937  42.43068  1.000 190.97306 ? 45  LEU D CD1 1 
ATOM   6305 C CD2 . LEU D 4 64  ? 5.86336   29.39806  41.58853  1.000 181.93775 ? 45  LEU D CD2 1 
ATOM   6306 N N   . GLU D 4 65  ? 6.68308   25.23553  43.64726  1.000 186.81128 ? 46  GLU D N   1 
ATOM   6307 C CA  . GLU D 4 65  ? 7.26027   23.90118  43.68895  1.000 188.73721 ? 46  GLU D CA  1 
ATOM   6308 C C   . GLU D 4 65  ? 7.58916   23.45588  42.27230  1.000 187.43853 ? 46  GLU D C   1 
ATOM   6309 O O   . GLU D 4 65  ? 6.89595   23.81625  41.31750  1.000 184.09529 ? 46  GLU D O   1 
ATOM   6310 C CB  . GLU D 4 65  ? 6.30742   22.88276  44.33530  1.000 186.42590 ? 46  GLU D CB  1 
ATOM   6311 C CG  . GLU D 4 65  ? 5.61229   23.37102  45.59502  1.000 187.41902 ? 46  GLU D CG  1 
ATOM   6312 C CD  . GLU D 4 65  ? 4.91919   22.25047  46.34571  1.000 192.42573 ? 46  GLU D CD  1 
ATOM   6313 O OE1 . GLU D 4 65  ? 5.15923   21.07161  46.00907  1.000 194.72152 ? 46  GLU D OE1 1 
ATOM   6314 O OE2 . GLU D 4 65  ? 4.13730   22.54748  47.27345  1.000 194.01686 ? 46  GLU D OE2 1 
ATOM   6315 N N   . TRP D 4 66  ? 8.65385   22.66862  42.14067  1.000 176.34546 ? 47  TRP D N   1 
ATOM   6316 C CA  . TRP D 4 66  ? 9.01093   22.09409  40.84965  1.000 176.44346 ? 47  TRP D CA  1 
ATOM   6317 C C   . TRP D 4 66  ? 8.22433   20.80636  40.63695  1.000 174.70267 ? 47  TRP D C   1 
ATOM   6318 O O   . TRP D 4 66  ? 8.31833   19.87429  41.44297  1.000 176.01898 ? 47  TRP D O   1 
ATOM   6319 C CB  . TRP D 4 66  ? 10.51166  21.82998  40.76485  1.000 180.57660 ? 47  TRP D CB  1 
ATOM   6320 C CG  . TRP D 4 66  ? 10.87930  20.99329  39.58084  1.000 181.03614 ? 47  TRP D CG  1 
ATOM   6321 C CD1 . TRP D 4 66  ? 10.77605  21.34373  38.26607  1.000 180.14632 ? 47  TRP D CD1 1 
ATOM   6322 C CD2 . TRP D 4 66  ? 11.40149  19.65996  39.60086  1.000 182.84242 ? 47  TRP D CD2 1 
ATOM   6323 N NE1 . TRP D 4 66  ? 11.20294  20.31174  37.46635  1.000 181.19894 ? 47  TRP D NE1 1 
ATOM   6324 C CE2 . TRP D 4 66  ? 11.59366  19.26686  38.26172  1.000 182.75027 ? 47  TRP D CE2 1 
ATOM   6325 C CE3 . TRP D 4 66  ? 11.72792  18.76151  40.62089  1.000 192.06087 ? 47  TRP D CE3 1 
ATOM   6326 C CZ2 . TRP D 4 66  ? 12.09669  18.01475  37.91652  1.000 184.33431 ? 47  TRP D CZ2 1 
ATOM   6327 C CZ3 . TRP D 4 66  ? 12.22970  17.51998  40.27584  1.000 195.17478 ? 47  TRP D CZ3 1 
ATOM   6328 C CH2 . TRP D 4 66  ? 12.40734  17.15751  38.93557  1.000 194.41534 ? 47  TRP D CH2 1 
ATOM   6329 N N   . VAL D 4 67  ? 7.45094   20.75422  39.55318  1.000 177.64254 ? 48  VAL D N   1 
ATOM   6330 C CA  . VAL D 4 67  ? 6.57542   19.61823  39.28556  1.000 176.16825 ? 48  VAL D CA  1 
ATOM   6331 C C   . VAL D 4 67  ? 7.32650   18.53965  38.51723  1.000 178.04466 ? 48  VAL D C   1 
ATOM   6332 O O   . VAL D 4 67  ? 7.42571   17.39825  38.97804  1.000 179.32684 ? 48  VAL D O   1 
ATOM   6333 C CB  . VAL D 4 67  ? 5.31238   20.05289  38.52104  1.000 173.15389 ? 48  VAL D CB  1 
ATOM   6334 C CG1 . VAL D 4 67  ? 4.53676   18.83363  38.04999  1.000 172.38376 ? 48  VAL D CG1 1 
ATOM   6335 C CG2 . VAL D 4 67  ? 4.44023   20.92589  39.40187  1.000 171.35517 ? 48  VAL D CG2 1 
ATOM   6336 N N   . ALA D 4 68  ? 7.84483   18.88469  37.34044  1.000 178.60294 ? 49  ALA D N   1 
ATOM   6337 C CA  . ALA D 4 68  ? 8.57003   17.93078  36.50974  1.000 180.40852 ? 49  ALA D CA  1 
ATOM   6338 C C   . ALA D 4 68  ? 9.19347   18.67261  35.33770  1.000 181.63370 ? 49  ALA D C   1 
ATOM   6339 O O   . ALA D 4 68  ? 8.82756   19.81201  35.03658  1.000 180.68084 ? 49  ALA D O   1 
ATOM   6340 C CB  . ALA D 4 68  ? 7.65832   16.80729  36.00159  1.000 178.81940 ? 49  ALA D CB  1 
ATOM   6341 N N   . THR D 4 69  ? 10.14078  18.00558  34.67993  1.000 173.90217 ? 50  THR D N   1 
ATOM   6342 C CA  . THR D 4 69  ? 10.77804  18.52405  33.47936  1.000 175.55861 ? 50  THR D CA  1 
ATOM   6343 C C   . THR D 4 69  ? 11.01195  17.37315  32.51103  1.000 176.20091 ? 50  THR D C   1 
ATOM   6344 O O   . THR D 4 69  ? 11.25071  16.23412  32.92147  1.000 176.86862 ? 50  THR D O   1 
ATOM   6345 C CB  . THR D 4 69  ? 12.10366  19.24120  33.79194  1.000 179.54202 ? 50  THR D CB  1 
ATOM   6346 O OG1 . THR D 4 69  ? 12.67469  19.74882  32.57918  1.000 182.62044 ? 50  THR D OG1 1 
ATOM   6347 C CG2 . THR D 4 69  ? 13.09284  18.29590  34.45992  1.000 183.20579 ? 50  THR D CG2 1 
ATOM   6348 N N   . ILE D 4 70  ? 10.92807  17.67918  31.21857  1.000 175.45993 ? 51  ILE D N   1 
ATOM   6349 C CA  . ILE D 4 70  ? 11.02747  16.67093  30.17329  1.000 175.71861 ? 51  ILE D CA  1 
ATOM   6350 C C   . ILE D 4 70  ? 12.16785  17.03596  29.23230  1.000 179.28174 ? 51  ILE D C   1 
ATOM   6351 O O   . ILE D 4 70  ? 12.55053  18.20349  29.10942  1.000 181.09935 ? 51  ILE D O   1 
ATOM   6352 C CB  . ILE D 4 70  ? 9.69269   16.52375  29.40567  1.000 172.57313 ? 51  ILE D CB  1 
ATOM   6353 C CG1 . ILE D 4 70  ? 9.72249   15.29740  28.49158  1.000 172.66702 ? 51  ILE D CG1 1 
ATOM   6354 C CG2 . ILE D 4 70  ? 9.38446   17.79080  28.62246  1.000 172.76089 ? 51  ILE D CG2 1 
ATOM   6355 C CD1 . ILE D 4 70  ? 8.37936   14.66028  28.28347  1.000 169.36206 ? 51  ILE D CD1 1 
ATOM   6356 N N   . SER D 4 71  ? 12.72305  16.01834  28.57686  1.000 164.93683 ? 52  SER D N   1 
ATOM   6357 C CA  . SER D 4 71  ? 13.85816  16.19924  27.68512  1.000 168.67722 ? 52  SER D CA  1 
ATOM   6358 C C   . SER D 4 71  ? 13.42527  16.89584  26.39472  1.000 168.69566 ? 52  SER D C   1 
ATOM   6359 O O   . SER D 4 71  ? 12.25058  17.20676  26.17799  1.000 165.76006 ? 52  SER D O   1 
ATOM   6360 C CB  . SER D 4 71  ? 14.50929  14.85138  27.37899  1.000 169.92139 ? 52  SER D CB  1 
ATOM   6361 O OG  . SER D 4 71  ? 15.60362  14.99728  26.49125  1.000 173.69477 ? 52  SER D OG  1 
ATOM   6362 N N   . SER D 4 72  ? 14.40629  17.13807  25.52008  1.000 168.92315 ? 53  SER D N   1 
ATOM   6363 C CA  . SER D 4 72  ? 14.12491  17.78780  24.24436  1.000 169.87110 ? 53  SER D CA  1 
ATOM   6364 C C   . SER D 4 72  ? 13.33450  16.87862  23.31308  1.000 167.22684 ? 53  SER D C   1 
ATOM   6365 O O   . SER D 4 72  ? 12.51098  17.36151  22.52624  1.000 166.20850 ? 53  SER D O   1 
ATOM   6366 C CB  . SER D 4 72  ? 15.43189  18.21961  23.57868  1.000 174.96250 ? 53  SER D CB  1 
ATOM   6367 O OG  . SER D 4 72  ? 16.28780  18.86207  24.50746  1.000 177.45646 ? 53  SER D OG  1 
ATOM   6368 N N   . GLY D 4 73  ? 13.56862  15.57086  23.38663  1.000 178.42588 ? 54  GLY D N   1 
ATOM   6369 C CA  . GLY D 4 73  ? 12.85745  14.61625  22.55877  1.000 175.97646 ? 54  GLY D CA  1 
ATOM   6370 C C   . GLY D 4 73  ? 12.15854  13.54544  23.36678  1.000 172.97128 ? 54  GLY D C   1 
ATOM   6371 O O   . GLY D 4 73  ? 11.88306  12.45095  22.86006  1.000 171.91031 ? 54  GLY D O   1 
ATOM   6372 N N   . ALA D 4 74  ? 11.89175  13.84655  24.63830  1.000 175.52499 ? 55  ALA D N   1 
ATOM   6373 C CA  . ALA D 4 74  ? 11.10773  13.01280  25.54945  1.000 172.98474 ? 55  ALA D CA  1 
ATOM   6374 C C   . ALA D 4 74  ? 11.82268  11.73015  25.96547  1.000 174.77147 ? 55  ALA D C   1 
ATOM   6375 O O   . ALA D 4 74  ? 11.18643  10.82067  26.50840  1.000 173.38421 ? 55  ALA D O   1 
ATOM   6376 C CB  . ALA D 4 74  ? 9.73770   12.66930  24.95700  1.000 169.60947 ? 55  ALA D CB  1 
ATOM   6377 N N   . SER D 4 75  ? 13.13862  11.63332  25.75781  1.000 188.71356 ? 56  SER D N   1 
ATOM   6378 C CA  . SER D 4 75  ? 13.85947  10.43991  26.19296  1.000 190.79373 ? 56  SER D CA  1 
ATOM   6379 C C   . SER D 4 75  ? 14.11562  10.43458  27.69496  1.000 191.55029 ? 56  SER D C   1 
ATOM   6380 O O   . SER D 4 75  ? 14.17736  9.35608   28.29403  1.000 192.72006 ? 56  SER D O   1 
ATOM   6381 C CB  . SER D 4 75  ? 15.18551  10.30616  25.43898  1.000 173.74713 ? 56  SER D CB  1 
ATOM   6382 O OG  . SER D 4 75  ? 14.97174  10.26408  24.03358  1.000 174.18647 ? 56  SER D OG  1 
ATOM   6383 N N   . TYR D 4 76  ? 14.25120  11.60706  28.31434  1.000 175.26051 ? 57  TYR D N   1 
ATOM   6384 C CA  . TYR D 4 76  ? 14.54414  11.72181  29.73645  1.000 176.14276 ? 57  TYR D CA  1 
ATOM   6385 C C   . TYR D 4 76  ? 13.47224  12.55631  30.42299  1.000 173.19089 ? 57  TYR D C   1 
ATOM   6386 O O   . TYR D 4 76  ? 12.96188  13.52291  29.84706  1.000 171.65415 ? 57  TYR D O   1 
ATOM   6387 C CB  . TYR D 4 76  ? 15.91630  12.36239  29.97593  1.000 179.99098 ? 57  TYR D CB  1 
ATOM   6388 C CG  . TYR D 4 76  ? 17.07097  11.68159  29.27504  1.000 183.33098 ? 57  TYR D CG  1 
ATOM   6389 C CD1 . TYR D 4 76  ? 17.76142  10.64086  29.88303  1.000 185.50710 ? 57  TYR D CD1 1 
ATOM   6390 C CD2 . TYR D 4 76  ? 17.47717  12.08620  28.00875  1.000 184.65036 ? 57  TYR D CD2 1 
ATOM   6391 C CE1 . TYR D 4 76  ? 18.82212  10.02064  29.25010  1.000 188.59170 ? 57  TYR D CE1 1 
ATOM   6392 C CE2 . TYR D 4 76  ? 18.53722  11.46829  27.36629  1.000 187.70715 ? 57  TYR D CE2 1 
ATOM   6393 C CZ  . TYR D 4 76  ? 19.20447  10.43654  27.99369  1.000 189.54577 ? 57  TYR D CZ  1 
ATOM   6394 O OH  . TYR D 4 76  ? 20.25814  9.81558   27.36557  1.000 192.54524 ? 57  TYR D OH  1 
ATOM   6395 N N   . THR D 4 77  ? 13.13343  12.17681  31.65442  1.000 182.07115 ? 58  THR D N   1 
ATOM   6396 C CA  . THR D 4 77  ? 12.21006  12.93602  32.48825  1.000 179.65133 ? 58  THR D CA  1 
ATOM   6397 C C   . THR D 4 77  ? 12.69334  12.89530  33.93163  1.000 181.49067 ? 58  THR D C   1 
ATOM   6398 O O   . THR D 4 77  ? 13.39921  11.96889  34.33861  1.000 189.85114 ? 58  THR D O   1 
ATOM   6399 C CB  . THR D 4 77  ? 10.76854  12.39535  32.41738  1.000 176.33886 ? 58  THR D CB  1 
ATOM   6400 O OG1 . THR D 4 77  ? 10.75750  11.00713  32.77138  1.000 177.38529 ? 58  THR D OG1 1 
ATOM   6401 C CG2 . THR D 4 77  ? 10.17964  12.56717  31.02022  1.000 174.43137 ? 58  THR D CG2 1 
ATOM   6402 N N   . HIS D 4 78  ? 12.30293  13.90771  34.70518  1.000 181.42339 ? 59  HIS D N   1 
ATOM   6403 C CA  . HIS D 4 78  ? 12.67028  13.99734  36.11220  1.000 183.04008 ? 59  HIS D CA  1 
ATOM   6404 C C   . HIS D 4 78  ? 11.46331  14.44778  36.92236  1.000 180.18196 ? 59  HIS D C   1 
ATOM   6405 O O   . HIS D 4 78  ? 10.63903  15.23685  36.45274  1.000 177.39347 ? 59  HIS D O   1 
ATOM   6406 C CB  . HIS D 4 78  ? 13.84268  14.96446  36.33856  1.000 185.92129 ? 59  HIS D CB  1 
ATOM   6407 C CG  . HIS D 4 78  ? 15.10419  14.56345  35.63851  1.000 189.43554 ? 59  HIS D CG  1 
ATOM   6408 N ND1 . HIS D 4 78  ? 16.09389  13.82409  36.25014  1.000 194.45704 ? 59  HIS D ND1 1 
ATOM   6409 C CD2 . HIS D 4 78  ? 15.53905  14.80410  34.37908  1.000 190.17078 ? 59  HIS D CD2 1 
ATOM   6410 C CE1 . HIS D 4 78  ? 17.08268  13.62452  35.39692  1.000 198.13556 ? 59  HIS D CE1 1 
ATOM   6411 N NE2 . HIS D 4 78  ? 16.77080  14.20878  34.25414  1.000 195.82284 ? 59  HIS D NE2 1 
ATOM   6412 N N   . TYR D 4 79  ? 11.36901  13.93353  38.14414  1.000 198.87527 ? 60  TYR D N   1 
ATOM   6413 C CA  . TYR D 4 79  ? 10.29077  14.24421  39.06878  1.000 195.92081 ? 60  TYR D CA  1 
ATOM   6414 C C   . TYR D 4 79  ? 10.86931  14.36933  40.46963  1.000 200.19718 ? 60  TYR D C   1 
ATOM   6415 O O   . TYR D 4 79  ? 11.89270  13.74589  40.77686  1.000 204.55921 ? 60  TYR D O   1 
ATOM   6416 C CB  . TYR D 4 79  ? 9.19872   13.16140  39.06706  1.000 195.46675 ? 60  TYR D CB  1 
ATOM   6417 C CG  . TYR D 4 79  ? 8.60221   12.85863  37.71039  1.000 191.77742 ? 60  TYR D CG  1 
ATOM   6418 C CD1 . TYR D 4 79  ? 9.20761   11.95015  36.85231  1.000 193.91953 ? 60  TYR D CD1 1 
ATOM   6419 C CD2 . TYR D 4 79  ? 7.42337   13.46511  37.29639  1.000 186.50564 ? 60  TYR D CD2 1 
ATOM   6420 C CE1 . TYR D 4 79  ? 8.66478   11.66473  35.61511  1.000 191.13913 ? 60  TYR D CE1 1 
ATOM   6421 C CE2 . TYR D 4 79  ? 6.87238   13.18551  36.06022  1.000 177.73270 ? 60  TYR D CE2 1 
ATOM   6422 C CZ  . TYR D 4 79  ? 7.49715   12.28413  35.22452  1.000 181.69237 ? 60  TYR D CZ  1 
ATOM   6423 O OH  . TYR D 4 79  ? 6.95393   12.00011  33.99301  1.000 177.13221 ? 60  TYR D OH  1 
ATOM   6424 N N   . PRO D 4 80  ? 10.24787  15.16530  41.33393  1.000 202.17498 ? 61  PRO D N   1 
ATOM   6425 C CA  . PRO D 4 80  ? 10.68423  15.23066  42.72978  1.000 204.90396 ? 61  PRO D CA  1 
ATOM   6426 C C   . PRO D 4 80  ? 10.09878  14.07666  43.53478  1.000 206.41129 ? 61  PRO D C   1 
ATOM   6427 O O   . PRO D 4 80  ? 9.18784   13.37329  43.09776  1.000 204.73779 ? 61  PRO D O   1 
ATOM   6428 C CB  . PRO D 4 80  ? 10.13435  16.57879  43.20165  1.000 202.51612 ? 61  PRO D CB  1 
ATOM   6429 C CG  . PRO D 4 80  ? 8.88349   16.74154  42.40454  1.000 196.56502 ? 61  PRO D CG  1 
ATOM   6430 C CD  . PRO D 4 80  ? 9.15346   16.10942  41.05924  1.000 196.33536 ? 61  PRO D CD  1 
ATOM   6431 N N   . ASP D 4 81  ? 10.63819  13.90296  44.74413  1.000 210.95444 ? 62  ASP D N   1 
ATOM   6432 C CA  . ASP D 4 81  ? 10.20973  12.80541  45.60554  1.000 212.87335 ? 62  ASP D CA  1 
ATOM   6433 C C   . ASP D 4 81  ? 8.73810   12.90194  45.98867  1.000 210.46141 ? 62  ASP D C   1 
ATOM   6434 O O   . ASP D 4 81  ? 8.14200   11.88783  46.36729  1.000 212.22753 ? 62  ASP D O   1 
ATOM   6435 C CB  . ASP D 4 81  ? 11.07155  12.76559  46.86821  1.000 217.14885 ? 62  ASP D CB  1 
ATOM   6436 C CG  . ASP D 4 81  ? 12.55276  12.84701  46.56528  1.000 219.63070 ? 62  ASP D CG  1 
ATOM   6437 O OD1 . ASP D 4 81  ? 12.95114  12.43255  45.45743  1.000 219.24421 ? 62  ASP D OD1 1 
ATOM   6438 O OD2 . ASP D 4 81  ? 13.31525  13.32970  47.42904  1.000 222.29765 ? 62  ASP D OD2 1 
ATOM   6439 N N   . SER D 4 82  ? 8.13874   14.09119  45.89432  1.000 208.11014 ? 63  SER D N   1 
ATOM   6440 C CA  . SER D 4 82  ? 6.74850   14.25974  46.30721  1.000 205.97511 ? 63  SER D CA  1 
ATOM   6441 C C   . SER D 4 82  ? 5.78772   13.60682  45.31906  1.000 203.59812 ? 63  SER D C   1 
ATOM   6442 O O   . SER D 4 82  ? 4.92314   12.81478  45.71164  1.000 204.69844 ? 63  SER D O   1 
ATOM   6443 C CB  . SER D 4 82  ? 6.42937   15.74719  46.46699  1.000 203.23168 ? 63  SER D CB  1 
ATOM   6444 O OG  . SER D 4 82  ? 6.79525   16.47662  45.30820  1.000 200.70966 ? 63  SER D OG  1 
ATOM   6445 N N   . VAL D 4 83  ? 5.91830   13.92779  44.03492  1.000 202.31705 ? 64  VAL D N   1 
ATOM   6446 C CA  . VAL D 4 83  ? 4.97621   13.46626  43.02272  1.000 199.91723 ? 64  VAL D CA  1 
ATOM   6447 C C   . VAL D 4 83  ? 5.56700   12.34037  42.16961  1.000 201.43753 ? 64  VAL D C   1 
ATOM   6448 O O   . VAL D 4 83  ? 5.12334   12.12264  41.04221  1.000 199.94607 ? 64  VAL D O   1 
ATOM   6449 C CB  . VAL D 4 83  ? 4.48199   14.62661  42.14487  1.000 196.31179 ? 64  VAL D CB  1 
ATOM   6450 C CG1 . VAL D 4 83  ? 3.79090   15.67943  42.99749  1.000 194.88299 ? 64  VAL D CG1 1 
ATOM   6451 C CG2 . VAL D 4 83  ? 5.63758   15.24024  41.37174  1.000 196.58179 ? 64  VAL D CG2 1 
ATOM   6452 N N   . LYS D 4 84  ? 6.55475   11.61596  42.69220  1.000 201.41480 ? 65  LYS D N   1 
ATOM   6453 C CA  . LYS D 4 84  ? 7.14604   10.51218  41.94642  1.000 203.85393 ? 65  LYS D CA  1 
ATOM   6454 C C   . LYS D 4 84  ? 6.12234   9.40464   41.72903  1.000 204.48202 ? 65  LYS D C   1 
ATOM   6455 O O   . LYS D 4 84  ? 5.44454   8.97436   42.66678  1.000 205.88037 ? 65  LYS D O   1 
ATOM   6456 C CB  . LYS D 4 84  ? 8.36399   9.96183   42.68797  1.000 207.96464 ? 65  LYS D CB  1 
ATOM   6457 C CG  . LYS D 4 84  ? 9.00273   8.76099   42.00642  1.000 210.79078 ? 65  LYS D CG  1 
ATOM   6458 C CD  . LYS D 4 84  ? 9.90715   7.99288   42.95610  1.000 214.80455 ? 65  LYS D CD  1 
ATOM   6459 C CE  . LYS D 4 84  ? 10.44030  6.72738   42.30286  1.000 217.76686 ? 65  LYS D CE  1 
ATOM   6460 N NZ  . LYS D 4 84  ? 11.14817  5.85380   43.27849  1.000 221.66224 ? 65  LYS D NZ  1 
ATOM   6461 N N   . GLY D 4 85  ? 6.01111   8.94471   40.48222  1.000 209.60229 ? 66  GLY D N   1 
ATOM   6462 C CA  . GLY D 4 85  ? 5.09151   7.88428   40.12952  1.000 210.50388 ? 66  GLY D CA  1 
ATOM   6463 C C   . GLY D 4 85  ? 3.63679   8.28801   40.04112  1.000 207.60848 ? 66  GLY D C   1 
ATOM   6464 O O   . GLY D 4 85  ? 2.82828   7.51329   39.51308  1.000 208.30807 ? 66  GLY D O   1 
ATOM   6465 N N   . ARG D 4 86  ? 3.27313   9.47082   40.53423  1.000 206.02420 ? 67  ARG D N   1 
ATOM   6466 C CA  . ARG D 4 86  ? 1.88998   9.92820   40.51981  1.000 203.55015 ? 67  ARG D CA  1 
ATOM   6467 C C   . ARG D 4 86  ? 1.57987   10.77787  39.29474  1.000 199.83916 ? 67  ARG D C   1 
ATOM   6468 O O   . ARG D 4 86  ? 0.49589   10.65579  38.71396  1.000 198.71638 ? 67  ARG D O   1 
ATOM   6469 C CB  . ARG D 4 86  ? 1.59392   10.72047  41.79569  1.000 203.15409 ? 67  ARG D CB  1 
ATOM   6470 C CG  . ARG D 4 86  ? 2.25582   10.13348  43.03204  1.000 206.88583 ? 67  ARG D CG  1 
ATOM   6471 C CD  . ARG D 4 86  ? 2.12218   11.03770  44.24790  1.000 206.64056 ? 67  ARG D CD  1 
ATOM   6472 N NE  . ARG D 4 86  ? 0.73597   11.19618  44.66979  1.000 206.33998 ? 67  ARG D NE  1 
ATOM   6473 C CZ  . ARG D 4 86  ? 0.06196   12.33680  44.61921  1.000 203.17753 ? 67  ARG D CZ  1 
ATOM   6474 N NH1 . ARG D 4 86  ? 0.62629   13.45539  44.19425  1.000 199.84480 ? 67  ARG D NH1 1 
ATOM   6475 N NH2 . ARG D 4 86  ? -1.20842  12.35707  45.01136  1.000 203.78475 ? 67  ARG D NH2 1 
ATOM   6476 N N   . PHE D 4 87  ? 2.51059   11.63770  38.89315  1.000 199.49098 ? 68  PHE D N   1 
ATOM   6477 C CA  . PHE D 4 87  ? 2.33853   12.50940  37.74116  1.000 194.29978 ? 68  PHE D CA  1 
ATOM   6478 C C   . PHE D 4 87  ? 3.16974   11.98455  36.57571  1.000 195.15734 ? 68  PHE D C   1 
ATOM   6479 O O   . PHE D 4 87  ? 4.12110   11.22013  36.75929  1.000 198.39813 ? 68  PHE D O   1 
ATOM   6480 C CB  . PHE D 4 87  ? 2.73781   13.95577  38.06776  1.000 192.30612 ? 68  PHE D CB  1 
ATOM   6481 C CG  . PHE D 4 87  ? 1.86904   14.62243  39.11218  1.000 191.42074 ? 68  PHE D CG  1 
ATOM   6482 C CD1 . PHE D 4 87  ? 0.83535   13.93778  39.73497  1.000 192.62272 ? 68  PHE D CD1 1 
ATOM   6483 C CD2 . PHE D 4 87  ? 2.08640   15.94522  39.46068  1.000 187.66608 ? 68  PHE D CD2 1 
ATOM   6484 C CE1 . PHE D 4 87  ? 0.04734   14.55300  40.68978  1.000 192.29004 ? 68  PHE D CE1 1 
ATOM   6485 C CE2 . PHE D 4 87  ? 1.29756   16.56784  40.41237  1.000 188.15825 ? 68  PHE D CE2 1 
ATOM   6486 C CZ  . PHE D 4 87  ? 0.27682   15.87008  41.02661  1.000 190.20147 ? 68  PHE D CZ  1 
ATOM   6487 N N   . THR D 4 88  ? 2.80153   12.40228  35.36542  1.000 182.53485 ? 69  THR D N   1 
ATOM   6488 C CA  . THR D 4 88  ? 3.44206   11.90766  34.14864  1.000 181.49516 ? 69  THR D CA  1 
ATOM   6489 C C   . THR D 4 88  ? 3.54242   13.04457  33.14209  1.000 178.97361 ? 69  THR D C   1 
ATOM   6490 O O   . THR D 4 88  ? 2.53502   13.44642  32.55253  1.000 176.96488 ? 69  THR D O   1 
ATOM   6491 C CB  . THR D 4 88  ? 2.66417   10.73010  33.55759  1.000 187.55125 ? 69  THR D CB  1 
ATOM   6492 O OG1 . THR D 4 88  ? 2.49660   9.71658   34.55689  1.000 195.66639 ? 69  THR D OG1 1 
ATOM   6493 C CG2 . THR D 4 88  ? 3.40817   10.14301  32.36786  1.000 185.96196 ? 69  THR D CG2 1 
ATOM   6494 N N   . ILE D 4 89  ? 4.75463   13.55580  32.94027  1.000 170.73060 ? 70  ILE D N   1 
ATOM   6495 C CA  . ILE D 4 89  ? 4.98616   14.58978  31.93839  1.000 170.29760 ? 70  ILE D CA  1 
ATOM   6496 C C   . ILE D 4 89  ? 5.18564   13.93240  30.57826  1.000 170.64799 ? 70  ILE D C   1 
ATOM   6497 O O   . ILE D 4 89  ? 5.66699   12.79770  30.47297  1.000 171.91748 ? 70  ILE D O   1 
ATOM   6498 C CB  . ILE D 4 89  ? 6.18840   15.47239  32.33513  1.000 172.36837 ? 70  ILE D CB  1 
ATOM   6499 C CG1 . ILE D 4 89  ? 6.22033   16.75402  31.49864  1.000 172.24847 ? 70  ILE D CG1 1 
ATOM   6500 C CG2 . ILE D 4 89  ? 7.49644   14.70874  32.19375  1.000 175.18500 ? 70  ILE D CG2 1 
ATOM   6501 C CD1 . ILE D 4 89  ? 7.30426   17.72583  31.91532  1.000 174.48571 ? 70  ILE D CD1 1 
ATOM   6502 N N   . SER D 4 90  ? 4.79395   14.64382  29.52444  1.000 166.18700 ? 71  SER D N   1 
ATOM   6503 C CA  . SER D 4 90  ? 4.86316   14.11727  28.16807  1.000 166.46306 ? 71  SER D CA  1 
ATOM   6504 C C   . SER D 4 90  ? 4.75043   15.27425  27.18762  1.000 166.59263 ? 71  SER D C   1 
ATOM   6505 O O   . SER D 4 90  ? 4.11085   16.28762  27.47987  1.000 165.59661 ? 71  SER D O   1 
ATOM   6506 C CB  . SER D 4 90  ? 3.76174   13.08342  27.91394  1.000 164.71158 ? 71  SER D CB  1 
ATOM   6507 O OG  . SER D 4 90  ? 2.53683   13.49690  28.49398  1.000 162.59393 ? 71  SER D OG  1 
ATOM   6508 N N   . ARG D 4 91  ? 5.37346   15.11256  26.02180  1.000 155.31377 ? 72  ARG D N   1 
ATOM   6509 C CA  . ARG D 4 91  ? 5.37826   16.15858  25.00961  1.000 154.53564 ? 72  ARG D CA  1 
ATOM   6510 C C   . ARG D 4 91  ? 5.13552   15.55611  23.63403  1.000 156.02735 ? 72  ARG D C   1 
ATOM   6511 O O   . ARG D 4 91  ? 5.60540   14.45499  23.33314  1.000 157.91742 ? 72  ARG D O   1 
ATOM   6512 C CB  . ARG D 4 91  ? 6.69895   16.94310  25.02022  1.000 154.42075 ? 72  ARG D CB  1 
ATOM   6513 C CG  . ARG D 4 91  ? 7.94461   16.09799  24.80646  1.000 156.29670 ? 72  ARG D CG  1 
ATOM   6514 C CD  . ARG D 4 91  ? 9.20210   16.92293  25.03382  1.000 156.32850 ? 72  ARG D CD  1 
ATOM   6515 N NE  . ARG D 4 91  ? 9.30727   18.03799  24.09986  1.000 156.04915 ? 72  ARG D NE  1 
ATOM   6516 C CZ  . ARG D 4 91  ? 10.14841  19.05399  24.23812  1.000 156.09330 ? 72  ARG D CZ  1 
ATOM   6517 N NH1 . ARG D 4 91  ? 10.96111  19.14197  25.27846  1.000 156.25427 ? 72  ARG D NH1 1 
ATOM   6518 N NH2 . ARG D 4 91  ? 10.17167  20.00807  23.31164  1.000 156.32894 ? 72  ARG D NH2 1 
ATOM   6519 N N   . ASP D 4 92  ? 4.39296   16.28852  22.80797  1.000 162.19877 ? 73  ASP D N   1 
ATOM   6520 C CA  . ASP D 4 92  ? 4.06343   15.89844  21.43884  1.000 161.95766 ? 73  ASP D CA  1 
ATOM   6521 C C   . ASP D 4 92  ? 4.71733   16.91827  20.51047  1.000 164.90346 ? 73  ASP D C   1 
ATOM   6522 O O   . ASP D 4 92  ? 4.10556   17.92628  20.14855  1.000 165.18307 ? 73  ASP D O   1 
ATOM   6523 C CB  . ASP D 4 92  ? 2.54299   15.83421  21.24152  1.000 159.10521 ? 73  ASP D CB  1 
ATOM   6524 C CG  . ASP D 4 92  ? 2.14411   15.40532  19.83889  1.000 158.62018 ? 73  ASP D CG  1 
ATOM   6525 O OD1 . ASP D 4 92  ? 3.02922   15.01677  19.04749  1.000 160.29688 ? 73  ASP D OD1 1 
ATOM   6526 O OD2 . ASP D 4 92  ? 0.93463   15.45752  19.52841  1.000 156.51434 ? 73  ASP D OD2 1 
ATOM   6527 N N   . ASN D 4 93  ? 5.96477   16.64819  20.11937  1.000 156.52584 ? 74  ASN D N   1 
ATOM   6528 C CA  . ASN D 4 93  ? 6.69605   17.56747  19.25601  1.000 159.94311 ? 74  ASN D CA  1 
ATOM   6529 C C   . ASN D 4 93  ? 6.16064   17.59656  17.83102  1.000 159.42681 ? 74  ASN D C   1 
ATOM   6530 O O   . ASN D 4 93  ? 6.61906   18.42287  17.03491  1.000 162.17618 ? 74  ASN D O   1 
ATOM   6531 C CB  . ASN D 4 93  ? 8.18285   17.21003  19.24759  1.000 162.85321 ? 74  ASN D CB  1 
ATOM   6532 C CG  . ASN D 4 93  ? 8.81564   17.33177  20.61942  1.000 163.74962 ? 74  ASN D CG  1 
ATOM   6533 O OD1 . ASN D 4 93  ? 8.17823   17.05310  21.63505  1.000 161.04777 ? 74  ASN D OD1 1 
ATOM   6534 N ND2 . ASN D 4 93  ? 10.07246  17.75923  20.65733  1.000 167.58603 ? 74  ASN D ND2 1 
ATOM   6535 N N   . ALA D 4 94  ? 5.21443   16.72069  17.48799  1.000 169.34144 ? 75  ALA D N   1 
ATOM   6536 C CA  . ALA D 4 94  ? 4.55303   16.82268  16.19204  1.000 168.38036 ? 75  ALA D CA  1 
ATOM   6537 C C   . ALA D 4 94  ? 3.56969   17.98646  16.17801  1.000 168.37199 ? 75  ALA D C   1 
ATOM   6538 O O   . ALA D 4 94  ? 3.57106   18.80453  15.25068  1.000 170.47696 ? 75  ALA D O   1 
ATOM   6539 C CB  . ALA D 4 94  ? 3.84640   15.50910  15.85605  1.000 165.20284 ? 75  ALA D CB  1 
ATOM   6540 N N   . LYS D 4 95  ? 2.72658   18.07983  17.20436  1.000 174.67526 ? 76  LYS D N   1 
ATOM   6541 C CA  . LYS D 4 95  ? 1.78243   19.17946  17.35134  1.000 174.67905 ? 76  LYS D CA  1 
ATOM   6542 C C   . LYS D 4 95  ? 2.34959   20.34258  18.15537  1.000 177.87156 ? 76  LYS D C   1 
ATOM   6543 O O   . LYS D 4 95  ? 1.66538   21.36077  18.30738  1.000 180.19325 ? 76  LYS D O   1 
ATOM   6544 C CB  . LYS D 4 95  ? 0.49207   18.68327  18.01301  1.000 159.80960 ? 76  LYS D CB  1 
ATOM   6545 C CG  . LYS D 4 95  ? -0.25523  17.62395  17.21813  1.000 161.73623 ? 76  LYS D CG  1 
ATOM   6546 C CD  . LYS D 4 95  ? -1.50733  17.16998  17.95319  1.000 161.39625 ? 76  LYS D CD  1 
ATOM   6547 C CE  . LYS D 4 95  ? -2.27039  16.12341  17.15720  1.000 163.78884 ? 76  LYS D CE  1 
ATOM   6548 N NZ  . LYS D 4 95  ? -2.73686  16.65205  15.84497  1.000 165.19225 ? 76  LYS D NZ  1 
ATOM   6549 N N   . ASN D 4 96  ? 3.57344   20.21141  18.67148  1.000 164.84685 ? 77  ASN D N   1 
ATOM   6550 C CA  . ASN D 4 96  ? 4.23191   21.24771  19.46836  1.000 167.87752 ? 77  ASN D CA  1 
ATOM   6551 C C   . ASN D 4 96  ? 3.39450   21.61641  20.69533  1.000 165.58967 ? 77  ASN D C   1 
ATOM   6552 O O   . ASN D 4 96  ? 3.01591   22.77014  20.90600  1.000 167.11947 ? 77  ASN D O   1 
ATOM   6553 C CB  . ASN D 4 96  ? 4.54417   22.48437  18.61672  1.000 174.36547 ? 77  ASN D CB  1 
ATOM   6554 C CG  . ASN D 4 96  ? 5.58829   22.21010  17.55157  1.000 178.84870 ? 77  ASN D CG  1 
ATOM   6555 O OD1 . ASN D 4 96  ? 5.71845   21.08546  17.06978  1.000 174.54875 ? 77  ASN D OD1 1 
ATOM   6556 N ND2 . ASN D 4 96  ? 6.34209   23.23937  17.18150  1.000 188.14569 ? 77  ASN D ND2 1 
ATOM   6557 N N   . THR D 4 97  ? 3.10853   20.60051  21.50916  1.000 164.90396 ? 78  THR D N   1 
ATOM   6558 C CA  . THR D 4 97  ? 2.35477   20.77170  22.74445  1.000 162.47570 ? 78  THR D CA  1 
ATOM   6559 C C   . THR D 4 97  ? 2.96153   19.90039  23.83463  1.000 161.10517 ? 78  THR D C   1 
ATOM   6560 O O   . THR D 4 97  ? 3.44165   18.79545  23.56637  1.000 160.75160 ? 78  THR D O   1 
ATOM   6561 C CB  . THR D 4 97  ? 0.86755   20.41188  22.57530  1.000 159.27835 ? 78  THR D CB  1 
ATOM   6562 O OG1 . THR D 4 97  ? 0.74786   19.07345  22.07875  1.000 157.39033 ? 78  THR D OG1 1 
ATOM   6563 C CG2 . THR D 4 97  ? 0.17331   21.37427  21.62011  1.000 160.64757 ? 78  THR D CG2 1 
ATOM   6564 N N   . LEU D 4 98  ? 2.94014   20.41019  25.06158  1.000 161.41230 ? 79  LEU D N   1 
ATOM   6565 C CA  . LEU D 4 98  ? 3.39180   19.68894  26.24183  1.000 160.19394 ? 79  LEU D CA  1 
ATOM   6566 C C   . LEU D 4 98  ? 2.18680   19.19060  27.03440  1.000 156.89244 ? 79  LEU D C   1 
ATOM   6567 O O   . LEU D 4 98  ? 1.08694   19.73871  26.94156  1.000 155.64323 ? 79  LEU D O   1 
ATOM   6568 C CB  . LEU D 4 98  ? 4.27413   20.58809  27.11578  1.000 162.04664 ? 79  LEU D CB  1 
ATOM   6569 C CG  . LEU D 4 98  ? 4.87624   20.02181  28.40628  1.000 161.42927 ? 79  LEU D CG  1 
ATOM   6570 C CD1 . LEU D 4 98  ? 5.91624   18.94666  28.11200  1.000 162.84201 ? 79  LEU D CD1 1 
ATOM   6571 C CD2 . LEU D 4 98  ? 5.46761   21.13846  29.25223  1.000 162.89871 ? 79  LEU D CD2 1 
ATOM   6572 N N   . TYR D 4 99  ? 2.40138   18.13160  27.81503  1.000 166.12605 ? 80  TYR D N   1 
ATOM   6573 C CA  . TYR D 4 99  ? 1.32615   17.52057  28.58274  1.000 163.70641 ? 80  TYR D CA  1 
ATOM   6574 C C   . TYR D 4 99  ? 1.80580   17.19920  29.99141  1.000 163.92338 ? 80  TYR D C   1 
ATOM   6575 O O   . TYR D 4 99  ? 2.98838   17.32996  30.31970  1.000 165.79223 ? 80  TYR D O   1 
ATOM   6576 C CB  . TYR D 4 99  ? 0.80247   16.25055  27.90268  1.000 162.73990 ? 80  TYR D CB  1 
ATOM   6577 C CG  . TYR D 4 99  ? 0.28722   16.47969  26.50346  1.000 162.53659 ? 80  TYR D CG  1 
ATOM   6578 C CD1 . TYR D 4 99  ? -1.02154  16.88619  26.28246  1.000 160.85749 ? 80  TYR D CD1 1 
ATOM   6579 C CD2 . TYR D 4 99  ? 1.11054   16.29303  25.40273  1.000 164.24080 ? 80  TYR D CD2 1 
ATOM   6580 C CE1 . TYR D 4 99  ? -1.49599  17.09905  25.00274  1.000 160.85311 ? 80  TYR D CE1 1 
ATOM   6581 C CE2 . TYR D 4 99  ? 0.64588   16.50298  24.12068  1.000 164.23838 ? 80  TYR D CE2 1 
ATOM   6582 C CZ  . TYR D 4 99  ? -0.65779  16.90445  23.92532  1.000 162.51093 ? 80  TYR D CZ  1 
ATOM   6583 O OH  . TYR D 4 99  ? -1.12309  17.11403  22.64753  1.000 162.60040 ? 80  TYR D OH  1 
ATOM   6584 N N   . LEU D 4 100 ? 0.85535   16.76982  30.82469  1.000 166.73600 ? 81  LEU D N   1 
ATOM   6585 C CA  . LEU D 4 100 ? 1.11877   16.35780  32.19848  1.000 167.25849 ? 81  LEU D CA  1 
ATOM   6586 C C   . LEU D 4 100 ? -0.07948  15.59520  32.75172  1.000 168.31925 ? 81  LEU D C   1 
ATOM   6587 O O   . LEU D 4 100 ? -1.15029  16.17635  32.95697  1.000 167.57721 ? 81  LEU D O   1 
ATOM   6588 C CB  . LEU D 4 100 ? 1.43649   17.56941  33.07727  1.000 165.88692 ? 81  LEU D CB  1 
ATOM   6589 C CG  . LEU D 4 100 ? 1.61619   17.31460  34.57578  1.000 166.48112 ? 81  LEU D CG  1 
ATOM   6590 C CD1 . LEU D 4 100 ? 2.74722   16.32982  34.83348  1.000 168.06144 ? 81  LEU D CD1 1 
ATOM   6591 C CD2 . LEU D 4 100 ? 1.85771   18.62237  35.31611  1.000 165.32034 ? 81  LEU D CD2 1 
ATOM   6592 N N   . GLN D 4 101 ? 0.08763   14.29605  32.99130  1.000 182.99704 ? 82  GLN D N   1 
ATOM   6593 C CA  . GLN D 4 101 ? -0.99125  13.42946  33.45788  1.000 185.31247 ? 82  GLN D CA  1 
ATOM   6594 C C   . GLN D 4 101 ? -0.80240  13.16626  34.94795  1.000 192.16992 ? 82  GLN D C   1 
ATOM   6595 O O   . GLN D 4 101 ? 0.16773   12.51863  35.35247  1.000 195.47109 ? 82  GLN D O   1 
ATOM   6596 C CB  . GLN D 4 101 ? -1.01368  12.12408  32.66557  1.000 191.98180 ? 82  GLN D CB  1 
ATOM   6597 C CG  . GLN D 4 101 ? -1.97370  11.07744  33.20815  1.000 197.19622 ? 82  GLN D CG  1 
ATOM   6598 C CD  . GLN D 4 101 ? -3.42663  11.49583  33.09630  1.000 195.72707 ? 82  GLN D CD  1 
ATOM   6599 O OE1 . GLN D 4 101 ? -3.99588  11.51926  32.00505  1.000 194.46622 ? 82  GLN D OE1 1 
ATOM   6600 N NE2 . GLN D 4 101 ? -4.03626  11.82535  34.22909  1.000 196.36101 ? 82  GLN D NE2 1 
ATOM   6601 N N   . MET D 4 102 ? -1.73499  13.66036  35.75727  1.000 196.47917 ? 83  MET D N   1 
ATOM   6602 C CA  . MET D 4 102 ? -1.67858  13.54716  37.20751  1.000 197.95240 ? 83  MET D CA  1 
ATOM   6603 C C   . MET D 4 102 ? -2.67016  12.49226  37.68231  1.000 202.61225 ? 83  MET D C   1 
ATOM   6604 O O   . MET D 4 102 ? -3.77283  12.38042  37.13964  1.000 203.42890 ? 83  MET D O   1 
ATOM   6605 C CB  . MET D 4 102 ? -1.97938  14.89942  37.85653  1.000 196.54550 ? 83  MET D CB  1 
ATOM   6606 C CG  . MET D 4 102 ? -0.98688  15.98885  37.47280  1.000 194.52222 ? 83  MET D CG  1 
ATOM   6607 S SD  . MET D 4 102 ? -1.73090  17.62708  37.37534  1.000 188.11514 ? 83  MET D SD  1 
ATOM   6608 C CE  . MET D 4 102 ? -2.87370  17.39342  36.01559  1.000 191.57483 ? 83  MET D CE  1 
ATOM   6609 N N   . SER D 4 103 ? -2.27747  11.71878  38.69589  1.000 202.35054 ? 84  SER D N   1 
ATOM   6610 C CA  . SER D 4 103 ? -3.07301  10.58373  39.14664  1.000 205.38145 ? 84  SER D CA  1 
ATOM   6611 C C   . SER D 4 103 ? -3.00235  10.45467  40.66278  1.000 207.78895 ? 84  SER D C   1 
ATOM   6612 O O   . SER D 4 103 ? -2.10043  10.99013  41.31152  1.000 207.30259 ? 84  SER D O   1 
ATOM   6613 C CB  . SER D 4 103 ? -2.60452  9.27653   38.49199  1.000 207.93203 ? 84  SER D CB  1 
ATOM   6614 O OG  . SER D 4 103 ? -2.61066  9.38092   37.07935  1.000 206.08574 ? 84  SER D OG  1 
ATOM   6615 N N   . SER D 4 104 ? -3.97089  9.71649   41.21449  1.000 213.62256 ? 85  SER D N   1 
ATOM   6616 C CA  . SER D 4 104 ? -4.07948  9.46309   42.65511  1.000 216.95596 ? 85  SER D CA  1 
ATOM   6617 C C   . SER D 4 104 ? -3.97317  10.76259  43.44929  1.000 214.73303 ? 85  SER D C   1 
ATOM   6618 O O   . SER D 4 104 ? -3.23943  10.86424  44.43343  1.000 216.71424 ? 85  SER D O   1 
ATOM   6619 C CB  . SER D 4 104 ? -3.02877  8.45437   43.11678  1.000 220.67868 ? 85  SER D CB  1 
ATOM   6620 O OG  . SER D 4 104 ? -1.74365  9.04685   43.17688  1.000 218.83258 ? 85  SER D OG  1 
ATOM   6621 N N   . LEU D 4 105 ? -4.72895  11.76252  43.00886  1.000 214.69383 ? 86  LEU D N   1 
ATOM   6622 C CA  . LEU D 4 105 ? -4.53543  13.12630  43.47585  1.000 212.21101 ? 86  LEU D CA  1 
ATOM   6623 C C   . LEU D 4 105 ? -4.93105  13.28654  44.94073  1.000 215.16554 ? 86  LEU D C   1 
ATOM   6624 O O   . LEU D 4 105 ? -5.84804  12.63076  45.43990  1.000 218.62935 ? 86  LEU D O   1 
ATOM   6625 C CB  . LEU D 4 105 ? -5.33867  14.09076  42.60461  1.000 208.96450 ? 86  LEU D CB  1 
ATOM   6626 C CG  . LEU D 4 105 ? -4.84697  14.14196  41.15853  1.000 206.41825 ? 86  LEU D CG  1 
ATOM   6627 C CD1 . LEU D 4 105 ? -5.93071  14.64661  40.22255  1.000 204.81343 ? 86  LEU D CD1 1 
ATOM   6628 C CD2 . LEU D 4 105 ? -3.61141  15.02009  41.07282  1.000 204.24305 ? 86  LEU D CD2 1 
ATOM   6629 N N   . ARG D 4 106 ? -4.21751  14.17217  45.62643  1.000 227.26506 ? 87  ARG D N   1 
ATOM   6630 C CA  . ARG D 4 106 ? -4.49343  14.54232  47.00421  1.000 229.70822 ? 87  ARG D CA  1 
ATOM   6631 C C   . ARG D 4 106 ? -4.95627  15.99384  47.06360  1.000 226.45046 ? 87  ARG D C   1 
ATOM   6632 O O   . ARG D 4 106 ? -4.87945  16.73577  46.07969  1.000 222.48102 ? 87  ARG D O   1 
ATOM   6633 C CB  . ARG D 4 106 ? -3.25012  14.34281  47.87957  1.000 194.05314 ? 87  ARG D CB  1 
ATOM   6634 C CG  . ARG D 4 106 ? -2.70665  12.92149  47.89017  1.000 196.92832 ? 87  ARG D CG  1 
ATOM   6635 C CD  . ARG D 4 106 ? -3.62444  11.97809  48.64875  1.000 200.57252 ? 87  ARG D CD  1 
ATOM   6636 N NE  . ARG D 4 106 ? -3.09933  10.61837  48.68424  1.000 203.88667 ? 87  ARG D NE  1 
ATOM   6637 C CZ  . ARG D 4 106 ? -3.40075  9.67640   47.80097  1.000 205.15334 ? 87  ARG D CZ  1 
ATOM   6638 N NH1 . ARG D 4 106 ? -4.23407  9.90890   46.79983  1.000 203.36291 ? 87  ARG D NH1 1 
ATOM   6639 N NH2 . ARG D 4 106 ? -2.85019  8.47183   47.92346  1.000 208.62141 ? 87  ARG D NH2 1 
ATOM   6640 N N   . SER D 4 107 ? -5.44005  16.39767  48.24255  1.000 221.69065 ? 88  SER D N   1 
ATOM   6641 C CA  . SER D 4 107 ? -5.89324  17.77395  48.42016  1.000 218.98236 ? 88  SER D CA  1 
ATOM   6642 C C   . SER D 4 107 ? -4.74350  18.76865  48.31107  1.000 215.86463 ? 88  SER D C   1 
ATOM   6643 O O   . SER D 4 107 ? -4.94368  19.89217  47.83571  1.000 213.09990 ? 88  SER D O   1 
ATOM   6644 C CB  . SER D 4 107 ? -6.59855  17.92871  49.76797  1.000 222.71745 ? 88  SER D CB  1 
ATOM   6645 O OG  . SER D 4 107 ? -5.75673  17.51765  50.82889  1.000 226.40338 ? 88  SER D OG  1 
ATOM   6646 N N   . GLU D 4 108 ? -3.53896  18.37824  48.73711  1.000 216.59733 ? 89  GLU D N   1 
ATOM   6647 C CA  . GLU D 4 108 ? -2.38221  19.26040  48.62444  1.000 214.92957 ? 89  GLU D CA  1 
ATOM   6648 C C   . GLU D 4 108 ? -2.02658  19.55909  47.17556  1.000 211.06796 ? 89  GLU D C   1 
ATOM   6649 O O   . GLU D 4 108 ? -1.38311  20.57735  46.89903  1.000 208.98518 ? 89  GLU D O   1 
ATOM   6650 C CB  . GLU D 4 108 ? -1.17847  18.63875  49.33494  1.000 217.98183 ? 89  GLU D CB  1 
ATOM   6651 C CG  . GLU D 4 108 ? -1.39645  18.37374  50.81663  1.000 221.96291 ? 89  GLU D CG  1 
ATOM   6652 C CD  . GLU D 4 108 ? -0.34542  17.45407  51.40299  1.000 226.12457 ? 89  GLU D CD  1 
ATOM   6653 O OE1 . GLU D 4 108 ? 0.39327   16.82046  50.62109  1.000 225.62525 ? 89  GLU D OE1 1 
ATOM   6654 O OE2 . GLU D 4 108 ? -0.25909  17.36155  52.64499  1.000 230.37117 ? 89  GLU D OE2 1 
ATOM   6655 N N   . ASP D 4 109 ? -2.43304  18.69711  46.24490  1.000 211.44073 ? 90  ASP D N   1 
ATOM   6656 C CA  . ASP D 4 109 ? -2.14862  18.89276  44.82901  1.000 206.66733 ? 90  ASP D CA  1 
ATOM   6657 C C   . ASP D 4 109 ? -2.90544  20.07122  44.22642  1.000 204.12607 ? 90  ASP D C   1 
ATOM   6658 O O   . ASP D 4 109 ? -2.78570  20.31161  43.01909  1.000 202.39062 ? 90  ASP D O   1 
ATOM   6659 C CB  . ASP D 4 109 ? -2.47556  17.61395  44.05635  1.000 208.06471 ? 90  ASP D CB  1 
ATOM   6660 C CG  . ASP D 4 109 ? -1.84947  16.38263  44.67843  1.000 212.66263 ? 90  ASP D CG  1 
ATOM   6661 O OD1 . ASP D 4 109 ? -1.12725  16.52275  45.68896  1.000 214.34395 ? 90  ASP D OD1 1 
ATOM   6662 O OD2 . ASP D 4 109 ? -2.08375  15.27361  44.15752  1.000 214.34727 ? 90  ASP D OD2 1 
ATOM   6663 N N   . THR D 4 110 ? -3.68035  20.79951  45.02677  1.000 195.52901 ? 91  THR D N   1 
ATOM   6664 C CA  . THR D 4 110 ? -4.39248  21.98424  44.55921  1.000 193.96443 ? 91  THR D CA  1 
ATOM   6665 C C   . THR D 4 110 ? -3.40447  23.13898  44.44485  1.000 191.90509 ? 91  THR D C   1 
ATOM   6666 O O   . THR D 4 110 ? -2.87750  23.61419  45.45613  1.000 192.88993 ? 91  THR D O   1 
ATOM   6667 C CB  . THR D 4 110 ? -5.52924  22.33174  45.51733  1.000 196.07263 ? 91  THR D CB  1 
ATOM   6668 O OG1 . THR D 4 110 ? -6.41776  21.21394  45.63523  1.000 199.53700 ? 91  THR D OG1 1 
ATOM   6669 C CG2 . THR D 4 110 ? -6.30214  23.53701  45.00721  1.000 194.85355 ? 91  THR D CG2 1 
ATOM   6670 N N   . ALA D 4 111 ? -3.15027  23.59233  43.21984  1.000 176.64009 ? 92  ALA D N   1 
ATOM   6671 C CA  . ALA D 4 111 ? -2.20258  24.67550  42.97909  1.000 176.65617 ? 92  ALA D CA  1 
ATOM   6672 C C   . ALA D 4 111 ? -2.41759  25.21307  41.56927  1.000 175.52832 ? 92  ALA D C   1 
ATOM   6673 O O   . ALA D 4 111 ? -3.28176  24.73904  40.82597  1.000 174.57947 ? 92  ALA D O   1 
ATOM   6674 C CB  . ALA D 4 111 ? -0.75831  24.20421  43.17909  1.000 178.57298 ? 92  ALA D CB  1 
ATOM   6675 N N   . MET D 4 112 ? -1.62019  26.21951  41.21123  1.000 180.98029 ? 93  MET D N   1 
ATOM   6676 C CA  . MET D 4 112 ? -1.62299  26.81006  39.87570  1.000 181.08753 ? 93  MET D CA  1 
ATOM   6677 C C   . MET D 4 112 ? -0.42770  26.24886  39.11622  1.000 180.42915 ? 93  MET D C   1 
ATOM   6678 O O   . MET D 4 112 ? 0.72296   26.54299  39.45406  1.000 180.80672 ? 93  MET D O   1 
ATOM   6679 C CB  . MET D 4 112 ? -1.55643  28.33431  39.95416  1.000 182.62368 ? 93  MET D CB  1 
ATOM   6680 C CG  . MET D 4 112 ? -1.32004  29.01403  38.61335  1.000 184.23313 ? 93  MET D CG  1 
ATOM   6681 S SD  . MET D 4 112 ? -2.80241  29.14819  37.59615  1.000 186.32273 ? 93  MET D SD  1 
ATOM   6682 C CE  . MET D 4 112 ? -3.32434  30.81801  37.98101  1.000 190.31929 ? 93  MET D CE  1 
ATOM   6683 N N   . TYR D 4 113 ? -0.69695  25.44706  38.09190  1.000 176.77392 ? 94  TYR D N   1 
ATOM   6684 C CA  . TYR D 4 113 ? 0.34737   24.69204  37.40577  1.000 176.67009 ? 94  TYR D CA  1 
ATOM   6685 C C   . TYR D 4 113 ? 0.85103   25.46719  36.19296  1.000 178.69970 ? 94  TYR D C   1 
ATOM   6686 O O   . TYR D 4 113 ? 0.09476   25.71804  35.24787  1.000 180.13896 ? 94  TYR D O   1 
ATOM   6687 C CB  . TYR D 4 113 ? -0.17362  23.31634  37.00316  1.000 175.72184 ? 94  TYR D CB  1 
ATOM   6688 C CG  . TYR D 4 113 ? -0.30663  22.37712  38.17918  1.000 175.21269 ? 94  TYR D CG  1 
ATOM   6689 C CD1 . TYR D 4 113 ? -1.41105  22.43488  39.01951  1.000 175.47722 ? 94  TYR D CD1 1 
ATOM   6690 C CD2 . TYR D 4 113 ? 0.68106   21.44404  38.45787  1.000 175.62682 ? 94  TYR D CD2 1 
ATOM   6691 C CE1 . TYR D 4 113 ? -1.52964  21.58289  40.09872  1.000 176.37576 ? 94  TYR D CE1 1 
ATOM   6692 C CE2 . TYR D 4 113 ? 0.56994   20.58697  39.53183  1.000 176.48056 ? 94  TYR D CE2 1 
ATOM   6693 C CZ  . TYR D 4 113 ? -0.53714  20.65994  40.34997  1.000 176.97679 ? 94  TYR D CZ  1 
ATOM   6694 O OH  . TYR D 4 113 ? -0.65073  19.80714  41.42399  1.000 179.25175 ? 94  TYR D OH  1 
ATOM   6695 N N   . TYR D 4 114 ? 2.12796   25.84164  36.22658  1.000 172.86326 ? 95  TYR D N   1 
ATOM   6696 C CA  . TYR D 4 114 ? 2.75628   26.62889  35.17589  1.000 176.14851 ? 95  TYR D CA  1 
ATOM   6697 C C   . TYR D 4 114 ? 3.56179   25.73943  34.23667  1.000 177.52087 ? 95  TYR D C   1 
ATOM   6698 O O   . TYR D 4 114 ? 4.18600   24.76513  34.66611  1.000 176.50310 ? 95  TYR D O   1 
ATOM   6699 C CB  . TYR D 4 114 ? 3.67332   27.69991  35.77135  1.000 178.13746 ? 95  TYR D CB  1 
ATOM   6700 C CG  . TYR D 4 114 ? 2.94726   28.86325  36.40319  1.000 178.25372 ? 95  TYR D CG  1 
ATOM   6701 C CD1 . TYR D 4 114 ? 2.33219   29.82746  35.61809  1.000 181.27563 ? 95  TYR D CD1 1 
ATOM   6702 C CD2 . TYR D 4 114 ? 2.89309   29.00866  37.78287  1.000 176.45278 ? 95  TYR D CD2 1 
ATOM   6703 C CE1 . TYR D 4 114 ? 1.67176   30.89613  36.18706  1.000 182.20905 ? 95  TYR D CE1 1 
ATOM   6704 C CE2 . TYR D 4 114 ? 2.23581   30.07714  38.36203  1.000 177.12736 ? 95  TYR D CE2 1 
ATOM   6705 C CZ  . TYR D 4 114 ? 1.62811   31.01861  37.55882  1.000 179.89088 ? 95  TYR D CZ  1 
ATOM   6706 O OH  . TYR D 4 114 ? 0.97208   32.08485  38.12995  1.000 181.37216 ? 95  TYR D OH  1 
ATOM   6707 N N   . CYS D 4 115 ? 3.55626   26.09748  32.95311  1.000 167.13498 ? 96  CYS D N   1 
ATOM   6708 C CA  . CYS D 4 115 ? 4.29732   25.39710  31.90678  1.000 169.12875 ? 96  CYS D CA  1 
ATOM   6709 C C   . CYS D 4 115 ? 5.42432   26.31308  31.44062  1.000 173.64166 ? 96  CYS D C   1 
ATOM   6710 O O   . CYS D 4 115 ? 5.17427   27.32400  30.77541  1.000 177.73666 ? 96  CYS D O   1 
ATOM   6711 C CB  . CYS D 4 115 ? 3.36125   25.01535  30.75926  1.000 169.06090 ? 96  CYS D CB  1 
ATOM   6712 S SG  . CYS D 4 115 ? 4.10789   24.62972  29.15680  1.000 173.08587 ? 96  CYS D SG  1 
ATOM   6713 N N   . GLY D 4 116 ? 6.65475   25.96800  31.79540  1.000 160.76652 ? 97  GLY D N   1 
ATOM   6714 C CA  . GLY D 4 116 ? 7.80568   26.82647  31.54772  1.000 164.59624 ? 97  GLY D CA  1 
ATOM   6715 C C   . GLY D 4 116 ? 8.84778   26.14663  30.68191  1.000 167.43710 ? 97  GLY D C   1 
ATOM   6716 O O   . GLY D 4 116 ? 9.10311   24.95013  30.82932  1.000 166.43994 ? 97  GLY D O   1 
ATOM   6717 N N   . ARG D 4 117 ? 9.45041   26.92096  29.78399  1.000 163.32990 ? 98  ARG D N   1 
ATOM   6718 C CA  . ARG D 4 117 ? 10.47514  26.42818  28.87316  1.000 166.49586 ? 98  ARG D CA  1 
ATOM   6719 C C   . ARG D 4 117 ? 11.85545  26.74367  29.43572  1.000 169.32615 ? 98  ARG D C   1 
ATOM   6720 O O   . ARG D 4 117 ? 12.13787  27.89292  29.78988  1.000 171.02019 ? 98  ARG D O   1 
ATOM   6721 C CB  . ARG D 4 117 ? 10.31178  27.05125  27.48488  1.000 169.57153 ? 98  ARG D CB  1 
ATOM   6722 C CG  . ARG D 4 117 ? 11.36148  26.61477  26.47608  1.000 172.86865 ? 98  ARG D CG  1 
ATOM   6723 C CD  . ARG D 4 117 ? 12.28362  27.76407  26.09714  1.000 177.49786 ? 98  ARG D CD  1 
ATOM   6724 N NE  . ARG D 4 117 ? 12.03654  28.24829  24.74387  1.000 182.63614 ? 98  ARG D NE  1 
ATOM   6725 C CZ  . ARG D 4 117 ? 12.62155  29.31327  24.21251  1.000 191.55989 ? 98  ARG D CZ  1 
ATOM   6726 N NH1 . ARG D 4 117 ? 13.48568  30.04202  24.89989  1.000 202.16599 ? 98  ARG D NH1 1 
ATOM   6727 N NH2 . ARG D 4 117 ? 12.33038  29.65754  22.96120  1.000 200.38160 ? 98  ARG D NH2 1 
ATOM   6728 N N   . GLN D 4 118 ? 12.71010  25.72621  29.51108  1.000 170.12293 ? 99  GLN D N   1 
ATOM   6729 C CA  . GLN D 4 118 ? 14.03844  25.89256  30.07910  1.000 173.02972 ? 99  GLN D CA  1 
ATOM   6730 C C   . GLN D 4 118 ? 14.98022  26.57922  29.09347  1.000 177.29982 ? 99  GLN D C   1 
ATOM   6731 O O   . GLN D 4 118 ? 14.77978  26.55873  27.87604  1.000 178.52275 ? 99  GLN D O   1 
ATOM   6732 C CB  . GLN D 4 118 ? 14.62817  24.54357  30.49094  1.000 172.93113 ? 99  GLN D CB  1 
ATOM   6733 C CG  . GLN D 4 118 ? 14.48441  24.21889  31.96691  1.000 171.11131 ? 99  GLN D CG  1 
ATOM   6734 C CD  . GLN D 4 118 ? 15.47562  23.16549  32.42526  1.000 173.24578 ? 99  GLN D CD  1 
ATOM   6735 O OE1 . GLN D 4 118 ? 16.54319  23.00284  31.83327  1.000 176.85696 ? 99  GLN D OE1 1 
ATOM   6736 N NE2 . GLN D 4 118 ? 15.12669  22.44352  33.48407  1.000 171.29879 ? 99  GLN D NE2 1 
ATOM   6737 N N   . VAL D 4 119 ? 16.02821  27.18624  29.64586  1.000 180.58788 ? 100 VAL D N   1 
ATOM   6738 C CA  . VAL D 4 119 ? 17.05732  27.84451  28.84930  1.000 184.50786 ? 100 VAL D CA  1 
ATOM   6739 C C   . VAL D 4 119 ? 17.97693  26.79001  28.24965  1.000 187.65369 ? 100 VAL D C   1 
ATOM   6740 O O   . VAL D 4 119 ? 18.32502  25.80080  28.90618  1.000 185.37448 ? 100 VAL D O   1 
ATOM   6741 C CB  . VAL D 4 119 ? 17.84163  28.85063  29.71247  1.000 192.70780 ? 100 VAL D CB  1 
ATOM   6742 C CG1 . VAL D 4 119 ? 18.99185  29.46100  28.92324  1.000 197.54227 ? 100 VAL D CG1 1 
ATOM   6743 C CG2 . VAL D 4 119 ? 16.91455  29.94060  30.23165  1.000 194.38284 ? 100 VAL D CG2 1 
ATOM   6744 N N   . ASN D 4 120 ? 18.37486  26.99411  26.99015  1.000 193.67976 ? 101 ASN D N   1 
ATOM   6745 C CA  . ASN D 4 120 ? 19.25897  26.05722  26.30853  1.000 193.22675 ? 101 ASN D CA  1 
ATOM   6746 C C   . ASN D 4 120 ? 20.48075  26.72808  25.68909  1.000 197.18567 ? 101 ASN D C   1 
ATOM   6747 O O   . ASN D 4 120 ? 21.15153  26.10499  24.85582  1.000 196.05634 ? 101 ASN D O   1 
ATOM   6748 C CB  . ASN D 4 120 ? 18.49778  25.28779  25.22357  1.000 191.58345 ? 101 ASN D CB  1 
ATOM   6749 C CG  . ASN D 4 120 ? 18.34760  26.08539  23.94254  1.000 196.43259 ? 101 ASN D CG  1 
ATOM   6750 O OD1 . ASN D 4 120 ? 18.06400  27.28421  23.97171  1.000 198.54481 ? 101 ASN D OD1 1 
ATOM   6751 N ND2 . ASN D 4 120 ? 18.54630  25.42325  22.80665  1.000 200.24357 ? 101 ASN D ND2 1 
ATOM   6752 N N   . ARG D 4 121 ? 20.77733  27.97789  26.05532  1.000 201.75290 ? 102 ARG D N   1 
ATOM   6753 C CA  . ARG D 4 121 ? 21.98342  28.65268  25.58760  1.000 204.51846 ? 102 ARG D CA  1 
ATOM   6754 C C   . ARG D 4 121 ? 23.18453  27.74502  25.81908  1.000 201.55535 ? 102 ARG D C   1 
ATOM   6755 O O   . ARG D 4 121 ? 23.83165  27.29349  24.86804  1.000 200.91984 ? 102 ARG D O   1 
ATOM   6756 C CB  . ARG D 4 121 ? 22.18204  29.98666  26.31202  1.000 208.16932 ? 102 ARG D CB  1 
ATOM   6757 C CG  . ARG D 4 121 ? 21.08031  31.01105  26.06559  1.000 212.12096 ? 102 ARG D CG  1 
ATOM   6758 C CD  . ARG D 4 121 ? 21.33601  32.31541  26.82135  1.000 215.49865 ? 102 ARG D CD  1 
ATOM   6759 N NE  . ARG D 4 121 ? 22.48959  33.04612  26.30715  1.000 220.64301 ? 102 ARG D NE  1 
ATOM   6760 C CZ  . ARG D 4 121 ? 23.65064  33.16341  26.93792  1.000 223.80901 ? 102 ARG D CZ  1 
ATOM   6761 N NH1 . ARG D 4 121 ? 23.85249  32.61336  28.12415  1.000 222.44502 ? 102 ARG D NH1 1 
ATOM   6762 N NH2 . ARG D 4 121 ? 24.63159  33.85744  26.36736  1.000 228.35427 ? 102 ARG D NH2 1 
ATOM   6763 N N   . HIS D 4 122 ? 23.47105  27.47046  27.08843  1.000 215.41464 ? 103 HIS D N   1 
ATOM   6764 C CA  . HIS D 4 122 ? 24.42070  26.43866  27.46927  1.000 212.88642 ? 103 HIS D CA  1 
ATOM   6765 C C   . HIS D 4 122 ? 23.64464  25.13365  27.65891  1.000 209.79214 ? 103 HIS D C   1 
ATOM   6766 O O   . HIS D 4 122 ? 22.68434  25.08580  28.43440  1.000 209.00155 ? 103 HIS D O   1 
ATOM   6767 C CB  . HIS D 4 122 ? 25.18311  26.82876  28.73467  1.000 213.66437 ? 103 HIS D CB  1 
ATOM   6768 C CG  . HIS D 4 122 ? 25.87935  28.15305  28.64154  1.000 218.21592 ? 103 HIS D CG  1 
ATOM   6769 N ND1 . HIS D 4 122 ? 25.21141  29.35321  28.76145  1.000 218.64275 ? 103 HIS D ND1 1 
ATOM   6770 C CD2 . HIS D 4 122 ? 27.18469  28.46549  28.45413  1.000 222.69549 ? 103 HIS D CD2 1 
ATOM   6771 C CE1 . HIS D 4 122 ? 26.07471  30.34677  28.64724  1.000 223.29058 ? 103 HIS D CE1 1 
ATOM   6772 N NE2 . HIS D 4 122 ? 27.27827  29.83556  28.45994  1.000 225.77012 ? 103 HIS D NE2 1 
ATOM   6773 N N   . ASP D 4 123 ? 24.04519  24.08890  26.93492  1.000 206.23869 ? 104 ASP D N   1 
ATOM   6774 C CA  . ASP D 4 123 ? 23.28504  22.85413  26.85449  1.000 203.16582 ? 104 ASP D CA  1 
ATOM   6775 C C   . ASP D 4 123 ? 23.36389  22.11729  28.18418  1.000 202.03652 ? 104 ASP D C   1 
ATOM   6776 O O   . ASP D 4 123 ? 24.31933  21.37484  28.44808  1.000 201.74802 ? 104 ASP D O   1 
ATOM   6777 C CB  . ASP D 4 123 ? 23.81063  21.98329  25.70323  1.000 201.79340 ? 104 ASP D CB  1 
ATOM   6778 C CG  . ASP D 4 123 ? 23.57875  22.62386  24.33553  1.000 202.78420 ? 104 ASP D CG  1 
ATOM   6779 O OD1 . ASP D 4 123 ? 23.35053  23.83663  24.26936  1.000 205.46785 ? 104 ASP D OD1 1 
ATOM   6780 O OD2 . ASP D 4 123 ? 23.62888  21.88658  23.32085  1.000 201.27531 ? 104 ASP D OD2 1 
ATOM   6781 N N   . ARG D 4 124 ? 22.35450  22.29680  29.01931  1.000 204.36677 ? 105 ARG D N   1 
ATOM   6782 C CA  . ARG D 4 124 ? 22.28721  21.61901  30.30367  1.000 203.42237 ? 105 ARG D CA  1 
ATOM   6783 C C   . ARG D 4 124 ? 20.85882  21.15147  30.53987  1.000 199.44804 ? 105 ARG D C   1 
ATOM   6784 O O   . ARG D 4 124 ? 19.90313  21.75019  30.04265  1.000 196.86442 ? 105 ARG D O   1 
ATOM   6785 C CB  . ARG D 4 124 ? 22.75328  22.52297  31.45967  1.000 204.66787 ? 105 ARG D CB  1 
ATOM   6786 C CG  . ARG D 4 124 ? 22.98418  21.77798  32.76454  1.000 204.68714 ? 105 ARG D CG  1 
ATOM   6787 C CD  . ARG D 4 124 ? 23.78000  22.60628  33.75210  1.000 205.95508 ? 105 ARG D CD  1 
ATOM   6788 N NE  . ARG D 4 124 ? 24.16781  21.82190  34.91796  1.000 206.33178 ? 105 ARG D NE  1 
ATOM   6789 C CZ  . ARG D 4 124 ? 23.50394  21.80375  36.06547  1.000 205.52306 ? 105 ARG D CZ  1 
ATOM   6790 N NH1 . ARG D 4 124 ? 22.41631  22.53497  36.24692  1.000 203.72669 ? 105 ARG D NH1 1 
ATOM   6791 N NH2 . ARG D 4 124 ? 23.94417  21.03453  37.05704  1.000 206.66741 ? 105 ARG D NH2 1 
ATOM   6792 N N   . ALA D 4 125 ? 20.72711  20.05485  31.28800  1.000 206.64019 ? 106 ALA D N   1 
ATOM   6793 C CA  . ALA D 4 125 ? 19.41524  19.49577  31.58722  1.000 198.01275 ? 106 ALA D CA  1 
ATOM   6794 C C   . ALA D 4 125 ? 18.66253  20.31117  32.62941  1.000 191.86938 ? 106 ALA D C   1 
ATOM   6795 O O   . ALA D 4 125 ? 17.42767  20.34225  32.60736  1.000 184.84461 ? 106 ALA D O   1 
ATOM   6796 C CB  . ALA D 4 125 ? 19.56097  18.04975  32.06480  1.000 198.05845 ? 106 ALA D CB  1 
ATOM   6797 N N   . LEU D 4 126 ? 19.37459  20.95939  33.54773  1.000 198.40389 ? 107 LEU D N   1 
ATOM   6798 C CA  . LEU D 4 126 ? 18.76731  21.76637  34.59952  1.000 195.82591 ? 107 LEU D CA  1 
ATOM   6799 C C   . LEU D 4 126 ? 19.16545  23.21997  34.39012  1.000 201.11692 ? 107 LEU D C   1 
ATOM   6800 O O   . LEU D 4 126 ? 20.35052  23.55968  34.47329  1.000 206.66331 ? 107 LEU D O   1 
ATOM   6801 C CB  . LEU D 4 126 ? 19.19818  21.27864  35.98541  1.000 198.38896 ? 107 LEU D CB  1 
ATOM   6802 C CG  . LEU D 4 126 ? 18.77012  22.11153  37.19556  1.000 197.18063 ? 107 LEU D CG  1 
ATOM   6803 C CD1 . LEU D 4 126 ? 17.25812  22.26197  37.24771  1.000 186.97854 ? 107 LEU D CD1 1 
ATOM   6804 C CD2 . LEU D 4 126 ? 19.29087  21.48887  38.48298  1.000 200.25684 ? 107 LEU D CD2 1 
ATOM   6805 N N   . ASP D 4 127 ? 18.17922  24.07298  34.12073  1.000 196.76352 ? 108 ASP D N   1 
ATOM   6806 C CA  . ASP D 4 127 ? 18.42742  25.48526  33.86977  1.000 202.86838 ? 108 ASP D CA  1 
ATOM   6807 C C   . ASP D 4 127 ? 17.20654  26.28927  34.29625  1.000 192.17813 ? 108 ASP D C   1 
ATOM   6808 O O   . ASP D 4 127 ? 16.18125  25.73594  34.70345  1.000 182.45688 ? 108 ASP D O   1 
ATOM   6809 C CB  . ASP D 4 127 ? 18.76403  25.73508  32.39566  1.000 208.64025 ? 108 ASP D CB  1 
ATOM   6810 C CG  . ASP D 4 127 ? 20.25250  25.68611  32.12065  1.000 212.86568 ? 108 ASP D CG  1 
ATOM   6811 O OD1 . ASP D 4 127 ? 21.03575  26.04132  33.02573  1.000 213.85648 ? 108 ASP D OD1 1 
ATOM   6812 O OD2 . ASP D 4 127 ? 20.63967  25.29840  30.99836  1.000 214.00070 ? 108 ASP D OD2 1 
ATOM   6813 N N   . ALA D 4 128 ? 17.32826  27.61083  34.19815  1.000 199.23735 ? 109 ALA D N   1 
ATOM   6814 C CA  . ALA D 4 128 ? 16.21685  28.49706  34.49714  1.000 188.38812 ? 109 ALA D CA  1 
ATOM   6815 C C   . ALA D 4 128 ? 15.17969  28.43854  33.37838  1.000 181.00958 ? 109 ALA D C   1 
ATOM   6816 O O   . ALA D 4 128 ? 15.41879  27.89651  32.29387  1.000 182.19142 ? 109 ALA D O   1 
ATOM   6817 C CB  . ALA D 4 128 ? 16.71386  29.92880  34.69283  1.000 202.47262 ? 109 ALA D CB  1 
ATOM   6818 N N   . MET D 4 129 ? 14.01011  29.00816  33.65077  1.000 185.91634 ? 110 MET D N   1 
ATOM   6819 C CA  . MET D 4 129 ? 12.90203  29.01935  32.69858  1.000 182.53653 ? 110 MET D CA  1 
ATOM   6820 C C   . MET D 4 129 ? 12.91717  30.34235  31.94239  1.000 187.86348 ? 110 MET D C   1 
ATOM   6821 O O   . MET D 4 129 ? 12.60501  31.39523  32.50812  1.000 187.75471 ? 110 MET D O   1 
ATOM   6822 C CB  . MET D 4 129 ? 11.57204  28.79429  33.40693  1.000 174.94155 ? 110 MET D CB  1 
ATOM   6823 C CG  . MET D 4 129 ? 11.42368  27.39356  33.97380  1.000 172.54284 ? 110 MET D CG  1 
ATOM   6824 S SD  . MET D 4 129 ? 9.79234   27.06256  34.65731  1.000 167.25783 ? 110 MET D SD  1 
ATOM   6825 C CE  . MET D 4 129 ? 9.98951   25.34787  35.12972  1.000 166.10255 ? 110 MET D CE  1 
ATOM   6826 N N   . ASP D 4 130 ? 13.28687  30.27790  30.66199  1.000 179.16354 ? 111 ASP D N   1 
ATOM   6827 C CA  . ASP D 4 130 ? 13.36258  31.47751  29.83441  1.000 188.60792 ? 111 ASP D CA  1 
ATOM   6828 C C   . ASP D 4 130 ? 12.02127  32.19743  29.78977  1.000 183.31315 ? 111 ASP D C   1 
ATOM   6829 O O   . ASP D 4 130 ? 11.93870  33.40185  30.05648  1.000 192.81672 ? 111 ASP D O   1 
ATOM   6830 C CB  . ASP D 4 130 ? 13.82091  31.09769  28.42485  1.000 197.68236 ? 111 ASP D CB  1 
ATOM   6831 C CG  . ASP D 4 130 ? 14.56530  32.21775  27.72635  1.000 213.84718 ? 111 ASP D CG  1 
ATOM   6832 O OD1 . ASP D 4 130 ? 14.27710  33.40161  28.00347  1.000 218.24160 ? 111 ASP D OD1 1 
ATOM   6833 O OD2 . ASP D 4 130 ? 15.44630  31.90970  26.89692  1.000 220.46273 ? 111 ASP D OD2 1 
ATOM   6834 N N   . TYR D 4 131 ? 10.95687  31.47105  29.46220  1.000 179.07982 ? 112 TYR D N   1 
ATOM   6835 C CA  . TYR D 4 131 ? 9.62079   32.03695  29.37379  1.000 177.20090 ? 112 TYR D CA  1 
ATOM   6836 C C   . TYR D 4 131 ? 8.64428   31.16450  30.14545  1.000 170.85477 ? 112 TYR D C   1 
ATOM   6837 O O   . TYR D 4 131 ? 8.71534   29.93321  30.08688  1.000 169.02203 ? 112 TYR D O   1 
ATOM   6838 C CB  . TYR D 4 131 ? 9.17204   32.16801  27.91620  1.000 184.19825 ? 112 TYR D CB  1 
ATOM   6839 C CG  . TYR D 4 131 ? 10.12348  32.97591  27.06620  1.000 203.90150 ? 112 TYR D CG  1 
ATOM   6840 C CD1 . TYR D 4 131 ? 10.12473  34.36274  27.12091  1.000 212.82988 ? 112 TYR D CD1 1 
ATOM   6841 C CD2 . TYR D 4 131 ? 11.02233  32.35257  26.21110  1.000 208.94802 ? 112 TYR D CD2 1 
ATOM   6842 C CE1 . TYR D 4 131 ? 10.99358  35.10720  26.34738  1.000 225.04994 ? 112 TYR D CE1 1 
ATOM   6843 C CE2 . TYR D 4 131 ? 11.89489  33.08841  25.43276  1.000 222.18169 ? 112 TYR D CE2 1 
ATOM   6844 C CZ  . TYR D 4 131 ? 11.87615  34.46517  25.50474  1.000 229.56320 ? 112 TYR D CZ  1 
ATOM   6845 O OH  . TYR D 4 131 ? 12.74329  35.20235  24.73148  1.000 238.32620 ? 112 TYR D OH  1 
ATOM   6846 N N   . TRP D 4 132 ? 7.73694   31.81048  30.86850  1.000 189.42543 ? 113 TRP D N   1 
ATOM   6847 C CA  . TRP D 4 132 ? 6.70255   31.13318  31.63200  1.000 180.98966 ? 113 TRP D CA  1 
ATOM   6848 C C   . TRP D 4 132 ? 5.36305   31.25971  30.91957  1.000 180.96830 ? 113 TRP D C   1 
ATOM   6849 O O   . TRP D 4 132 ? 5.16949   32.11883  30.05532  1.000 187.53960 ? 113 TRP D O   1 
ATOM   6850 C CB  . TRP D 4 132 ? 6.59772   31.70785  33.04863  1.000 177.50887 ? 113 TRP D CB  1 
ATOM   6851 C CG  . TRP D 4 132 ? 7.78977   31.42318  33.91412  1.000 177.45059 ? 113 TRP D CG  1 
ATOM   6852 C CD1 . TRP D 4 132 ? 9.09665   31.69350  33.62746  1.000 183.54738 ? 113 TRP D CD1 1 
ATOM   6853 C CD2 . TRP D 4 132 ? 7.78041   30.83021  35.21860  1.000 172.45490 ? 113 TRP D CD2 1 
ATOM   6854 N NE1 . TRP D 4 132 ? 9.90152   31.29551  34.66688  1.000 182.71070 ? 113 TRP D NE1 1 
ATOM   6855 C CE2 . TRP D 4 132 ? 9.11792   30.76277  35.65639  1.000 176.18815 ? 113 TRP D CE2 1 
ATOM   6856 C CE3 . TRP D 4 132 ? 6.77156   30.34477  36.05598  1.000 167.90591 ? 113 TRP D CE3 1 
ATOM   6857 C CZ2 . TRP D 4 132 ? 9.47230   30.23070  36.89461  1.000 174.40551 ? 113 TRP D CZ2 1 
ATOM   6858 C CZ3 . TRP D 4 132 ? 7.12532   29.81779  37.28501  1.000 167.00467 ? 113 TRP D CZ3 1 
ATOM   6859 C CH2 . TRP D 4 132 ? 8.46388   29.76448  37.69228  1.000 169.88352 ? 113 TRP D CH2 1 
ATOM   6860 N N   . GLY D 4 133 ? 4.43132   30.38860  31.29785  1.000 178.01413 ? 114 GLY D N   1 
ATOM   6861 C CA  . GLY D 4 133 ? 3.11253   30.37638  30.70921  1.000 178.33379 ? 114 GLY D CA  1 
ATOM   6862 C C   . GLY D 4 133 ? 2.07207   31.07078  31.57705  1.000 176.21155 ? 114 GLY D C   1 
ATOM   6863 O O   . GLY D 4 133 ? 2.32908   31.47719  32.70645  1.000 173.61069 ? 114 GLY D O   1 
ATOM   6864 N N   . GLN D 4 134 ? 0.86910   31.19413  31.01054  1.000 184.82592 ? 115 GLN D N   1 
ATOM   6865 C CA  . GLN D 4 134 ? -0.21857  31.87846  31.70327  1.000 184.03362 ? 115 GLN D CA  1 
ATOM   6866 C C   . GLN D 4 134 ? -0.57571  31.17567  33.00652  1.000 176.94636 ? 115 GLN D C   1 
ATOM   6867 O O   . GLN D 4 134 ? -0.89080  31.82850  34.00884  1.000 175.94479 ? 115 GLN D O   1 
ATOM   6868 C CB  . GLN D 4 134 ? -1.44048  31.96240  30.79009  1.000 188.01143 ? 115 GLN D CB  1 
ATOM   6869 C CG  . GLN D 4 134 ? -1.14064  32.50946  29.40483  1.000 192.60691 ? 115 GLN D CG  1 
ATOM   6870 C CD  . GLN D 4 134 ? -2.27474  32.26663  28.43083  1.000 197.36396 ? 115 GLN D CD  1 
ATOM   6871 O OE1 . GLN D 4 134 ? -2.97737  31.25981  28.51941  1.000 196.15505 ? 115 GLN D OE1 1 
ATOM   6872 N NE2 . GLN D 4 134 ? -2.46438  33.19270  27.49838  1.000 203.45624 ? 115 GLN D NE2 1 
ATOM   6873 N N   . GLY D 4 135 ? -0.53100  29.84698  33.01237  1.000 190.26075 ? 116 GLY D N   1 
ATOM   6874 C CA  . GLY D 4 135 ? -0.87676  29.08546  34.19404  1.000 184.99576 ? 116 GLY D CA  1 
ATOM   6875 C C   . GLY D 4 135 ? -2.34724  28.72721  34.25520  1.000 184.28348 ? 116 GLY D C   1 
ATOM   6876 O O   . GLY D 4 135 ? -3.21200  29.59420  34.10255  1.000 187.35532 ? 116 GLY D O   1 
ATOM   6877 N N   . THR D 4 136 ? -2.64228  27.44701  34.47265  1.000 189.52395 ? 117 THR D N   1 
ATOM   6878 C CA  . THR D 4 136 ? -4.00815  26.96454  34.63509  1.000 189.46974 ? 117 THR D CA  1 
ATOM   6879 C C   . THR D 4 136 ? -4.10483  26.25060  35.97656  1.000 186.63015 ? 117 THR D C   1 
ATOM   6880 O O   . THR D 4 136 ? -3.34385  25.31422  36.24507  1.000 184.62962 ? 117 THR D O   1 
ATOM   6881 C CB  . THR D 4 136 ? -4.41858  26.04358  33.47925  1.000 190.75775 ? 117 THR D CB  1 
ATOM   6882 O OG1 . THR D 4 136 ? -5.67847  25.42613  33.77344  1.000 191.21773 ? 117 THR D OG1 1 
ATOM   6883 C CG2 . THR D 4 136 ? -3.36639  24.96901  33.22216  1.000 188.79258 ? 117 THR D CG2 1 
ATOM   6884 N N   . SER D 4 137 ? -5.02484  26.70391  36.82121  1.000 196.35048 ? 118 SER D N   1 
ATOM   6885 C CA  . SER D 4 137 ? -5.12472  26.20946  38.18593  1.000 195.40407 ? 118 SER D CA  1 
ATOM   6886 C C   . SER D 4 137 ? -6.10635  25.04796  38.28045  1.000 195.62387 ? 118 SER D C   1 
ATOM   6887 O O   . SER D 4 137 ? -7.09205  24.97682  37.54161  1.000 197.27807 ? 118 SER D O   1 
ATOM   6888 C CB  . SER D 4 137 ? -5.55632  27.32938  39.13434  1.000 197.30210 ? 118 SER D CB  1 
ATOM   6889 O OG  . SER D 4 137 ? -5.60557  26.86885  40.47397  1.000 198.56041 ? 118 SER D OG  1 
ATOM   6890 N N   . VAL D 4 138 ? -5.82405  24.13395  39.20825  1.000 194.19142 ? 119 VAL D N   1 
ATOM   6891 C CA  . VAL D 4 138 ? -6.67489  22.98227  39.47207  1.000 195.57218 ? 119 VAL D CA  1 
ATOM   6892 C C   . VAL D 4 138 ? -7.13453  23.03838  40.92687  1.000 199.16937 ? 119 VAL D C   1 
ATOM   6893 O O   . VAL D 4 138 ? -6.61156  23.79958  41.74139  1.000 196.20591 ? 119 VAL D O   1 
ATOM   6894 C CB  . VAL D 4 138 ? -5.96567  21.64554  39.17637  1.000 194.41716 ? 119 VAL D CB  1 
ATOM   6895 C CG1 . VAL D 4 138 ? -5.22375  21.71430  37.84979  1.000 192.49121 ? 119 VAL D CG1 1 
ATOM   6896 C CG2 . VAL D 4 138 ? -5.02284  21.27845  40.31245  1.000 193.69217 ? 119 VAL D CG2 1 
ATOM   6897 N N   . THR D 4 139 ? -8.12682  22.20874  41.24417  1.000 208.08105 ? 120 THR D N   1 
ATOM   6898 C CA  . THR D 4 139 ? -8.69448  22.14365  42.58360  1.000 209.84110 ? 120 THR D CA  1 
ATOM   6899 C C   . THR D 4 139 ? -9.07944  20.70570  42.89938  1.000 212.78137 ? 120 THR D C   1 
ATOM   6900 O O   . THR D 4 139 ? -9.49921  19.95163  42.01740  1.000 213.34684 ? 120 THR D O   1 
ATOM   6901 C CB  . THR D 4 139 ? -9.91911  23.06387  42.73509  1.000 210.90908 ? 120 THR D CB  1 
ATOM   6902 O OG1 . THR D 4 139 ? -10.68833 23.05163  41.52605  1.000 211.51731 ? 120 THR D OG1 1 
ATOM   6903 C CG2 . THR D 4 139 ? -9.48446  24.48460  43.05303  1.000 209.83974 ? 120 THR D CG2 1 
ATOM   6904 N N   . VAL D 4 140 ? -8.92962  20.33146  44.16896  1.000 215.43288 ? 121 VAL D N   1 
ATOM   6905 C CA  . VAL D 4 140 ? -9.22646  18.98287  44.64366  1.000 217.96140 ? 121 VAL D CA  1 
ATOM   6906 C C   . VAL D 4 140 ? -10.16331 19.10780  45.83613  1.000 220.84655 ? 121 VAL D C   1 
ATOM   6907 O O   . VAL D 4 140 ? -9.74025  19.53291  46.91927  1.000 221.71547 ? 121 VAL D O   1 
ATOM   6908 C CB  . VAL D 4 140 ? -7.95532  18.21310  45.03003  1.000 218.63339 ? 121 VAL D CB  1 
ATOM   6909 C CG1 . VAL D 4 140 ? -8.29561  16.78294  45.40498  1.000 222.38751 ? 121 VAL D CG1 1 
ATOM   6910 C CG2 . VAL D 4 140 ? -6.94353  18.24424  43.89317  1.000 216.00732 ? 121 VAL D CG2 1 
ATOM   6911 N N   . SER D 4 141 ? -11.43061 18.74204  45.64360  1.000 222.49201 ? 122 SER D N   1 
ATOM   6912 C CA  . SER D 4 141 ? -12.41866 18.83000  46.71089  1.000 225.64991 ? 122 SER D CA  1 
ATOM   6913 C C   . SER D 4 141 ? -13.60829 17.94622  46.36508  1.000 227.79142 ? 122 SER D C   1 
ATOM   6914 O O   . SER D 4 141 ? -13.86550 17.69469  45.17990  1.000 225.94937 ? 122 SER D O   1 
ATOM   6915 C CB  . SER D 4 141 ? -12.86526 20.28094  46.93704  1.000 224.21381 ? 122 SER D CB  1 
ATOM   6916 O OG  . SER D 4 141 ? -11.85977 21.01142  47.62269  1.000 223.27365 ? 122 SER D OG  1 
ATOM   6917 N N   . PRO D 4 142 ? -14.32249 17.43121  47.36785  1.000 229.75586 ? 123 PRO D N   1 
ATOM   6918 C CA  . PRO D 4 142 ? -15.50585 16.60050  47.11255  1.000 241.22750 ? 123 PRO D CA  1 
ATOM   6919 C C   . PRO D 4 142 ? -16.80425 17.35330  46.85994  1.000 239.97101 ? 123 PRO D C   1 
ATOM   6920 O O   . PRO D 4 142 ? -17.83152 16.69857  46.64527  1.000 250.15122 ? 123 PRO D O   1 
ATOM   6921 C CB  . PRO D 4 142 ? -15.62163 15.77470  48.41058  1.000 213.12413 ? 123 PRO D CB  1 
ATOM   6922 C CG  . PRO D 4 142 ? -14.28676 15.86226  49.06263  1.000 212.02435 ? 123 PRO D CG  1 
ATOM   6923 C CD  . PRO D 4 142 ? -13.82175 17.24408  48.74120  1.000 208.39362 ? 123 PRO D CD  1 
ATOM   6924 N N   . ALA D 4 143 ? -16.81171 18.68224  46.89649  1.000 241.16735 ? 124 ALA D N   1 
ATOM   6925 C CA  . ALA D 4 143 ? -18.02682 19.44955  46.66755  1.000 240.89061 ? 124 ALA D CA  1 
ATOM   6926 C C   . ALA D 4 143 ? -18.20851 19.67921  45.17206  1.000 232.42721 ? 124 ALA D C   1 
ATOM   6927 O O   . ALA D 4 143 ? -17.36989 20.32238  44.53410  1.000 218.57736 ? 124 ALA D O   1 
ATOM   6928 C CB  . ALA D 4 143 ? -17.97148 20.78097  47.41590  1.000 233.88784 ? 124 ALA D CB  1 
ATOM   6929 N N   . LYS D 4 144 ? -19.30111 19.15985  44.61566  1.000 232.64575 ? 125 LYS D N   1 
ATOM   6930 C CA  . LYS D 4 144 ? -19.54548 19.29587  43.18590  1.000 229.11450 ? 125 LYS D CA  1 
ATOM   6931 C C   . LYS D 4 144 ? -19.75776 20.75914  42.80827  1.000 226.41470 ? 125 LYS D C   1 
ATOM   6932 O O   . LYS D 4 144 ? -20.21977 21.57373  43.61228  1.000 226.42804 ? 125 LYS D O   1 
ATOM   6933 C CB  . LYS D 4 144 ? -20.75429 18.45960  42.77208  1.000 228.10286 ? 125 LYS D CB  1 
ATOM   6934 C CG  . LYS D 4 144 ? -20.60061 16.97567  43.06199  1.000 231.65767 ? 125 LYS D CG  1 
ATOM   6935 C CD  . LYS D 4 144 ? -19.40823 16.39679  42.31938  1.000 232.43601 ? 125 LYS D CD  1 
ATOM   6936 C CE  . LYS D 4 144 ? -19.05706 15.01068  42.83150  1.000 237.26035 ? 125 LYS D CE  1 
ATOM   6937 N NZ  . LYS D 4 144 ? -18.65145 15.04479  44.26327  1.000 241.01339 ? 125 LYS D NZ  1 
ATOM   6938 N N   . THR D 4 145 ? -19.41922 21.08385  41.56067  1.000 230.94254 ? 126 THR D N   1 
ATOM   6939 C CA  . THR D 4 145 ? -19.39992 22.47331  41.11148  1.000 229.34993 ? 126 THR D CA  1 
ATOM   6940 C C   . THR D 4 145 ? -20.79934 23.07960  41.13808  1.000 227.04565 ? 126 THR D C   1 
ATOM   6941 O O   . THR D 4 145 ? -21.73336 22.53902  40.54017  1.000 224.98502 ? 126 THR D O   1 
ATOM   6942 C CB  . THR D 4 145 ? -18.81091 22.55970  39.70378  1.000 228.41902 ? 126 THR D CB  1 
ATOM   6943 O OG1 . THR D 4 145 ? -19.65758 21.86235  38.78124  1.000 226.25055 ? 126 THR D OG1 1 
ATOM   6944 C CG2 . THR D 4 145 ? -17.42196 21.94303  39.66975  1.000 230.27290 ? 126 THR D CG2 1 
ATOM   6945 N N   . THR D 4 146 ? -20.93966 24.20733  41.83401  1.000 233.21308 ? 127 THR D N   1 
ATOM   6946 C CA  . THR D 4 146 ? -22.19780 24.93230  41.92063  1.000 230.98110 ? 127 THR D CA  1 
ATOM   6947 C C   . THR D 4 146 ? -22.04973 26.28510  41.24916  1.000 230.35549 ? 127 THR D C   1 
ATOM   6948 O O   . THR D 4 146 ? -21.11917 27.03482  41.58267  1.000 232.28941 ? 127 THR D O   1 
ATOM   6949 C CB  . THR D 4 146 ? -22.62623 25.11732  43.38302  1.000 232.16425 ? 127 THR D CB  1 
ATOM   6950 O OG1 . THR D 4 146 ? -21.61864 25.84946  44.09374  1.000 234.26715 ? 127 THR D OG1 1 
ATOM   6951 C CG2 . THR D 4 146 ? -22.83024 23.76668  44.04850  1.000 233.95432 ? 127 THR D CG2 1 
ATOM   6952 N N   . PRO D 4 147 ? -22.93109 26.63332  40.30686  1.000 240.75262 ? 128 PRO D N   1 
ATOM   6953 C CA  . PRO D 4 147 ? -22.72636 27.86096  39.53473  1.000 241.12246 ? 128 PRO D CA  1 
ATOM   6954 C C   . PRO D 4 147 ? -22.99592 29.09870  40.38015  1.000 241.91735 ? 128 PRO D C   1 
ATOM   6955 O O   . PRO D 4 147 ? -23.73991 29.03430  41.36667  1.000 240.85247 ? 128 PRO D O   1 
ATOM   6956 C CB  . PRO D 4 147 ? -23.74043 27.73324  38.38696  1.000 238.44576 ? 128 PRO D CB  1 
ATOM   6957 C CG  . PRO D 4 147 ? -24.80583 26.86597  38.93980  1.000 236.02638 ? 128 PRO D CG  1 
ATOM   6958 C CD  . PRO D 4 147 ? -24.12290 25.88612  39.85706  1.000 237.99533 ? 128 PRO D CD  1 
ATOM   6959 N N   . PRO D 4 148 ? -22.39307 30.22810  40.03079  1.000 233.90923 ? 129 PRO D N   1 
ATOM   6960 C CA  . PRO D 4 148 ? -22.54957 31.43707  40.84371  1.000 235.18866 ? 129 PRO D CA  1 
ATOM   6961 C C   . PRO D 4 148 ? -23.85767 32.15595  40.54213  1.000 233.79849 ? 129 PRO D C   1 
ATOM   6962 O O   . PRO D 4 148 ? -24.53422 31.89825  39.54504  1.000 232.25323 ? 129 PRO D O   1 
ATOM   6963 C CB  . PRO D 4 148 ? -21.34735 32.28739  40.43486  1.000 238.43794 ? 129 PRO D CB  1 
ATOM   6964 C CG  . PRO D 4 148 ? -21.09772 31.88755  39.01879  1.000 238.50585 ? 129 PRO D CG  1 
ATOM   6965 C CD  . PRO D 4 148 ? -21.42925 30.41964  38.93470  1.000 235.83239 ? 129 PRO D CD  1 
ATOM   6966 N N   . SER D 4 149 ? -24.19502 33.08507  41.43150  1.000 231.82344 ? 130 SER D N   1 
ATOM   6967 C CA  . SER D 4 149 ? -25.36028 33.94611  41.29594  1.000 231.02645 ? 130 SER D CA  1 
ATOM   6968 C C   . SER D 4 149 ? -24.86810 35.37875  41.13725  1.000 235.06751 ? 130 SER D C   1 
ATOM   6969 O O   . SER D 4 149 ? -24.27558 35.94278  42.06282  1.000 237.50187 ? 130 SER D O   1 
ATOM   6970 C CB  . SER D 4 149 ? -26.29014 33.81206  42.50251  1.000 228.97549 ? 130 SER D CB  1 
ATOM   6971 O OG  . SER D 4 149 ? -25.61267 34.11398  43.71150  1.000 231.09687 ? 130 SER D OG  1 
ATOM   6972 N N   . VAL D 4 150 ? -25.11736 35.96518  39.96944  1.000 235.89378 ? 131 VAL D N   1 
ATOM   6973 C CA  . VAL D 4 150 ? -24.63841 37.30593  39.65069  1.000 239.35688 ? 131 VAL D CA  1 
ATOM   6974 C C   . VAL D 4 150 ? -25.70767 38.31503  40.04663  1.000 239.58551 ? 131 VAL D C   1 
ATOM   6975 O O   . VAL D 4 150 ? -26.84033 38.25897  39.55552  1.000 238.21254 ? 131 VAL D O   1 
ATOM   6976 C CB  . VAL D 4 150 ? -24.28686 37.42929  38.16143  1.000 241.55357 ? 131 VAL D CB  1 
ATOM   6977 C CG1 . VAL D 4 150 ? -23.92692 38.86907  37.81936  1.000 245.89853 ? 131 VAL D CG1 1 
ATOM   6978 C CG2 . VAL D 4 150 ? -23.14264 36.49204  37.80966  1.000 241.73289 ? 131 VAL D CG2 1 
ATOM   6979 N N   . TYR D 4 151 ? -25.34659 39.24112  40.93071  1.000 245.34867 ? 132 TYR D N   1 
ATOM   6980 C CA  . TYR D 4 151 ? -26.26235 40.26648  41.41433  1.000 246.05440 ? 132 TYR D CA  1 
ATOM   6981 C C   . TYR D 4 151 ? -25.68392 41.64398  41.12015  1.000 251.34898 ? 132 TYR D C   1 
ATOM   6982 O O   . TYR D 4 151 ? -24.58731 41.96670  41.60977  1.000 253.54466 ? 132 TYR D O   1 
ATOM   6983 C CB  . TYR D 4 151 ? -26.51824 40.09686  42.91341  1.000 243.92657 ? 132 TYR D CB  1 
ATOM   6984 C CG  . TYR D 4 151 ? -27.14531 38.76826  43.27202  1.000 239.84114 ? 132 TYR D CG  1 
ATOM   6985 C CD1 . TYR D 4 151 ? -28.15366 38.22162  42.48951  1.000 236.85768 ? 132 TYR D CD1 1 
ATOM   6986 C CD2 . TYR D 4 151 ? -26.72118 38.05524  44.38521  1.000 238.68858 ? 132 TYR D CD2 1 
ATOM   6987 C CE1 . TYR D 4 151 ? -28.72773 37.00652  42.81040  1.000 233.77366 ? 132 TYR D CE1 1 
ATOM   6988 C CE2 . TYR D 4 151 ? -27.28889 36.83966  44.71492  1.000 235.32191 ? 132 TYR D CE2 1 
ATOM   6989 C CZ  . TYR D 4 151 ? -28.29205 36.32009  43.92466  1.000 233.43775 ? 132 TYR D CZ  1 
ATOM   6990 O OH  . TYR D 4 151 ? -28.85922 35.10879  44.24920  1.000 232.06155 ? 132 TYR D OH  1 
ATOM   6991 N N   . PRO D 4 152 ? -26.36192 42.48064  40.33831  1.000 243.30440 ? 133 PRO D N   1 
ATOM   6992 C CA  . PRO D 4 152 ? -25.81495 43.80329  40.02060  1.000 249.77979 ? 133 PRO D CA  1 
ATOM   6993 C C   . PRO D 4 152 ? -25.87029 44.73956  41.21855  1.000 251.39272 ? 133 PRO D C   1 
ATOM   6994 O O   . PRO D 4 152 ? -26.63781 44.54834  42.16432  1.000 247.88208 ? 133 PRO D O   1 
ATOM   6995 C CB  . PRO D 4 152 ? -26.72024 44.29702  38.88815  1.000 252.62386 ? 133 PRO D CB  1 
ATOM   6996 C CG  . PRO D 4 152 ? -28.01451 43.59589  39.12138  1.000 246.99571 ? 133 PRO D CG  1 
ATOM   6997 C CD  . PRO D 4 152 ? -27.65824 42.24275  39.67971  1.000 241.32348 ? 133 PRO D CD  1 
ATOM   6998 N N   . LEU D 4 153 ? -25.03278 45.77642  41.16044  1.000 235.17800 ? 134 LEU D N   1 
ATOM   6999 C CA  . LEU D 4 153 ? -24.89256 46.73757  42.25631  1.000 238.20063 ? 134 LEU D CA  1 
ATOM   7000 C C   . LEU D 4 153 ? -24.88097 48.14265  41.66003  1.000 243.15374 ? 134 LEU D C   1 
ATOM   7001 O O   . LEU D 4 153 ? -23.85856 48.58997  41.13177  1.000 247.81969 ? 134 LEU D O   1 
ATOM   7002 C CB  . LEU D 4 153 ? -23.62596 46.46919  43.06180  1.000 235.38181 ? 134 LEU D CB  1 
ATOM   7003 C CG  . LEU D 4 153 ? -23.38144 45.03104  43.52819  1.000 230.83588 ? 134 LEU D CG  1 
ATOM   7004 C CD1 . LEU D 4 153 ? -21.97556 44.87625  44.08559  1.000 228.34011 ? 134 LEU D CD1 1 
ATOM   7005 C CD2 . LEU D 4 153 ? -24.41628 44.61018  44.56019  1.000 232.02933 ? 134 LEU D CD2 1 
ATOM   7006 N N   . ALA D 4 154 ? -26.01678 48.83606  41.75116  0.000 230.16826 ? 135 ALA D N   1 
ATOM   7007 C CA  . ALA D 4 154 ? -26.14487 50.19855  41.26211  0.000 235.25832 ? 135 ALA D CA  1 
ATOM   7008 C C   . ALA D 4 154 ? -26.31999 51.17139  42.42541  0.000 239.56159 ? 135 ALA D C   1 
ATOM   7009 O O   . ALA D 4 154 ? -26.93942 50.83070  43.43816  0.000 239.76817 ? 135 ALA D O   1 
ATOM   7010 C CB  . ALA D 4 154 ? -27.33484 50.33470  40.30442  0.000 238.00685 ? 135 ALA D CB  1 
ATOM   7011 N N   . PRO D 4 155 ? -25.77870 52.39542  42.31736  0.000 230.92733 ? 136 PRO D N   1 
ATOM   7012 C CA  . PRO D 4 155 ? -25.89642 53.38443  43.39330  0.000 235.57684 ? 136 PRO D CA  1 
ATOM   7013 C C   . PRO D 4 155 ? -27.23554 54.11581  43.38114  0.000 241.24406 ? 136 PRO D C   1 
ATOM   7014 O O   . PRO D 4 155 ? -27.25126 55.33003  43.58517  0.000 246.74597 ? 136 PRO D O   1 
ATOM   7015 C CB  . PRO D 4 155 ? -24.74945 54.34914  43.09737  0.000 237.67025 ? 136 PRO D CB  1 
ATOM   7016 C CG  . PRO D 4 155 ? -24.63040 54.31289  41.61476  0.000 236.98999 ? 136 PRO D CG  1 
ATOM   7017 C CD  . PRO D 4 155 ? -24.95791 52.89689  41.20005  0.000 231.34077 ? 136 PRO D CD  1 
ATOM   7018 N N   . ASN D 4 162 ? -23.36821 62.88400  42.60957  0.000 271.56453 ? 143 ASN D N   1 
ATOM   7019 C CA  . ASN D 4 162 ? -23.44520 62.28581  41.28245  0.000 268.08523 ? 143 ASN D CA  1 
ATOM   7020 C C   . ASN D 4 162 ? -22.20865 62.65220  40.46584  0.000 268.59615 ? 143 ASN D C   1 
ATOM   7021 O O   . ASN D 4 162 ? -22.31378 63.23936  39.38893  0.000 272.39785 ? 143 ASN D O   1 
ATOM   7022 C CB  . ASN D 4 162 ? -24.71823 62.73911  40.56307  0.000 272.67046 ? 143 ASN D CB  1 
ATOM   7023 C CG  . ASN D 4 162 ? -25.19688 61.73467  39.53206  0.000 267.70335 ? 143 ASN D CG  1 
ATOM   7024 O OD1 . ASN D 4 162 ? -24.39722 61.04854  38.89576  0.000 262.64237 ? 143 ASN D OD1 1 
ATOM   7025 N ND2 . ASN D 4 162 ? -26.51121 61.64050  39.36629  0.000 269.40719 ? 143 ASN D ND2 1 
ATOM   7026 N N   . SER D 4 163 ? -21.03567 62.30124  40.99093  0.000 265.03773 ? 144 SER D N   1 
ATOM   7027 C CA  . SER D 4 163 ? -19.76322 62.62117  40.35677  0.000 265.54252 ? 144 SER D CA  1 
ATOM   7028 C C   . SER D 4 163 ? -18.83832 61.41866  40.45026  0.000 257.50935 ? 144 SER D C   1 
ATOM   7029 O O   . SER D 4 163 ? -18.67618 60.84486  41.53155  0.000 254.07071 ? 144 SER D O   1 
ATOM   7030 C CB  . SER D 4 163 ? -19.10819 63.84158  41.01424  0.000 272.27857 ? 144 SER D CB  1 
ATOM   7031 O OG  . SER D 4 163 ? -17.78713 64.02907  40.53733  0.000 272.28418 ? 144 SER D OG  1 
ATOM   7032 N N   . MET D 4 164 ? -18.22929 61.05399  39.32184  0.000 261.41662 ? 145 MET D N   1 
ATOM   7033 C CA  . MET D 4 164 ? -17.33803 59.89792  39.22452  0.000 254.06019 ? 145 MET D CA  1 
ATOM   7034 C C   . MET D 4 164 ? -18.00076 58.65623  39.82170  0.000 247.82181 ? 145 MET D C   1 
ATOM   7035 O O   . MET D 4 164 ? -17.55584 58.09137  40.82268  0.000 244.41123 ? 145 MET D O   1 
ATOM   7036 C CB  . MET D 4 164 ? -15.99065 60.18723  39.89137  0.000 254.55007 ? 145 MET D CB  1 
ATOM   7037 C CG  . MET D 4 164 ? -15.24062 61.36217  39.28290  0.000 260.86546 ? 145 MET D CG  1 
ATOM   7038 S SD  . MET D 4 164 ? -15.05217 61.21783  37.49505  0.000 260.26546 ? 145 MET D SD  1 
ATOM   7039 C CE  . MET D 4 164 ? -15.97782 62.64844  36.94262  0.000 269.64059 ? 145 MET D CE  1 
ATOM   7040 N N   . VAL D 4 165 ? -19.09142 58.24273  39.17616  1.000 251.85296 ? 146 VAL D N   1 
ATOM   7041 C CA  . VAL D 4 165 ? -19.94122 57.18803  39.71444  1.000 247.31385 ? 146 VAL D CA  1 
ATOM   7042 C C   . VAL D 4 165 ? -19.19083 55.86366  39.71151  1.000 239.86957 ? 146 VAL D C   1 
ATOM   7043 O O   . VAL D 4 165 ? -18.55761 55.48818  38.71612  1.000 237.41217 ? 146 VAL D O   1 
ATOM   7044 C CB  . VAL D 4 165 ? -21.24709 57.09243  38.91202  1.000 248.52733 ? 146 VAL D CB  1 
ATOM   7045 C CG1 . VAL D 4 165 ? -22.14462 56.00417  39.48089  1.000 244.32812 ? 146 VAL D CG1 1 
ATOM   7046 C CG2 . VAL D 4 165 ? -21.96364 58.43324  38.91268  1.000 256.39277 ? 146 VAL D CG2 1 
ATOM   7047 N N   . THR D 4 166 ? -19.25667 55.15239  40.83308  1.000 238.43743 ? 147 THR D N   1 
ATOM   7048 C CA  . THR D 4 166 ? -18.66063 53.83185  40.97732  1.000 231.68833 ? 147 THR D CA  1 
ATOM   7049 C C   . THR D 4 166 ? -19.71747 52.76212  40.72838  1.000 228.17818 ? 147 THR D C   1 
ATOM   7050 O O   . THR D 4 166 ? -20.84758 52.86857  41.21348  1.000 230.15899 ? 147 THR D O   1 
ATOM   7051 C CB  . THR D 4 166 ? -18.05252 53.66664  42.37415  1.000 230.56833 ? 147 THR D CB  1 
ATOM   7052 O OG1 . THR D 4 166 ? -16.83551 54.41793  42.45779  1.000 232.81783 ? 147 THR D OG1 1 
ATOM   7053 C CG2 . THR D 4 166 ? -17.76470 52.20292  42.67752  1.000 223.99657 ? 147 THR D CG2 1 
ATOM   7054 N N   . LEU D 4 167 ? -19.34945 51.73898  39.96075  1.000 242.19784 ? 148 LEU D N   1 
ATOM   7055 C CA  . LEU D 4 167 ? -20.25770 50.66342  39.58494  1.000 238.44038 ? 148 LEU D CA  1 
ATOM   7056 C C   . LEU D 4 167 ? -19.79376 49.35187  40.20117  1.000 230.42265 ? 148 LEU D C   1 
ATOM   7057 O O   . LEU D 4 167 ? -18.59929 49.04137  40.18588  1.000 229.47697 ? 148 LEU D O   1 
ATOM   7058 C CB  . LEU D 4 167 ? -20.33116 50.52260  38.06404  1.000 242.47237 ? 148 LEU D CB  1 
ATOM   7059 C CG  . LEU D 4 167 ? -20.68828 51.79667  37.30302  1.000 251.29320 ? 148 LEU D CG  1 
ATOM   7060 C CD1 . LEU D 4 167 ? -20.26539 51.67778  35.85217  1.000 255.46296 ? 148 LEU D CD1 1 
ATOM   7061 C CD2 . LEU D 4 167 ? -22.17762 52.08088  37.40903  1.000 252.65796 ? 148 LEU D CD2 1 
ATOM   7062 N N   . GLY D 4 168 ? -20.74075 48.58044  40.72889  1.000 241.64235 ? 149 GLY D N   1 
ATOM   7063 C CA  . GLY D 4 168 ? -20.41290 47.33304  41.39242  1.000 234.90054 ? 149 GLY D CA  1 
ATOM   7064 C C   . GLY D 4 168 ? -21.04092 46.10779  40.76104  1.000 230.58202 ? 149 GLY D C   1 
ATOM   7065 O O   . GLY D 4 168 ? -22.07299 46.20099  40.08940  1.000 231.37549 ? 149 GLY D O   1 
ATOM   7066 N N   . CYS D 4 169 ? -20.41788 44.95029  40.97533  1.000 235.55456 ? 150 CYS D N   1 
ATOM   7067 C CA  . CYS D 4 169 ? -20.92701 43.67643  40.47501  1.000 231.20588 ? 150 CYS D CA  1 
ATOM   7068 C C   . CYS D 4 169 ? -20.55268 42.59454  41.47491  1.000 225.73531 ? 150 CYS D C   1 
ATOM   7069 O O   . CYS D 4 169 ? -19.36792 42.40651  41.76654  1.000 225.24343 ? 150 CYS D O   1 
ATOM   7070 C CB  . CYS D 4 169 ? -20.35751 43.35673  39.08939  1.000 233.62384 ? 150 CYS D CB  1 
ATOM   7071 S SG  . CYS D 4 169 ? -20.83748 41.74336  38.40577  1.000 228.48247 ? 150 CYS D SG  1 
ATOM   7072 N N   . LEU D 4 170 ? -21.55258 41.88621  41.99211  1.000 233.75928 ? 151 LEU D N   1 
ATOM   7073 C CA  . LEU D 4 170 ? -21.35613 40.89784  43.04272  1.000 229.71860 ? 151 LEU D CA  1 
ATOM   7074 C C   . LEU D 4 170 ? -21.48108 39.48712  42.48180  1.000 226.84329 ? 151 LEU D C   1 
ATOM   7075 O O   . LEU D 4 170 ? -22.36387 39.20679  41.66456  1.000 226.10106 ? 151 LEU D O   1 
ATOM   7076 C CB  . LEU D 4 170 ? -22.36434 41.10124  44.17890  1.000 227.98084 ? 151 LEU D CB  1 
ATOM   7077 C CG  . LEU D 4 170 ? -22.32402 40.09106  45.32785  1.000 224.81119 ? 151 LEU D CG  1 
ATOM   7078 C CD1 . LEU D 4 170 ? -22.23259 40.79830  46.67079  1.000 224.92107 ? 151 LEU D CD1 1 
ATOM   7079 C CD2 . LEU D 4 170 ? -23.54445 39.19010  45.28111  1.000 221.99083 ? 151 LEU D CD2 1 
ATOM   7080 N N   . VAL D 4 171 ? -20.58804 38.60538  42.92645  1.000 226.23554 ? 152 VAL D N   1 
ATOM   7081 C CA  . VAL D 4 171 ? -20.59779 37.19163  42.56356  1.000 223.77437 ? 152 VAL D CA  1 
ATOM   7082 C C   . VAL D 4 171 ? -20.61325 36.39776  43.86264  1.000 221.53376 ? 152 VAL D C   1 
ATOM   7083 O O   . VAL D 4 171 ? -19.60583 36.35592  44.57964  1.000 220.38444 ? 152 VAL D O   1 
ATOM   7084 C CB  . VAL D 4 171 ? -19.39008 36.80195  41.70025  1.000 222.61617 ? 152 VAL D CB  1 
ATOM   7085 C CG1 . VAL D 4 171 ? -19.34558 35.29418  41.50085  1.000 220.89099 ? 152 VAL D CG1 1 
ATOM   7086 C CG2 . VAL D 4 171 ? -19.44050 37.52019  40.35955  1.000 225.98659 ? 152 VAL D CG2 1 
ATOM   7087 N N   . LYS D 4 172 ? -21.74570 35.77074  44.16955  1.000 219.65527 ? 153 LYS D N   1 
ATOM   7088 C CA  . LYS D 4 172 ? -21.92580 35.06338  45.42848  1.000 218.39750 ? 153 LYS D CA  1 
ATOM   7089 C C   . LYS D 4 172 ? -22.31095 33.61368  45.17365  1.000 215.72816 ? 153 LYS D C   1 
ATOM   7090 O O   . LYS D 4 172 ? -23.04590 33.31134  44.22835  1.000 213.90461 ? 153 LYS D O   1 
ATOM   7091 C CB  . LYS D 4 172 ? -22.99864 35.73381  46.29420  1.000 218.12213 ? 153 LYS D CB  1 
ATOM   7092 C CG  . LYS D 4 172 ? -23.07936 35.17307  47.70287  1.000 218.44874 ? 153 LYS D CG  1 
ATOM   7093 C CD  . LYS D 4 172 ? -24.48275 35.26615  48.26168  1.000 221.84365 ? 153 LYS D CD  1 
ATOM   7094 C CE  . LYS D 4 172 ? -24.81594 34.02187  49.06755  1.000 222.13584 ? 153 LYS D CE  1 
ATOM   7095 N NZ  . LYS D 4 172 ? -26.19388 34.06747  49.62631  1.000 225.74667 ? 153 LYS D NZ  1 
ATOM   7096 N N   . GLY D 4 173 ? -21.80985 32.72362  46.02739  1.000 225.41590 ? 154 GLY D N   1 
ATOM   7097 C CA  . GLY D 4 173 ? -22.20135 31.32957  46.00459  1.000 223.93789 ? 154 GLY D CA  1 
ATOM   7098 C C   . GLY D 4 173 ? -21.70688 30.54952  44.80524  1.000 223.48274 ? 154 GLY D C   1 
ATOM   7099 O O   . GLY D 4 173 ? -22.47914 30.26334  43.88547  1.000 221.57835 ? 154 GLY D O   1 
ATOM   7100 N N   . TYR D 4 174 ? -20.42490 30.19061  44.80256  1.000 226.28680 ? 155 TYR D N   1 
ATOM   7101 C CA  . TYR D 4 174 ? -19.87247 29.39469  43.71767  1.000 226.08363 ? 155 TYR D CA  1 
ATOM   7102 C C   . TYR D 4 174 ? -18.74918 28.52015  44.25284  1.000 227.40611 ? 155 TYR D C   1 
ATOM   7103 O O   . TYR D 4 174 ? -18.17570 28.78460  45.31290  1.000 228.70945 ? 155 TYR D O   1 
ATOM   7104 C CB  . TYR D 4 174 ? -19.36798 30.27413  42.56503  1.000 226.72507 ? 155 TYR D CB  1 
ATOM   7105 C CG  . TYR D 4 174 ? -18.04902 30.96987  42.82292  1.000 228.16552 ? 155 TYR D CG  1 
ATOM   7106 C CD1 . TYR D 4 174 ? -18.00241 32.19662  43.47213  1.000 229.15243 ? 155 TYR D CD1 1 
ATOM   7107 C CD2 . TYR D 4 174 ? -16.85126 30.40773  42.39791  1.000 228.18001 ? 155 TYR D CD2 1 
ATOM   7108 C CE1 . TYR D 4 174 ? -16.79978 32.83674  43.70283  1.000 227.04660 ? 155 TYR D CE1 1 
ATOM   7109 C CE2 . TYR D 4 174 ? -15.64569 31.03871  42.62570  1.000 223.11952 ? 155 TYR D CE2 1 
ATOM   7110 C CZ  . TYR D 4 174 ? -15.62537 32.25301  43.27641  1.000 223.71784 ? 155 TYR D CZ  1 
ATOM   7111 O OH  . TYR D 4 174 ? -14.42415 32.88291  43.50200  1.000 221.08943 ? 155 TYR D OH  1 
ATOM   7112 N N   . PHE D 4 175 ? -18.44058 27.47241  43.49369  1.000 221.11402 ? 156 PHE D N   1 
ATOM   7113 C CA  . PHE D 4 175 ? -17.38107 26.53095  43.82536  1.000 222.51525 ? 156 PHE D CA  1 
ATOM   7114 C C   . PHE D 4 175 ? -16.99835 25.75629  42.57081  1.000 222.17125 ? 156 PHE D C   1 
ATOM   7115 O O   . PHE D 4 175 ? -17.88054 25.26463  41.85579  1.000 221.04293 ? 156 PHE D O   1 
ATOM   7116 C CB  . PHE D 4 175 ? -17.82956 25.57785  44.93532  1.000 223.94549 ? 156 PHE D CB  1 
ATOM   7117 C CG  . PHE D 4 175 ? -16.72987 24.70622  45.46720  1.000 226.04957 ? 156 PHE D CG  1 
ATOM   7118 C CD1 . PHE D 4 175 ? -15.85442 25.18679  46.42434  1.000 227.06038 ? 156 PHE D CD1 1 
ATOM   7119 C CD2 . PHE D 4 175 ? -16.57305 23.40720  45.01536  1.000 227.10912 ? 156 PHE D CD2 1 
ATOM   7120 C CE1 . PHE D 4 175 ? -14.84057 24.39293  46.91887  1.000 228.71992 ? 156 PHE D CE1 1 
ATOM   7121 C CE2 . PHE D 4 175 ? -15.55942 22.60830  45.50757  1.000 228.94337 ? 156 PHE D CE2 1 
ATOM   7122 C CZ  . PHE D 4 175 ? -14.69409 23.10352  46.46060  1.000 229.65641 ? 156 PHE D CZ  1 
ATOM   7123 N N   . PRO D 4 176 ? -15.69970 25.61982  42.26418  1.000 222.29212 ? 157 PRO D N   1 
ATOM   7124 C CA  . PRO D 4 176 ? -14.57397 26.15904  43.02628  1.000 223.03285 ? 157 PRO D CA  1 
ATOM   7125 C C   . PRO D 4 176 ? -13.89519 27.35396  42.35731  1.000 221.72633 ? 157 PRO D C   1 
ATOM   7126 O O   . PRO D 4 176 ? -14.36615 27.84810  41.33164  1.000 221.40301 ? 157 PRO D O   1 
ATOM   7127 C CB  . PRO D 4 176 ? -13.61542 24.96878  43.08351  1.000 223.94373 ? 157 PRO D CB  1 
ATOM   7128 C CG  . PRO D 4 176 ? -13.93920 24.15429  41.81291  1.000 223.68998 ? 157 PRO D CG  1 
ATOM   7129 C CD  . PRO D 4 176 ? -15.22460 24.70234  41.21767  1.000 222.40708 ? 157 PRO D CD  1 
ATOM   7130 N N   . GLU D 4 177 ? -12.79067 27.80338  42.94960  1.000 221.24430 ? 158 GLU D N   1 
ATOM   7131 C CA  . GLU D 4 177 ? -11.97060 28.84423  42.34957  1.000 218.27435 ? 158 GLU D CA  1 
ATOM   7132 C C   . GLU D 4 177 ? -11.38807 28.33011  41.03215  1.000 218.50881 ? 158 GLU D C   1 
ATOM   7133 O O   . GLU D 4 177 ? -11.06645 27.14386  40.91643  1.000 221.71326 ? 158 GLU D O   1 
ATOM   7134 C CB  . GLU D 4 177 ? -10.84923 29.24081  43.31137  1.000 217.23436 ? 158 GLU D CB  1 
ATOM   7135 C CG  . GLU D 4 177 ? -10.34381 30.67446  43.18645  1.000 217.25738 ? 158 GLU D CG  1 
ATOM   7136 C CD  . GLU D 4 177 ? -11.39584 31.70420  43.55961  1.000 218.09806 ? 158 GLU D CD  1 
ATOM   7137 O OE1 . GLU D 4 177 ? -12.18122 31.44317  44.49569  1.000 218.44462 ? 158 GLU D OE1 1 
ATOM   7138 O OE2 . GLU D 4 177 ? -11.43883 32.77369  42.91405  1.000 219.28004 ? 158 GLU D OE2 1 
ATOM   7139 N N   . PRO D 4 178 ? -11.22535 29.19864  40.01788  1.000 216.38188 ? 159 PRO D N   1 
ATOM   7140 C CA  . PRO D 4 178 ? -11.49922 30.63620  39.96191  1.000 217.16105 ? 159 PRO D CA  1 
ATOM   7141 C C   . PRO D 4 178 ? -12.70636 31.02620  39.11157  1.000 218.92434 ? 159 PRO D C   1 
ATOM   7142 O O   . PRO D 4 178 ? -13.43772 30.16347  38.62515  1.000 220.45732 ? 159 PRO D O   1 
ATOM   7143 C CB  . PRO D 4 178 ? -10.21791 31.18874  39.33948  1.000 218.60840 ? 159 PRO D CB  1 
ATOM   7144 C CG  . PRO D 4 178 ? -9.68727  30.02905  38.46835  1.000 219.11930 ? 159 PRO D CG  1 
ATOM   7145 C CD  . PRO D 4 178 ? -10.46982 28.78142  38.82543  1.000 217.55166 ? 159 PRO D CD  1 
ATOM   7146 N N   . VAL D 4 179 ? -12.89374 32.33416  38.94013  1.000 216.49536 ? 160 VAL D N   1 
ATOM   7147 C CA  . VAL D 4 179 ? -13.96516 32.89720  38.12430  1.000 222.68622 ? 160 VAL D CA  1 
ATOM   7148 C C   . VAL D 4 179 ? -13.43239 34.14696  37.43604  1.000 229.41054 ? 160 VAL D C   1 
ATOM   7149 O O   . VAL D 4 179 ? -12.86551 35.02814  38.09095  1.000 230.17235 ? 160 VAL D O   1 
ATOM   7150 C CB  . VAL D 4 179 ? -15.21610 33.23071  38.96342  1.000 224.71381 ? 160 VAL D CB  1 
ATOM   7151 C CG1 . VAL D 4 179 ? -16.05628 34.29507  38.27602  1.000 228.46969 ? 160 VAL D CG1 1 
ATOM   7152 C CG2 . VAL D 4 179 ? -16.04682 31.97971  39.20230  1.000 223.21075 ? 160 VAL D CG2 1 
ATOM   7153 N N   . THR D 4 180 ? -13.60910 34.22087  36.11869  1.000 220.46042 ? 161 THR D N   1 
ATOM   7154 C CA  . THR D 4 180 ? -13.15783 35.36132  35.33377  1.000 226.71297 ? 161 THR D CA  1 
ATOM   7155 C C   . THR D 4 180 ? -14.25060 36.42150  35.26656  1.000 230.12336 ? 161 THR D C   1 
ATOM   7156 O O   . THR D 4 180 ? -15.42416 36.10799  35.04643  1.000 229.42723 ? 161 THR D O   1 
ATOM   7157 C CB  . THR D 4 180 ? -12.76750 34.92206  33.92035  1.000 229.61688 ? 161 THR D CB  1 
ATOM   7158 O OG1 . THR D 4 180 ? -11.69144 33.97820  33.99122  1.000 228.73282 ? 161 THR D OG1 1 
ATOM   7159 C CG2 . THR D 4 180 ? -12.33369 36.11563  33.08096  1.000 235.07524 ? 161 THR D CG2 1 
ATOM   7160 N N   . VAL D 4 181 ? -13.85709 37.67910  35.46534  1.000 225.28225 ? 162 VAL D N   1 
ATOM   7161 C CA  . VAL D 4 181 ? -14.77269 38.81260  35.43063  1.000 229.82033 ? 162 VAL D CA  1 
ATOM   7162 C C   . VAL D 4 181 ? -14.16541 39.90900  34.56546  1.000 237.19031 ? 162 VAL D C   1 
ATOM   7163 O O   . VAL D 4 181 ? -12.98004 40.23227  34.70428  1.000 238.70188 ? 162 VAL D O   1 
ATOM   7164 C CB  . VAL D 4 181 ? -15.07591 39.34966  36.84595  1.000 226.77199 ? 162 VAL D CB  1 
ATOM   7165 C CG1 . VAL D 4 181 ? -15.95273 40.58967  36.77061  1.000 231.55821 ? 162 VAL D CG1 1 
ATOM   7166 C CG2 . VAL D 4 181 ? -15.74528 38.27738  37.69403  1.000 220.88446 ? 162 VAL D CG2 1 
ATOM   7167 N N   . THR D 4 182 ? -14.97680 40.47477  33.67335  1.000 231.53593 ? 163 THR D N   1 
ATOM   7168 C CA  . THR D 4 182 ? -14.56796 41.58897  32.82916  1.000 240.22072 ? 163 THR D CA  1 
ATOM   7169 C C   . THR D 4 182 ? -15.72323 42.57481  32.71733  1.000 244.57402 ? 163 THR D C   1 
ATOM   7170 O O   . THR D 4 182 ? -16.86500 42.27245  33.07516  1.000 240.75766 ? 163 THR D O   1 
ATOM   7171 C CB  . THR D 4 182 ? -14.12836 41.11611  31.43569  1.000 243.56158 ? 163 THR D CB  1 
ATOM   7172 O OG1 . THR D 4 182 ? -14.98310 40.05435  30.99275  1.000 238.88256 ? 163 THR D OG1 1 
ATOM   7173 C CG2 . THR D 4 182 ? -12.68637 40.63177  31.45816  1.000 242.15373 ? 163 THR D CG2 1 
ATOM   7174 N N   . TRP D 4 183 ? -15.41709 43.76832  32.21286  1.000 241.26175 ? 164 TRP D N   1 
ATOM   7175 C CA  . TRP D 4 183 ? -16.40402 44.82827  32.03707  1.000 245.83673 ? 164 TRP D CA  1 
ATOM   7176 C C   . TRP D 4 183 ? -16.43851 45.24203  30.57328  1.000 253.42788 ? 164 TRP D C   1 
ATOM   7177 O O   . TRP D 4 183 ? -15.41765 45.66944  30.02274  1.000 258.56478 ? 164 TRP D O   1 
ATOM   7178 C CB  . TRP D 4 183 ? -16.09064 46.02990  32.93106  1.000 248.08705 ? 164 TRP D CB  1 
ATOM   7179 C CG  . TRP D 4 183 ? -16.52652 45.84461  34.35122  1.000 241.73457 ? 164 TRP D CG  1 
ATOM   7180 C CD1 . TRP D 4 183 ? -15.73992 45.51432  35.41589  1.000 236.86336 ? 164 TRP D CD1 1 
ATOM   7181 C CD2 . TRP D 4 183 ? -17.85919 45.97090  34.86058  1.000 239.68564 ? 164 TRP D CD2 1 
ATOM   7182 N NE1 . TRP D 4 183 ? -16.49999 45.43177  36.55789  1.000 232.42866 ? 164 TRP D NE1 1 
ATOM   7183 C CE2 . TRP D 4 183 ? -17.80510 45.70508  36.24269  1.000 233.96077 ? 164 TRP D CE2 1 
ATOM   7184 C CE3 . TRP D 4 183 ? -19.09303 46.28329  34.28149  1.000 241.96171 ? 164 TRP D CE3 1 
ATOM   7185 C CZ2 . TRP D 4 183 ? -18.93553 45.74796  37.05500  1.000 230.77495 ? 164 TRP D CZ2 1 
ATOM   7186 C CZ3 . TRP D 4 183 ? -20.21448 46.32208  35.08917  1.000 238.19179 ? 164 TRP D CZ3 1 
ATOM   7187 C CH2 . TRP D 4 183 ? -20.12844 46.05508  36.46047  1.000 232.76851 ? 164 TRP D CH2 1 
ATOM   7188 N N   . ASN D 4 184 ? -17.61488 45.11609  29.95290  1.000 242.88952 ? 165 ASN D N   1 
ATOM   7189 C CA  . ASN D 4 184 ? -17.82140 45.46753  28.54548  1.000 250.57073 ? 165 ASN D CA  1 
ATOM   7190 C C   . ASN D 4 184 ? -16.87663 44.69048  27.63079  1.000 252.14561 ? 165 ASN D C   1 
ATOM   7191 O O   . ASN D 4 184 ? -16.27919 45.24894  26.70782  1.000 260.25636 ? 165 ASN D O   1 
ATOM   7192 C CB  . ASN D 4 184 ? -17.67895 46.97474  28.32085  1.000 259.19499 ? 165 ASN D CB  1 
ATOM   7193 C CG  . ASN D 4 184 ? -18.69954 47.77878  29.09844  1.000 258.54037 ? 165 ASN D CG  1 
ATOM   7194 O OD1 . ASN D 4 184 ? -19.18620 47.34165  30.14011  1.000 251.55224 ? 165 ASN D OD1 1 
ATOM   7195 N ND2 . ASN D 4 184 ? -19.03181 48.96112  28.59336  1.000 266.11846 ? 165 ASN D ND2 1 
ATOM   7196 N N   . SER D 4 185 ? -16.74253 43.38840  27.89510  1.000 249.71637 ? 166 SER D N   1 
ATOM   7197 C CA  . SER D 4 185 ? -15.91153 42.49157  27.08823  1.000 249.69224 ? 166 SER D CA  1 
ATOM   7198 C C   . SER D 4 185 ? -14.46256 42.97166  27.03047  1.000 255.25303 ? 166 SER D C   1 
ATOM   7199 O O   . SER D 4 185 ? -13.78468 42.84063  26.00924  1.000 260.55995 ? 166 SER D O   1 
ATOM   7200 C CB  . SER D 4 185 ? -16.48641 42.32226  25.67964  1.000 253.22722 ? 166 SER D CB  1 
ATOM   7201 O OG  . SER D 4 185 ? -17.79345 41.77680  25.72606  1.000 246.68142 ? 166 SER D OG  1 
ATOM   7202 N N   . GLY D 4 186 ? -13.98518 43.53785  28.13610  1.000 247.64526 ? 167 GLY D N   1 
ATOM   7203 C CA  . GLY D 4 186 ? -12.60896 43.98253  28.21332  1.000 250.97701 ? 167 GLY D CA  1 
ATOM   7204 C C   . GLY D 4 186 ? -12.33481 45.35121  27.63722  1.000 260.38858 ? 167 GLY D C   1 
ATOM   7205 O O   . GLY D 4 186 ? -11.17415 45.67095  27.36254  1.000 263.91655 ? 167 GLY D O   1 
ATOM   7206 N N   . SER D 4 187 ? -13.36567 46.17636  27.44266  1.000 253.56002 ? 168 SER D N   1 
ATOM   7207 C CA  . SER D 4 187 ? -13.13915 47.51948  26.92020  1.000 261.55624 ? 168 SER D CA  1 
ATOM   7208 C C   . SER D 4 187 ? -12.75266 48.48997  28.02898  1.000 260.07286 ? 168 SER D C   1 
ATOM   7209 O O   . SER D 4 187 ? -11.93692 49.39247  27.81062  1.000 265.27876 ? 168 SER D O   1 
ATOM   7210 C CB  . SER D 4 187 ? -14.38362 48.02331  26.18845  1.000 266.07464 ? 168 SER D CB  1 
ATOM   7211 O OG  . SER D 4 187 ? -15.30325 48.60960  27.09233  1.000 263.92862 ? 168 SER D OG  1 
ATOM   7212 N N   . LEU D 4 188 ? -13.32418 48.32167  29.21776  1.000 255.57152 ? 169 LEU D N   1 
ATOM   7213 C CA  . LEU D 4 188 ? -13.04716 49.19007  30.35333  1.000 253.86957 ? 169 LEU D CA  1 
ATOM   7214 C C   . LEU D 4 188 ? -11.96136 48.57252  31.22331  1.000 247.57475 ? 169 LEU D C   1 
ATOM   7215 O O   . LEU D 4 188 ? -12.08717 47.42505  31.66407  1.000 240.91334 ? 169 LEU D O   1 
ATOM   7216 C CB  . LEU D 4 188 ? -14.31124 49.43171  31.17938  1.000 251.24246 ? 169 LEU D CB  1 
ATOM   7217 C CG  . LEU D 4 188 ? -15.39655 50.28120  30.51730  1.000 257.56975 ? 169 LEU D CG  1 
ATOM   7218 C CD1 . LEU D 4 188 ? -16.57852 50.46204  31.45447  1.000 254.49481 ? 169 LEU D CD1 1 
ATOM   7219 C CD2 . LEU D 4 188 ? -14.83333 51.62811  30.09312  1.000 264.15304 ? 169 LEU D CD2 1 
ATOM   7220 N N   . SER D 4 189 ? -10.89946 49.33750  31.46539  1.000 253.73319 ? 170 SER D N   1 
ATOM   7221 C CA  . SER D 4 189 ? -9.80427  48.89770  32.32444  1.000 248.60282 ? 170 SER D CA  1 
ATOM   7222 C C   . SER D 4 189 ? -9.23615  49.99392  33.21498  1.000 248.88980 ? 170 SER D C   1 
ATOM   7223 O O   . SER D 4 189 ? -8.69956  49.67218  34.28000  1.000 243.56944 ? 170 SER D O   1 
ATOM   7224 C CB  . SER D 4 189 ? -8.66785  48.30573  31.47995  1.000 250.72378 ? 170 SER D CB  1 
ATOM   7225 O OG  . SER D 4 189 ? -8.20928  49.24040  30.51877  1.000 257.53928 ? 170 SER D OG  1 
ATOM   7226 N N   . SER D 4 190 ? -9.33358  51.26547  32.83346  1.000 254.11357 ? 171 SER D N   1 
ATOM   7227 C CA  . SER D 4 190 ? -8.80576  52.34466  33.65646  1.000 254.15915 ? 171 SER D CA  1 
ATOM   7228 C C   . SER D 4 190 ? -9.62269  52.48825  34.93430  1.000 250.57670 ? 171 SER D C   1 
ATOM   7229 O O   . SER D 4 190 ? -10.84606 52.65139  34.88799  1.000 252.06655 ? 171 SER D O   1 
ATOM   7230 C CB  . SER D 4 190 ? -8.81465  53.65777  32.87570  1.000 261.16925 ? 171 SER D CB  1 
ATOM   7231 O OG  . SER D 4 190 ? -10.13350 54.01638  32.50006  1.000 264.03882 ? 171 SER D OG  1 
ATOM   7232 N N   . GLY D 4 191 ? -8.94087  52.42800  36.07596  1.000 254.77404 ? 172 GLY D N   1 
ATOM   7233 C CA  . GLY D 4 191 ? -9.58531  52.59903  37.36324  1.000 251.59836 ? 172 GLY D CA  1 
ATOM   7234 C C   . GLY D 4 191 ? -10.64820 51.56193  37.66063  1.000 247.73267 ? 172 GLY D C   1 
ATOM   7235 O O   . GLY D 4 191 ? -11.75326 51.90370  38.09264  1.000 248.32541 ? 172 GLY D O   1 
ATOM   7236 N N   . VAL D 4 192 ? -10.32908 50.29092  37.43009  1.000 237.24436 ? 173 VAL D N   1 
ATOM   7237 C CA  . VAL D 4 192 ? -11.24318 49.18321  37.68100  1.000 230.90936 ? 173 VAL D CA  1 
ATOM   7238 C C   . VAL D 4 192 ? -10.59129 48.24498  38.68623  1.000 224.99938 ? 173 VAL D C   1 
ATOM   7239 O O   . VAL D 4 192 ? -9.42903  47.85784  38.51779  1.000 224.24394 ? 173 VAL D O   1 
ATOM   7240 C CB  . VAL D 4 192 ? -11.60071 48.43218  36.38502  1.000 232.26503 ? 173 VAL D CB  1 
ATOM   7241 C CG1 . VAL D 4 192 ? -12.64847 47.36255  36.66344  1.000 227.07613 ? 173 VAL D CG1 1 
ATOM   7242 C CG2 . VAL D 4 192 ? -12.08837 49.40446  35.32135  1.000 240.08047 ? 173 VAL D CG2 1 
ATOM   7243 N N   . HIS D 4 193 ? -11.33839 47.88123  39.72579  1.000 227.31148 ? 174 HIS D N   1 
ATOM   7244 C CA  . HIS D 4 193 ? -10.85646 46.99769  40.77739  1.000 220.92892 ? 174 HIS D CA  1 
ATOM   7245 C C   . HIS D 4 193 ? -11.72620 45.74980  40.84185  1.000 215.40310 ? 174 HIS D C   1 
ATOM   7246 O O   . HIS D 4 193 ? -12.95213 45.82796  40.71430  1.000 216.58820 ? 174 HIS D O   1 
ATOM   7247 C CB  . HIS D 4 193 ? -10.85761 47.70411  42.13972  1.000 220.22455 ? 174 HIS D CB  1 
ATOM   7248 C CG  . HIS D 4 193 ? -10.03686 48.95621  42.17471  1.000 225.35603 ? 174 HIS D CG  1 
ATOM   7249 N ND1 . HIS D 4 193 ? -8.85092  49.05008  42.87085  1.000 224.49192 ? 174 HIS D ND1 1 
ATOM   7250 C CD2 . HIS D 4 193 ? -10.23274 50.16723  41.60125  1.000 232.01239 ? 174 HIS D CD2 1 
ATOM   7251 C CE1 . HIS D 4 193 ? -8.35126  50.26425  42.72405  1.000 231.47845 ? 174 HIS D CE1 1 
ATOM   7252 N NE2 . HIS D 4 193 ? -9.17021  50.96175  41.95768  1.000 236.17805 ? 174 HIS D NE2 1 
ATOM   7253 N N   . THR D 4 194 ? -11.08513 44.59852  41.03629  1.000 224.77802 ? 175 THR D N   1 
ATOM   7254 C CA  . THR D 4 194 ? -11.77607 43.32240  41.20304  1.000 219.39347 ? 175 THR D CA  1 
ATOM   7255 C C   . THR D 4 194 ? -11.29720 42.70252  42.50866  1.000 214.18529 ? 175 THR D C   1 
ATOM   7256 O O   . THR D 4 194 ? -10.12362 42.33782  42.63416  1.000 212.76552 ? 175 THR D O   1 
ATOM   7257 C CB  . THR D 4 194 ? -11.52087 42.38754  40.02003  1.000 219.07943 ? 175 THR D CB  1 
ATOM   7258 O OG1 . THR D 4 194 ? -12.12518 42.93455  38.84117  1.000 224.84012 ? 175 THR D OG1 1 
ATOM   7259 C CG2 . THR D 4 194 ? -12.10629 41.00898  40.29109  1.000 213.69267 ? 175 THR D CG2 1 
ATOM   7260 N N   . PHE D 4 195 ? -12.20475 42.58170  43.47250  1.000 216.36485 ? 176 PHE D N   1 
ATOM   7261 C CA  . PHE D 4 195 ? -11.84541 42.20814  44.82869  1.000 212.58820 ? 176 PHE D CA  1 
ATOM   7262 C C   . PHE D 4 195 ? -11.73012 40.68962  44.97406  1.000 207.54266 ? 176 PHE D C   1 
ATOM   7263 O O   . PHE D 4 195 ? -12.46884 39.93747  44.33174  1.000 204.52399 ? 176 PHE D O   1 
ATOM   7264 C CB  . PHE D 4 195 ? -12.87071 42.75997  45.81272  1.000 212.78389 ? 176 PHE D CB  1 
ATOM   7265 C CG  . PHE D 4 195 ? -12.94704 44.26410  45.81977  1.000 217.50488 ? 176 PHE D CG  1 
ATOM   7266 C CD1 . PHE D 4 195 ? -13.74475 44.93845  44.90801  1.000 221.51798 ? 176 PHE D CD1 1 
ATOM   7267 C CD2 . PHE D 4 195 ? -12.20949 45.00394  46.72900  1.000 218.49730 ? 176 PHE D CD2 1 
ATOM   7268 C CE1 . PHE D 4 195 ? -13.80849 46.32228  44.90780  1.000 227.64654 ? 176 PHE D CE1 1 
ATOM   7269 C CE2 . PHE D 4 195 ? -12.26942 46.38689  46.73351  1.000 223.55813 ? 176 PHE D CE2 1 
ATOM   7270 C CZ  . PHE D 4 195 ? -13.07079 47.04618  45.82313  1.000 228.72203 ? 176 PHE D CZ  1 
ATOM   7271 N N   . PRO D 4 196 ? -10.80585 40.22300  45.81072  1.000 209.05080 ? 177 PRO D N   1 
ATOM   7272 C CA  . PRO D 4 196 ? -10.51203 38.78754  45.87474  1.000 201.24615 ? 177 PRO D CA  1 
ATOM   7273 C C   . PRO D 4 196 ? -11.68183 37.97785  46.41467  1.000 198.28531 ? 177 PRO D C   1 
ATOM   7274 O O   . PRO D 4 196 ? -12.65260 38.50069  46.96573  1.000 202.02283 ? 177 PRO D O   1 
ATOM   7275 C CB  . PRO D 4 196 ? -9.30625  38.71444  46.81940  1.000 200.35840 ? 177 PRO D CB  1 
ATOM   7276 C CG  . PRO D 4 196 ? -8.69908  40.07604  46.76328  1.000 207.03418 ? 177 PRO D CG  1 
ATOM   7277 C CD  . PRO D 4 196 ? -9.85675  41.01229  46.60971  1.000 210.28395 ? 177 PRO D CD  1 
ATOM   7278 N N   . ALA D 4 197 ? -11.55623 36.66438  46.25538  1.000 211.29581 ? 178 ALA D N   1 
ATOM   7279 C CA  . ALA D 4 197 ? -12.58639 35.72052  46.66165  1.000 209.22016 ? 178 ALA D CA  1 
ATOM   7280 C C   . ALA D 4 197 ? -12.33373 35.23868  48.08419  1.000 208.67693 ? 178 ALA D C   1 
ATOM   7281 O O   . ALA D 4 197 ? -11.19190 34.96407  48.46437  1.000 207.52621 ? 178 ALA D O   1 
ATOM   7282 C CB  . ALA D 4 197 ? -12.62566 34.52840  45.70566  1.000 204.91449 ? 178 ALA D CB  1 
ATOM   7283 N N   . VAL D 4 198 ? -13.40589 35.13739  48.86711  1.000 212.47227 ? 179 VAL D N   1 
ATOM   7284 C CA  . VAL D 4 198 ? -13.33879 34.66180  50.24409  1.000 212.90187 ? 179 VAL D CA  1 
ATOM   7285 C C   . VAL D 4 198 ? -14.20296 33.41111  50.37274  1.000 214.45591 ? 179 VAL D C   1 
ATOM   7286 O O   . VAL D 4 198 ? -15.18262 33.23377  49.64015  1.000 214.93099 ? 179 VAL D O   1 
ATOM   7287 C CB  . VAL D 4 198 ? -13.77712 35.75421  51.24397  1.000 213.99005 ? 179 VAL D CB  1 
ATOM   7288 C CG1 . VAL D 4 198 ? -12.77757 36.90636  51.25111  1.000 214.30891 ? 179 VAL D CG1 1 
ATOM   7289 C CG2 . VAL D 4 198 ? -15.15860 36.25918  50.88956  1.000 214.81769 ? 179 VAL D CG2 1 
ATOM   7290 N N   . LEU D 4 199 ? -13.83476 32.54545  51.31923  1.000 214.81455 ? 180 LEU D N   1 
ATOM   7291 C CA  . LEU D 4 199 ? -14.40907 31.20849  51.44539  1.000 217.47581 ? 180 LEU D CA  1 
ATOM   7292 C C   . LEU D 4 199 ? -15.60306 31.23867  52.39667  1.000 218.99956 ? 180 LEU D C   1 
ATOM   7293 O O   . LEU D 4 199 ? -15.46306 31.58813  53.57396  1.000 221.37662 ? 180 LEU D O   1 
ATOM   7294 C CB  . LEU D 4 199 ? -13.33332 30.22954  51.93091  1.000 218.58523 ? 180 LEU D CB  1 
ATOM   7295 C CG  . LEU D 4 199 ? -13.63682 28.73238  51.91580  1.000 217.15708 ? 180 LEU D CG  1 
ATOM   7296 C CD1 . LEU D 4 199 ? -12.38823 27.95470  51.54819  1.000 214.98278 ? 180 LEU D CD1 1 
ATOM   7297 C CD2 . LEU D 4 199 ? -14.15738 28.28701  53.27016  1.000 221.36733 ? 180 LEU D CD2 1 
ATOM   7298 N N   . GLN D 4 200 ? -16.76921 30.85692  51.88576  1.000 225.81205 ? 181 GLN D N   1 
ATOM   7299 C CA  . GLN D 4 200 ? -18.05962 31.01650  52.56527  1.000 226.80101 ? 181 GLN D CA  1 
ATOM   7300 C C   . GLN D 4 200 ? -18.61753 29.64729  52.93999  1.000 229.23955 ? 181 GLN D C   1 
ATOM   7301 O O   . GLN D 4 200 ? -19.50862 29.12783  52.26764  1.000 231.65558 ? 181 GLN D O   1 
ATOM   7302 C CB  . GLN D 4 200 ? -19.03607 31.73775  51.64390  1.000 223.97777 ? 181 GLN D CB  1 
ATOM   7303 C CG  . GLN D 4 200 ? -19.22855 33.22040  51.85762  1.000 224.51569 ? 181 GLN D CG  1 
ATOM   7304 C CD  . GLN D 4 200 ? -20.48396 33.69917  51.16345  1.000 222.21289 ? 181 GLN D CD  1 
ATOM   7305 O OE1 . GLN D 4 200 ? -21.05543 33.00169  50.31758  1.000 219.69497 ? 181 GLN D OE1 1 
ATOM   7306 N NE2 . GLN D 4 200 ? -20.87549 34.91956  51.45809  1.000 223.20327 ? 181 GLN D NE2 1 
ATOM   7307 N N   . SER D 4 201 ? -18.11900 29.08715  54.04131  1.000 223.60383 ? 182 SER D N   1 
ATOM   7308 C CA  . SER D 4 201 ? -18.61047 27.82226  54.58883  1.000 226.84466 ? 182 SER D CA  1 
ATOM   7309 C C   . SER D 4 201 ? -18.87473 26.80800  53.47898  1.000 225.66665 ? 182 SER D C   1 
ATOM   7310 O O   . SER D 4 201 ? -20.01200 26.40607  53.23172  1.000 224.51561 ? 182 SER D O   1 
ATOM   7311 C CB  . SER D 4 201 ? -19.86533 28.05616  55.43203  1.000 228.58593 ? 182 SER D CB  1 
ATOM   7312 O OG  . SER D 4 201 ? -19.51917 28.63694  56.67576  1.000 230.56249 ? 182 SER D OG  1 
ATOM   7313 N N   . ASP D 4 202 ? -17.79106 26.43850  52.78344  1.000 231.67201 ? 183 ASP D N   1 
ATOM   7314 C CA  . ASP D 4 202 ? -17.77308 25.48003  51.66066  1.000 230.57391 ? 183 ASP D CA  1 
ATOM   7315 C C   . ASP D 4 202 ? -18.27281 26.10131  50.35282  1.000 226.27359 ? 183 ASP D C   1 
ATOM   7316 O O   . ASP D 4 202 ? -18.58343 25.39129  49.38857  1.000 224.29445 ? 183 ASP D O   1 
ATOM   7317 C CB  . ASP D 4 202 ? -18.56421 24.20627  51.99891  1.000 233.90350 ? 183 ASP D CB  1 
ATOM   7318 C CG  . ASP D 4 202 ? -18.35700 23.09094  50.97615  1.000 234.67141 ? 183 ASP D CG  1 
ATOM   7319 O OD1 . ASP D 4 202 ? -17.19943 22.71190  50.72036  1.000 234.88927 ? 183 ASP D OD1 1 
ATOM   7320 O OD2 . ASP D 4 202 ? -19.35869 22.60686  50.41078  1.000 235.03653 ? 183 ASP D OD2 1 
ATOM   7321 N N   . LEU D 4 203 ? -18.36267 27.42848  50.28714  1.000 227.19305 ? 184 LEU D N   1 
ATOM   7322 C CA  . LEU D 4 203 ? -18.62382 28.12776  49.03140  1.000 224.06003 ? 184 LEU D CA  1 
ATOM   7323 C C   . LEU D 4 203 ? -17.74328 29.37371  48.99100  1.000 224.36514 ? 184 LEU D C   1 
ATOM   7324 O O   . LEU D 4 203 ? -17.06976 29.71519  49.96259  1.000 226.05763 ? 184 LEU D O   1 
ATOM   7325 C CB  . LEU D 4 203 ? -20.11527 28.48138  48.85774  1.000 222.38035 ? 184 LEU D CB  1 
ATOM   7326 C CG  . LEU D 4 203 ? -21.01897 27.47262  48.12196  1.000 220.48188 ? 184 LEU D CG  1 
ATOM   7327 C CD1 . LEU D 4 203 ? -21.52461 26.35630  49.03343  1.000 218.15952 ? 184 LEU D CD1 1 
ATOM   7328 C CD2 . LEU D 4 203 ? -22.19565 28.16315  47.46118  1.000 222.78365 ? 184 LEU D CD2 1 
ATOM   7329 N N   . TYR D 4 204 ? -17.71914 30.03331  47.83473  1.000 226.06371 ? 185 TYR D N   1 
ATOM   7330 C CA  . TYR D 4 204 ? -16.89954 31.22356  47.63079  1.000 226.48492 ? 185 TYR D CA  1 
ATOM   7331 C C   . TYR D 4 204 ? -17.76673 32.39025  47.16402  1.000 226.25617 ? 185 TYR D C   1 
ATOM   7332 O O   . TYR D 4 204 ? -18.89594 32.20998  46.70009  1.000 225.11754 ? 185 TYR D O   1 
ATOM   7333 C CB  . TYR D 4 204 ? -15.77065 30.96190  46.61964  1.000 225.76641 ? 185 TYR D CB  1 
ATOM   7334 C CG  . TYR D 4 204 ? -14.71157 29.99440  47.10434  1.000 223.05060 ? 185 TYR D CG  1 
ATOM   7335 C CD1 . TYR D 4 204 ? -13.61100 30.43755  47.83062  1.000 220.77077 ? 185 TYR D CD1 1 
ATOM   7336 C CD2 . TYR D 4 204 ? -14.80873 28.63715  46.82904  1.000 223.03036 ? 185 TYR D CD2 1 
ATOM   7337 C CE1 . TYR D 4 204 ? -12.64157 29.54768  48.27571  1.000 218.31849 ? 185 TYR D CE1 1 
ATOM   7338 C CE2 . TYR D 4 204 ? -13.84684 27.74477  47.26888  1.000 220.60262 ? 185 TYR D CE2 1 
ATOM   7339 C CZ  . TYR D 4 204 ? -12.76752 28.20298  47.99016  1.000 218.21528 ? 185 TYR D CZ  1 
ATOM   7340 O OH  . TYR D 4 204 ? -11.81169 27.31313  48.42632  1.000 218.50849 ? 185 TYR D OH  1 
ATOM   7341 N N   . THR D 4 205 ? -17.21452 33.60010  47.26772  1.000 220.34803 ? 186 THR D N   1 
ATOM   7342 C CA  . THR D 4 205 ? -17.94610 34.82323  46.96096  1.000 220.48683 ? 186 THR D CA  1 
ATOM   7343 C C   . THR D 4 205 ? -16.95323 35.96694  46.79195  1.000 220.23463 ? 186 THR D C   1 
ATOM   7344 O O   . THR D 4 205 ? -16.01732 36.09977  47.58414  1.000 219.73773 ? 186 THR D O   1 
ATOM   7345 C CB  . THR D 4 205 ? -18.95773 35.15788  48.06756  1.000 222.20987 ? 186 THR D CB  1 
ATOM   7346 O OG1 . THR D 4 205 ? -19.99671 34.17164  48.08407  1.000 223.18439 ? 186 THR D OG1 1 
ATOM   7347 C CG2 . THR D 4 205 ? -19.57073 36.53155  47.85025  1.000 222.78163 ? 186 THR D CG2 1 
ATOM   7348 N N   . LEU D 4 206 ? -17.15474 36.77679  45.75110  1.000 218.83408 ? 187 LEU D N   1 
ATOM   7349 C CA  . LEU D 4 206 ? -16.32242 37.94793  45.50447  1.000 219.68608 ? 187 LEU D CA  1 
ATOM   7350 C C   . LEU D 4 206 ? -17.17404 39.02951  44.84684  1.000 223.10136 ? 187 LEU D C   1 
ATOM   7351 O O   . LEU D 4 206 ? -18.37353 38.85174  44.61568  1.000 223.21000 ? 187 LEU D O   1 
ATOM   7352 C CB  . LEU D 4 206 ? -15.09902 37.58804  44.64940  1.000 215.63913 ? 187 LEU D CB  1 
ATOM   7353 C CG  . LEU D 4 206 ? -15.30020 37.04410  43.22937  1.000 218.25236 ? 187 LEU D CG  1 
ATOM   7354 C CD1 . LEU D 4 206 ? -15.37705 38.15921  42.19233  1.000 221.93731 ? 187 LEU D CD1 1 
ATOM   7355 C CD2 . LEU D 4 206 ? -14.19002 36.07156  42.87106  1.000 213.81574 ? 187 LEU D CD2 1 
ATOM   7356 N N   . SER D 4 207 ? -16.53855 40.16041  44.54137  1.000 210.42810 ? 188 SER D N   1 
ATOM   7357 C CA  . SER D 4 207 ? -17.21597 41.27576  43.89464  1.000 214.21548 ? 188 SER D CA  1 
ATOM   7358 C C   . SER D 4 207 ? -16.19749 42.09317  43.11024  1.000 218.09609 ? 188 SER D C   1 
ATOM   7359 O O   . SER D 4 207 ? -14.99042 41.84818  43.17418  1.000 217.15267 ? 188 SER D O   1 
ATOM   7360 C CB  . SER D 4 207 ? -17.94813 42.15123  44.91689  1.000 215.09652 ? 188 SER D CB  1 
ATOM   7361 O OG  . SER D 4 207 ? -17.05279 42.65449  45.89337  1.000 215.62190 ? 188 SER D OG  1 
ATOM   7362 N N   . SER D 4 208 ? -16.69957 43.07933  42.36742  1.000 209.73802 ? 189 SER D N   1 
ATOM   7363 C CA  . SER D 4 208 ? -15.84619 43.93823  41.55786  1.000 214.62867 ? 189 SER D CA  1 
ATOM   7364 C C   . SER D 4 208 ? -16.43703 45.33967  41.50338  1.000 222.69443 ? 189 SER D C   1 
ATOM   7365 O O   . SER D 4 208 ? -17.65086 45.52355  41.62873  1.000 223.21183 ? 189 SER D O   1 
ATOM   7366 C CB  . SER D 4 208 ? -15.67127 43.38821  40.13741  1.000 216.31697 ? 189 SER D CB  1 
ATOM   7367 O OG  . SER D 4 208 ? -14.91212 44.28016  39.33974  1.000 223.04380 ? 189 SER D OG  1 
ATOM   7368 N N   . SER D 4 209 ? -15.56278 46.32546  41.30387  1.000 216.77582 ? 190 SER D N   1 
ATOM   7369 C CA  . SER D 4 209 ? -15.95986 47.72608  41.24605  1.000 222.55145 ? 190 SER D CA  1 
ATOM   7370 C C   . SER D 4 209 ? -15.25273 48.41577  40.08909  1.000 228.49011 ? 190 SER D C   1 
ATOM   7371 O O   . SER D 4 209 ? -14.03868 48.26662  39.92476  1.000 228.09475 ? 190 SER D O   1 
ATOM   7372 C CB  . SER D 4 209 ? -15.63685 48.44496  42.56034  1.000 221.88349 ? 190 SER D CB  1 
ATOM   7373 O OG  . SER D 4 209 ? -15.57575 49.84632  42.36657  1.000 227.99290 ? 190 SER D OG  1 
ATOM   7374 N N   . VAL D 4 210 ? -16.01034 49.17317  39.29699  1.000 227.54036 ? 191 VAL D N   1 
ATOM   7375 C CA  . VAL D 4 210 ? -15.47178 49.94647  38.18369  1.000 230.03402 ? 191 VAL D CA  1 
ATOM   7376 C C   . VAL D 4 210 ? -15.95195 51.38513  38.31974  1.000 236.31127 ? 191 VAL D C   1 
ATOM   7377 O O   . VAL D 4 210 ? -17.14144 51.62906  38.55120  1.000 238.45885 ? 191 VAL D O   1 
ATOM   7378 C CB  . VAL D 4 210 ? -15.88411 49.35644  36.81947  1.000 228.23949 ? 191 VAL D CB  1 
ATOM   7379 C CG1 . VAL D 4 210 ? -17.35659 48.99267  36.81666  1.000 228.34403 ? 191 VAL D CG1 1 
ATOM   7380 C CG2 . VAL D 4 210 ? -15.57711 50.33523  35.69531  1.000 232.08375 ? 191 VAL D CG2 1 
ATOM   7381 N N   . THR D 4 211 ? -15.02805 52.33250  38.18519  1.000 234.63690 ? 192 THR D N   1 
ATOM   7382 C CA  . THR D 4 211 ? -15.33266 53.75169  38.30475  1.000 240.59257 ? 192 THR D CA  1 
ATOM   7383 C C   . THR D 4 211 ? -15.36663 54.38606  36.91948  1.000 247.86324 ? 192 THR D C   1 
ATOM   7384 O O   . THR D 4 211 ? -14.46842 54.15507  36.10262  1.000 250.26826 ? 192 THR D O   1 
ATOM   7385 C CB  . THR D 4 211 ? -14.30255 54.45708  39.18750  1.000 241.84569 ? 192 THR D CB  1 
ATOM   7386 O OG1 . THR D 4 211 ? -14.00075 53.63570  40.32311  1.000 234.21896 ? 192 THR D OG1 1 
ATOM   7387 C CG2 . THR D 4 211 ? -14.84494 55.79272  39.67560  1.000 246.17688 ? 192 THR D CG2 1 
ATOM   7388 N N   . VAL D 4 212 ? -16.40140 55.18070  36.66141  1.000 251.34703 ? 193 VAL D N   1 
ATOM   7389 C CA  . VAL D 4 212 ? -16.61925 55.78952  35.34910  1.000 259.09235 ? 193 VAL D CA  1 
ATOM   7390 C C   . VAL D 4 212 ? -17.02455 57.24425  35.53169  1.000 264.55397 ? 193 VAL D C   1 
ATOM   7391 O O   . VAL D 4 212 ? -17.47875 57.65120  36.61012  1.000 263.17027 ? 193 VAL D O   1 
ATOM   7392 C CB  . VAL D 4 212 ? -17.70049 55.04159  34.54184  1.000 257.91983 ? 193 VAL D CB  1 
ATOM   7393 C CG1 . VAL D 4 212 ? -17.26292 53.61434  34.24148  1.000 253.10413 ? 193 VAL D CG1 1 
ATOM   7394 C CG2 . VAL D 4 212 ? -19.02176 55.05932  35.29041  1.000 255.68264 ? 193 VAL D CG2 1 
ATOM   7395 N N   . PRO D 4 213 ? -16.85865 58.05933  34.48630  1.000 268.08946 ? 194 PRO D N   1 
ATOM   7396 C CA  . PRO D 4 213 ? -17.33623 59.44559  34.55646  1.000 273.12123 ? 194 PRO D CA  1 
ATOM   7397 C C   . PRO D 4 213 ? -18.85240 59.49397  34.65367  1.000 274.80046 ? 194 PRO D C   1 
ATOM   7398 O O   . PRO D 4 213 ? -19.56140 58.70835  34.02160  1.000 274.49495 ? 194 PRO D O   1 
ATOM   7399 C CB  . PRO D 4 213 ? -16.83710 60.06642  33.24613  1.000 278.67867 ? 194 PRO D CB  1 
ATOM   7400 C CG  . PRO D 4 213 ? -15.69998 59.20028  32.82707  1.000 276.25216 ? 194 PRO D CG  1 
ATOM   7401 C CD  . PRO D 4 213 ? -16.05457 57.81749  33.27711  1.000 270.53291 ? 194 PRO D CD  1 
ATOM   7402 N N   . SER D 4 214 ? -19.34586 60.43967  35.45545  1.000 267.99053 ? 195 SER D N   1 
ATOM   7403 C CA  . SER D 4 214 ? -20.76821 60.47105  35.78019  1.000 269.65426 ? 195 SER D CA  1 
ATOM   7404 C C   . SER D 4 214 ? -21.62600 60.74291  34.55271  1.000 272.92977 ? 195 SER D C   1 
ATOM   7405 O O   . SER D 4 214 ? -22.81392 60.39860  34.53567  1.000 272.61113 ? 195 SER D O   1 
ATOM   7406 C CB  . SER D 4 214 ? -21.03853 61.51803  36.86087  1.000 275.55255 ? 195 SER D CB  1 
ATOM   7407 O OG  . SER D 4 214 ? -22.42253 61.61314  37.15187  1.000 277.78309 ? 195 SER D OG  1 
ATOM   7408 N N   . SER D 4 215 ? -21.04888 61.35025  33.51723  1.000 284.44040 ? 196 SER D N   1 
ATOM   7409 C CA  . SER D 4 215 ? -21.82513 61.64008  32.31748  1.000 289.89872 ? 196 SER D CA  1 
ATOM   7410 C C   . SER D 4 215 ? -22.09813 60.37854  31.50430  1.000 286.87182 ? 196 SER D C   1 
ATOM   7411 O O   . SER D 4 215 ? -23.10804 60.30434  30.79248  1.000 288.17773 ? 196 SER D O   1 
ATOM   7412 C CB  . SER D 4 215 ? -21.10010 62.68010  31.46293  1.000 295.76376 ? 196 SER D CB  1 
ATOM   7413 O OG  . SER D 4 215 ? -19.87142 62.16745  30.97599  1.000 293.79112 ? 196 SER D OG  1 
ATOM   7414 N N   . THR D 4 216 ? -21.23166 59.36976  31.61729  1.000 294.98514 ? 197 THR D N   1 
ATOM   7415 C CA  . THR D 4 216 ? -21.34715 58.17550  30.78864  1.000 291.81739 ? 197 THR D CA  1 
ATOM   7416 C C   . THR D 4 216 ? -22.42138 57.20984  31.27494  1.000 286.23380 ? 197 THR D C   1 
ATOM   7417 O O   . THR D 4 216 ? -22.85180 56.34632  30.50264  1.000 285.21253 ? 197 THR D O   1 
ATOM   7418 C CB  . THR D 4 216 ? -20.00005 57.45364  30.71920  1.000 289.18386 ? 197 THR D CB  1 
ATOM   7419 O OG1 . THR D 4 216 ? -19.62046 57.02129  32.03120  1.000 282.69739 ? 197 THR D OG1 1 
ATOM   7420 C CG2 . THR D 4 216 ? -18.93074 58.38890  30.17265  1.000 294.74374 ? 197 THR D CG2 1 
ATOM   7421 N N   . TRP D 4 217 ? -22.85935 57.32785  32.52678  1.000 303.99542 ? 198 TRP D N   1 
ATOM   7422 C CA  . TRP D 4 217 ? -23.93115 56.49909  33.05261  1.000 298.42972 ? 198 TRP D CA  1 
ATOM   7423 C C   . TRP D 4 217 ? -25.00290 57.39539  33.65742  1.000 299.95971 ? 198 TRP D C   1 
ATOM   7424 O O   . TRP D 4 217 ? -24.67748 58.39106  34.31509  1.000 302.58732 ? 198 TRP D O   1 
ATOM   7425 C CB  . TRP D 4 217 ? -23.40601 55.51617  34.11300  1.000 290.92085 ? 198 TRP D CB  1 
ATOM   7426 C CG  . TRP D 4 217 ? -24.17960 54.23057  34.18640  1.000 283.62109 ? 198 TRP D CG  1 
ATOM   7427 C CD1 . TRP D 4 217 ? -23.99064 53.11862  33.41936  1.000 280.28385 ? 198 TRP D CD1 1 
ATOM   7428 C CD2 . TRP D 4 217 ? -25.26034 53.92333  35.07779  1.000 277.67106 ? 198 TRP D CD2 1 
ATOM   7429 N NE1 . TRP D 4 217 ? -24.88747 52.14013  33.77326  1.000 272.37718 ? 198 TRP D NE1 1 
ATOM   7430 C CE2 . TRP D 4 217 ? -25.67937 52.60932  34.78799  1.000 270.45522 ? 198 TRP D CE2 1 
ATOM   7431 C CE3 . TRP D 4 217 ? -25.91850 54.63391  36.08650  1.000 277.63472 ? 198 TRP D CE3 1 
ATOM   7432 C CZ2 . TRP D 4 217 ? -26.72278 51.98949  35.47351  1.000 262.98450 ? 198 TRP D CZ2 1 
ATOM   7433 C CZ3 . TRP D 4 217 ? -26.95527 54.01679  36.76541  1.000 270.29997 ? 198 TRP D CZ3 1 
ATOM   7434 C CH2 . TRP D 4 217 ? -27.34648 52.70803  36.45596  1.000 262.92541 ? 198 TRP D CH2 1 
ATOM   7435 N N   . PRO D 4 218 ? -26.29138 57.06970  33.46740  1.000 298.98419 ? 199 PRO D N   1 
ATOM   7436 C CA  . PRO D 4 218 ? -26.81619 55.88497  32.77993  1.000 293.71160 ? 199 PRO D CA  1 
ATOM   7437 C C   . PRO D 4 218 ? -27.00162 56.05446  31.27395  1.000 298.84982 ? 199 PRO D C   1 
ATOM   7438 O O   . PRO D 4 218 ? -27.79672 55.32410  30.68311  1.000 295.29130 ? 199 PRO D O   1 
ATOM   7439 C CB  . PRO D 4 218 ? -28.17025 55.68105  33.45600  1.000 287.61629 ? 199 PRO D CB  1 
ATOM   7440 C CG  . PRO D 4 218 ? -28.62001 57.07172  33.75588  1.000 293.39515 ? 199 PRO D CG  1 
ATOM   7441 C CD  . PRO D 4 218 ? -27.37241 57.86560  34.07641  1.000 299.66339 ? 199 PRO D CD  1 
ATOM   7442 N N   . SER D 4 219 ? -26.28188 56.99837  30.66304  1.000 285.70850 ? 200 SER D N   1 
ATOM   7443 C CA  . SER D 4 219 ? -26.44646 57.22959  29.23143  1.000 291.28936 ? 200 SER D CA  1 
ATOM   7444 C C   . SER D 4 219 ? -25.92876 56.05897  28.40482  1.000 288.41533 ? 200 SER D C   1 
ATOM   7445 O O   . SER D 4 219 ? -26.49857 55.74640  27.35303  1.000 288.14371 ? 200 SER D O   1 
ATOM   7446 C CB  . SER D 4 219 ? -25.74217 58.52305  28.82173  1.000 300.50769 ? 200 SER D CB  1 
ATOM   7447 O OG  . SER D 4 219 ? -24.36571 58.48317  29.15352  1.000 299.86701 ? 200 SER D OG  1 
ATOM   7448 N N   . GLU D 4 220 ? -24.86403 55.40249  28.85660  1.000 290.91055 ? 201 GLU D N   1 
ATOM   7449 C CA  . GLU D 4 220 ? -24.28138 54.27386  28.14924  1.000 288.28928 ? 201 GLU D CA  1 
ATOM   7450 C C   . GLU D 4 220 ? -24.25117 53.05252  29.06018  1.000 278.76186 ? 201 GLU D C   1 
ATOM   7451 O O   . GLU D 4 220 ? -24.25101 53.16526  30.28922  1.000 275.14379 ? 201 GLU D O   1 
ATOM   7452 C CB  . GLU D 4 220 ? -22.87505 54.61205  27.63610  1.000 293.81605 ? 201 GLU D CB  1 
ATOM   7453 C CG  . GLU D 4 220 ? -22.87596 55.71603  26.58498  1.000 302.55840 ? 201 GLU D CG  1 
ATOM   7454 C CD  . GLU D 4 220 ? -21.48316 56.14978  26.17388  1.000 306.28334 ? 201 GLU D CD  1 
ATOM   7455 O OE1 . GLU D 4 220 ? -20.51810 55.82765  26.89727  1.000 302.53115 ? 201 GLU D OE1 1 
ATOM   7456 O OE2 . GLU D 4 220 ? -21.35456 56.81594  25.12479  1.000 312.53415 ? 201 GLU D OE2 1 
ATOM   7457 N N   . THR D 4 221 ? -24.22689 51.87695  28.43803  1.000 279.14399 ? 202 THR D N   1 
ATOM   7458 C CA  . THR D 4 221 ? -24.46179 50.61427  29.12730  1.000 269.99155 ? 202 THR D CA  1 
ATOM   7459 C C   . THR D 4 221 ? -23.14867 49.91629  29.45937  1.000 267.98556 ? 202 THR D C   1 
ATOM   7460 O O   . THR D 4 221 ? -22.29091 49.74166  28.58707  1.000 271.69229 ? 202 THR D O   1 
ATOM   7461 C CB  . THR D 4 221 ? -25.34029 49.69513  28.27539  1.000 265.61407 ? 202 THR D CB  1 
ATOM   7462 O OG1 . THR D 4 221 ? -26.66831 50.22957  28.20807  1.000 265.39431 ? 202 THR D OG1 1 
ATOM   7463 C CG2 . THR D 4 221 ? -25.39001 48.29251  28.86678  1.000 255.95265 ? 202 THR D CG2 1 
ATOM   7464 N N   . VAL D 4 222 ? -23.00519 49.51387  30.72063  1.000 267.75411 ? 203 VAL D N   1 
ATOM   7465 C CA  . VAL D 4 222 ? -21.90189 48.67966  31.18105  1.000 264.08247 ? 203 VAL D CA  1 
ATOM   7466 C C   . VAL D 4 222 ? -22.46915 47.33123  31.60229  1.000 254.57811 ? 203 VAL D C   1 
ATOM   7467 O O   . VAL D 4 222 ? -23.52024 47.26447  32.25091  1.000 250.03198 ? 203 VAL D O   1 
ATOM   7468 C CB  . VAL D 4 222 ? -21.13278 49.34381  32.33968  1.000 264.64544 ? 203 VAL D CB  1 
ATOM   7469 C CG1 . VAL D 4 222 ? -20.26415 50.47358  31.81532  1.000 273.06678 ? 203 VAL D CG1 1 
ATOM   7470 C CG2 . VAL D 4 222 ? -22.10408 49.86411  33.38809  1.000 262.38537 ? 203 VAL D CG2 1 
ATOM   7471 N N   . THR D 4 223 ? -21.77803 46.25591  31.22903  1.000 257.44939 ? 204 THR D N   1 
ATOM   7472 C CA  . THR D 4 223 ? -22.25821 44.90253  31.47638  1.000 248.27302 ? 204 THR D CA  1 
ATOM   7473 C C   . THR D 4 223 ? -21.17984 44.08830  32.17424  1.000 243.65261 ? 204 THR D C   1 
ATOM   7474 O O   . THR D 4 223 ? -20.04808 43.99953  31.68691  1.000 246.78272 ? 204 THR D O   1 
ATOM   7475 C CB  . THR D 4 223 ? -22.67383 44.21370  30.17110  1.000 247.58408 ? 204 THR D CB  1 
ATOM   7476 O OG1 . THR D 4 223 ? -23.64552 45.01914  29.49231  1.000 252.32036 ? 204 THR D OG1 1 
ATOM   7477 C CG2 . THR D 4 223 ? -23.27307 42.84481  30.45838  1.000 237.86815 ? 204 THR D CG2 1 
ATOM   7478 N N   . CYS D 4 224 ? -21.53714 43.49709  33.31151  1.000 246.04080 ? 205 CYS D N   1 
ATOM   7479 C CA  . CYS D 4 224 ? -20.63019 42.60255  34.01644  1.000 241.47933 ? 205 CYS D CA  1 
ATOM   7480 C C   . CYS D 4 224 ? -20.53397 41.27874  33.26692  1.000 237.90903 ? 205 CYS D C   1 
ATOM   7481 O O   . CYS D 4 224 ? -21.55395 40.66370  32.94086  1.000 234.32494 ? 205 CYS D O   1 
ATOM   7482 C CB  . CYS D 4 224 ? -21.12253 42.38065  35.44756  1.000 235.90349 ? 205 CYS D CB  1 
ATOM   7483 S SG  . CYS D 4 224 ? -19.91580 41.66382  36.59349  1.000 231.96838 ? 205 CYS D SG  1 
ATOM   7484 N N   . ASN D 4 225 ? -19.30812 40.84464  32.98246  1.000 238.43395 ? 206 ASN D N   1 
ATOM   7485 C CA  . ASN D 4 225 ? -19.05800 39.63198  32.20431  1.000 235.70482 ? 206 ASN D CA  1 
ATOM   7486 C C   . ASN D 4 225 ? -18.40216 38.60063  33.11770  1.000 229.46223 ? 206 ASN D C   1 
ATOM   7487 O O   . ASN D 4 225 ? -17.18949 38.63938  33.34161  1.000 230.09449 ? 206 ASN D O   1 
ATOM   7488 C CB  . ASN D 4 225 ? -18.18607 39.93549  30.98904  1.000 241.75838 ? 206 ASN D CB  1 
ATOM   7489 C CG  . ASN D 4 225 ? -18.67756 41.13547  30.20324  1.000 248.93341 ? 206 ASN D CG  1 
ATOM   7490 O OD1 . ASN D 4 225 ? -17.90730 42.04264  29.88830  1.000 255.90646 ? 206 ASN D OD1 1 
ATOM   7491 N ND2 . ASN D 4 225 ? -19.96748 41.14985  29.88849  1.000 247.48218 ? 206 ASN D ND2 1 
ATOM   7492 N N   . VAL D 4 226 ? -19.20595 37.67231  33.63174  1.000 239.02667 ? 207 VAL D N   1 
ATOM   7493 C CA  . VAL D 4 226 ? -18.74670 36.65551  34.57095  1.000 233.48569 ? 207 VAL D CA  1 
ATOM   7494 C C   . VAL D 4 226 ? -18.62054 35.32643  33.83911  1.000 231.12668 ? 207 VAL D C   1 
ATOM   7495 O O   . VAL D 4 226 ? -19.36172 35.04123  32.89093  1.000 231.29290 ? 207 VAL D O   1 
ATOM   7496 C CB  . VAL D 4 226 ? -19.70776 36.54942  35.77537  1.000 230.20199 ? 207 VAL D CB  1 
ATOM   7497 C CG1 . VAL D 4 226 ? -19.11177 35.68188  36.87329  1.000 226.74744 ? 207 VAL D CG1 1 
ATOM   7498 C CG2 . VAL D 4 226 ? -20.04280 37.93494  36.30813  1.000 233.43919 ? 207 VAL D CG2 1 
ATOM   7499 N N   . ALA D 4 227 ? -17.66770 34.50377  34.27754  1.000 232.63521 ? 208 ALA D N   1 
ATOM   7500 C CA  . ALA D 4 227 ? -17.43587 33.20410  33.65981  1.000 231.61647 ? 208 ALA D CA  1 
ATOM   7501 C C   . ALA D 4 227 ? -16.86992 32.24099  34.69268  1.000 229.27401 ? 208 ALA D C   1 
ATOM   7502 O O   . ALA D 4 227 ? -15.88500 32.55943  35.36524  1.000 226.70768 ? 208 ALA D O   1 
ATOM   7503 C CB  . ALA D 4 227 ? -16.48190 33.32414  32.46624  1.000 234.50827 ? 208 ALA D CB  1 
ATOM   7504 N N   . HIS D 4 228 ? -17.49293 31.06954  34.81193  1.000 233.40775 ? 209 HIS D N   1 
ATOM   7505 C CA  . HIS D 4 228 ? -17.02246 30.02033  35.71027  1.000 231.44374 ? 209 HIS D CA  1 
ATOM   7506 C C   . HIS D 4 228 ? -16.58786 28.82031  34.88136  1.000 230.62539 ? 209 HIS D C   1 
ATOM   7507 O O   . HIS D 4 228 ? -17.44421 28.13781  34.29635  1.000 228.37732 ? 209 HIS D O   1 
ATOM   7508 C CB  . HIS D 4 228 ? -18.11737 29.61994  36.70066  1.000 228.59218 ? 209 HIS D CB  1 
ATOM   7509 C CG  . HIS D 4 228 ? -17.63627 28.73819  37.81081  1.000 227.68668 ? 209 HIS D CG  1 
ATOM   7510 N ND1 . HIS D 4 228 ? -18.49523 28.04194  38.63373  1.000 225.97398 ? 209 HIS D ND1 1 
ATOM   7511 C CD2 . HIS D 4 228 ? -16.38545 28.44471  38.23836  1.000 228.66617 ? 209 HIS D CD2 1 
ATOM   7512 C CE1 . HIS D 4 228 ? -17.79436 27.35470  39.51786  1.000 226.51113 ? 209 HIS D CE1 1 
ATOM   7513 N NE2 . HIS D 4 228 ? -16.51159 27.58190  39.29990  1.000 227.74762 ? 209 HIS D NE2 1 
ATOM   7514 N N   . PRO D 4 229 ? -15.28723 28.52424  34.79404  1.000 232.56420 ? 210 PRO D N   1 
ATOM   7515 C CA  . PRO D 4 229 ? -14.84698 27.46454  33.86888  1.000 232.34616 ? 210 PRO D CA  1 
ATOM   7516 C C   . PRO D 4 229 ? -15.31545 26.07185  34.25618  1.000 229.67654 ? 210 PRO D C   1 
ATOM   7517 O O   . PRO D 4 229 ? -15.70051 25.29091  33.37621  1.000 228.07482 ? 210 PRO D O   1 
ATOM   7518 C CB  . PRO D 4 229 ? -13.31465 27.57976  33.91265  1.000 234.74348 ? 210 PRO D CB  1 
ATOM   7519 C CG  . PRO D 4 229 ? -13.04092 28.95601  34.42829  1.000 235.35898 ? 210 PRO D CG  1 
ATOM   7520 C CD  . PRO D 4 229 ? -14.15214 29.25059  35.38506  1.000 233.94962 ? 210 PRO D CD  1 
ATOM   7521 N N   . ALA D 4 230 ? -15.29426 25.73492  35.54912  1.000 231.98597 ? 211 ALA D N   1 
ATOM   7522 C CA  . ALA D 4 230 ? -15.57331 24.36246  35.96370  1.000 230.48619 ? 211 ALA D CA  1 
ATOM   7523 C C   . ALA D 4 230 ? -16.98830 23.92857  35.60273  1.000 228.03267 ? 211 ALA D C   1 
ATOM   7524 O O   . ALA D 4 230 ? -17.22825 22.73936  35.36422  1.000 226.89094 ? 211 ALA D O   1 
ATOM   7525 C CB  . ALA D 4 230 ? -15.34211 24.21004  37.46709  1.000 231.11251 ? 211 ALA D CB  1 
ATOM   7526 N N   . SER D 4 231 ? -17.93391 24.86664  35.55192  1.000 239.68806 ? 212 SER D N   1 
ATOM   7527 C CA  . SER D 4 231 ? -19.32354 24.54754  35.24731  1.000 236.91074 ? 212 SER D CA  1 
ATOM   7528 C C   . SER D 4 231 ? -19.80470 25.18017  33.94724  1.000 235.94495 ? 212 SER D C   1 
ATOM   7529 O O   . SER D 4 231 ? -21.01600 25.20315  33.69620  1.000 233.28650 ? 212 SER D O   1 
ATOM   7530 C CB  . SER D 4 231 ? -20.23174 24.97704  36.40323  1.000 236.16199 ? 212 SER D CB  1 
ATOM   7531 O OG  . SER D 4 231 ? -20.14061 26.37241  36.62968  1.000 237.23014 ? 212 SER D OG  1 
ATOM   7532 N N   . SER D 4 232 ? -18.89328 25.69441  33.11905  1.000 235.86381 ? 213 SER D N   1 
ATOM   7533 C CA  . SER D 4 232 ? -19.21107 26.30789  31.82852  1.000 235.86984 ? 213 SER D CA  1 
ATOM   7534 C C   . SER D 4 232 ? -20.19634 27.46697  31.95565  1.000 235.63888 ? 213 SER D C   1 
ATOM   7535 O O   . SER D 4 232 ? -20.91073 27.78526  30.99940  1.000 235.06068 ? 213 SER D O   1 
ATOM   7536 C CB  . SER D 4 232 ? -19.74719 25.26974  30.83370  1.000 232.83541 ? 213 SER D CB  1 
ATOM   7537 O OG  . SER D 4 232 ? -21.00337 24.75912  31.24686  1.000 229.18262 ? 213 SER D OG  1 
ATOM   7538 N N   . THR D 4 233 ? -20.24361 28.11102  33.11808  1.000 233.75203 ? 214 THR D N   1 
ATOM   7539 C CA  . THR D 4 233 ? -21.17442 29.20510  33.34926  1.000 233.82209 ? 214 THR D CA  1 
ATOM   7540 C C   . THR D 4 233 ? -20.65634 30.49364  32.71774  1.000 238.03294 ? 214 THR D C   1 
ATOM   7541 O O   . THR D 4 233 ? -19.45080 30.75708  32.68808  1.000 241.24361 ? 214 THR D O   1 
ATOM   7542 C CB  . THR D 4 233 ? -21.39954 29.40268  34.85082  1.000 233.43137 ? 214 THR D CB  1 
ATOM   7543 O OG1 . THR D 4 233 ? -21.79090 28.15681  35.44125  1.000 230.49668 ? 214 THR D OG1 1 
ATOM   7544 C CG2 . THR D 4 233 ? -22.49019 30.43457  35.10945  1.000 233.27090 ? 214 THR D CG2 1 
ATOM   7545 N N   . LYS D 4 234 ? -21.58948 31.29827  32.20065  1.000 227.83526 ? 215 LYS D N   1 
ATOM   7546 C CA  . LYS D 4 234 ? -21.23742 32.55261  31.53610  1.000 232.83420 ? 215 LYS D CA  1 
ATOM   7547 C C   . LYS D 4 234 ? -22.44988 33.47937  31.63452  1.000 232.78102 ? 215 LYS D C   1 
ATOM   7548 O O   . LYS D 4 234 ? -23.42293 33.30529  30.89601  1.000 230.40302 ? 215 LYS D O   1 
ATOM   7549 C CB  . LYS D 4 234 ? -20.83368 32.30684  30.09159  1.000 234.35630 ? 215 LYS D CB  1 
ATOM   7550 C CG  . LYS D 4 234 ? -20.62850 33.56379  29.26664  1.000 240.62388 ? 215 LYS D CG  1 
ATOM   7551 C CD  . LYS D 4 234 ? -20.42895 33.20954  27.80218  1.000 241.76525 ? 215 LYS D CD  1 
ATOM   7552 C CE  . LYS D 4 234 ? -20.40520 34.44743  26.92393  1.000 248.40338 ? 215 LYS D CE  1 
ATOM   7553 N NZ  . LYS D 4 234 ? -20.34201 34.09416  25.47882  1.000 248.93062 ? 215 LYS D NZ  1 
ATOM   7554 N N   . VAL D 4 235 ? -22.37928 34.44967  32.54284  1.000 232.61681 ? 216 VAL D N   1 
ATOM   7555 C CA  . VAL D 4 235 ? -23.47194 35.38128  32.79645  1.000 232.88559 ? 216 VAL D CA  1 
ATOM   7556 C C   . VAL D 4 235 ? -23.03479 36.77776  32.37816  1.000 238.69663 ? 216 VAL D C   1 
ATOM   7557 O O   . VAL D 4 235 ? -21.90574 37.19714  32.65922  1.000 241.98210 ? 216 VAL D O   1 
ATOM   7558 C CB  . VAL D 4 235 ? -23.89837 35.36185  34.27765  1.000 230.10578 ? 216 VAL D CB  1 
ATOM   7559 C CG1 . VAL D 4 235 ? -25.20937 36.10650  34.46222  1.000 229.08899 ? 216 VAL D CG1 1 
ATOM   7560 C CG2 . VAL D 4 235 ? -24.01397 33.93134  34.78097  1.000 225.17766 ? 216 VAL D CG2 1 
ATOM   7561 N N   . ASP D 4 236 ? -23.93633 37.50003  31.70407  1.000 231.92056 ? 217 ASP D N   1 
ATOM   7562 C CA  . ASP D 4 236 ? -23.69302 38.87273  31.24986  1.000 238.89493 ? 217 ASP D CA  1 
ATOM   7563 C C   . ASP D 4 236 ? -24.84826 39.74386  31.74104  1.000 239.22872 ? 217 ASP D C   1 
ATOM   7564 O O   . ASP D 4 236 ? -25.76709 40.06409  30.98360  1.000 240.40756 ? 217 ASP D O   1 
ATOM   7565 C CB  . ASP D 4 236 ? -23.54190 38.93453  29.72728  1.000 242.54751 ? 217 ASP D CB  1 
ATOM   7566 C CG  . ASP D 4 236 ? -22.23782 38.33147  29.24352  1.000 244.21964 ? 217 ASP D CG  1 
ATOM   7567 O OD1 . ASP D 4 236 ? -21.25548 38.33632  30.01486  1.000 244.50577 ? 217 ASP D OD1 1 
ATOM   7568 O OD2 . ASP D 4 236 ? -22.19374 37.85831  28.08815  1.000 244.70817 ? 217 ASP D OD2 1 
ATOM   7569 N N   . LYS D 4 237 ? -24.79618 40.13053  33.01299  1.000 234.86069 ? 218 LYS D N   1 
ATOM   7570 C CA  . LYS D 4 237 ? -25.81595 40.97989  33.61527  1.000 235.38974 ? 218 LYS D CA  1 
ATOM   7571 C C   . LYS D 4 237 ? -25.31702 42.41920  33.64924  1.000 242.70541 ? 218 LYS D C   1 
ATOM   7572 O O   . LYS D 4 237 ? -24.28852 42.71166  34.26919  1.000 244.58980 ? 218 LYS D O   1 
ATOM   7573 C CB  . LYS D 4 237 ? -26.17536 40.49855  35.02090  1.000 229.90119 ? 218 LYS D CB  1 
ATOM   7574 C CG  . LYS D 4 237 ? -26.97119 39.20427  35.04057  1.000 226.48203 ? 218 LYS D CG  1 
ATOM   7575 C CD  . LYS D 4 237 ? -27.49727 38.88896  36.43118  1.000 226.85030 ? 218 LYS D CD  1 
ATOM   7576 C CE  . LYS D 4 237 ? -28.52076 39.91790  36.88292  1.000 231.21784 ? 218 LYS D CE  1 
ATOM   7577 N NZ  . LYS D 4 237 ? -29.11733 39.56328  38.19979  1.000 231.93147 ? 218 LYS D NZ  1 
ATOM   7578 N N   . LYS D 4 238 ? -26.04681 43.30886  32.98332  1.000 235.68100 ? 219 LYS D N   1 
ATOM   7579 C CA  . LYS D 4 238 ? -25.69647 44.71798  32.93597  1.000 243.54538 ? 219 LYS D CA  1 
ATOM   7580 C C   . LYS D 4 238 ? -26.22629 45.44631  34.16817  1.000 243.01239 ? 219 LYS D C   1 
ATOM   7581 O O   . LYS D 4 238 ? -27.10031 44.95577  34.88801  1.000 236.84479 ? 219 LYS D O   1 
ATOM   7582 C CB  . LYS D 4 238 ? -26.25169 45.36186  31.66556  1.000 248.34090 ? 219 LYS D CB  1 
ATOM   7583 C CG  . LYS D 4 238 ? -27.74766 45.16351  31.48689  1.000 243.66588 ? 219 LYS D CG  1 
ATOM   7584 C CD  . LYS D 4 238 ? -28.22434 45.66976  30.13673  1.000 248.12831 ? 219 LYS D CD  1 
ATOM   7585 C CE  . LYS D 4 238 ? -29.71885 45.44700  29.96918  1.000 245.99347 ? 219 LYS D CE  1 
ATOM   7586 N NZ  . LYS D 4 238 ? -30.20809 45.90825  28.64150  1.000 249.77163 ? 219 LYS D NZ  1 
ATOM   7587 N N   . ILE D 4 239 ? -25.68335 46.63629  34.40301  1.000 242.57068 ? 220 ILE D N   1 
ATOM   7588 C CA  . ILE D 4 239 ? -26.09245 47.44974  35.54054  1.000 242.82210 ? 220 ILE D CA  1 
ATOM   7589 C C   . ILE D 4 239 ? -27.25924 48.34955  35.15067  1.000 246.09341 ? 220 ILE D C   1 
ATOM   7590 O O   . ILE D 4 239 ? -27.22726 49.00750  34.11065  1.000 252.62252 ? 220 ILE D O   1 
ATOM   7591 C CB  . ILE D 4 239 ? -24.91774 48.28290  36.08095  1.000 247.89152 ? 220 ILE D CB  1 
ATOM   7592 C CG1 . ILE D 4 239 ? -23.73779 47.37534  36.43465  1.000 243.76045 ? 220 ILE D CG1 1 
ATOM   7593 C CG2 . ILE D 4 239 ? -25.35272 49.09102  37.29384  1.000 248.00768 ? 220 ILE D CG2 1 
ATOM   7594 C CD1 . ILE D 4 239 ? -24.05347 46.35232  37.50162  1.000 235.20781 ? 220 ILE D CD1 1 
ATOM   7595 N N   . ASP E 5 21  ? 17.87782  17.65692  47.80925  1.000 218.34601 ? 1   ASP E N   1 
ATOM   7596 C CA  . ASP E 5 21  ? 17.09476  18.85332  48.09802  1.000 220.10690 ? 1   ASP E CA  1 
ATOM   7597 C C   . ASP E 5 21  ? 17.99275  20.01652  48.49520  1.000 225.65697 ? 1   ASP E C   1 
ATOM   7598 O O   . ASP E 5 21  ? 19.13755  19.81723  48.90345  1.000 229.78739 ? 1   ASP E O   1 
ATOM   7599 C CB  . ASP E 5 21  ? 16.08013  18.58208  49.21140  1.000 221.81995 ? 1   ASP E CB  1 
ATOM   7600 C CG  . ASP E 5 21  ? 15.01800  17.58258  48.80386  1.000 216.16996 ? 1   ASP E CG  1 
ATOM   7601 O OD1 . ASP E 5 21  ? 14.93703  17.25560  47.60346  1.000 210.23497 ? 1   ASP E OD1 1 
ATOM   7602 O OD2 . ASP E 5 21  ? 14.26673  17.11645  49.68426  1.000 218.00014 ? 1   ASP E OD2 1 
ATOM   7603 N N   . ILE E 5 22  ? 17.46445  21.23093  48.36135  1.000 216.89148 ? 2   ILE E N   1 
ATOM   7604 C CA  . ILE E 5 22  ? 18.13808  22.44844  48.80005  1.000 221.75461 ? 2   ILE E CA  1 
ATOM   7605 C C   . ILE E 5 22  ? 17.09685  23.38155  49.40316  1.000 223.75262 ? 2   ILE E C   1 
ATOM   7606 O O   . ILE E 5 22  ? 16.00454  23.54886  48.84993  1.000 220.17578 ? 2   ILE E O   1 
ATOM   7607 C CB  . ILE E 5 22  ? 18.88940  23.14520  47.64303  1.000 220.36274 ? 2   ILE E CB  1 
ATOM   7608 C CG1 . ILE E 5 22  ? 20.06113  22.28994  47.15766  1.000 219.66070 ? 2   ILE E CG1 1 
ATOM   7609 C CG2 . ILE E 5 22  ? 19.40359  24.50513  48.08340  1.000 224.69173 ? 2   ILE E CG2 1 
ATOM   7610 C CD1 . ILE E 5 22  ? 20.96902  23.00278  46.18235  1.000 219.49138 ? 2   ILE E CD1 1 
ATOM   7611 N N   . VAL E 5 23  ? 17.43013  23.97847  50.54660  1.000 221.44488 ? 3   VAL E N   1 
ATOM   7612 C CA  . VAL E 5 23  ? 16.58127  24.96892  51.20495  1.000 224.13971 ? 3   VAL E CA  1 
ATOM   7613 C C   . VAL E 5 23  ? 17.05164  26.35723  50.79346  1.000 224.17008 ? 3   VAL E C   1 
ATOM   7614 O O   . VAL E 5 23  ? 18.25089  26.65784  50.85301  1.000 226.42141 ? 3   VAL E O   1 
ATOM   7615 C CB  . VAL E 5 23  ? 16.61308  24.80097  52.73446  1.000 230.69310 ? 3   VAL E CB  1 
ATOM   7616 C CG1 . VAL E 5 23  ? 16.06159  26.04215  53.42749  1.000 234.71316 ? 3   VAL E CG1 1 
ATOM   7617 C CG2 . VAL E 5 23  ? 15.82080  23.57128  53.14517  1.000 230.04460 ? 3   VAL E CG2 1 
ATOM   7618 N N   . MET E 5 24  ? 16.11307  27.20283  50.37419  1.000 225.97906 ? 4   MET E N   1 
ATOM   7619 C CA  . MET E 5 24  ? 16.41543  28.54941  49.89043  1.000 225.45939 ? 4   MET E CA  1 
ATOM   7620 C C   . MET E 5 24  ? 15.87350  29.56359  50.89493  1.000 229.20124 ? 4   MET E C   1 
ATOM   7621 O O   . MET E 5 24  ? 14.76493  30.08238  50.75607  1.000 227.45321 ? 4   MET E O   1 
ATOM   7622 C CB  . MET E 5 24  ? 15.83231  28.76631  48.49226  1.000 219.56789 ? 4   MET E CB  1 
ATOM   7623 C CG  . MET E 5 24  ? 16.42186  27.84682  47.43851  1.000 216.00599 ? 4   MET E CG  1 
ATOM   7624 S SD  . MET E 5 24  ? 18.22441  27.83692  47.48675  1.000 218.86966 ? 4   MET E SD  1 
ATOM   7625 C CE  . MET E 5 24  ? 18.58976  29.55220  47.12869  1.000 219.58100 ? 4   MET E CE  1 
ATOM   7626 N N   . SER E 5 25  ? 16.67719  29.84651  51.91789  1.000 231.46269 ? 5   SER E N   1 
ATOM   7627 C CA  . SER E 5 25  ? 16.32280  30.84265  52.92424  1.000 235.44510 ? 5   SER E CA  1 
ATOM   7628 C C   . SER E 5 25  ? 16.43125  32.23679  52.31653  1.000 232.99858 ? 5   SER E C   1 
ATOM   7629 O O   . SER E 5 25  ? 17.52671  32.68862  51.96758  1.000 232.88457 ? 5   SER E O   1 
ATOM   7630 C CB  . SER E 5 25  ? 17.22717  30.69892  54.14455  1.000 241.78919 ? 5   SER E CB  1 
ATOM   7631 O OG  . SER E 5 25  ? 18.58844  30.60650  53.76213  1.000 241.62835 ? 5   SER E OG  1 
ATOM   7632 N N   . GLN E 5 26  ? 15.29567  32.92158  52.19208  1.000 243.18238 ? 6   GLN E N   1 
ATOM   7633 C CA  . GLN E 5 26  ? 15.22072  34.22225  51.53637  1.000 240.73713 ? 6   GLN E CA  1 
ATOM   7634 C C   . GLN E 5 26  ? 14.52553  35.20539  52.46556  1.000 243.53975 ? 6   GLN E C   1 
ATOM   7635 O O   . GLN E 5 26  ? 13.34749  35.02650  52.79146  1.000 244.06310 ? 6   GLN E O   1 
ATOM   7636 C CB  . GLN E 5 26  ? 14.47307  34.11594  50.20345  1.000 234.95611 ? 6   GLN E CB  1 
ATOM   7637 C CG  . GLN E 5 26  ? 14.24306  35.43770  49.49154  1.000 232.22482 ? 6   GLN E CG  1 
ATOM   7638 C CD  . GLN E 5 26  ? 13.37534  35.28056  48.25678  1.000 226.99724 ? 6   GLN E CD  1 
ATOM   7639 O OE1 . GLN E 5 26  ? 12.82439  34.20881  48.00498  1.000 225.18570 ? 6   GLN E OE1 1 
ATOM   7640 N NE2 . GLN E 5 26  ? 13.25083  36.34898  47.47897  1.000 224.70101 ? 6   GLN E NE2 1 
ATOM   7641 N N   . SER E 5 27  ? 15.24937  36.23862  52.88538  1.000 241.70050 ? 7   SER E N   1 
ATOM   7642 C CA  . SER E 5 27  ? 14.73277  37.25842  53.78305  1.000 245.01431 ? 7   SER E CA  1 
ATOM   7643 C C   . SER E 5 27  ? 14.92936  38.63474  53.16598  1.000 243.05485 ? 7   SER E C   1 
ATOM   7644 O O   . SER E 5 27  ? 15.87008  38.84095  52.39254  1.000 241.49232 ? 7   SER E O   1 
ATOM   7645 C CB  . SER E 5 27  ? 15.43581  37.20106  55.14825  1.000 251.53492 ? 7   SER E CB  1 
ATOM   7646 O OG  . SER E 5 27  ? 16.76780  37.67523  55.05656  1.000 252.36956 ? 7   SER E OG  1 
ATOM   7647 N N   . PRO E 5 28  ? 14.05743  39.60529  53.49150  1.000 244.97728 ? 8   PRO E N   1 
ATOM   7648 C CA  . PRO E 5 28  ? 12.90363  39.49840  54.39147  1.000 247.61582 ? 8   PRO E CA  1 
ATOM   7649 C C   . PRO E 5 28  ? 11.63798  39.01348  53.68954  1.000 243.64382 ? 8   PRO E C   1 
ATOM   7650 O O   . PRO E 5 28  ? 11.54082  39.10568  52.46775  1.000 238.27857 ? 8   PRO E O   1 
ATOM   7651 C CB  . PRO E 5 28  ? 12.72814  40.93263  54.88522  1.000 249.67878 ? 8   PRO E CB  1 
ATOM   7652 C CG  . PRO E 5 28  ? 13.14158  41.75618  53.71377  1.000 245.58829 ? 8   PRO E CG  1 
ATOM   7653 C CD  . PRO E 5 28  ? 14.25134  40.99048  53.02457  1.000 244.07935 ? 8   PRO E CD  1 
ATOM   7654 N N   . SER E 5 29  ? 10.67498  38.50520  54.46234  1.000 247.20841 ? 9   SER E N   1 
ATOM   7655 C CA  . SER E 5 29  ? 9.42098   38.05409  53.86793  1.000 244.40186 ? 9   SER E CA  1 
ATOM   7656 C C   . SER E 5 29  ? 8.55009   39.22647  53.43371  1.000 241.88069 ? 9   SER E C   1 
ATOM   7657 O O   . SER E 5 29  ? 7.79702   39.10962  52.46033  1.000 237.07938 ? 9   SER E O   1 
ATOM   7658 C CB  . SER E 5 29  ? 8.66248   37.16063  54.84977  1.000 250.17464 ? 9   SER E CB  1 
ATOM   7659 O OG  . SER E 5 29  ? 9.34990   35.94000  55.06559  1.000 251.82971 ? 9   SER E OG  1 
ATOM   7660 N N   . SER E 5 30  ? 8.63575   40.35436  54.13516  1.000 243.28131 ? 10  SER E N   1 
ATOM   7661 C CA  . SER E 5 30  ? 7.90153   41.56008  53.78383  1.000 240.90911 ? 10  SER E CA  1 
ATOM   7662 C C   . SER E 5 30  ? 8.87120   42.72946  53.70458  1.000 240.10720 ? 10  SER E C   1 
ATOM   7663 O O   . SER E 5 30  ? 9.88633   42.76070  54.40557  1.000 243.55758 ? 10  SER E O   1 
ATOM   7664 C CB  . SER E 5 30  ? 6.79289   41.86302  54.80065  1.000 245.50404 ? 10  SER E CB  1 
ATOM   7665 O OG  . SER E 5 30  ? 7.32616   42.02442  56.10352  1.000 251.41356 ? 10  SER E OG  1 
ATOM   7666 N N   . LEU E 5 31  ? 8.55132   43.69628  52.84600  1.000 237.06330 ? 11  LEU E N   1 
ATOM   7667 C CA  . LEU E 5 31  ? 9.45656   44.81612  52.62271  1.000 237.02058 ? 11  LEU E CA  1 
ATOM   7668 C C   . LEU E 5 31  ? 8.67480   46.00342  52.08185  1.000 234.38562 ? 11  LEU E C   1 
ATOM   7669 O O   . LEU E 5 31  ? 7.85254   45.84480  51.17436  1.000 230.05521 ? 11  LEU E O   1 
ATOM   7670 C CB  . LEU E 5 31  ? 10.57608  44.41726  51.65589  1.000 235.10212 ? 11  LEU E CB  1 
ATOM   7671 C CG  . LEU E 5 31  ? 11.81358  45.31096  51.61538  1.000 236.66742 ? 11  LEU E CG  1 
ATOM   7672 C CD1 . LEU E 5 31  ? 12.15112  45.82984  53.00272  1.000 241.39184 ? 11  LEU E CD1 1 
ATOM   7673 C CD2 . LEU E 5 31  ? 12.97765  44.52325  51.05232  1.000 236.17905 ? 11  LEU E CD2 1 
ATOM   7674 N N   . ALA E 5 32  ? 8.93702   47.18588  52.63885  1.000 232.21251 ? 12  ALA E N   1 
ATOM   7675 C CA  . ALA E 5 32  ? 8.28117   48.42227  52.22740  1.000 230.11985 ? 12  ALA E CA  1 
ATOM   7676 C C   . ALA E 5 32  ? 9.34331   49.47935  51.96619  1.000 229.81488 ? 12  ALA E C   1 
ATOM   7677 O O   . ALA E 5 32  ? 10.15205  49.77805  52.85032  1.000 233.38684 ? 12  ALA E O   1 
ATOM   7678 C CB  . ALA E 5 32  ? 7.29101   48.90462  53.29141  1.000 232.32917 ? 12  ALA E CB  1 
ATOM   7679 N N   . VAL E 5 33  ? 9.34348   50.04374  50.75623  1.000 232.81491 ? 13  VAL E N   1 
ATOM   7680 C CA  . VAL E 5 33  ? 10.32955  51.03669  50.34444  1.000 233.37037 ? 13  VAL E CA  1 
ATOM   7681 C C   . VAL E 5 33  ? 9.61063   52.20866  49.68452  1.000 230.65347 ? 13  VAL E C   1 
ATOM   7682 O O   . VAL E 5 33  ? 8.42394   52.14224  49.36794  1.000 228.01114 ? 13  VAL E O   1 
ATOM   7683 C CB  . VAL E 5 33  ? 11.38825  50.45188  49.38649  1.000 232.55668 ? 13  VAL E CB  1 
ATOM   7684 C CG1 . VAL E 5 33  ? 12.00223  49.18608  49.96540  1.000 234.78165 ? 13  VAL E CG1 1 
ATOM   7685 C CG2 . VAL E 5 33  ? 10.77556  50.18548  48.02081  1.000 228.43416 ? 13  VAL E CG2 1 
ATOM   7686 N N   . SER E 5 34  ? 10.35377  53.28981  49.47328  1.000 226.60018 ? 14  SER E N   1 
ATOM   7687 C CA  . SER E 5 34  ? 9.83325   54.48016  48.81713  1.000 224.61505 ? 14  SER E CA  1 
ATOM   7688 C C   . SER E 5 34  ? 10.22180  54.48385  47.34010  1.000 222.33200 ? 14  SER E C   1 
ATOM   7689 O O   . SER E 5 34  ? 10.95685  53.62004  46.85771  1.000 222.47336 ? 14  SER E O   1 
ATOM   7690 C CB  . SER E 5 34  ? 10.34014  55.74696  49.51356  1.000 227.41325 ? 14  SER E CB  1 
ATOM   7691 O OG  . SER E 5 34  ? 9.85965   55.82113  50.84628  1.000 229.76290 ? 14  SER E OG  1 
ATOM   7692 N N   . VAL E 5 35  ? 9.71524   55.47882  46.62254  1.000 209.01051 ? 15  VAL E N   1 
ATOM   7693 C CA  . VAL E 5 35  ? 9.89496   55.56693  45.17923  1.000 207.29772 ? 15  VAL E CA  1 
ATOM   7694 C C   . VAL E 5 35  ? 11.21221  56.26667  44.87760  1.000 210.12015 ? 15  VAL E C   1 
ATOM   7695 O O   . VAL E 5 35  ? 11.46597  57.37540  45.35973  1.000 213.11770 ? 15  VAL E O   1 
ATOM   7696 C CB  . VAL E 5 35  ? 8.71732   56.30636  44.52239  1.000 205.85291 ? 15  VAL E CB  1 
ATOM   7697 C CG1 . VAL E 5 35  ? 8.89122   56.36508  43.01725  1.000 204.22076 ? 15  VAL E CG1 1 
ATOM   7698 C CG2 . VAL E 5 35  ? 7.39972   55.64136  44.89037  1.000 203.44161 ? 15  VAL E CG2 1 
ATOM   7699 N N   . GLY E 5 36  ? 12.04721  55.62118  44.07003  1.000 217.63051 ? 16  GLY E N   1 
ATOM   7700 C CA  . GLY E 5 36  ? 13.28343  56.22537  43.61621  1.000 220.24315 ? 16  GLY E CA  1 
ATOM   7701 C C   . GLY E 5 36  ? 14.51059  55.88760  44.43152  1.000 222.95962 ? 16  GLY E C   1 
ATOM   7702 O O   . GLY E 5 36  ? 15.44660  56.69429  44.47872  1.000 226.23688 ? 16  GLY E O   1 
ATOM   7703 N N   . GLU E 5 37  ? 14.55039  54.71391  45.05882  1.000 238.75006 ? 17  GLU E N   1 
ATOM   7704 C CA  . GLU E 5 37  ? 15.65907  54.36163  45.93480  1.000 242.17980 ? 17  GLU E CA  1 
ATOM   7705 C C   . GLU E 5 37  ? 16.28262  53.02605  45.54330  1.000 242.45960 ? 17  GLU E C   1 
ATOM   7706 O O   . GLU E 5 37  ? 15.92190  52.43740  44.51892  1.000 240.30861 ? 17  GLU E O   1 
ATOM   7707 C CB  . GLU E 5 37  ? 15.18701  54.30427  47.38862  1.000 242.46004 ? 17  GLU E CB  1 
ATOM   7708 C CG  . GLU E 5 37  ? 14.12998  53.24028  47.63184  1.000 239.64337 ? 17  GLU E CG  1 
ATOM   7709 C CD  . GLU E 5 37  ? 14.14312  52.71615  49.05223  1.000 241.80026 ? 17  GLU E CD  1 
ATOM   7710 O OE1 . GLU E 5 37  ? 13.65118  53.42202  49.95788  1.000 242.90243 ? 17  GLU E OE1 1 
ATOM   7711 O OE2 . GLU E 5 37  ? 14.65766  51.59772  49.26350  1.000 242.72142 ? 17  GLU E OE2 1 
ATOM   7712 N N   . LYS E 5 38  ? 17.21439  52.54529  46.36043  1.000 248.18813 ? 18  LYS E N   1 
ATOM   7713 C CA  . LYS E 5 38  ? 17.83584  51.24261  46.18783  1.000 248.77947 ? 18  LYS E CA  1 
ATOM   7714 C C   . LYS E 5 38  ? 17.38916  50.31736  47.31023  1.000 248.10325 ? 18  LYS E C   1 
ATOM   7715 O O   . LYS E 5 38  ? 17.37138  50.71238  48.48040  1.000 249.72165 ? 18  LYS E O   1 
ATOM   7716 C CB  . LYS E 5 38  ? 19.36341  51.35158  46.19388  1.000 253.02962 ? 18  LYS E CB  1 
ATOM   7717 C CG  . LYS E 5 38  ? 19.94443  52.34280  45.20182  1.000 255.19734 ? 18  LYS E CG  1 
ATOM   7718 C CD  . LYS E 5 38  ? 21.41616  52.58103  45.49763  1.000 260.09819 ? 18  LYS E CD  1 
ATOM   7719 C CE  . LYS E 5 38  ? 21.97696  53.70815  44.65359  1.000 263.10128 ? 18  LYS E CE  1 
ATOM   7720 N NZ  . LYS E 5 38  ? 23.30424  54.15839  45.15550  1.000 267.79212 ? 18  LYS E NZ  1 
ATOM   7721 N N   . VAL E 5 39  ? 17.03120  49.08747  46.95340  1.000 238.31424 ? 19  VAL E N   1 
ATOM   7722 C CA  . VAL E 5 39  ? 16.66750  48.06370  47.92398  1.000 238.21407 ? 19  VAL E CA  1 
ATOM   7723 C C   . VAL E 5 39  ? 17.40869  46.78412  47.56267  1.000 238.92173 ? 19  VAL E C   1 
ATOM   7724 O O   . VAL E 5 39  ? 17.59122  46.47123  46.38033  1.000 237.78782 ? 19  VAL E O   1 
ATOM   7725 C CB  . VAL E 5 39  ? 15.13989  47.83970  47.98120  1.000 234.99793 ? 19  VAL E CB  1 
ATOM   7726 C CG1 . VAL E 5 39  ? 14.61272  47.28575  46.66526  1.000 232.17081 ? 19  VAL E CG1 1 
ATOM   7727 C CG2 . VAL E 5 39  ? 14.77671  46.93419  49.14577  1.000 235.17726 ? 19  VAL E CG2 1 
ATOM   7728 N N   . THR E 5 40  ? 17.85712  46.05821  48.58125  1.000 241.04803 ? 20  THR E N   1 
ATOM   7729 C CA  . THR E 5 40  ? 18.75407  44.91875  48.40574  1.000 242.31755 ? 20  THR E CA  1 
ATOM   7730 C C   . THR E 5 40  ? 18.01694  43.62733  48.74619  1.000 240.73366 ? 20  THR E C   1 
ATOM   7731 O O   . THR E 5 40  ? 17.92814  43.24078  49.91528  1.000 242.71961 ? 20  THR E O   1 
ATOM   7732 C CB  . THR E 5 40  ? 19.99937  45.08537  49.27083  1.000 246.33406 ? 20  THR E CB  1 
ATOM   7733 O OG1 . THR E 5 40  ? 19.61028  45.24217  50.64093  1.000 247.91346 ? 20  THR E OG1 1 
ATOM   7734 C CG2 . THR E 5 40  ? 20.79099  46.31186  48.83604  1.000 248.01145 ? 20  THR E CG2 1 
ATOM   7735 N N   . MET E 5 41  ? 17.49493  42.95906  47.71943  1.000 240.90010 ? 21  MET E N   1 
ATOM   7736 C CA  . MET E 5 41  ? 16.93066  41.62792  47.90116  1.000 239.25743 ? 21  MET E CA  1 
ATOM   7737 C C   . MET E 5 41  ? 18.01616  40.67329  48.37898  1.000 241.34882 ? 21  MET E C   1 
ATOM   7738 O O   . MET E 5 41  ? 19.10777  40.63365  47.81071  1.000 242.66978 ? 21  MET E O   1 
ATOM   7739 C CB  . MET E 5 41  ? 16.33422  41.12186  46.58653  1.000 234.49864 ? 21  MET E CB  1 
ATOM   7740 C CG  . MET E 5 41  ? 15.30700  42.03872  45.94127  1.000 231.38045 ? 21  MET E CG  1 
ATOM   7741 S SD  . MET E 5 41  ? 13.75513  42.11425  46.85288  1.000 230.83530 ? 21  MET E SD  1 
ATOM   7742 C CE  . MET E 5 41  ? 13.92579  43.69495  47.67248  1.000 234.17264 ? 21  MET E CE  1 
ATOM   7743 N N   . SER E 5 42  ? 17.72164  39.90091  49.42092  1.000 240.67696 ? 22  SER E N   1 
ATOM   7744 C CA  . SER E 5 42  ? 18.69806  38.99475  50.00989  1.000 243.07131 ? 22  SER E CA  1 
ATOM   7745 C C   . SER E 5 42  ? 18.17871  37.56447  49.97565  1.000 240.88430 ? 22  SER E C   1 
ATOM   7746 O O   . SER E 5 42  ? 17.00521  37.31036  50.26565  1.000 239.62793 ? 22  SER E O   1 
ATOM   7747 C CB  . SER E 5 42  ? 19.03035  39.39757  51.45180  1.000 248.03821 ? 22  SER E CB  1 
ATOM   7748 O OG  . SER E 5 42  ? 20.08010  38.60308  51.97755  1.000 251.17045 ? 22  SER E OG  1 
ATOM   7749 N N   . CYS E 5 43  ? 19.06219  36.63482  49.61786  1.000 243.19639 ? 23  CYS E N   1 
ATOM   7750 C CA  . CYS E 5 43  ? 18.72944  35.21901  49.58034  1.000 241.47566 ? 23  CYS E CA  1 
ATOM   7751 C C   . CYS E 5 43  ? 19.99868  34.40840  49.78789  1.000 243.74201 ? 23  CYS E C   1 
ATOM   7752 O O   . CYS E 5 43  ? 21.04884  34.73458  49.22819  1.000 244.25721 ? 23  CYS E O   1 
ATOM   7753 C CB  . CYS E 5 43  ? 18.07133  34.82780  48.25483  1.000 236.63030 ? 23  CYS E CB  1 
ATOM   7754 S SG  . CYS E 5 43  ? 17.65206  33.07688  48.13753  1.000 234.34060 ? 23  CYS E SG  1 
ATOM   7755 N N   . LYS E 5 44  ? 19.89282  33.34977  50.58757  1.000 232.90506 ? 24  LYS E N   1 
ATOM   7756 C CA  . LYS E 5 44  ? 21.02163  32.48264  50.88941  1.000 235.41878 ? 24  LYS E CA  1 
ATOM   7757 C C   . LYS E 5 44  ? 20.60383  31.02746  50.73819  1.000 233.48774 ? 24  LYS E C   1 
ATOM   7758 O O   . LYS E 5 44  ? 19.51615  30.63614  51.17181  1.000 233.11672 ? 24  LYS E O   1 
ATOM   7759 C CB  . LYS E 5 44  ? 21.55474  32.73773  52.30492  1.000 240.85817 ? 24  LYS E CB  1 
ATOM   7760 C CG  . LYS E 5 44  ? 22.86117  32.02617  52.61292  1.000 243.67423 ? 24  LYS E CG  1 
ATOM   7761 C CD  . LYS E 5 44  ? 23.50305  32.58020  53.87330  1.000 249.19501 ? 24  LYS E CD  1 
ATOM   7762 C CE  . LYS E 5 44  ? 24.87937  31.97971  54.10256  1.000 251.99584 ? 24  LYS E CE  1 
ATOM   7763 N NZ  . LYS E 5 44  ? 25.62058  32.69153  55.18043  1.000 256.84675 ? 24  LYS E NZ  1 
ATOM   7764 N N   . SER E 5 45  ? 21.47248  30.23215  50.12188  1.000 236.83790 ? 25  SER E N   1 
ATOM   7765 C CA  . SER E 5 45  ? 21.20172  28.82474  49.87359  1.000 234.90253 ? 25  SER E CA  1 
ATOM   7766 C C   . SER E 5 45  ? 21.74939  27.95863  51.00421  1.000 239.64051 ? 25  SER E C   1 
ATOM   7767 O O   . SER E 5 45  ? 22.62166  28.37064  51.77248  1.000 243.62356 ? 25  SER E O   1 
ATOM   7768 C CB  . SER E 5 45  ? 21.80989  28.38801  48.53967  1.000 231.26191 ? 25  SER E CB  1 
ATOM   7769 O OG  . SER E 5 45  ? 21.61150  27.00292  48.31544  1.000 229.43952 ? 25  SER E OG  1 
ATOM   7770 N N   . SER E 5 46  ? 21.21878  26.73640  51.09603  1.000 236.68677 ? 26  SER E N   1 
ATOM   7771 C CA  . SER E 5 46  ? 21.69334  25.80357  52.11327  1.000 241.14963 ? 26  SER E CA  1 
ATOM   7772 C C   . SER E 5 46  ? 23.08002  25.27516  51.76975  1.000 241.44766 ? 26  SER E C   1 
ATOM   7773 O O   . SER E 5 46  ? 23.95168  25.18738  52.64244  1.000 245.77321 ? 26  SER E O   1 
ATOM   7774 C CB  . SER E 5 46  ? 20.70457  24.64917  52.27328  1.000 239.26130 ? 26  SER E CB  1 
ATOM   7775 O OG  . SER E 5 46  ? 20.68137  23.83409  51.11452  1.000 234.16586 ? 26  SER E OG  1 
ATOM   7776 N N   . GLN E 5 47  ? 23.30081  24.91696  50.50827  1.000 248.00263 ? 27  GLN E N   1 
ATOM   7777 C CA  . GLN E 5 47  ? 24.59423  24.45955  50.02960  1.000 247.90522 ? 27  GLN E CA  1 
ATOM   7778 C C   . GLN E 5 47  ? 25.13707  25.45441  49.01175  1.000 245.97780 ? 27  GLN E C   1 
ATOM   7779 O O   . GLN E 5 47  ? 24.40614  26.30019  48.48849  1.000 243.72973 ? 27  GLN E O   1 
ATOM   7780 C CB  . GLN E 5 47  ? 24.49595  23.06324  49.39818  1.000 244.94203 ? 27  GLN E CB  1 
ATOM   7781 C CG  . GLN E 5 47  ? 23.46137  22.15047  50.04401  1.000 244.25502 ? 27  GLN E CG  1 
ATOM   7782 C CD  . GLN E 5 47  ? 23.80534  21.77933  51.47417  1.000 248.79451 ? 27  GLN E CD  1 
ATOM   7783 O OE1 . GLN E 5 47  ? 24.97324  21.76882  51.86347  1.000 252.45659 ? 27  GLN E OE1 1 
ATOM   7784 N NE2 . GLN E 5 47  ? 22.78396  21.47089  52.26578  1.000 248.60232 ? 27  GLN E NE2 1 
ATOM   7785 N N   . SER E 5 48  ? 26.43384  25.34489  48.73510  1.000 236.87037 ? 28  SER E N   1 
ATOM   7786 C CA  . SER E 5 48  ? 27.06725  26.22432  47.76537  1.000 236.30555 ? 28  SER E CA  1 
ATOM   7787 C C   . SER E 5 48  ? 26.53150  25.95452  46.36176  1.000 231.80618 ? 28  SER E C   1 
ATOM   7788 O O   . SER E 5 48  ? 26.02532  24.87154  46.05477  1.000 229.06562 ? 28  SER E O   1 
ATOM   7789 C CB  . SER E 5 48  ? 28.58505  26.04652  47.78698  1.000 238.99748 ? 28  SER E CB  1 
ATOM   7790 O OG  . SER E 5 48  ? 29.19829  26.79703  46.75299  1.000 238.90488 ? 28  SER E OG  1 
ATOM   7791 N N   . LEU E 5 49  ? 26.65004  26.96443  45.50311  1.000 230.23125 ? 29  LEU E N   1 
ATOM   7792 C CA  . LEU E 5 49  ? 26.17692  26.89554  44.12573  1.000 226.70804 ? 29  LEU E CA  1 
ATOM   7793 C C   . LEU E 5 49  ? 27.24913  27.38415  43.16309  1.000 228.65133 ? 29  LEU E C   1 
ATOM   7794 O O   . LEU E 5 49  ? 26.96089  28.09589  42.19840  1.000 227.99560 ? 29  LEU E O   1 
ATOM   7795 C CB  . LEU E 5 49  ? 24.89750  27.71009  43.93913  1.000 224.28708 ? 29  LEU E CB  1 
ATOM   7796 C CG  . LEU E 5 49  ? 23.79552  27.66411  45.00145  1.000 223.68839 ? 29  LEU E CG  1 
ATOM   7797 C CD1 . LEU E 5 49  ? 22.68648  28.64463  44.64801  1.000 221.36709 ? 29  LEU E CD1 1 
ATOM   7798 C CD2 . LEU E 5 49  ? 23.23320  26.26229  45.16951  1.000 221.51329 ? 29  LEU E CD2 1 
ATOM   7799 N N   . PHE E 5 50  ? 28.50485  27.00949  43.39876  1.000 226.87912 ? 30  PHE E N   1 
ATOM   7800 C CA  . PHE E 5 50  ? 29.62956  27.53348  42.62409  1.000 230.13849 ? 30  PHE E CA  1 
ATOM   7801 C C   . PHE E 5 50  ? 30.48341  26.37283  42.12131  1.000 229.88710 ? 30  PHE E C   1 
ATOM   7802 O O   . PHE E 5 50  ? 31.24470  25.77572  42.88829  1.000 231.43790 ? 30  PHE E O   1 
ATOM   7803 C CB  . PHE E 5 50  ? 30.45461  28.50695  43.46162  1.000 235.06333 ? 30  PHE E CB  1 
ATOM   7804 C CG  . PHE E 5 50  ? 31.46947  29.28412  42.67082  1.000 239.19319 ? 30  PHE E CG  1 
ATOM   7805 C CD1 . PHE E 5 50  ? 31.08508  30.37349  41.90597  1.000 239.97863 ? 30  PHE E CD1 1 
ATOM   7806 C CD2 . PHE E 5 50  ? 32.80927  28.93490  42.70408  1.000 242.99546 ? 30  PHE E CD2 1 
ATOM   7807 C CE1 . PHE E 5 50  ? 32.01659  31.09405  41.18193  1.000 244.77672 ? 30  PHE E CE1 1 
ATOM   7808 C CE2 . PHE E 5 50  ? 33.74566  29.65163  41.98250  1.000 247.75240 ? 30  PHE E CE2 1 
ATOM   7809 C CZ  . PHE E 5 50  ? 33.34867  30.73294  41.22142  1.000 248.88323 ? 30  PHE E CZ  1 
ATOM   7810 N N   . TYR E 5 51  ? 30.34976  26.05643  40.83464  1.000 237.33469 ? 31  TYR E N   1 
ATOM   7811 C CA  . TYR E 5 51  ? 31.23818  25.09397  40.19808  1.000 237.39809 ? 31  TYR E CA  1 
ATOM   7812 C C   . TYR E 5 51  ? 32.68550  25.56586  40.29002  1.000 242.82289 ? 31  TYR E C   1 
ATOM   7813 O O   . TYR E 5 51  ? 32.97152  26.76628  40.30215  1.000 246.73097 ? 31  TYR E O   1 
ATOM   7814 C CB  . TYR E 5 51  ? 30.86354  24.91507  38.72958  1.000 235.51853 ? 31  TYR E CB  1 
ATOM   7815 C CG  . TYR E 5 51  ? 29.91849  23.78185  38.39645  1.000 229.97438 ? 31  TYR E CG  1 
ATOM   7816 C CD1 . TYR E 5 51  ? 28.80651  23.51586  39.17955  1.000 226.54244 ? 31  TYR E CD1 1 
ATOM   7817 C CD2 . TYR E 5 51  ? 30.12421  23.00061  37.26567  1.000 228.50658 ? 31  TYR E CD2 1 
ATOM   7818 C CE1 . TYR E 5 51  ? 27.93683  22.48731  38.86093  1.000 221.94581 ? 31  TYR E CE1 1 
ATOM   7819 C CE2 . TYR E 5 51  ? 29.26172  21.97283  36.93811  1.000 223.52470 ? 31  TYR E CE2 1 
ATOM   7820 C CZ  . TYR E 5 51  ? 28.16953  21.72117  37.73952  1.000 220.26720 ? 31  TYR E CZ  1 
ATOM   7821 O OH  . TYR E 5 51  ? 27.30472  20.70047  37.42216  1.000 215.48934 ? 31  TYR E OH  1 
ATOM   7822 N N   . SER E 5 52  ? 33.60914  24.60324  40.33611  1.000 235.16112 ? 32  SER E N   1 
ATOM   7823 C CA  . SER E 5 52  ? 35.02800  24.94496  40.38520  1.000 240.63120 ? 32  SER E CA  1 
ATOM   7824 C C   . SER E 5 52  ? 35.53019  25.40783  39.02119  1.000 243.83384 ? 32  SER E C   1 
ATOM   7825 O O   . SER E 5 52  ? 36.14384  26.47545  38.90371  1.000 249.09057 ? 32  SER E O   1 
ATOM   7826 C CB  . SER E 5 52  ? 35.84135  23.74844  40.88224  1.000 240.20593 ? 32  SER E CB  1 
ATOM   7827 O OG  . SER E 5 52  ? 35.41004  23.32920  42.16586  1.000 238.48251 ? 32  SER E OG  1 
ATOM   7828 N N   . SER E 5 53  ? 35.27796  24.61588  37.97529  1.000 242.75216 ? 33  SER E N   1 
ATOM   7829 C CA  . SER E 5 53  ? 35.74348  24.97244  36.63834  1.000 246.34356 ? 33  SER E CA  1 
ATOM   7830 C C   . SER E 5 53  ? 34.83178  26.00445  35.98261  1.000 246.83207 ? 33  SER E C   1 
ATOM   7831 O O   . SER E 5 53  ? 35.31373  26.98167  35.40069  1.000 252.27699 ? 33  SER E O   1 
ATOM   7832 C CB  . SER E 5 53  ? 35.84078  23.72358  35.76098  1.000 243.53557 ? 33  SER E CB  1 
ATOM   7833 O OG  . SER E 5 53  ? 34.55261  23.20540  35.48078  1.000 241.47382 ? 33  SER E OG  1 
ATOM   7834 N N   . ASN E 5 54  ? 33.51247  25.79425  36.05659  1.000 241.56553 ? 34  ASN E N   1 
ATOM   7835 C CA  . ASN E 5 54  ? 32.56363  26.71297  35.42773  1.000 241.65481 ? 34  ASN E CA  1 
ATOM   7836 C C   . ASN E 5 54  ? 32.75043  28.13779  35.93846  1.000 246.01669 ? 34  ASN E C   1 
ATOM   7837 O O   . ASN E 5 54  ? 32.61635  29.09954  35.17305  1.000 249.36193 ? 34  ASN E O   1 
ATOM   7838 C CB  . ASN E 5 54  ? 31.13343  26.22717  35.68740  1.000 235.02105 ? 34  ASN E CB  1 
ATOM   7839 C CG  . ASN E 5 54  ? 30.08701  26.90172  34.80518  1.000 233.76681 ? 34  ASN E CG  1 
ATOM   7840 O OD1 . ASN E 5 54  ? 29.00428  26.34848  34.59874  1.000 233.76553 ? 34  ASN E OD1 1 
ATOM   7841 N ND2 . ASN E 5 54  ? 30.39557  28.08546  34.28536  1.000 233.33288 ? 34  ASN E ND2 1 
ATOM   7842 N N   . GLN E 5 55  ? 33.05436  28.28998  37.22828  1.000 236.14546 ? 35  GLN E N   1 
ATOM   7843 C CA  . GLN E 5 55  ? 33.26534  29.59862  37.85136  1.000 240.01596 ? 35  GLN E CA  1 
ATOM   7844 C C   . GLN E 5 55  ? 32.03365  30.49102  37.72657  1.000 237.85318 ? 35  GLN E C   1 
ATOM   7845 O O   . GLN E 5 55  ? 32.14912  31.70162  37.53570  1.000 241.77674 ? 35  GLN E O   1 
ATOM   7846 C CB  . GLN E 5 55  ? 34.49723  30.31148  37.28044  1.000 247.43614 ? 35  GLN E CB  1 
ATOM   7847 C CG  . GLN E 5 55  ? 35.80769  29.92668  37.94772  1.000 252.27175 ? 35  GLN E CG  1 
ATOM   7848 C CD  . GLN E 5 55  ? 36.79313  31.07086  37.95602  1.000 258.97013 ? 35  GLN E CD  1 
ATOM   7849 O OE1 . GLN E 5 55  ? 37.55226  31.25781  37.00722  1.000 263.22881 ? 35  GLN E OE1 1 
ATOM   7850 N NE2 . GLN E 5 55  ? 36.77046  31.86141  39.02176  1.000 259.40501 ? 35  GLN E NE2 1 
ATOM   7851 N N   . LYS E 5 56  ? 30.84567  29.89744  37.83795  1.000 233.13070 ? 36  LYS E N   1 
ATOM   7852 C CA  . LYS E 5 56  ? 29.59871  30.64918  37.80121  1.000 230.26954 ? 36  LYS E CA  1 
ATOM   7853 C C   . LYS E 5 56  ? 28.64256  30.07602  38.83781  1.000 225.25114 ? 36  LYS E C   1 
ATOM   7854 O O   . LYS E 5 56  ? 28.82921  28.96328  39.33609  1.000 223.26995 ? 36  LYS E O   1 
ATOM   7855 C CB  . LYS E 5 56  ? 28.96017  30.62780  36.40230  1.000 228.84729 ? 36  LYS E CB  1 
ATOM   7856 C CG  . LYS E 5 56  ? 29.84893  31.21201  35.30957  1.000 234.49043 ? 36  LYS E CG  1 
ATOM   7857 C CD  . LYS E 5 56  ? 29.04987  31.80923  34.16393  1.000 234.87316 ? 36  LYS E CD  1 
ATOM   7858 C CE  . LYS E 5 56  ? 28.36642  30.74101  33.33014  1.000 231.20130 ? 36  LYS E CE  1 
ATOM   7859 N NZ  . LYS E 5 56  ? 27.64334  31.34400  32.17577  1.000 231.94764 ? 36  LYS E NZ  1 
ATOM   7860 N N   . ASN E 5 57  ? 27.61322  30.85342  39.16454  1.000 232.78612 ? 37  ASN E N   1 
ATOM   7861 C CA  . ASN E 5 57  ? 26.63353  30.47077  40.17168  1.000 228.95383 ? 37  ASN E CA  1 
ATOM   7862 C C   . ASN E 5 57  ? 25.29426  30.15443  39.51917  1.000 223.78700 ? 37  ASN E C   1 
ATOM   7863 O O   . ASN E 5 57  ? 24.90451  30.78934  38.53533  1.000 223.52528 ? 37  ASN E O   1 
ATOM   7864 C CB  . ASN E 5 57  ? 26.46324  31.57118  41.22159  1.000 230.71027 ? 37  ASN E CB  1 
ATOM   7865 C CG  . ASN E 5 57  ? 27.60694  31.60648  42.21773  1.000 234.43423 ? 37  ASN E CG  1 
ATOM   7866 O OD1 . ASN E 5 57  ? 27.64016  30.82467  43.16797  1.000 233.70728 ? 37  ASN E OD1 1 
ATOM   7867 N ND2 . ASN E 5 57  ? 28.54994  32.51709  42.00671  1.000 239.11040 ? 37  ASN E ND2 1 
ATOM   7868 N N   . TYR E 5 58  ? 24.59175  29.17197  40.07711  1.000 221.68925 ? 38  TYR E N   1 
ATOM   7869 C CA  . TYR E 5 58  ? 23.35224  28.66928  39.48687  1.000 216.59551 ? 38  TYR E CA  1 
ATOM   7870 C C   . TYR E 5 58  ? 22.15072  29.17785  40.28312  1.000 214.58115 ? 38  TYR E C   1 
ATOM   7871 O O   . TYR E 5 58  ? 21.44368  28.42564  40.95359  1.000 212.01534 ? 38  TYR E O   1 
ATOM   7872 C CB  . TYR E 5 58  ? 23.37120  27.14306  39.43646  1.000 213.82088 ? 38  TYR E CB  1 
ATOM   7873 C CG  . TYR E 5 58  ? 24.38796  26.53147  38.49498  1.000 215.05032 ? 38  TYR E CG  1 
ATOM   7874 C CD1 . TYR E 5 58  ? 25.75078  26.64787  38.73623  1.000 219.62933 ? 38  TYR E CD1 1 
ATOM   7875 C CD2 . TYR E 5 58  ? 23.98088  25.80254  37.38492  1.000 211.70123 ? 38  TYR E CD2 1 
ATOM   7876 C CE1 . TYR E 5 58  ? 26.67817  26.07932  37.88627  1.000 221.05850 ? 38  TYR E CE1 1 
ATOM   7877 C CE2 . TYR E 5 58  ? 24.90209  25.22670  36.53024  1.000 213.07702 ? 38  TYR E CE2 1 
ATOM   7878 C CZ  . TYR E 5 58  ? 26.24880  25.36862  36.78588  1.000 217.83968 ? 38  TYR E CZ  1 
ATOM   7879 O OH  . TYR E 5 58  ? 27.16863  24.79798  35.93682  1.000 219.48555 ? 38  TYR E OH  1 
ATOM   7880 N N   . LEU E 5 59  ? 21.91637  30.48487  40.19038  1.000 214.08042 ? 39  LEU E N   1 
ATOM   7881 C CA  . LEU E 5 59  ? 20.78725  31.10582  40.86793  1.000 212.38407 ? 39  LEU E CA  1 
ATOM   7882 C C   . LEU E 5 59  ? 20.04403  32.01943  39.90644  1.000 210.56118 ? 39  LEU E C   1 
ATOM   7883 O O   . LEU E 5 59  ? 20.66069  32.72753  39.10479  1.000 212.92826 ? 39  LEU E O   1 
ATOM   7884 C CB  . LEU E 5 59  ? 21.23030  31.90481  42.09651  1.000 216.21701 ? 39  LEU E CB  1 
ATOM   7885 C CG  . LEU E 5 59  ? 20.08215  32.22972  43.05528  1.000 214.97266 ? 39  LEU E CG  1 
ATOM   7886 C CD1 . LEU E 5 59  ? 19.85504  31.08118  44.02633  1.000 215.11941 ? 39  LEU E CD1 1 
ATOM   7887 C CD2 . LEU E 5 59  ? 20.32062  33.53007  43.79610  1.000 218.28554 ? 39  LEU E CD2 1 
ATOM   7888 N N   . ALA E 5 60  ? 18.71643  32.00528  39.99940  1.000 210.14327 ? 40  ALA E N   1 
ATOM   7889 C CA  . ALA E 5 60  ? 17.85995  32.81024  39.14300  1.000 207.27891 ? 40  ALA E CA  1 
ATOM   7890 C C   . ALA E 5 60  ? 16.83674  33.55273  39.98838  1.000 206.22078 ? 40  ALA E C   1 
ATOM   7891 O O   . ALA E 5 60  ? 16.27112  32.99181  40.93186  1.000 205.44012 ? 40  ALA E O   1 
ATOM   7892 C CB  . ALA E 5 60  ? 17.14676  31.94378  38.09935  1.000 201.87987 ? 40  ALA E CB  1 
ATOM   7893 N N   . TRP E 5 61  ? 16.60689  34.81648  39.64602  1.000 209.46839 ? 41  TRP E N   1 
ATOM   7894 C CA  . TRP E 5 61  ? 15.60133  35.64356  40.29495  1.000 205.95253 ? 41  TRP E CA  1 
ATOM   7895 C C   . TRP E 5 61  ? 14.43828  35.86261  39.33733  1.000 198.02821 ? 41  TRP E C   1 
ATOM   7896 O O   . TRP E 5 61  ? 14.64275  36.11649  38.14612  1.000 197.34594 ? 41  TRP E O   1 
ATOM   7897 C CB  . TRP E 5 61  ? 16.18682  36.99094  40.73002  1.000 213.11694 ? 41  TRP E CB  1 
ATOM   7898 C CG  . TRP E 5 61  ? 17.36040  36.87519  41.66172  1.000 218.24762 ? 41  TRP E CG  1 
ATOM   7899 C CD1 . TRP E 5 61  ? 18.61834  36.45401  41.34482  1.000 221.11871 ? 41  TRP E CD1 1 
ATOM   7900 C CD2 . TRP E 5 61  ? 17.38735  37.19931  43.05810  1.000 220.64751 ? 41  TRP E CD2 1 
ATOM   7901 N NE1 . TRP E 5 61  ? 19.42547  36.48993  42.45516  1.000 224.76925 ? 41  TRP E NE1 1 
ATOM   7902 C CE2 . TRP E 5 61  ? 18.69390  36.94352  43.52073  1.000 224.60738 ? 41  TRP E CE2 1 
ATOM   7903 C CE3 . TRP E 5 61  ? 16.43377  37.67732  43.96185  1.000 220.15327 ? 41  TRP E CE3 1 
ATOM   7904 C CZ2 . TRP E 5 61  ? 19.07066  37.14906  44.84635  1.000 227.87556 ? 41  TRP E CZ2 1 
ATOM   7905 C CZ3 . TRP E 5 61  ? 16.80996  37.88036  45.27770  1.000 223.75626 ? 41  TRP E CZ3 1 
ATOM   7906 C CH2 . TRP E 5 61  ? 18.11676  37.61684  45.70711  1.000 227.49075 ? 41  TRP E CH2 1 
ATOM   7907 N N   . TYR E 5 62  ? 13.21882  35.75517  39.85886  1.000 203.91429 ? 42  TYR E N   1 
ATOM   7908 C CA  . TYR E 5 62  ? 12.01381  35.89569  39.05629  1.000 198.29000 ? 42  TYR E CA  1 
ATOM   7909 C C   . TYR E 5 62  ? 11.11571  36.96414  39.65978  1.000 197.59946 ? 42  TYR E C   1 
ATOM   7910 O O   . TYR E 5 62  ? 11.12568  37.19549  40.87118  1.000 201.70903 ? 42  TYR E O   1 
ATOM   7911 C CB  . TYR E 5 62  ? 11.24232  34.56996  38.95236  1.000 193.40858 ? 42  TYR E CB  1 
ATOM   7912 C CG  . TYR E 5 62  ? 12.04525  33.42709  38.37170  1.000 193.41185 ? 42  TYR E CG  1 
ATOM   7913 C CD1 . TYR E 5 62  ? 12.88834  32.66940  39.17320  1.000 196.93783 ? 42  TYR E CD1 1 
ATOM   7914 C CD2 . TYR E 5 62  ? 11.95235  33.09848  37.02569  1.000 189.53089 ? 42  TYR E CD2 1 
ATOM   7915 C CE1 . TYR E 5 62  ? 13.62246  31.62324  38.65067  1.000 196.67994 ? 42  TYR E CE1 1 
ATOM   7916 C CE2 . TYR E 5 62  ? 12.68486  32.05336  36.49319  1.000 189.64529 ? 42  TYR E CE2 1 
ATOM   7917 C CZ  . TYR E 5 62  ? 13.51718  31.31933  37.31108  1.000 193.06071 ? 42  TYR E CZ  1 
ATOM   7918 O OH  . TYR E 5 62  ? 14.24651  30.27702  36.78837  1.000 193.09497 ? 42  TYR E OH  1 
ATOM   7919 N N   . GLN E 5 63  ? 10.33548  37.61227  38.80012  1.000 209.31349 ? 43  GLN E N   1 
ATOM   7920 C CA  . GLN E 5 63  ? 9.39120   38.64782  39.20620  1.000 206.04745 ? 43  GLN E CA  1 
ATOM   7921 C C   . GLN E 5 63  ? 7.97860   38.13286  38.95427  1.000 197.98841 ? 43  GLN E C   1 
ATOM   7922 O O   . GLN E 5 63  ? 7.57352   37.95056  37.80064  1.000 193.40777 ? 43  GLN E O   1 
ATOM   7923 C CB  . GLN E 5 63  ? 9.65335   39.95135  38.45160  1.000 207.56198 ? 43  GLN E CB  1 
ATOM   7924 C CG  . GLN E 5 63  ? 8.48633   40.92169  38.46829  1.000 203.63058 ? 43  GLN E CG  1 
ATOM   7925 C CD  . GLN E 5 63  ? 8.90147   42.35473  38.20223  1.000 208.85892 ? 43  GLN E CD  1 
ATOM   7926 O OE1 . GLN E 5 63  ? 9.20819   43.10539  39.12866  1.000 210.50143 ? 43  GLN E OE1 1 
ATOM   7927 N NE2 . GLN E 5 63  ? 8.90503   42.74497  36.93324  1.000 211.81043 ? 43  GLN E NE2 1 
ATOM   7928 N N   . GLN E 5 64  ? 7.23753   37.89017  40.03075  1.000 205.32945 ? 44  GLN E N   1 
ATOM   7929 C CA  . GLN E 5 64  ? 5.85457   37.42563  39.96033  1.000 202.20852 ? 44  GLN E CA  1 
ATOM   7930 C C   . GLN E 5 64  ? 4.94547   38.60544  40.29105  1.000 203.79571 ? 44  GLN E C   1 
ATOM   7931 O O   . GLN E 5 64  ? 4.62537   38.85687  41.45373  1.000 208.43946 ? 44  GLN E O   1 
ATOM   7932 C CB  . GLN E 5 64  ? 5.60958   36.25465  40.91077  1.000 204.43670 ? 44  GLN E CB  1 
ATOM   7933 C CG  . GLN E 5 64  ? 4.27130   35.56613  40.68129  1.000 202.26769 ? 44  GLN E CG  1 
ATOM   7934 C CD  . GLN E 5 64  ? 3.52372   35.27505  41.97003  1.000 206.67184 ? 44  GLN E CD  1 
ATOM   7935 O OE1 . GLN E 5 64  ? 2.41292   35.76238  42.17797  1.000 206.85051 ? 44  GLN E OE1 1 
ATOM   7936 N NE2 . GLN E 5 64  ? 4.12444   34.46859  42.83663  1.000 211.28783 ? 44  GLN E NE2 1 
ATOM   7937 N N   . LYS E 5 65  ? 4.54088   39.33345  39.25519  1.000 209.45432 ? 45  LYS E N   1 
ATOM   7938 C CA  . LYS E 5 65  ? 3.61632   40.44097  39.44036  1.000 210.88583 ? 45  LYS E CA  1 
ATOM   7939 C C   . LYS E 5 65  ? 2.31772   39.92997  40.06032  1.000 212.20845 ? 45  LYS E C   1 
ATOM   7940 O O   . LYS E 5 65  ? 1.87811   38.81582  39.74878  1.000 208.78639 ? 45  LYS E O   1 
ATOM   7941 C CB  . LYS E 5 65  ? 3.32107   41.12627  38.10434  1.000 208.03596 ? 45  LYS E CB  1 
ATOM   7942 C CG  . LYS E 5 65  ? 4.53648   41.67461  37.37117  1.000 208.59642 ? 45  LYS E CG  1 
ATOM   7943 C CD  . LYS E 5 65  ? 5.05038   42.95788  38.00379  1.000 217.06415 ? 45  LYS E CD  1 
ATOM   7944 C CE  . LYS E 5 65  ? 5.66446   43.87798  36.95848  1.000 218.04659 ? 45  LYS E CE  1 
ATOM   7945 N NZ  . LYS E 5 65  ? 4.62724   44.46175  36.05949  1.000 214.04683 ? 45  LYS E NZ  1 
ATOM   7946 N N   . PRO E 5 66  ? 1.68503   40.70444  40.94062  1.000 211.29731 ? 46  PRO E N   1 
ATOM   7947 C CA  . PRO E 5 66  ? 0.40557   40.26839  41.51642  1.000 214.32497 ? 46  PRO E CA  1 
ATOM   7948 C C   . PRO E 5 66  ? -0.64952  40.08949  40.43436  1.000 209.13115 ? 46  PRO E C   1 
ATOM   7949 O O   . PRO E 5 66  ? -0.84457  40.95781  39.58045  1.000 204.62183 ? 46  PRO E O   1 
ATOM   7950 C CB  . PRO E 5 66  ? 0.04474   41.40149  42.48563  1.000 217.90035 ? 46  PRO E CB  1 
ATOM   7951 C CG  . PRO E 5 66  ? 0.84600   42.57782  42.02379  1.000 215.57219 ? 46  PRO E CG  1 
ATOM   7952 C CD  . PRO E 5 66  ? 2.11555   42.00949  41.47042  1.000 215.26317 ? 46  PRO E CD  1 
ATOM   7953 N N   . GLY E 5 67  ? -1.32593  38.94386  40.47380  1.000 215.91086 ? 47  GLY E N   1 
ATOM   7954 C CA  . GLY E 5 67  ? -2.28581  38.59469  39.44623  1.000 211.31569 ? 47  GLY E CA  1 
ATOM   7955 C C   . GLY E 5 67  ? -1.62277  38.36429  38.10481  1.000 203.54274 ? 47  GLY E C   1 
ATOM   7956 O O   . GLY E 5 67  ? -2.07633  38.88857  37.08256  1.000 199.49909 ? 47  GLY E O   1 
ATOM   7957 N N   . GLN E 5 68  ? -0.54817  37.57864  38.09673  1.000 199.67579 ? 48  GLN E N   1 
ATOM   7958 C CA  . GLN E 5 68  ? 0.24101   37.37255  36.88994  1.000 194.20980 ? 48  GLN E CA  1 
ATOM   7959 C C   . GLN E 5 68  ? 1.20516   36.21771  37.12293  1.000 193.89563 ? 48  GLN E C   1 
ATOM   7960 O O   . GLN E 5 68  ? 1.48211   35.83544  38.26367  1.000 198.09831 ? 48  GLN E O   1 
ATOM   7961 C CB  . GLN E 5 68  ? 1.00162   38.64754  36.50084  1.000 194.55365 ? 48  GLN E CB  1 
ATOM   7962 C CG  . GLN E 5 68  ? 1.62816   38.62828  35.11545  1.000 190.59441 ? 48  GLN E CG  1 
ATOM   7963 C CD  . GLN E 5 68  ? 1.94248   40.01763  34.60513  1.000 190.56880 ? 48  GLN E CD  1 
ATOM   7964 O OE1 . GLN E 5 68  ? 3.01569   40.26238  34.05489  1.000 191.33370 ? 48  GLN E OE1 1 
ATOM   7965 N NE2 . GLN E 5 68  ? 1.00088   40.93787  34.78069  1.000 193.04651 ? 48  GLN E NE2 1 
ATOM   7966 N N   . SER E 5 69  ? 1.70207   35.66291  36.02125  1.000 191.41056 ? 49  SER E N   1 
ATOM   7967 C CA  . SER E 5 69  ? 2.71707   34.62535  36.04835  1.000 190.86567 ? 49  SER E CA  1 
ATOM   7968 C C   . SER E 5 69  ? 4.09785   35.22783  36.29607  1.000 193.89451 ? 49  SER E C   1 
ATOM   7969 O O   . SER E 5 69  ? 4.33355   36.40438  36.01089  1.000 194.78987 ? 49  SER E O   1 
ATOM   7970 C CB  . SER E 5 69  ? 2.70913   33.86054  34.72937  1.000 184.95754 ? 49  SER E CB  1 
ATOM   7971 O OG  . SER E 5 69  ? 2.84854   34.74216  33.62901  1.000 182.58592 ? 49  SER E OG  1 
ATOM   7972 N N   . PRO E 5 70  ? 5.02847   34.44379  36.83371  1.000 181.87425 ? 50  PRO E N   1 
ATOM   7973 C CA  . PRO E 5 70  ? 6.38859   34.94692  37.04947  1.000 185.45535 ? 50  PRO E CA  1 
ATOM   7974 C C   . PRO E 5 70  ? 7.19111   34.97625  35.75541  1.000 183.43519 ? 50  PRO E C   1 
ATOM   7975 O O   . PRO E 5 70  ? 6.87587   34.29846  34.77702  1.000 178.92703 ? 50  PRO E O   1 
ATOM   7976 C CB  . PRO E 5 70  ? 6.99192   33.94205  38.04181  1.000 190.05513 ? 50  PRO E CB  1 
ATOM   7977 C CG  . PRO E 5 70  ? 5.83858   33.10398  38.52925  1.000 188.73032 ? 50  PRO E CG  1 
ATOM   7978 C CD  . PRO E 5 70  ? 4.84163   33.10830  37.42126  1.000 182.52288 ? 50  PRO E CD  1 
ATOM   7979 N N   . LYS E 5 71  ? 8.25324   35.78162  35.76989  1.000 179.97060 ? 51  LYS E N   1 
ATOM   7980 C CA  . LYS E 5 71  ? 9.13477   35.91566  34.61726  1.000 183.46987 ? 51  LYS E CA  1 
ATOM   7981 C C   . LYS E 5 71  ? 10.56564  36.11577  35.09872  1.000 192.79572 ? 51  LYS E C   1 
ATOM   7982 O O   . LYS E 5 71  ? 10.80538  36.74651  36.13172  1.000 198.25075 ? 51  LYS E O   1 
ATOM   7983 C CB  . LYS E 5 71  ? 8.70109   37.07551  33.70840  1.000 177.40931 ? 51  LYS E CB  1 
ATOM   7984 C CG  . LYS E 5 71  ? 7.41258   36.81122  32.93405  1.000 172.03986 ? 51  LYS E CG  1 
ATOM   7985 C CD  . LYS E 5 71  ? 7.05604   37.96382  32.00573  1.000 169.74423 ? 51  LYS E CD  1 
ATOM   7986 C CE  . LYS E 5 71  ? 6.62177   39.19708  32.78345  1.000 173.26056 ? 51  LYS E CE  1 
ATOM   7987 N NZ  . LYS E 5 71  ? 5.35673   38.96636  33.53728  1.000 171.47192 ? 51  LYS E NZ  1 
ATOM   7988 N N   . LEU E 5 72  ? 11.51205  35.58214  34.32802  1.000 181.18053 ? 52  LEU E N   1 
ATOM   7989 C CA  . LEU E 5 72  ? 12.91360  35.56070  34.72870  1.000 191.11990 ? 52  LEU E CA  1 
ATOM   7990 C C   . LEU E 5 72  ? 13.53044  36.95431  34.67130  1.000 196.84838 ? 52  LEU E C   1 
ATOM   7991 O O   . LEU E 5 72  ? 13.15457  37.79499  33.85006  1.000 196.54622 ? 52  LEU E O   1 
ATOM   7992 C CB  . LEU E 5 72  ? 13.70370  34.60358  33.83347  1.000 191.59857 ? 52  LEU E CB  1 
ATOM   7993 C CG  . LEU E 5 72  ? 15.22783  34.53781  33.99732  1.000 198.37777 ? 52  LEU E CG  1 
ATOM   7994 C CD1 . LEU E 5 72  ? 15.61708  33.91484  35.33113  1.000 199.56228 ? 52  LEU E CD1 1 
ATOM   7995 C CD2 . LEU E 5 72  ? 15.87054  33.79346  32.83779  1.000 203.24673 ? 52  LEU E CD2 1 
ATOM   7996 N N   . LEU E 5 73  ? 14.49222  37.19343  35.56300  1.000 196.37321 ? 53  LEU E N   1 
ATOM   7997 C CA  . LEU E 5 73  ? 15.21851  38.45761  35.61304  1.000 203.18238 ? 53  LEU E CA  1 
ATOM   7998 C C   . LEU E 5 73  ? 16.68502  38.25229  35.25074  1.000 213.05551 ? 53  LEU E C   1 
ATOM   7999 O O   . LEU E 5 73  ? 17.10805  38.64580  34.16282  1.000 216.44405 ? 53  LEU E O   1 
ATOM   8000 C CB  . LEU E 5 73  ? 15.07630  39.09714  36.99481  1.000 204.66886 ? 53  LEU E CB  1 
ATOM   8001 C CG  . LEU E 5 73  ? 13.64391  39.20566  37.51619  1.000 199.06155 ? 53  LEU E CG  1 
ATOM   8002 C CD1 . LEU E 5 73  ? 13.62873  39.79901  38.91305  1.000 201.84150 ? 53  LEU E CD1 1 
ATOM   8003 C CD2 . LEU E 5 73  ? 12.79340  40.03195  36.56931  1.000 196.64010 ? 53  LEU E CD2 1 
ATOM   8004 N N   . ILE E 5 74  ? 17.48058  37.64999  36.13247  1.000 206.75472 ? 54  ILE E N   1 
ATOM   8005 C CA  . ILE E 5 74  ? 18.90196  37.43867  35.89090  1.000 212.63424 ? 54  ILE E CA  1 
ATOM   8006 C C   . ILE E 5 74  ? 19.20592  35.95128  36.00737  1.000 210.80399 ? 54  ILE E C   1 
ATOM   8007 O O   . ILE E 5 74  ? 18.75649  35.28785  36.95005  1.000 207.87378 ? 54  ILE E O   1 
ATOM   8008 C CB  . ILE E 5 74  ? 19.77890  38.25917  36.85766  1.000 218.11463 ? 54  ILE E CB  1 
ATOM   8009 C CG1 . ILE E 5 74  ? 19.47665  37.90348  38.31410  1.000 216.29622 ? 54  ILE E CG1 1 
ATOM   8010 C CG2 . ILE E 5 74  ? 19.58562  39.74958  36.62004  1.000 220.82747 ? 54  ILE E CG2 1 
ATOM   8011 C CD1 . ILE E 5 74  ? 20.58864  38.27930  39.26714  1.000 221.25563 ? 54  ILE E CD1 1 
ATOM   8012 N N   . TYR E 5 75  ? 19.95477  35.42983  35.04148  1.000 208.64327 ? 55  TYR E N   1 
ATOM   8013 C CA  . TYR E 5 75  ? 20.49253  34.07960  35.10761  1.000 207.89823 ? 55  TYR E CA  1 
ATOM   8014 C C   . TYR E 5 75  ? 21.98292  34.12938  35.43074  1.000 213.71782 ? 55  TYR E C   1 
ATOM   8015 O O   . TYR E 5 75  ? 22.64861  35.15202  35.25281  1.000 218.80331 ? 55  TYR E O   1 
ATOM   8016 C CB  . TYR E 5 75  ? 20.24838  33.31562  33.80022  1.000 205.14909 ? 55  TYR E CB  1 
ATOM   8017 C CG  . TYR E 5 75  ? 20.57767  34.06784  32.52660  1.000 209.31299 ? 55  TYR E CG  1 
ATOM   8018 C CD1 . TYR E 5 75  ? 19.66541  34.95052  31.96449  1.000 207.15897 ? 55  TYR E CD1 1 
ATOM   8019 C CD2 . TYR E 5 75  ? 21.78620  33.87113  31.86917  1.000 215.33742 ? 55  TYR E CD2 1 
ATOM   8020 C CE1 . TYR E 5 75  ? 19.95424  35.63231  30.79902  1.000 211.62477 ? 55  TYR E CE1 1 
ATOM   8021 C CE2 . TYR E 5 75  ? 22.08335  34.54863  30.69906  1.000 219.97333 ? 55  TYR E CE2 1 
ATOM   8022 C CZ  . TYR E 5 75  ? 21.16309  35.42778  30.16982  1.000 218.45926 ? 55  TYR E CZ  1 
ATOM   8023 O OH  . TYR E 5 75  ? 21.45091  36.10578  29.00757  1.000 223.52892 ? 55  TYR E OH  1 
ATOM   8024 N N   . TRP E 5 76  ? 22.49660  33.00735  35.92983  1.000 212.51162 ? 56  TRP E N   1 
ATOM   8025 C CA  . TRP E 5 76  ? 23.86874  32.89923  36.42132  1.000 217.39928 ? 56  TRP E CA  1 
ATOM   8026 C C   . TRP E 5 76  ? 24.16675  33.88509  37.55327  1.000 220.33103 ? 56  TRP E C   1 
ATOM   8027 O O   . TRP E 5 76  ? 25.32547  34.26516  37.75396  1.000 225.37236 ? 56  TRP E O   1 
ATOM   8028 C CB  . TRP E 5 76  ? 24.89046  33.07756  35.28651  1.000 222.54865 ? 56  TRP E CB  1 
ATOM   8029 C CG  . TRP E 5 76  ? 24.80742  32.01874  34.23848  1.000 220.48071 ? 56  TRP E CG  1 
ATOM   8030 C CD1 . TRP E 5 76  ? 24.45721  32.18369  32.93107  1.000 220.84226 ? 56  TRP E CD1 1 
ATOM   8031 C CD2 . TRP E 5 76  ? 25.07308  30.62389  34.41096  1.000 217.98950 ? 56  TRP E CD2 1 
ATOM   8032 N NE1 . TRP E 5 76  ? 24.49385  30.97780  32.27598  1.000 218.67049 ? 56  TRP E NE1 1 
ATOM   8033 C CE2 . TRP E 5 76  ? 24.86867  30.00339  33.16365  1.000 216.74601 ? 56  TRP E CE2 1 
ATOM   8034 C CE3 . TRP E 5 76  ? 25.46729  29.84005  35.49856  1.000 216.87208 ? 56  TRP E CE3 1 
ATOM   8035 C CZ2 . TRP E 5 76  ? 25.04435  28.63620  32.97438  1.000 214.20571 ? 56  TRP E CZ2 1 
ATOM   8036 C CZ3 . TRP E 5 76  ? 25.64072  28.48414  35.30968  1.000 214.43126 ? 56  TRP E CZ3 1 
ATOM   8037 C CH2 . TRP E 5 76  ? 25.42997  27.89506  34.05704  1.000 212.96849 ? 56  TRP E CH2 1 
ATOM   8038 N N   . ALA E 5 77  ? 23.14256  34.31203  38.29523  1.000 219.48193 ? 57  ALA E N   1 
ATOM   8039 C CA  . ALA E 5 77  ? 23.24366  35.19246  39.45940  1.000 221.72246 ? 57  ALA E CA  1 
ATOM   8040 C C   . ALA E 5 77  ? 23.87160  36.54756  39.14692  1.000 226.90445 ? 57  ALA E C   1 
ATOM   8041 O O   . ALA E 5 77  ? 24.18015  37.30761  40.07462  1.000 229.38850 ? 57  ALA E O   1 
ATOM   8042 C CB  . ALA E 5 77  ? 24.01546  34.52469  40.60624  1.000 223.20893 ? 57  ALA E CB  1 
ATOM   8043 N N   . SER E 5 78  ? 24.06031  36.88189  37.87031  1.000 216.23382 ? 58  SER E N   1 
ATOM   8044 C CA  . SER E 5 78  ? 24.66561  38.15446  37.49507  1.000 221.88534 ? 58  SER E CA  1 
ATOM   8045 C C   . SER E 5 78  ? 24.19197  38.59153  36.11559  1.000 222.39990 ? 58  SER E C   1 
ATOM   8046 O O   . SER E 5 78  ? 23.67945  39.70367  35.95331  1.000 224.68518 ? 58  SER E O   1 
ATOM   8047 C CB  . SER E 5 78  ? 26.19139  38.05279  37.52448  1.000 229.36607 ? 58  SER E CB  1 
ATOM   8048 O OG  . SER E 5 78  ? 26.78641  39.24093  37.03411  1.000 234.70195 ? 58  SER E OG  1 
ATOM   8049 N N   . THR E 5 79  ? 24.36965  37.72567  35.11925  1.000 222.10403 ? 59  THR E N   1 
ATOM   8050 C CA  . THR E 5 79  ? 23.91952  38.03045  33.76792  1.000 222.71583 ? 59  THR E CA  1 
ATOM   8051 C C   . THR E 5 79  ? 22.40832  38.22258  33.74925  1.000 216.42751 ? 59  THR E C   1 
ATOM   8052 O O   . THR E 5 79  ? 21.66300  37.46308  34.37120  1.000 210.49256 ? 59  THR E O   1 
ATOM   8053 C CB  . THR E 5 79  ? 24.31722  36.90463  32.81043  1.000 222.85695 ? 59  THR E CB  1 
ATOM   8054 O OG1 . THR E 5 79  ? 25.64498  36.45948  33.11585  1.000 226.63497 ? 59  THR E OG1 1 
ATOM   8055 C CG2 . THR E 5 79  ? 24.27454  37.38915  31.36860  1.000 226.66856 ? 59  THR E CG2 1 
ATOM   8056 N N   . ARG E 5 80  ? 21.95221  39.24760  33.03771  1.000 219.92044 ? 60  ARG E N   1 
ATOM   8057 C CA  . ARG E 5 80  ? 20.53477  39.56975  32.99376  1.000 214.13005 ? 60  ARG E CA  1 
ATOM   8058 C C   . ARG E 5 80  ? 19.92714  39.15944  31.65883  1.000 211.79188 ? 60  ARG E C   1 
ATOM   8059 O O   . ARG E 5 80  ? 20.61312  39.04497  30.63961  1.000 216.18884 ? 60  ARG E O   1 
ATOM   8060 C CB  . ARG E 5 80  ? 20.29540  41.06397  33.23681  1.000 217.76982 ? 60  ARG E CB  1 
ATOM   8061 C CG  . ARG E 5 80  ? 20.71753  41.96736  32.09395  1.000 224.23001 ? 60  ARG E CG  1 
ATOM   8062 C CD  . ARG E 5 80  ? 20.24896  43.38886  32.34451  1.000 224.26316 ? 60  ARG E CD  1 
ATOM   8063 N NE  . ARG E 5 80  ? 20.62382  43.84468  33.67716  1.000 224.50495 ? 60  ARG E NE  1 
ATOM   8064 C CZ  . ARG E 5 80  ? 21.74697  44.48981  33.95880  1.000 229.95838 ? 60  ARG E CZ  1 
ATOM   8065 N NH1 . ARG E 5 80  ? 22.62472  44.79261  33.01661  1.000 236.31398 ? 60  ARG E NH1 1 
ATOM   8066 N NH2 . ARG E 5 80  ? 21.99536  44.84049  35.21706  1.000 229.42775 ? 60  ARG E NH2 1 
ATOM   8067 N N   . GLU E 5 81  ? 18.61690  38.93819  31.68496  1.000 219.09337 ? 61  GLU E N   1 
ATOM   8068 C CA  . GLU E 5 81  ? 17.86994  38.56212  30.49796  1.000 215.77654 ? 61  GLU E CA  1 
ATOM   8069 C C   . GLU E 5 81  ? 17.66765  39.77418  29.59019  1.000 219.02267 ? 61  GLU E C   1 
ATOM   8070 O O   . GLU E 5 81  ? 17.74192  40.92846  30.02168  1.000 222.60159 ? 61  GLU E O   1 
ATOM   8071 C CB  . GLU E 5 81  ? 16.52039  37.95743  30.89590  1.000 206.76772 ? 61  GLU E CB  1 
ATOM   8072 C CG  . GLU E 5 81  ? 15.75379  37.30070  29.76116  1.000 201.05793 ? 61  GLU E CG  1 
ATOM   8073 C CD  . GLU E 5 81  ? 16.54530  36.19390  29.09852  1.000 202.59308 ? 61  GLU E CD  1 
ATOM   8074 O OE1 . GLU E 5 81  ? 16.81412  35.17318  29.76617  1.000 200.50389 ? 61  GLU E OE1 1 
ATOM   8075 O OE2 . GLU E 5 81  ? 16.91190  36.35180  27.91497  1.000 206.05634 ? 61  GLU E OE2 1 
ATOM   8076 N N   . SER E 5 82  ? 17.42663  39.49743  28.31017  1.000 214.08067 ? 62  SER E N   1 
ATOM   8077 C CA  . SER E 5 82  ? 17.07709  40.55366  27.37010  1.000 217.81426 ? 62  SER E CA  1 
ATOM   8078 C C   . SER E 5 82  ? 15.72425  41.14663  27.74328  1.000 211.99906 ? 62  SER E C   1 
ATOM   8079 O O   . SER E 5 82  ? 14.76226  40.41523  27.99758  1.000 203.43657 ? 62  SER E O   1 
ATOM   8080 C CB  . SER E 5 82  ? 17.04555  40.00904  25.94285  1.000 217.89342 ? 62  SER E CB  1 
ATOM   8081 O OG  . SER E 5 82  ? 16.03320  39.02906  25.79043  1.000 207.73457 ? 62  SER E OG  1 
ATOM   8082 N N   . GLY E 5 83  ? 15.65187  42.47338  27.78048  1.000 226.38270 ? 63  GLY E N   1 
ATOM   8083 C CA  . GLY E 5 83  ? 14.44956  43.15529  28.20882  1.000 221.28665 ? 63  GLY E CA  1 
ATOM   8084 C C   . GLY E 5 83  ? 14.32847  43.36277  29.70080  1.000 219.52688 ? 63  GLY E C   1 
ATOM   8085 O O   . GLY E 5 83  ? 13.25807  43.77128  30.16739  1.000 214.98931 ? 63  GLY E O   1 
ATOM   8086 N N   . VAL E 5 84  ? 15.38070  43.09516  30.45934  1.000 223.66735 ? 64  VAL E N   1 
ATOM   8087 C CA  . VAL E 5 84  ? 15.38843  43.27506  31.90911  1.000 222.69774 ? 64  VAL E CA  1 
ATOM   8088 C C   . VAL E 5 84  ? 16.02273  44.62624  32.21851  1.000 227.83537 ? 64  VAL E C   1 
ATOM   8089 O O   . VAL E 5 84  ? 17.07990  44.94086  31.65363  1.000 234.10177 ? 64  VAL E O   1 
ATOM   8090 C CB  . VAL E 5 84  ? 16.14733  42.13525  32.61352  1.000 222.00879 ? 64  VAL E CB  1 
ATOM   8091 C CG1 . VAL E 5 84  ? 16.51379  42.52191  34.03757  1.000 224.04048 ? 64  VAL E CG1 1 
ATOM   8092 C CG2 . VAL E 5 84  ? 15.30574  40.87098  32.60729  1.000 213.93012 ? 64  VAL E CG2 1 
ATOM   8093 N N   . PRO E 5 85  ? 15.41878  45.44318  33.08123  1.000 230.15985 ? 65  PRO E N   1 
ATOM   8094 C CA  . PRO E 5 85  ? 15.96635  46.78093  33.34103  1.000 234.12306 ? 65  PRO E CA  1 
ATOM   8095 C C   . PRO E 5 85  ? 17.37488  46.71462  33.91374  1.000 239.06583 ? 65  PRO E C   1 
ATOM   8096 O O   . PRO E 5 85  ? 17.67437  45.89861  34.78805  1.000 237.64837 ? 65  PRO E O   1 
ATOM   8097 C CB  . PRO E 5 85  ? 14.97692  47.37828  34.34734  1.000 229.62878 ? 65  PRO E CB  1 
ATOM   8098 C CG  . PRO E 5 85  ? 13.71331  46.60558  34.14724  1.000 223.71409 ? 65  PRO E CG  1 
ATOM   8099 C CD  . PRO E 5 85  ? 14.14721  45.21745  33.78893  1.000 223.80235 ? 65  PRO E CD  1 
ATOM   8100 N N   . ASP E 5 86  ? 18.24249  47.59643  33.40641  1.000 238.08810 ? 66  ASP E N   1 
ATOM   8101 C CA  . ASP E 5 86  ? 19.63419  47.63266  33.84626  1.000 243.35255 ? 66  ASP E CA  1 
ATOM   8102 C C   . ASP E 5 86  ? 19.77465  47.94344  35.33021  1.000 241.72911 ? 66  ASP E C   1 
ATOM   8103 O O   . ASP E 5 86  ? 20.83649  47.68271  35.90711  1.000 244.56582 ? 66  ASP E O   1 
ATOM   8104 C CB  . ASP E 5 86  ? 20.41869  48.66363  33.03291  1.000 250.22017 ? 66  ASP E CB  1 
ATOM   8105 C CG  . ASP E 5 86  ? 21.10709  48.05549  31.82866  1.000 255.46458 ? 66  ASP E CG  1 
ATOM   8106 O OD1 . ASP E 5 86  ? 20.87487  46.86101  31.54749  1.000 253.20102 ? 66  ASP E OD1 1 
ATOM   8107 O OD2 . ASP E 5 86  ? 21.88912  48.77074  31.16840  1.000 261.94242 ? 66  ASP E OD2 1 
ATOM   8108 N N   . ARG E 5 87  ? 18.73626  48.49821  35.95967  1.000 237.59042 ? 67  ARG E N   1 
ATOM   8109 C CA  . ARG E 5 87  ? 18.81343  48.79108  37.38609  1.000 236.33012 ? 67  ARG E CA  1 
ATOM   8110 C C   . ARG E 5 87  ? 18.91366  47.51947  38.21837  1.000 234.36460 ? 67  ARG E C   1 
ATOM   8111 O O   . ARG E 5 87  ? 19.50369  47.53872  39.30449  1.000 235.70258 ? 67  ARG E O   1 
ATOM   8112 C CB  . ARG E 5 87  ? 17.60482  49.62273  37.81715  1.000 232.42565 ? 67  ARG E CB  1 
ATOM   8113 C CG  . ARG E 5 87  ? 16.26335  49.07529  37.35438  1.000 227.13525 ? 67  ARG E CG  1 
ATOM   8114 C CD  . ARG E 5 87  ? 15.13249  50.01303  37.74747  1.000 224.11203 ? 67  ARG E CD  1 
ATOM   8115 N NE  . ARG E 5 87  ? 13.81678  49.47087  37.42878  1.000 218.69450 ? 67  ARG E NE  1 
ATOM   8116 C CZ  . ARG E 5 87  ? 13.09838  49.81500  36.36849  1.000 216.73756 ? 67  ARG E CZ  1 
ATOM   8117 N NH1 . ARG E 5 87  ? 13.53826  50.70523  35.49414  1.000 215.41271 ? 67  ARG E NH1 1 
ATOM   8118 N NH2 . ARG E 5 87  ? 11.90669  49.25428  36.18275  1.000 216.36393 ? 67  ARG E NH2 1 
ATOM   8119 N N   . PHE E 5 88  ? 18.35783  46.41244  37.72971  1.000 234.64687 ? 68  PHE E N   1 
ATOM   8120 C CA  . PHE E 5 88  ? 18.42432  45.13099  38.43091  1.000 232.85165 ? 68  PHE E CA  1 
ATOM   8121 C C   . PHE E 5 88  ? 19.81754  44.54412  38.24588  1.000 237.11401 ? 68  PHE E C   1 
ATOM   8122 O O   . PHE E 5 88  ? 20.12975  43.96978  37.20010  1.000 238.17025 ? 68  PHE E O   1 
ATOM   8123 C CB  . PHE E 5 88  ? 17.35428  44.17624  37.91429  1.000 228.29665 ? 68  PHE E CB  1 
ATOM   8124 C CG  . PHE E 5 88  ? 15.95353  44.58082  38.27010  1.000 223.81060 ? 68  PHE E CG  1 
ATOM   8125 C CD1 . PHE E 5 88  ? 15.40872  44.23266  39.49488  1.000 221.76950 ? 68  PHE E CD1 1 
ATOM   8126 C CD2 . PHE E 5 88  ? 15.17707  45.29877  37.37616  1.000 222.06273 ? 68  PHE E CD2 1 
ATOM   8127 C CE1 . PHE E 5 88  ? 14.11814  44.59874  39.82428  1.000 218.32408 ? 68  PHE E CE1 1 
ATOM   8128 C CE2 . PHE E 5 88  ? 13.88540  45.66744  37.69965  1.000 218.01547 ? 68  PHE E CE2 1 
ATOM   8129 C CZ  . PHE E 5 88  ? 13.35559  45.31698  38.92541  1.000 216.16400 ? 68  PHE E CZ  1 
ATOM   8130 N N   . THR E 5 89  ? 20.65985  44.68196  39.26726  1.000 235.48323 ? 69  THR E N   1 
ATOM   8131 C CA  . THR E 5 89  ? 22.02526  44.15799  39.25343  1.000 239.63715 ? 69  THR E CA  1 
ATOM   8132 C C   . THR E 5 89  ? 22.17357  43.17874  40.41458  1.000 238.33889 ? 69  THR E C   1 
ATOM   8133 O O   . THR E 5 89  ? 22.45164  43.58369  41.54801  1.000 239.41215 ? 69  THR E O   1 
ATOM   8134 C CB  . THR E 5 89  ? 23.05595  45.28399  39.34339  1.000 244.78969 ? 69  THR E CB  1 
ATOM   8135 O OG1 . THR E 5 89  ? 22.77370  46.11045  40.47953  1.000 243.80212 ? 69  THR E OG1 1 
ATOM   8136 C CG2 . THR E 5 89  ? 23.03466  46.13520  38.08172  1.000 247.35170 ? 69  THR E CG2 1 
ATOM   8137 N N   . GLY E 5 90  ? 21.98771  41.89292  40.13182  1.000 228.78927 ? 70  GLY E N   1 
ATOM   8138 C CA  . GLY E 5 90  ? 22.18944  40.87198  41.13776  1.000 227.91460 ? 70  GLY E CA  1 
ATOM   8139 C C   . GLY E 5 90  ? 23.65562  40.69537  41.48480  1.000 232.37834 ? 70  GLY E C   1 
ATOM   8140 O O   . GLY E 5 90  ? 24.55977  41.14548  40.78034  1.000 236.17554 ? 70  GLY E O   1 
ATOM   8141 N N   . SER E 5 91  ? 23.89243  40.01572  42.60279  1.000 240.95210 ? 71  SER E N   1 
ATOM   8142 C CA  . SER E 5 91  ? 25.24612  39.84725  43.11260  1.000 244.94522 ? 71  SER E CA  1 
ATOM   8143 C C   . SER E 5 91  ? 25.27029  38.66242  44.06728  1.000 243.96018 ? 71  SER E C   1 
ATOM   8144 O O   . SER E 5 91  ? 24.23393  38.07998  44.39332  1.000 239.52952 ? 71  SER E O   1 
ATOM   8145 C CB  . SER E 5 91  ? 25.73855  41.12288  43.80384  1.000 248.15236 ? 71  SER E CB  1 
ATOM   8146 O OG  . SER E 5 91  ? 24.76626  41.61341  44.71122  1.000 245.99781 ? 71  SER E OG  1 
ATOM   8147 N N   . GLY E 5 92  ? 26.46967  38.31543  44.50976  1.000 247.78652 ? 72  GLY E N   1 
ATOM   8148 C CA  . GLY E 5 92  ? 26.67171  37.22925  45.44274  1.000 247.63520 ? 72  GLY E CA  1 
ATOM   8149 C C   . GLY E 5 92  ? 27.37491  36.04496  44.79572  1.000 246.19392 ? 72  GLY E C   1 
ATOM   8150 O O   . GLY E 5 92  ? 27.38179  35.87080  43.57338  1.000 244.93150 ? 72  GLY E O   1 
ATOM   8151 N N   . SER E 5 93  ? 27.97698  35.21653  45.64717  1.000 246.60622 ? 73  SER E N   1 
ATOM   8152 C CA  . SER E 5 93  ? 28.67936  34.02477  45.19311  1.000 245.89065 ? 73  SER E CA  1 
ATOM   8153 C C   . SER E 5 93  ? 28.69051  32.99472  46.31195  1.000 245.08039 ? 73  SER E C   1 
ATOM   8154 O O   . SER E 5 93  ? 28.78892  33.34661  47.49029  1.000 247.32413 ? 73  SER E O   1 
ATOM   8155 C CB  . SER E 5 93  ? 30.11284  34.35037  44.75707  1.000 251.71386 ? 73  SER E CB  1 
ATOM   8156 O OG  . SER E 5 93  ? 30.78732  33.18704  44.30912  1.000 250.34051 ? 73  SER E OG  1 
ATOM   8157 N N   . GLY E 5 94  ? 28.58851  31.72363  45.93157  1.000 237.68540 ? 74  GLY E N   1 
ATOM   8158 C CA  . GLY E 5 94  ? 28.63610  30.63716  46.88933  1.000 238.62955 ? 74  GLY E CA  1 
ATOM   8159 C C   . GLY E 5 94  ? 27.30802  30.35856  47.56153  1.000 236.30285 ? 74  GLY E C   1 
ATOM   8160 O O   . GLY E 5 94  ? 26.52713  29.52540  47.09185  1.000 233.18422 ? 74  GLY E O   1 
ATOM   8161 N N   . THR E 5 95  ? 27.03888  31.05435  48.66380  1.000 242.67269 ? 75  THR E N   1 
ATOM   8162 C CA  . THR E 5 95  ? 25.82296  30.84353  49.43943  1.000 241.49441 ? 75  THR E CA  1 
ATOM   8163 C C   . THR E 5 95  ? 24.91209  32.06001  49.45011  1.000 240.66466 ? 75  THR E C   1 
ATOM   8164 O O   . THR E 5 95  ? 23.70782  31.92634  49.20440  1.000 237.29882 ? 75  THR E O   1 
ATOM   8165 C CB  . THR E 5 95  ? 26.17866  30.44615  50.88169  1.000 245.37503 ? 75  THR E CB  1 
ATOM   8166 O OG1 . THR E 5 95  ? 27.07765  31.41293  51.43965  1.000 249.19614 ? 75  THR E OG1 1 
ATOM   8167 C CG2 . THR E 5 95  ? 26.83115  29.07200  50.91115  1.000 245.59627 ? 75  THR E CG2 1 
ATOM   8168 N N   . ASP E 5 96  ? 25.44831  33.24471  49.73041  1.000 242.37087 ? 76  ASP E N   1 
ATOM   8169 C CA  . ASP E 5 96  ? 24.64632  34.45761  49.80328  1.000 241.91472 ? 76  ASP E CA  1 
ATOM   8170 C C   . ASP E 5 96  ? 24.58983  35.14308  48.44456  1.000 239.59708 ? 76  ASP E C   1 
ATOM   8171 O O   . ASP E 5 96  ? 25.60280  35.25630  47.74883  1.000 241.26242 ? 76  ASP E O   1 
ATOM   8172 C CB  . ASP E 5 96  ? 25.21545  35.41727  50.84956  1.000 246.73049 ? 76  ASP E CB  1 
ATOM   8173 C CG  . ASP E 5 96  ? 24.42979  36.71038  50.94227  1.000 246.63612 ? 76  ASP E CG  1 
ATOM   8174 O OD1 . ASP E 5 96  ? 23.25416  36.66458  51.36125  1.000 244.98830 ? 76  ASP E OD1 1 
ATOM   8175 O OD2 . ASP E 5 96  ? 24.98731  37.77301  50.59612  1.000 248.25621 ? 76  ASP E OD2 1 
ATOM   8176 N N   . PHE E 5 97  ? 23.39499  35.60017  48.07331  1.000 246.69124 ? 77  PHE E N   1 
ATOM   8177 C CA  . PHE E 5 97  ? 23.17508  36.28847  46.80971  1.000 244.84599 ? 77  PHE E CA  1 
ATOM   8178 C C   . PHE E 5 97  ? 22.21501  37.44583  47.03406  1.000 244.25081 ? 77  PHE E C   1 
ATOM   8179 O O   . PHE E 5 97  ? 21.22460  37.30531  47.75709  1.000 242.75816 ? 77  PHE E O   1 
ATOM   8180 C CB  . PHE E 5 97  ? 22.61178  35.34237  45.74373  1.000 240.50482 ? 77  PHE E CB  1 
ATOM   8181 C CG  . PHE E 5 97  ? 23.44632  34.11399  45.51810  1.000 240.68430 ? 77  PHE E CG  1 
ATOM   8182 C CD1 . PHE E 5 97  ? 24.49680  34.13041  44.61620  1.000 242.32776 ? 77  PHE E CD1 1 
ATOM   8183 C CD2 . PHE E 5 97  ? 23.17679  32.94099  46.20419  1.000 239.69825 ? 77  PHE E CD2 1 
ATOM   8184 C CE1 . PHE E 5 97  ? 25.26600  33.00144  44.40544  1.000 242.53895 ? 77  PHE E CE1 1 
ATOM   8185 C CE2 . PHE E 5 97  ? 23.94269  31.80884  45.99841  1.000 239.83526 ? 77  PHE E CE2 1 
ATOM   8186 C CZ  . PHE E 5 97  ? 24.98864  31.83935  45.09782  1.000 241.01823 ? 77  PHE E CZ  1 
ATOM   8187 N N   . THR E 5 98  ? 22.50585  38.58738  46.41046  1.000 242.23417 ? 78  THR E N   1 
ATOM   8188 C CA  . THR E 5 98  ? 21.72043  39.79395  46.63604  1.000 242.70092 ? 78  THR E CA  1 
ATOM   8189 C C   . THR E 5 98  ? 21.42612  40.50730  45.32448  1.000 241.04111 ? 78  THR E C   1 
ATOM   8190 O O   . THR E 5 98  ? 22.33901  40.77121  44.53654  1.000 243.00659 ? 78  THR E O   1 
ATOM   8191 C CB  . THR E 5 98  ? 22.43501  40.75235  47.59912  1.000 246.23347 ? 78  THR E CB  1 
ATOM   8192 O OG1 . THR E 5 98  ? 23.79281  40.93603  47.17997  1.000 249.20776 ? 78  THR E OG1 1 
ATOM   8193 C CG2 . THR E 5 98  ? 22.40896  40.20602  49.02268  1.000 248.06789 ? 78  THR E CG2 1 
ATOM   8194 N N   . LEU E 5 99  ? 20.15114  40.82493  45.10766  1.000 238.34126 ? 79  LEU E N   1 
ATOM   8195 C CA  . LEU E 5 99  ? 19.69258  41.61466  43.97395  1.000 236.76655 ? 79  LEU E CA  1 
ATOM   8196 C C   . LEU E 5 99  ? 19.41591  43.04670  44.41990  1.000 237.79077 ? 79  LEU E C   1 
ATOM   8197 O O   . LEU E 5 99  ? 19.00022  43.29213  45.55502  1.000 237.87574 ? 79  LEU E O   1 
ATOM   8198 C CB  . LEU E 5 99  ? 18.43098  40.99936  43.35864  1.000 231.74525 ? 79  LEU E CB  1 
ATOM   8199 C CG  . LEU E 5 99  ? 17.66547  41.78295  42.28651  1.000 229.99792 ? 79  LEU E CG  1 
ATOM   8200 C CD1 . LEU E 5 99  ? 18.51710  41.99420  41.04299  1.000 232.09893 ? 79  LEU E CD1 1 
ATOM   8201 C CD2 . LEU E 5 99  ? 16.35932  41.08461  41.93495  1.000 223.95150 ? 79  LEU E CD2 1 
ATOM   8202 N N   . THR E 5 100 ? 19.65084  43.99416  43.51294  1.000 239.44709 ? 80  THR E N   1 
ATOM   8203 C CA  . THR E 5 100 ? 19.53814  45.41222  43.82363  1.000 240.47280 ? 80  THR E CA  1 
ATOM   8204 C C   . THR E 5 100 ? 18.83865  46.14161  42.68571  1.000 238.52136 ? 80  THR E C   1 
ATOM   8205 O O   . THR E 5 100 ? 19.12741  45.89589  41.51178  1.000 238.94451 ? 80  THR E O   1 
ATOM   8206 C CB  . THR E 5 100 ? 20.92583  46.02597  44.08073  1.000 244.95337 ? 80  THR E CB  1 
ATOM   8207 O OG1 . THR E 5 100 ? 21.30506  45.80032  45.44441  1.000 246.22516 ? 80  THR E OG1 1 
ATOM   8208 C CG2 . THR E 5 100 ? 20.93859  47.52204  43.78889  1.000 246.51018 ? 80  THR E CG2 1 
ATOM   8209 N N   . ILE E 5 101 ? 17.91385  47.03150  43.04117  1.000 234.54791 ? 81  ILE E N   1 
ATOM   8210 C CA  . ILE E 5 101 ? 17.22228  47.89313  42.08824  1.000 232.87589 ? 81  ILE E CA  1 
ATOM   8211 C C   . ILE E 5 101 ? 17.79977  49.29346  42.24729  1.000 235.81018 ? 81  ILE E C   1 
ATOM   8212 O O   . ILE E 5 101 ? 17.63614  49.92361  43.29911  1.000 235.91774 ? 81  ILE E O   1 
ATOM   8213 C CB  . ILE E 5 101 ? 15.70404  47.89097  42.31016  1.000 228.54247 ? 81  ILE E CB  1 
ATOM   8214 C CG1 . ILE E 5 101 ? 15.24711  46.54226  42.86845  1.000 226.61380 ? 81  ILE E CG1 1 
ATOM   8215 C CG2 . ILE E 5 101 ? 14.97719  48.19396  41.00827  1.000 226.34537 ? 81  ILE E CG2 1 
ATOM   8216 C CD1 . ILE E 5 101 ? 13.76593  46.47857  43.17226  1.000 223.07914 ? 81  ILE E CD1 1 
ATOM   8217 N N   . SER E 5 102 ? 18.47276  49.78615  41.20311  1.000 240.33789 ? 82  SER E N   1 
ATOM   8218 C CA  . SER E 5 102 ? 19.15233  51.07609  41.29902  1.000 243.94336 ? 82  SER E CA  1 
ATOM   8219 C C   . SER E 5 102 ? 18.16695  52.21198  41.54787  1.000 241.72779 ? 82  SER E C   1 
ATOM   8220 O O   . SER E 5 102 ? 18.44579  53.12412  42.33510  1.000 243.34733 ? 82  SER E O   1 
ATOM   8221 C CB  . SER E 5 102 ? 19.96037  51.33878  40.02840  1.000 247.79030 ? 82  SER E CB  1 
ATOM   8222 O OG  . SER E 5 102 ? 20.87351  50.28476  39.77847  1.000 250.16254 ? 82  SER E OG  1 
ATOM   8223 N N   . SER E 5 103 ? 17.01097  52.17672  40.88713  1.000 245.26834 ? 83  SER E N   1 
ATOM   8224 C CA  . SER E 5 103 ? 15.98924  53.21287  41.04257  1.000 242.91928 ? 83  SER E CA  1 
ATOM   8225 C C   . SER E 5 103 ? 14.62397  52.53546  40.97274  1.000 237.89602 ? 83  SER E C   1 
ATOM   8226 O O   . SER E 5 103 ? 14.17181  52.14857  39.89125  1.000 236.13034 ? 83  SER E O   1 
ATOM   8227 C CB  . SER E 5 103 ? 16.13379  54.29446  39.97861  1.000 244.88918 ? 83  SER E CB  1 
ATOM   8228 O OG  . SER E 5 103 ? 16.17828  53.72873  38.68070  1.000 245.15164 ? 83  SER E OG  1 
ATOM   8229 N N   . VAL E 5 104 ? 13.97301  52.39880  42.13085  1.000 235.01492 ? 84  VAL E N   1 
ATOM   8230 C CA  . VAL E 5 104 ? 12.68505  51.71923  42.19339  1.000 230.80727 ? 84  VAL E CA  1 
ATOM   8231 C C   . VAL E 5 104 ? 11.63968  52.50343  41.41153  1.000 228.10438 ? 84  VAL E C   1 
ATOM   8232 O O   . VAL E 5 104 ? 11.58431  53.73887  41.46977  1.000 229.10617 ? 84  VAL E O   1 
ATOM   8233 C CB  . VAL E 5 104 ? 12.26086  51.52779  43.65976  1.000 230.76629 ? 84  VAL E CB  1 
ATOM   8234 C CG1 . VAL E 5 104 ? 10.83149  51.01156  43.75014  1.000 227.11196 ? 84  VAL E CG1 1 
ATOM   8235 C CG2 . VAL E 5 104 ? 13.21541  50.57749  44.36555  1.000 233.21625 ? 84  VAL E CG2 1 
ATOM   8236 N N   . LYS E 5 105 ? 10.80763  51.78246  40.66472  1.000 228.95621 ? 85  LYS E N   1 
ATOM   8237 C CA  . LYS E 5 105 ? 9.71242   52.36731  39.90731  1.000 225.88921 ? 85  LYS E CA  1 
ATOM   8238 C C   . LYS E 5 105 ? 8.37831   51.85528  40.43657  1.000 222.19566 ? 85  LYS E C   1 
ATOM   8239 O O   . LYS E 5 105 ? 8.31376   50.91858  41.23694  1.000 222.32897 ? 85  LYS E O   1 
ATOM   8240 C CB  . LYS E 5 105 ? 9.84343   52.05755  38.41128  1.000 225.46421 ? 85  LYS E CB  1 
ATOM   8241 C CG  . LYS E 5 105 ? 10.99328  52.77375  37.72819  1.000 229.82276 ? 85  LYS E CG  1 
ATOM   8242 C CD  . LYS E 5 105 ? 10.64232  53.08595  36.28531  1.000 229.40082 ? 85  LYS E CD  1 
ATOM   8243 C CE  . LYS E 5 105 ? 9.39092   53.94888  36.21027  1.000 225.98519 ? 85  LYS E CE  1 
ATOM   8244 N NZ  . LYS E 5 105 ? 8.89042   54.10140  34.81658  1.000 224.25118 ? 85  LYS E NZ  1 
ATOM   8245 N N   . ALA E 5 106 ? 7.30259   52.48801  39.97390  1.000 225.29721 ? 86  ALA E N   1 
ATOM   8246 C CA  . ALA E 5 106 ? 5.95015   52.14290  40.38803  1.000 221.34770 ? 86  ALA E CA  1 
ATOM   8247 C C   . ALA E 5 106 ? 5.33967   51.02791  39.54898  1.000 215.19073 ? 86  ALA E C   1 
ATOM   8248 O O   . ALA E 5 106 ? 4.15771   50.71459  39.72311  1.000 210.74274 ? 86  ALA E O   1 
ATOM   8249 C CB  . ALA E 5 106 ? 5.05130   53.38100  40.33673  1.000 218.03830 ? 86  ALA E CB  1 
ATOM   8250 N N   . GLU E 5 107 ? 6.11291   50.42371  38.64746  1.000 225.87441 ? 87  GLU E N   1 
ATOM   8251 C CA  . GLU E 5 107 ? 5.61036   49.35239  37.79947  1.000 220.59126 ? 87  GLU E CA  1 
ATOM   8252 C C   . GLU E 5 107 ? 6.07084   47.97141  38.23968  1.000 224.19926 ? 87  GLU E C   1 
ATOM   8253 O O   . GLU E 5 107 ? 5.44891   46.97649  37.85102  1.000 217.94889 ? 87  GLU E O   1 
ATOM   8254 C CB  . GLU E 5 107 ? 6.04259   49.58049  36.34575  1.000 220.45951 ? 87  GLU E CB  1 
ATOM   8255 C CG  . GLU E 5 107 ? 7.53294   49.39389  36.10780  1.000 228.06896 ? 87  GLU E CG  1 
ATOM   8256 C CD  . GLU E 5 107 ? 8.14356   50.53045  35.31326  1.000 231.36385 ? 87  GLU E CD  1 
ATOM   8257 O OE1 . GLU E 5 107 ? 7.44755   51.54367  35.09130  1.000 229.86975 ? 87  GLU E OE1 1 
ATOM   8258 O OE2 . GLU E 5 107 ? 9.32061   50.41131  34.91292  1.000 235.88167 ? 87  GLU E OE2 1 
ATOM   8259 N N   . ASP E 5 108 ? 7.13345   47.88552  39.03811  1.000 218.71802 ? 88  ASP E N   1 
ATOM   8260 C CA  . ASP E 5 108 ? 7.67833   46.59226  39.43048  1.000 220.17785 ? 88  ASP E CA  1 
ATOM   8261 C C   . ASP E 5 108 ? 7.52234   46.33484  40.92495  1.000 221.43343 ? 88  ASP E C   1 
ATOM   8262 O O   . ASP E 5 108 ? 8.51425   46.09484  41.62095  1.000 224.65421 ? 88  ASP E O   1 
ATOM   8263 C CB  . ASP E 5 108 ? 9.15407   46.50083  39.02642  1.000 223.53005 ? 88  ASP E CB  1 
ATOM   8264 C CG  . ASP E 5 108 ? 9.94138   47.74525  39.39395  1.000 226.96839 ? 88  ASP E CG  1 
ATOM   8265 O OD1 . ASP E 5 108 ? 9.44117   48.56002  40.19590  1.000 226.86849 ? 88  ASP E OD1 1 
ATOM   8266 O OD2 . ASP E 5 108 ? 11.06374  47.91139  38.87016  1.000 230.01281 ? 88  ASP E OD2 1 
ATOM   8267 N N   . LEU E 5 109 ? 6.28803   46.37758  41.42799  1.000 216.59931 ? 89  LEU E N   1 
ATOM   8268 C CA  . LEU E 5 109 ? 6.01554   46.07734  42.83676  1.000 217.14891 ? 89  LEU E CA  1 
ATOM   8269 C C   . LEU E 5 109 ? 5.63084   44.60922  42.99546  1.000 215.39506 ? 89  LEU E C   1 
ATOM   8270 O O   . LEU E 5 109 ? 4.53336   44.26625  43.42090  1.000 213.49484 ? 89  LEU E O   1 
ATOM   8271 C CB  . LEU E 5 109 ? 4.92247   47.00080  43.38403  1.000 215.38493 ? 89  LEU E CB  1 
ATOM   8272 C CG  . LEU E 5 109 ? 3.58533   47.27773  42.67716  1.000 211.33258 ? 89  LEU E CG  1 
ATOM   8273 C CD1 . LEU E 5 109 ? 2.44848   46.43388  43.23515  1.000 206.90587 ? 89  LEU E CD1 1 
ATOM   8274 C CD2 . LEU E 5 109 ? 3.22170   48.76183  42.75780  1.000 215.63197 ? 89  LEU E CD2 1 
ATOM   8275 N N   . ALA E 5 110 ? 6.55225   43.72660  42.64268  1.000 221.15593 ? 90  ALA E N   1 
ATOM   8276 C CA  . ALA E 5 110 ? 6.23016   42.31430  42.55831  1.000 213.34607 ? 90  ALA E CA  1 
ATOM   8277 C C   . ALA E 5 110 ? 7.01794   41.49987  43.57639  1.000 219.05776 ? 90  ALA E C   1 
ATOM   8278 O O   . ALA E 5 110 ? 8.04967   41.93144  44.10052  1.000 223.76762 ? 90  ALA E O   1 
ATOM   8279 C CB  . ALA E 5 110 ? 6.47589   41.77383  41.14561  1.000 206.26866 ? 90  ALA E CB  1 
ATOM   8280 N N   . VAL E 5 111 ? 6.48995   40.31206  43.86646  1.000 206.10239 ? 91  VAL E N   1 
ATOM   8281 C CA  . VAL E 5 111 ? 7.17284   39.36978  44.74410  1.000 212.37931 ? 91  VAL E CA  1 
ATOM   8282 C C   . VAL E 5 111 ? 8.33163   38.74505  43.97832  1.000 210.76829 ? 91  VAL E C   1 
ATOM   8283 O O   . VAL E 5 111 ? 8.12878   38.05691  42.97129  1.000 205.07559 ? 91  VAL E O   1 
ATOM   8284 C CB  . VAL E 5 111 ? 6.20306   38.29657  45.25389  1.000 212.62040 ? 91  VAL E CB  1 
ATOM   8285 C CG1 . VAL E 5 111 ? 6.85381   37.46036  46.35136  1.000 218.13305 ? 91  VAL E CG1 1 
ATOM   8286 C CG2 . VAL E 5 111 ? 4.90889   38.93103  45.74745  1.000 213.78175 ? 91  VAL E CG2 1 
ATOM   8287 N N   . TYR E 5 112 ? 9.55321   38.98731  44.44602  1.000 211.64940 ? 92  TYR E N   1 
ATOM   8288 C CA  . TYR E 5 112 ? 10.74234  38.43884  43.80658  1.000 211.57011 ? 92  TYR E CA  1 
ATOM   8289 C C   . TYR E 5 112 ? 11.07526  37.08407  44.41468  1.000 213.07679 ? 92  TYR E C   1 
ATOM   8290 O O   . TYR E 5 112 ? 11.07728  36.93004  45.63963  1.000 217.52199 ? 92  TYR E O   1 
ATOM   8291 C CB  . TYR E 5 112 ? 11.92792  39.39166  43.95017  1.000 216.27940 ? 92  TYR E CB  1 
ATOM   8292 C CG  . TYR E 5 112 ? 11.72194  40.71268  43.25046  1.000 215.52269 ? 92  TYR E CG  1 
ATOM   8293 C CD1 . TYR E 5 112 ? 11.84241  40.81195  41.87197  1.000 212.77287 ? 92  TYR E CD1 1 
ATOM   8294 C CD2 . TYR E 5 112 ? 11.40328  41.85913  43.96594  1.000 218.23365 ? 92  TYR E CD2 1 
ATOM   8295 C CE1 . TYR E 5 112 ? 11.65185  42.01442  41.22327  1.000 213.12529 ? 92  TYR E CE1 1 
ATOM   8296 C CE2 . TYR E 5 112 ? 11.21112  43.06923  43.32580  1.000 218.26803 ? 92  TYR E CE2 1 
ATOM   8297 C CZ  . TYR E 5 112 ? 11.33608  43.14064  41.95357  1.000 215.81953 ? 92  TYR E CZ  1 
ATOM   8298 O OH  . TYR E 5 112 ? 11.14604  44.34202  41.30892  1.000 217.10982 ? 92  TYR E OH  1 
ATOM   8299 N N   . TYR E 5 113 ? 11.35576  36.10569  43.55733  1.000 203.48530 ? 93  TYR E N   1 
ATOM   8300 C CA  . TYR E 5 113 ? 11.60103  34.73909  43.99176  1.000 204.49486 ? 93  TYR E CA  1 
ATOM   8301 C C   . TYR E 5 113 ? 13.03689  34.32876  43.70145  1.000 207.83303 ? 93  TYR E C   1 
ATOM   8302 O O   . TYR E 5 113 ? 13.60206  34.68210  42.66194  1.000 206.91131 ? 93  TYR E O   1 
ATOM   8303 C CB  . TYR E 5 113 ? 10.62565  33.76564  43.32774  1.000 199.20450 ? 93  TYR E CB  1 
ATOM   8304 C CG  . TYR E 5 113 ? 9.28953   33.73023  44.02561  1.000 199.53031 ? 93  TYR E CG  1 
ATOM   8305 C CD1 . TYR E 5 113 ? 9.13254   33.04174  45.22051  1.000 204.29548 ? 93  TYR E CD1 1 
ATOM   8306 C CD2 . TYR E 5 113 ? 8.19169   34.39974  43.50496  1.000 195.67451 ? 93  TYR E CD2 1 
ATOM   8307 C CE1 . TYR E 5 113 ? 7.91810   33.01183  45.87300  1.000 206.21563 ? 93  TYR E CE1 1 
ATOM   8308 C CE2 . TYR E 5 113 ? 6.97241   34.37554  44.15040  1.000 196.40601 ? 93  TYR E CE2 1 
ATOM   8309 C CZ  . TYR E 5 113 ? 6.84029   33.67993  45.33349  1.000 202.91245 ? 93  TYR E CZ  1 
ATOM   8310 O OH  . TYR E 5 113 ? 5.62512   33.65404  45.97842  1.000 205.93449 ? 93  TYR E OH  1 
ATOM   8311 N N   . CYS E 5 114 ? 13.61080  33.57126  44.63196  1.000 213.49620 ? 94  CYS E N   1 
ATOM   8312 C CA  . CYS E 5 114 ? 15.00486  33.14672  44.59575  1.000 215.69222 ? 94  CYS E CA  1 
ATOM   8313 C C   . CYS E 5 114 ? 15.03624  31.64395  44.34931  1.000 214.08867 ? 94  CYS E C   1 
ATOM   8314 O O   . CYS E 5 114 ? 14.67557  30.85832  45.23193  1.000 215.34833 ? 94  CYS E O   1 
ATOM   8315 C CB  . CYS E 5 114 ? 15.69842  33.51037  45.90601  1.000 220.64626 ? 94  CYS E CB  1 
ATOM   8316 S SG  . CYS E 5 114 ? 17.32737  32.79144  46.15494  1.000 224.04617 ? 94  CYS E SG  1 
ATOM   8317 N N   . GLN E 5 115 ? 15.46563  31.24532  43.15531  1.000 211.54702 ? 95  GLN E N   1 
ATOM   8318 C CA  . GLN E 5 115 ? 15.44357  29.84991  42.74345  1.000 209.22926 ? 95  GLN E CA  1 
ATOM   8319 C C   . GLN E 5 115 ? 16.84938  29.37109  42.41374  1.000 211.39103 ? 95  GLN E C   1 
ATOM   8320 O O   . GLN E 5 115 ? 17.63120  30.08995  41.78326  1.000 212.56265 ? 95  GLN E O   1 
ATOM   8321 C CB  . GLN E 5 115 ? 14.53055  29.64954  41.53144  1.000 203.17929 ? 95  GLN E CB  1 
ATOM   8322 C CG  . GLN E 5 115 ? 14.31811  28.19595  41.14826  1.000 199.78635 ? 95  GLN E CG  1 
ATOM   8323 C CD  . GLN E 5 115 ? 15.03516  27.81568  39.86960  1.000 197.32459 ? 95  GLN E CD  1 
ATOM   8324 O OE1 . GLN E 5 115 ? 15.93193  28.52358  39.41126  1.000 200.52071 ? 95  GLN E OE1 1 
ATOM   8325 N NE2 . GLN E 5 115 ? 14.63800  26.69293  39.28204  1.000 193.29810 ? 95  GLN E NE2 1 
ATOM   8326 N N   . GLN E 5 116 ? 17.15973  28.15240  42.84223  1.000 206.31561 ? 96  GLN E N   1 
ATOM   8327 C CA  . GLN E 5 116 ? 18.42386  27.50299  42.53744  1.000 207.60919 ? 96  GLN E CA  1 
ATOM   8328 C C   . GLN E 5 116 ? 18.22000  26.43851  41.46718  1.000 203.54121 ? 96  GLN E C   1 
ATOM   8329 O O   . GLN E 5 116 ? 17.14329  25.84826  41.34827  1.000 200.19198 ? 96  GLN E O   1 
ATOM   8330 C CB  . GLN E 5 116 ? 19.02964  26.87150  43.79462  1.000 210.95458 ? 96  GLN E CB  1 
ATOM   8331 C CG  . GLN E 5 116 ? 18.10416  25.90043  44.52423  1.000 209.60977 ? 96  GLN E CG  1 
ATOM   8332 C CD  . GLN E 5 116 ? 18.24327  24.46576  44.04551  1.000 206.85658 ? 96  GLN E CD  1 
ATOM   8333 O OE1 . GLN E 5 116 ? 19.08113  24.15772  43.19821  1.000 205.92849 ? 96  GLN E OE1 1 
ATOM   8334 N NE2 . GLN E 5 116 ? 17.42034  23.57886  44.59291  1.000 205.55239 ? 96  GLN E NE2 1 
ATOM   8335 N N   . TYR E 5 117 ? 19.26721  26.20286  40.68305  1.000 204.03108 ? 97  TYR E N   1 
ATOM   8336 C CA  . TYR E 5 117 ? 19.28482  25.11968  39.70432  1.000 202.44317 ? 97  TYR E CA  1 
ATOM   8337 C C   . TYR E 5 117 ? 20.67850  24.50056  39.66547  1.000 204.83876 ? 97  TYR E C   1 
ATOM   8338 O O   . TYR E 5 117 ? 21.25539  24.25507  38.60560  1.000 204.58482 ? 97  TYR E O   1 
ATOM   8339 C CB  . TYR E 5 117 ? 18.82847  25.60205  38.32497  1.000 200.04727 ? 97  TYR E CB  1 
ATOM   8340 C CG  . TYR E 5 117 ? 19.55825  26.81019  37.77473  1.000 201.19997 ? 97  TYR E CG  1 
ATOM   8341 C CD1 . TYR E 5 117 ? 19.21097  28.09669  38.16747  1.000 201.64148 ? 97  TYR E CD1 1 
ATOM   8342 C CD2 . TYR E 5 117 ? 20.57009  26.66515  36.83478  1.000 202.47608 ? 97  TYR E CD2 1 
ATOM   8343 C CE1 . TYR E 5 117 ? 19.86791  29.20177  37.65812  1.000 205.34462 ? 97  TYR E CE1 1 
ATOM   8344 C CE2 . TYR E 5 117 ? 21.23234  27.76362  36.32036  1.000 206.35267 ? 97  TYR E CE2 1 
ATOM   8345 C CZ  . TYR E 5 117 ? 20.87732  29.02931  36.73479  1.000 207.74072 ? 97  TYR E CZ  1 
ATOM   8346 O OH  . TYR E 5 117 ? 21.53342  30.12619  36.22390  1.000 211.99240 ? 97  TYR E OH  1 
ATOM   8347 N N   . TYR E 5 118 ? 21.22760  24.23467  40.85052  1.000 213.62971 ? 98  TYR E N   1 
ATOM   8348 C CA  . TYR E 5 118 ? 22.55253  23.64605  40.99732  1.000 216.36070 ? 98  TYR E CA  1 
ATOM   8349 C C   . TYR E 5 118 ? 22.51114  22.12403  40.95842  1.000 213.39781 ? 98  TYR E C   1 
ATOM   8350 O O   . TYR E 5 118 ? 23.42220  21.49282  40.41184  1.000 213.66433 ? 98  TYR E O   1 
ATOM   8351 C CB  . TYR E 5 118 ? 23.18316  24.11840  42.30868  1.000 221.22134 ? 98  TYR E CB  1 
ATOM   8352 C CG  . TYR E 5 118 ? 24.66578  23.85953  42.42440  1.000 224.75514 ? 98  TYR E CG  1 
ATOM   8353 C CD1 . TYR E 5 118 ? 25.57035  24.54090  41.62360  1.000 226.67567 ? 98  TYR E CD1 1 
ATOM   8354 C CD2 . TYR E 5 118 ? 25.16315  22.95053  43.34955  1.000 226.61070 ? 98  TYR E CD2 1 
ATOM   8355 C CE1 . TYR E 5 118 ? 26.92610  24.31914  41.73286  1.000 230.01579 ? 98  TYR E CE1 1 
ATOM   8356 C CE2 . TYR E 5 118 ? 26.52100  22.71973  43.46430  1.000 229.68410 ? 98  TYR E CE2 1 
ATOM   8357 C CZ  . TYR E 5 118 ? 27.39780  23.40679  42.65209  1.000 231.18145 ? 98  TYR E CZ  1 
ATOM   8358 O OH  . TYR E 5 118 ? 28.75119  23.18325  42.76046  1.000 234.12404 ? 98  TYR E OH  1 
ATOM   8359 N N   . SER E 5 119 ? 21.46991  21.52549  41.53203  1.000 217.05386 ? 99  SER E N   1 
ATOM   8360 C CA  . SER E 5 119 ? 21.29434  20.08056  41.51340  1.000 213.49555 ? 99  SER E CA  1 
ATOM   8361 C C   . SER E 5 119 ? 19.81589  19.77043  41.68808  1.000 209.02162 ? 99  SER E C   1 
ATOM   8362 O O   . SER E 5 119 ? 19.04633  20.58887  42.19828  1.000 210.02992 ? 99  SER E O   1 
ATOM   8363 C CB  . SER E 5 119 ? 22.12448  19.39363  42.60361  1.000 217.28832 ? 99  SER E CB  1 
ATOM   8364 O OG  . SER E 5 119 ? 23.51175  19.54861  42.36244  1.000 221.03871 ? 99  SER E OG  1 
ATOM   8365 N N   . TYR E 5 120 ? 19.43047  18.57650  41.25268  1.000 213.25980 ? 100 TYR E N   1 
ATOM   8366 C CA  . TYR E 5 120 ? 18.04143  18.16138  41.36872  1.000 208.90020 ? 100 TYR E CA  1 
ATOM   8367 C C   . TYR E 5 120 ? 17.69658  17.87899  42.82965  1.000 211.84779 ? 100 TYR E C   1 
ATOM   8368 O O   . TYR E 5 120 ? 18.48407  17.25178  43.54494  1.000 215.08096 ? 100 TYR E O   1 
ATOM   8369 C CB  . TYR E 5 120 ? 17.78000  16.91750  40.51997  1.000 202.71797 ? 100 TYR E CB  1 
ATOM   8370 C CG  . TYR E 5 120 ? 17.65895  17.19758  39.03950  1.000 198.99365 ? 100 TYR E CG  1 
ATOM   8371 C CD1 . TYR E 5 120 ? 16.90803  18.26967  38.57577  1.000 199.08554 ? 100 TYR E CD1 1 
ATOM   8372 C CD2 . TYR E 5 120 ? 18.29896  16.39322  38.10593  1.000 196.11904 ? 100 TYR E CD2 1 
ATOM   8373 C CE1 . TYR E 5 120 ? 16.79504  18.53086  37.22377  1.000 196.39025 ? 100 TYR E CE1 1 
ATOM   8374 C CE2 . TYR E 5 120 ? 18.19255  16.64703  36.75119  1.000 193.71901 ? 100 TYR E CE2 1 
ATOM   8375 C CZ  . TYR E 5 120 ? 17.43931  17.71739  36.31628  1.000 193.82515 ? 100 TYR E CZ  1 
ATOM   8376 O OH  . TYR E 5 120 ? 17.32827  17.97771  34.96985  1.000 191.01275 ? 100 TYR E OH  1 
ATOM   8377 N N   . PRO E 5 121 ? 16.52414  18.32545  43.30539  1.000 200.13988 ? 101 PRO E N   1 
ATOM   8378 C CA  . PRO E 5 121 ? 15.53753  19.10569  42.55293  1.000 197.26449 ? 101 PRO E CA  1 
ATOM   8379 C C   . PRO E 5 121 ? 15.73483  20.61515  42.69020  1.000 201.30332 ? 101 PRO E C   1 
ATOM   8380 O O   . PRO E 5 121 ? 16.35658  21.06381  43.65350  1.000 206.50938 ? 101 PRO E O   1 
ATOM   8381 C CB  . PRO E 5 121 ? 14.21860  18.67684  43.18953  1.000 196.29603 ? 101 PRO E CB  1 
ATOM   8382 C CG  . PRO E 5 121 ? 14.58359  18.45330  44.61936  1.000 201.92927 ? 101 PRO E CG  1 
ATOM   8383 C CD  . PRO E 5 121 ? 16.00387  17.92536  44.62461  1.000 203.34345 ? 101 PRO E CD  1 
ATOM   8384 N N   . PRO E 5 122 ? 15.21410  21.38904  41.73474  1.000 195.61300 ? 102 PRO E N   1 
ATOM   8385 C CA  . PRO E 5 122 ? 15.30347  22.85447  41.82837  1.000 199.35743 ? 102 PRO E CA  1 
ATOM   8386 C C   . PRO E 5 122 ? 14.19914  23.40454  42.72079  1.000 200.96799 ? 102 PRO E C   1 
ATOM   8387 O O   . PRO E 5 122 ? 13.01379  23.15988  42.48548  1.000 197.18285 ? 102 PRO E O   1 
ATOM   8388 C CB  . PRO E 5 122 ? 15.13583  23.31011  40.37434  1.000 195.49641 ? 102 PRO E CB  1 
ATOM   8389 C CG  . PRO E 5 122 ? 14.29069  22.24676  39.75644  1.000 189.28406 ? 102 PRO E CG  1 
ATOM   8390 C CD  . PRO E 5 122 ? 14.64781  20.95007  40.44615  1.000 189.32996 ? 102 PRO E CD  1 
ATOM   8391 N N   . THR E 5 123 ? 14.59132  24.14963  43.74970  1.000 199.13058 ? 103 THR E N   1 
ATOM   8392 C CA  . THR E 5 123 ? 13.65521  24.73648  44.69554  1.000 201.65039 ? 103 THR E CA  1 
ATOM   8393 C C   . THR E 5 123 ? 13.69269  26.25612  44.59606  1.000 203.65081 ? 103 THR E C   1 
ATOM   8394 O O   . THR E 5 123 ? 14.70383  26.84666  44.20548  1.000 204.57706 ? 103 THR E O   1 
ATOM   8395 C CB  . THR E 5 123 ? 13.96896  24.30304  46.13193  1.000 206.36477 ? 103 THR E CB  1 
ATOM   8396 O OG1 . THR E 5 123 ? 15.29359  24.72322  46.48022  1.000 210.21621 ? 103 THR E OG1 1 
ATOM   8397 C CG2 . THR E 5 123 ? 13.86843  22.78932  46.26589  1.000 204.36191 ? 103 THR E CG2 1 
ATOM   8398 N N   . PHE E 5 124 ? 12.57606  26.88272  44.95360  1.000 207.48382 ? 104 PHE E N   1 
ATOM   8399 C CA  . PHE E 5 124 ? 12.43461  28.32791  44.91094  1.000 208.56973 ? 104 PHE E CA  1 
ATOM   8400 C C   . PHE E 5 124 ? 12.56371  28.91068  46.31674  1.000 213.56816 ? 104 PHE E C   1 
ATOM   8401 O O   . PHE E 5 124 ? 12.77091  28.19793  47.30177  1.000 216.78507 ? 104 PHE E O   1 
ATOM   8402 C CB  . PHE E 5 124 ? 11.09698  28.71345  44.27533  1.000 204.51635 ? 104 PHE E CB  1 
ATOM   8403 C CG  . PHE E 5 124 ? 11.06117  28.54580  42.78242  1.000 196.76441 ? 104 PHE E CG  1 
ATOM   8404 C CD1 . PHE E 5 124 ? 10.98722  27.28548  42.21240  1.000 193.52475 ? 104 PHE E CD1 1 
ATOM   8405 C CD2 . PHE E 5 124 ? 11.08703  29.65174  41.94903  1.000 193.62805 ? 104 PHE E CD2 1 
ATOM   8406 C CE1 . PHE E 5 124 ? 10.95033  27.13079  40.83899  1.000 187.41970 ? 104 PHE E CE1 1 
ATOM   8407 C CE2 . PHE E 5 124 ? 11.04954  29.50433  40.57440  1.000 189.04169 ? 104 PHE E CE2 1 
ATOM   8408 C CZ  . PHE E 5 124 ? 10.98096  28.24174  40.01888  1.000 186.46617 ? 104 PHE E CZ  1 
ATOM   8409 N N   . GLY E 5 125 ? 12.43769  30.23573  46.40568  1.000 214.36687 ? 105 GLY E N   1 
ATOM   8410 C CA  . GLY E 5 125 ? 12.50738  30.93474  47.66776  1.000 219.12418 ? 105 GLY E CA  1 
ATOM   8411 C C   . GLY E 5 125 ? 11.12997  31.28517  48.21347  1.000 220.35971 ? 105 GLY E C   1 
ATOM   8412 O O   . GLY E 5 125 ? 10.09172  30.97235  47.63592  1.000 217.83920 ? 105 GLY E O   1 
ATOM   8413 N N   . GLY E 5 126 ? 11.14387  31.95455  49.36893  1.000 223.83934 ? 106 GLY E N   1 
ATOM   8414 C CA  . GLY E 5 126 ? 9.90357   32.37480  49.99470  1.000 226.24875 ? 106 GLY E CA  1 
ATOM   8415 C C   . GLY E 5 126 ? 9.25994   33.58649  49.35952  1.000 223.17205 ? 106 GLY E C   1 
ATOM   8416 O O   . GLY E 5 126 ? 8.04726   33.77466  49.49930  1.000 223.36901 ? 106 GLY E O   1 
ATOM   8417 N N   . GLY E 5 127 ? 10.03497  34.40370  48.66735  1.000 223.51690 ? 107 GLY E N   1 
ATOM   8418 C CA  . GLY E 5 127 ? 9.50758   35.59648  48.03848  1.000 219.05918 ? 107 GLY E CA  1 
ATOM   8419 C C   . GLY E 5 127 ? 9.69008   36.82902  48.90501  1.000 223.56588 ? 107 GLY E C   1 
ATOM   8420 O O   . GLY E 5 127 ? 9.64186   36.77239  50.13882  1.000 228.89310 ? 107 GLY E O   1 
ATOM   8421 N N   . THR E 5 128 ? 9.91057   37.96754  48.24850  1.000 227.42253 ? 108 THR E N   1 
ATOM   8422 C CA  . THR E 5 128 ? 10.08337  39.25678  48.91790  1.000 231.46406 ? 108 THR E CA  1 
ATOM   8423 C C   . THR E 5 128 ? 9.08238   40.23284  48.30654  1.000 226.85683 ? 108 THR E C   1 
ATOM   8424 O O   . THR E 5 128 ? 9.34696   40.82154  47.25378  1.000 224.05082 ? 108 THR E O   1 
ATOM   8425 C CB  . THR E 5 128 ? 11.51560  39.77413  48.78056  1.000 233.54787 ? 108 THR E CB  1 
ATOM   8426 O OG1 . THR E 5 128 ? 11.85930  39.87961  47.39250  1.000 232.29801 ? 108 THR E OG1 1 
ATOM   8427 C CG2 . THR E 5 128 ? 12.49674  38.83890  49.47134  1.000 237.23624 ? 108 THR E CG2 1 
ATOM   8428 N N   . LYS E 5 129 ? 7.93070   40.38979  48.95800  1.000 226.55885 ? 109 LYS E N   1 
ATOM   8429 C CA  . LYS E 5 129 ? 6.93375   41.34250  48.48999  1.000 223.97256 ? 109 LYS E CA  1 
ATOM   8430 C C   . LYS E 5 129 ? 7.51199   42.75023  48.49262  1.000 224.72023 ? 109 LYS E C   1 
ATOM   8431 O O   . LYS E 5 129 ? 8.26747   43.12773  49.39244  1.000 229.74265 ? 109 LYS E O   1 
ATOM   8432 C CB  . LYS E 5 129 ? 5.68847   41.30074  49.37623  1.000 225.42506 ? 109 LYS E CB  1 
ATOM   8433 C CG  . LYS E 5 129 ? 5.08532   39.92689  49.59226  1.000 225.90445 ? 109 LYS E CG  1 
ATOM   8434 C CD  . LYS E 5 129 ? 3.85249   40.04238  50.47594  1.000 230.87018 ? 109 LYS E CD  1 
ATOM   8435 C CE  . LYS E 5 129 ? 3.34255   38.68739  50.92692  1.000 233.82624 ? 109 LYS E CE  1 
ATOM   8436 N NZ  . LYS E 5 129 ? 2.18556   38.82986  51.85376  1.000 240.42843 ? 109 LYS E NZ  1 
ATOM   8437 N N   . LEU E 5 130 ? 7.15248   43.53179  47.48112  1.000 225.72695 ? 110 LEU E N   1 
ATOM   8438 C CA  . LEU E 5 130 ? 7.58458   44.91905  47.38737  1.000 227.10083 ? 110 LEU E CA  1 
ATOM   8439 C C   . LEU E 5 130 ? 6.39703   45.83651  47.66250  1.000 226.33018 ? 110 LEU E C   1 
ATOM   8440 O O   . LEU E 5 130 ? 5.83239   46.46209  46.76217  1.000 222.92328 ? 110 LEU E O   1 
ATOM   8441 C CB  . LEU E 5 130 ? 8.21568   45.20448  46.01739  1.000 224.69917 ? 110 LEU E CB  1 
ATOM   8442 C CG  . LEU E 5 130 ? 8.86330   46.58891  45.90262  1.000 227.01637 ? 110 LEU E CG  1 
ATOM   8443 C CD1 . LEU E 5 130 ? 9.91176   46.77248  46.98635  1.000 231.26809 ? 110 LEU E CD1 1 
ATOM   8444 C CD2 . LEU E 5 130 ? 9.47070   46.80695  44.52919  1.000 227.80918 ? 110 LEU E CD2 1 
ATOM   8445 N N   . GLU E 5 131 ? 6.00312   45.89456  48.93041  0.000 224.09885 ? 111 GLU E N   1 
ATOM   8446 C CA  . GLU E 5 131 ? 5.13106   46.96800  49.37568  0.000 224.40681 ? 111 GLU E CA  1 
ATOM   8447 C C   . GLU E 5 131 ? 5.89395   48.28449  49.29102  0.000 226.03874 ? 111 GLU E C   1 
ATOM   8448 O O   . GLU E 5 131 ? 7.12245   48.31696  49.38904  0.000 229.20304 ? 111 GLU E O   1 
ATOM   8449 C CB  . GLU E 5 131 ? 4.64393   46.70364  50.80054  0.000 229.88321 ? 111 GLU E CB  1 
ATOM   8450 C CG  . GLU E 5 131 ? 3.89284   45.38547  50.94524  0.000 230.16065 ? 111 GLU E CG  1 
ATOM   8451 C CD  . GLU E 5 131 ? 3.50965   45.07345  52.37815  0.000 236.80061 ? 111 GLU E CD  1 
ATOM   8452 O OE1 . GLU E 5 131 ? 4.08816   45.68676  53.29902  0.000 240.48110 ? 111 GLU E OE1 1 
ATOM   8453 O OE2 . GLU E 5 131 ? 2.62774   44.21247  52.58259  0.000 238.70575 ? 111 GLU E OE2 1 
ATOM   8454 N N   . ILE E 5 132 ? 5.17024   49.37677  49.06585  0.000 224.85311 ? 112 ILE E N   1 
ATOM   8455 C CA  . ILE E 5 132 ? 5.80851   50.66195  48.81116  0.000 226.98872 ? 112 ILE E CA  1 
ATOM   8456 C C   . ILE E 5 132 ? 5.20939   51.73221  49.71065  0.000 228.49858 ? 112 ILE E C   1 
ATOM   8457 O O   . ILE E 5 132 ? 4.01171   51.70855  50.01638  0.000 226.74220 ? 112 ILE E O   1 
ATOM   8458 C CB  . ILE E 5 132 ? 5.69850   51.07838  47.32863  0.000 223.31881 ? 112 ILE E CB  1 
ATOM   8459 C CG1 . ILE E 5 132 ? 4.23633   51.18982  46.90137  0.000 217.86029 ? 112 ILE E CG1 1 
ATOM   8460 C CG2 . ILE E 5 132 ? 6.44960   50.09773  46.43847  0.000 222.08505 ? 112 ILE E CG2 1 
ATOM   8461 C CD1 . ILE E 5 132 ? 4.06658   51.65752  45.47884  0.000 211.77712 ? 112 ILE E CD1 1 
ATOM   8462 N N   . LYS E 5 133 ? 6.05455   52.66861  50.13880  0.000 223.66605 ? 113 LYS E N   1 
ATOM   8463 C CA  . LYS E 5 133 ? 5.59736   53.84212  50.87011  0.000 225.04557 ? 113 LYS E CA  1 
ATOM   8464 C C   . LYS E 5 133 ? 5.01575   54.84562  49.88256  0.000 222.67408 ? 113 LYS E C   1 
ATOM   8465 O O   . LYS E 5 133 ? 5.68881   55.25364  48.92990  0.000 221.66834 ? 113 LYS E O   1 
ATOM   8466 C CB  . LYS E 5 133 ? 6.74051   54.46255  51.67049  0.000 228.19795 ? 113 LYS E CB  1 
ATOM   8467 C CG  . LYS E 5 133 ? 7.18315   53.63256  52.86605  0.000 230.86918 ? 113 LYS E CG  1 
ATOM   8468 C CD  . LYS E 5 133 ? 8.22759   54.36619  53.69214  0.000 234.02262 ? 113 LYS E CD  1 
ATOM   8469 C CE  . LYS E 5 133 ? 8.62487   53.56347  54.92009  0.000 236.69715 ? 113 LYS E CE  1 
ATOM   8470 N NZ  . LYS E 5 133 ? 9.63465   54.27811  55.74864  0.000 239.85049 ? 113 LYS E NZ  1 
ATOM   8471 N N   . ARG E 5 134 ? 3.76773   55.23663  50.11053  0.000 222.87254 ? 114 ARG E N   1 
ATOM   8472 C CA  . ARG E 5 134 ? 3.01754   56.09503  49.20864  0.000 218.78324 ? 114 ARG E CA  1 
ATOM   8473 C C   . ARG E 5 134 ? 2.64368   57.38327  49.93032  0.000 220.31475 ? 114 ARG E C   1 
ATOM   8474 O O   . ARG E 5 134 ? 2.52307   57.40782  51.15831  0.000 223.88067 ? 114 ARG E O   1 
ATOM   8475 C CB  . ARG E 5 134 ? 1.75826   55.36165  48.70737  0.000 213.11096 ? 114 ARG E CB  1 
ATOM   8476 C CG  . ARG E 5 134 ? 0.74453   56.19814  47.94317  0.000 209.01765 ? 114 ARG E CG  1 
ATOM   8477 C CD  . ARG E 5 134 ? 1.07390   56.28096  46.46539  0.000 204.26824 ? 114 ARG E CD  1 
ATOM   8478 N NE  . ARG E 5 134 ? 0.03768   56.99831  45.73309  0.000 202.47733 ? 114 ARG E NE  1 
ATOM   8479 C CZ  . ARG E 5 134 ? -0.02336  58.31837  45.62831  0.000 204.36898 ? 114 ARG E CZ  1 
ATOM   8480 N NH1 . ARG E 5 134 ? 0.88651   59.09792  46.18784  0.000 207.29295 ? 114 ARG E NH1 1 
ATOM   8481 N NH2 . ARG E 5 134 ? -1.02357  58.87017  44.94746  0.000 203.45951 ? 114 ARG E NH2 1 
ATOM   8482 N N   . ALA E 5 135 ? 2.48925   58.46402  49.16813  0.000 211.35094 ? 115 ALA E N   1 
ATOM   8483 C CA  . ALA E 5 135 ? 1.94978   59.68926  49.74023  0.000 213.87736 ? 115 ALA E CA  1 
ATOM   8484 C C   . ALA E 5 135 ? 0.52356   59.43798  50.21235  0.000 213.06648 ? 115 ALA E C   1 
ATOM   8485 O O   . ALA E 5 135 ? -0.30419  58.91414  49.46116  0.000 210.19193 ? 115 ALA E O   1 
ATOM   8486 C CB  . ALA E 5 135 ? 1.98679   60.82209  48.71435  0.000 214.05961 ? 115 ALA E CB  1 
ATOM   8487 N N   . ASP E 5 136 ? 0.24627   59.80082  51.46512  0.000 208.76338 ? 116 ASP E N   1 
ATOM   8488 C CA  . ASP E 5 136 ? -1.01914  59.44659  52.10010  0.000 208.50785 ? 116 ASP E CA  1 
ATOM   8489 C C   . ASP E 5 136 ? -2.20781  59.95095  51.29042  0.000 206.94531 ? 116 ASP E C   1 
ATOM   8490 O O   . ASP E 5 136 ? -2.23530  61.10396  50.85068  0.000 207.97289 ? 116 ASP E O   1 
ATOM   8491 C CB  . ASP E 5 136 ? -1.06866  60.00890  53.52122  0.000 212.28264 ? 116 ASP E CB  1 
ATOM   8492 C CG  . ASP E 5 136 ? -0.11451  59.29735  54.46038  0.000 213.82246 ? 116 ASP E CG  1 
ATOM   8493 O OD1 . ASP E 5 136 ? 0.12200   58.08644  54.26490  0.000 211.70781 ? 116 ASP E OD1 1 
ATOM   8494 O OD2 . ASP E 5 136 ? 0.39635   59.94651  55.39677  0.000 217.27926 ? 116 ASP E OD2 1 
ATOM   8495 N N   . ALA E 5 137 ? -3.18852  59.07260  51.08837  1.000 199.56221 ? 117 ALA E N   1 
ATOM   8496 C CA  . ALA E 5 137 ? -4.38399  59.37414  50.31663  1.000 197.95354 ? 117 ALA E CA  1 
ATOM   8497 C C   . ALA E 5 137 ? -5.61802  58.94666  51.10088  1.000 198.33333 ? 117 ALA E C   1 
ATOM   8498 O O   . ALA E 5 137 ? -5.53385  58.21285  52.08883  1.000 199.27402 ? 117 ALA E O   1 
ATOM   8499 C CB  . ALA E 5 137 ? -4.35234  58.68381  48.94644  1.000 194.34545 ? 117 ALA E CB  1 
ATOM   8500 N N   . ALA E 5 138 ? -6.80040  59.41666  50.63041  1.000 202.58654 ? 118 ALA E N   1 
ATOM   8501 C CA  . ALA E 5 138 ? -8.07370  59.20253  51.29998  1.000 203.32356 ? 118 ALA E CA  1 
ATOM   8502 C C   . ALA E 5 138 ? -8.86649  58.08249  50.63359  1.000 200.25422 ? 118 ALA E C   1 
ATOM   8503 O O   . ALA E 5 138 ? -8.77993  57.88725  49.41725  1.000 197.60646 ? 118 ALA E O   1 
ATOM   8504 C CB  . ALA E 5 138 ? -8.90912  60.48624  51.29187  1.000 205.12628 ? 118 ALA E CB  1 
ATOM   8505 N N   . PRO E 5 139 ? -9.64797  57.33138  51.41012  1.000 205.13088 ? 119 PRO E N   1 
ATOM   8506 C CA  . PRO E 5 139 ? -10.46204 56.25891  50.82568  1.000 204.08647 ? 119 PRO E CA  1 
ATOM   8507 C C   . PRO E 5 139 ? -11.76956 56.77929  50.24898  1.000 200.77731 ? 119 PRO E C   1 
ATOM   8508 O O   . PRO E 5 139 ? -12.40951 57.67543  50.80524  1.000 203.00918 ? 119 PRO E O   1 
ATOM   8509 C CB  . PRO E 5 139 ? -10.71506 55.32630  52.01610  1.000 211.79760 ? 119 PRO E CB  1 
ATOM   8510 C CG  . PRO E 5 139 ? -10.69672 56.23643  53.19630  1.000 215.97483 ? 119 PRO E CG  1 
ATOM   8511 C CD  . PRO E 5 139 ? -9.69797  57.32469  52.88345  1.000 212.00960 ? 119 PRO E CD  1 
ATOM   8512 N N   . THR E 5 140 ? -12.16657 56.19478  49.11996  1.000 214.50677 ? 120 THR E N   1 
ATOM   8513 C CA  . THR E 5 140 ? -13.39934 56.56333  48.42359  1.000 213.89059 ? 120 THR E CA  1 
ATOM   8514 C C   . THR E 5 140 ? -14.43344 55.47228  48.68946  1.000 213.77405 ? 120 THR E C   1 
ATOM   8515 O O   . THR E 5 140 ? -14.56152 54.51026  47.93147  1.000 211.87415 ? 120 THR E O   1 
ATOM   8516 C CB  . THR E 5 140 ? -13.14413 56.75341  46.93217  1.000 211.32370 ? 120 THR E CB  1 
ATOM   8517 O OG1 . THR E 5 140 ? -12.48252 55.59542  46.40638  1.000 208.74624 ? 120 THR E OG1 1 
ATOM   8518 C CG2 . THR E 5 140 ? -12.27431 57.98081  46.69323  1.000 212.44893 ? 120 THR E CG2 1 
ATOM   8519 N N   . VAL E 5 141 ? -15.17993 55.63335  49.78022  1.000 212.94272 ? 121 VAL E N   1 
ATOM   8520 C CA  . VAL E 5 141 ? -16.17127 54.64772  50.19675  1.000 213.08898 ? 121 VAL E CA  1 
ATOM   8521 C C   . VAL E 5 141 ? -17.43647 54.80866  49.36130  1.000 212.22490 ? 121 VAL E C   1 
ATOM   8522 O O   . VAL E 5 141 ? -17.78038 55.91049  48.91841  1.000 212.81785 ? 121 VAL E O   1 
ATOM   8523 C CB  . VAL E 5 141 ? -16.45450 54.78778  51.70792  1.000 218.42063 ? 121 VAL E CB  1 
ATOM   8524 C CG1 . VAL E 5 141 ? -16.99903 56.17032  52.02624  1.000 219.23846 ? 121 VAL E CG1 1 
ATOM   8525 C CG2 . VAL E 5 141 ? -17.40380 53.70127  52.19525  1.000 225.74766 ? 121 VAL E CG2 1 
ATOM   8526 N N   . SER E 5 142 ? -18.12791 53.69367  49.12167  1.000 227.28679 ? 122 SER E N   1 
ATOM   8527 C CA  . SER E 5 142 ? -19.35390 53.70254  48.32389  1.000 223.93629 ? 122 SER E CA  1 
ATOM   8528 C C   . SER E 5 142 ? -20.20420 52.50625  48.72227  1.000 231.31990 ? 122 SER E C   1 
ATOM   8529 O O   . SER E 5 142 ? -19.77950 51.36173  48.53747  1.000 233.27165 ? 122 SER E O   1 
ATOM   8530 C CB  . SER E 5 142 ? -19.03213 53.66001  46.82827  1.000 215.05978 ? 122 SER E CB  1 
ATOM   8531 O OG  . SER E 5 142 ? -18.13336 54.69254  46.46080  1.000 209.34840 ? 122 SER E OG  1 
ATOM   8532 N N   . ILE E 5 143 ? -21.40595 52.76545  49.24938  1.000 229.90086 ? 123 ILE E N   1 
ATOM   8533 C CA  . ILE E 5 143 ? -22.31203 51.72002  49.71567  1.000 239.11605 ? 123 ILE E CA  1 
ATOM   8534 C C   . ILE E 5 143 ? -23.28628 51.36075  48.59976  1.000 235.07867 ? 123 ILE E C   1 
ATOM   8535 O O   . ILE E 5 143 ? -23.67415 52.20757  47.78788  1.000 226.93784 ? 123 ILE E O   1 
ATOM   8536 C CB  . ILE E 5 143 ? -23.04694 52.17241  50.99796  1.000 246.00899 ? 123 ILE E CB  1 
ATOM   8537 C CG1 . ILE E 5 143 ? -23.99746 51.08339  51.50585  1.000 253.00417 ? 123 ILE E CG1 1 
ATOM   8538 C CG2 . ILE E 5 143 ? -23.79303 53.47776  50.75981  1.000 241.49014 ? 123 ILE E CG2 1 
ATOM   8539 C CD1 . ILE E 5 143 ? -24.60300 51.38155  52.85943  1.000 260.35650 ? 123 ILE E CD1 1 
ATOM   8540 N N   . PHE E 5 144 ? -23.68493 50.08372  48.55070  1.000 252.94162 ? 124 PHE E N   1 
ATOM   8541 C CA  . PHE E 5 144 ? -24.58810 49.58148  47.51687  1.000 249.79653 ? 124 PHE E CA  1 
ATOM   8542 C C   . PHE E 5 144 ? -25.67949 48.70457  48.12392  1.000 257.33567 ? 124 PHE E C   1 
ATOM   8543 O O   . PHE E 5 144 ? -25.37667 47.82271  48.94768  1.000 264.96185 ? 124 PHE E O   1 
ATOM   8544 C CB  . PHE E 5 144 ? -23.81128 48.79765  46.45673  1.000 245.31780 ? 124 PHE E CB  1 
ATOM   8545 C CG  . PHE E 5 144 ? -23.04462 49.66701  45.50688  1.000 232.06486 ? 124 PHE E CG  1 
ATOM   8546 C CD1 . PHE E 5 144 ? -21.76218 50.08994  45.81294  1.000 229.89429 ? 124 PHE E CD1 1 
ATOM   8547 C CD2 . PHE E 5 144 ? -23.60953 50.06570  44.30766  1.000 223.03740 ? 124 PHE E CD2 1 
ATOM   8548 C CE1 . PHE E 5 144 ? -21.05731 50.89370  44.93946  1.000 220.05595 ? 124 PHE E CE1 1 
ATOM   8549 C CE2 . PHE E 5 144 ? -22.90999 50.86791  43.43002  1.000 212.89197 ? 124 PHE E CE2 1 
ATOM   8550 C CZ  . PHE E 5 144 ? -21.63199 51.28236  43.74654  1.000 211.89082 ? 124 PHE E CZ  1 
ATOM   8551 N N   . PRO E 5 145 ? -26.93650 48.90121  47.73520  1.000 243.03986 ? 125 PRO E N   1 
ATOM   8552 C CA  . PRO E 5 145 ? -28.02991 48.10437  48.30040  1.000 250.96556 ? 125 PRO E CA  1 
ATOM   8553 C C   . PRO E 5 145 ? -28.16499 46.77248  47.58481  1.000 251.66350 ? 125 PRO E C   1 
ATOM   8554 O O   . PRO E 5 145 ? -27.65967 46.60534  46.46455  1.000 244.53755 ? 125 PRO E O   1 
ATOM   8555 C CB  . PRO E 5 145 ? -29.25932 48.99070  48.06141  1.000 248.12516 ? 125 PRO E CB  1 
ATOM   8556 C CG  . PRO E 5 145 ? -28.92833 49.71269  46.79652  1.000 237.38721 ? 125 PRO E CG  1 
ATOM   8557 C CD  . PRO E 5 145 ? -27.42973 49.93593  46.80832  1.000 234.85541 ? 125 PRO E CD  1 
ATOM   8558 N N   . PRO E 5 146 ? -28.83653 45.79829  48.19785  1.000 244.46310 ? 126 PRO E N   1 
ATOM   8559 C CA  . PRO E 5 146 ? -29.04639 44.51257  47.52488  1.000 245.29790 ? 126 PRO E CA  1 
ATOM   8560 C C   . PRO E 5 146 ? -29.95237 44.65519  46.31246  1.000 238.81170 ? 126 PRO E C   1 
ATOM   8561 O O   . PRO E 5 146 ? -30.77434 45.57062  46.21957  1.000 236.57131 ? 126 PRO E O   1 
ATOM   8562 C CB  . PRO E 5 146 ? -29.70314 43.64484  48.60708  1.000 255.24167 ? 126 PRO E CB  1 
ATOM   8563 C CG  . PRO E 5 146 ? -29.36919 44.31679  49.89909  1.000 260.01059 ? 126 PRO E CG  1 
ATOM   8564 C CD  . PRO E 5 146 ? -29.32732 45.77870  49.58502  1.000 253.12235 ? 126 PRO E CD  1 
ATOM   8565 N N   . SER E 5 147 ? -29.79345 43.72487  45.37626  1.000 251.21195 ? 127 SER E N   1 
ATOM   8566 C CA  . SER E 5 147 ? -30.57217 43.74288  44.14843  1.000 244.53186 ? 127 SER E CA  1 
ATOM   8567 C C   . SER E 5 147 ? -31.93225 43.08674  44.35826  1.000 249.67840 ? 127 SER E C   1 
ATOM   8568 O O   . SER E 5 147 ? -32.11242 42.24853  45.24563  1.000 257.92409 ? 127 SER E O   1 
ATOM   8569 C CB  . SER E 5 147 ? -29.81734 43.03029  43.02618  1.000 239.01490 ? 127 SER E CB  1 
ATOM   8570 O OG  . SER E 5 147 ? -30.58037 43.00754  41.83154  1.000 242.77972 ? 127 SER E OG  1 
ATOM   8571 N N   . SER E 5 148 ? -32.89815 43.48184  43.52383  1.000 240.44265 ? 128 SER E N   1 
ATOM   8572 C CA  . SER E 5 148 ? -34.23268 42.89711  43.61043  1.000 245.39404 ? 128 SER E CA  1 
ATOM   8573 C C   . SER E 5 148 ? -34.22128 41.43286  43.19111  1.000 247.74438 ? 128 SER E C   1 
ATOM   8574 O O   . SER E 5 148 ? -34.85603 40.59179  43.83866  1.000 253.43238 ? 128 SER E O   1 
ATOM   8575 C CB  . SER E 5 148 ? -35.21466 43.69588  42.75364  1.000 242.78305 ? 128 SER E CB  1 
ATOM   8576 O OG  . SER E 5 148 ? -35.37819 45.01067  43.25741  1.000 241.09282 ? 128 SER E OG  1 
ATOM   8577 N N   . GLU E 5 149 ? -33.50652 41.10869  42.10958  1.000 243.99784 ? 129 GLU E N   1 
ATOM   8578 C CA  . GLU E 5 149 ? -33.34771 39.71070  41.72347  1.000 245.57112 ? 129 GLU E CA  1 
ATOM   8579 C C   . GLU E 5 149 ? -32.59781 38.92858  42.79194  1.000 247.28052 ? 129 GLU E C   1 
ATOM   8580 O O   . GLU E 5 149 ? -32.75908 37.70752  42.90088  1.000 247.61465 ? 129 GLU E O   1 
ATOM   8581 C CB  . GLU E 5 149 ? -32.61784 39.61450  40.38296  1.000 239.51336 ? 129 GLU E CB  1 
ATOM   8582 C CG  . GLU E 5 149 ? -32.93804 40.74328  39.41159  1.000 234.16126 ? 129 GLU E CG  1 
ATOM   8583 C CD  . GLU E 5 149 ? -34.39688 40.77515  38.99512  1.000 236.66360 ? 129 GLU E CD  1 
ATOM   8584 O OE1 . GLU E 5 149 ? -35.05559 39.71454  39.03373  1.000 240.86154 ? 129 GLU E OE1 1 
ATOM   8585 O OE2 . GLU E 5 149 ? -34.88454 41.86460  38.62577  1.000 234.22992 ? 129 GLU E OE2 1 
ATOM   8586 N N   . GLN E 5 150 ? -31.77576 39.61698  43.58613  1.000 234.53401 ? 130 GLN E N   1 
ATOM   8587 C CA  . GLN E 5 150 ? -31.08910 38.97313  44.69967  1.000 238.27233 ? 130 GLN E CA  1 
ATOM   8588 C C   . GLN E 5 150 ? -32.06052 38.63656  45.82507  1.000 244.39688 ? 130 GLN E C   1 
ATOM   8589 O O   . GLN E 5 150 ? -31.93494 37.58798  46.46871  1.000 246.86813 ? 130 GLN E O   1 
ATOM   8590 C CB  . GLN E 5 150 ? -29.96525 39.88305  45.19576  1.000 240.03703 ? 130 GLN E CB  1 
ATOM   8591 C CG  . GLN E 5 150 ? -29.20449 39.38161  46.40507  1.000 244.91574 ? 130 GLN E CG  1 
ATOM   8592 C CD  . GLN E 5 150 ? -28.00055 40.24962  46.71452  1.000 245.63613 ? 130 GLN E CD  1 
ATOM   8593 O OE1 . GLN E 5 150 ? -27.76992 41.26508  46.05706  1.000 242.62006 ? 130 GLN E OE1 1 
ATOM   8594 N NE2 . GLN E 5 150 ? -27.22387 39.85288  47.71503  1.000 249.63822 ? 130 GLN E NE2 1 
ATOM   8595 N N   . LEU E 5 151 ? -33.04116 39.51071  46.07028  1.000 242.29606 ? 131 LEU E N   1 
ATOM   8596 C CA  . LEU E 5 151 ? -34.03486 39.24835  47.10675  1.000 248.43727 ? 131 LEU E CA  1 
ATOM   8597 C C   . LEU E 5 151 ? -34.91623 38.05701  46.75651  1.000 247.51026 ? 131 LEU E C   1 
ATOM   8598 O O   . LEU E 5 151 ? -35.40821 37.36686  47.65696  1.000 252.43525 ? 131 LEU E O   1 
ATOM   8599 C CB  . LEU E 5 151 ? -34.89943 40.48920  47.32934  1.000 250.88200 ? 131 LEU E CB  1 
ATOM   8600 C CG  . LEU E 5 151 ? -34.17316 41.79295  47.66458  1.000 251.69834 ? 131 LEU E CG  1 
ATOM   8601 C CD1 . LEU E 5 151 ? -35.12167 42.97542  47.54764  1.000 250.62364 ? 131 LEU E CD1 1 
ATOM   8602 C CD2 . LEU E 5 151 ? -33.55995 41.72903  49.05395  1.000 257.62909 ? 131 LEU E CD2 1 
ATOM   8603 N N   . THR E 5 152 ? -35.12913 37.80482  45.46208  1.000 249.90325 ? 132 THR E N   1 
ATOM   8604 C CA  . THR E 5 152 ? -35.98981 36.70040  45.04929  1.000 249.61356 ? 132 THR E CA  1 
ATOM   8605 C C   . THR E 5 152 ? -35.42771 35.36115  45.50850  1.000 249.64902 ? 132 THR E C   1 
ATOM   8606 O O   . THR E 5 152 ? -36.18489 34.44884  45.85977  1.000 252.21546 ? 132 THR E O   1 
ATOM   8607 C CB  . THR E 5 152 ? -36.16386 36.71176  43.53000  1.000 246.78687 ? 132 THR E CB  1 
ATOM   8608 O OG1 . THR E 5 152 ? -36.32720 38.06078  43.07476  1.000 246.27311 ? 132 THR E OG1 1 
ATOM   8609 C CG2 . THR E 5 152 ? -37.38694 35.89957  43.12679  1.000 248.70372 ? 132 THR E CG2 1 
ATOM   8610 N N   . SER E 5 153 ? -34.09918 35.22510  45.51362  1.000 245.34277 ? 133 SER E N   1 
ATOM   8611 C CA  . SER E 5 153 ? -33.48408 33.97484  45.94536  1.000 246.04836 ? 133 SER E CA  1 
ATOM   8612 C C   . SER E 5 153 ? -33.69205 33.72619  47.43436  1.000 253.47966 ? 133 SER E C   1 
ATOM   8613 O O   . SER E 5 153 ? -33.73214 32.56889  47.86745  1.000 254.98293 ? 133 SER E O   1 
ATOM   8614 C CB  . SER E 5 153 ? -31.99096 33.98303  45.61382  1.000 242.77733 ? 133 SER E CB  1 
ATOM   8615 O OG  . SER E 5 153 ? -31.77166 34.13779  44.22178  1.000 237.68109 ? 133 SER E OG  1 
ATOM   8616 N N   . GLY E 5 154 ? -33.82941 34.78603  48.22640  1.000 241.07917 ? 134 GLY E N   1 
ATOM   8617 C CA  . GLY E 5 154 ? -33.97969 34.66710  49.66753  1.000 248.33652 ? 134 GLY E CA  1 
ATOM   8618 C C   . GLY E 5 154 ? -32.85474 35.28262  50.47387  1.000 251.05026 ? 134 GLY E C   1 
ATOM   8619 O O   . GLY E 5 154 ? -32.85719 35.15007  51.70611  1.000 257.06260 ? 134 GLY E O   1 
ATOM   8620 N N   . GLY E 5 155 ? -31.88579 35.95067  49.84169  1.000 250.53187 ? 135 GLY E N   1 
ATOM   8621 C CA  . GLY E 5 155 ? -30.78968 36.57635  50.54283  1.000 252.93403 ? 135 GLY E CA  1 
ATOM   8622 C C   . GLY E 5 155 ? -30.79396 38.08488  50.34276  1.000 252.56201 ? 135 GLY E C   1 
ATOM   8623 O O   . GLY E 5 155 ? -31.50786 38.62648  49.49011  1.000 249.41957 ? 135 GLY E O   1 
ATOM   8624 N N   . ALA E 5 156 ? -29.97966 38.76003  51.15017  1.000 245.22295 ? 136 ALA E N   1 
ATOM   8625 C CA  . ALA E 5 156 ? -29.86059 40.21397  51.08109  1.000 245.08985 ? 136 ALA E CA  1 
ATOM   8626 C C   . ALA E 5 156 ? -28.50263 40.60447  51.63729  1.000 246.46220 ? 136 ALA E C   1 
ATOM   8627 O O   . ALA E 5 156 ? -28.23052 40.37119  52.81935  1.000 251.68082 ? 136 ALA E O   1 
ATOM   8628 C CB  . ALA E 5 156 ? -30.98397 40.89602  51.86119  1.000 250.03523 ? 136 ALA E CB  1 
ATOM   8629 N N   . SER E 5 157 ? -27.65512 41.19371  50.79620  1.000 239.72059 ? 137 SER E N   1 
ATOM   8630 C CA  . SER E 5 157 ? -26.29546 41.53507  51.18973  1.000 240.46331 ? 137 SER E CA  1 
ATOM   8631 C C   . SER E 5 157 ? -25.95199 42.93454  50.70335  1.000 237.57862 ? 137 SER E C   1 
ATOM   8632 O O   . SER E 5 157 ? -26.23090 43.28350  49.55274  1.000 230.29566 ? 137 SER E O   1 
ATOM   8633 C CB  . SER E 5 157 ? -25.29079 40.51660  50.63717  1.000 237.31655 ? 137 SER E CB  1 
ATOM   8634 O OG  . SER E 5 157 ? -25.52620 39.22460  51.17416  1.000 239.63797 ? 137 SER E OG  1 
ATOM   8635 N N   . VAL E 5 158 ? -25.34555 43.72797  51.58420  1.000 242.18066 ? 138 VAL E N   1 
ATOM   8636 C CA  . VAL E 5 158 ? -24.94114 45.09878  51.29272  1.000 235.05043 ? 138 VAL E CA  1 
ATOM   8637 C C   . VAL E 5 158 ? -23.42025 45.14616  51.22433  1.000 232.63448 ? 138 VAL E C   1 
ATOM   8638 O O   . VAL E 5 158 ? -22.73493 44.48285  52.01162  1.000 238.35969 ? 138 VAL E O   1 
ATOM   8639 C CB  . VAL E 5 158 ? -25.48494 46.07387  52.35721  1.000 237.69500 ? 138 VAL E CB  1 
ATOM   8640 C CG1 . VAL E 5 158 ? -25.04211 47.50497  52.07168  1.000 230.41163 ? 138 VAL E CG1 1 
ATOM   8641 C CG2 . VAL E 5 158 ? -27.00202 45.98646  52.43084  1.000 240.48017 ? 138 VAL E CG2 1 
ATOM   8642 N N   . VAL E 5 159 ? -22.89051 45.92628  50.28122  1.000 238.53211 ? 139 VAL E N   1 
ATOM   8643 C CA  . VAL E 5 159 ? -21.45266 46.00402  50.04329  1.000 235.42139 ? 139 VAL E CA  1 
ATOM   8644 C C   . VAL E 5 159 ? -21.02824 47.46587  49.98451  1.000 228.86180 ? 139 VAL E C   1 
ATOM   8645 O O   . VAL E 5 159 ? -21.63407 48.26500  49.26177  1.000 222.67052 ? 139 VAL E O   1 
ATOM   8646 C CB  . VAL E 5 159 ? -21.04677 45.26853  48.75046  1.000 230.86692 ? 139 VAL E CB  1 
ATOM   8647 C CG1 . VAL E 5 159 ? -19.59246 45.55459  48.40420  1.000 225.39846 ? 139 VAL E CG1 1 
ATOM   8648 C CG2 . VAL E 5 159 ? -21.26687 43.77089  48.90223  1.000 238.14812 ? 139 VAL E CG2 1 
ATOM   8649 N N   . CYS E 5 160 ? -19.98689 47.81036  50.74223  1.000 228.97284 ? 140 CYS E N   1 
ATOM   8650 C CA  . CYS E 5 160 ? -19.39993 49.14580  50.73918  1.000 223.55017 ? 140 CYS E CA  1 
ATOM   8651 C C   . CYS E 5 160 ? -18.02592 49.07562  50.08415  1.000 215.72228 ? 140 CYS E C   1 
ATOM   8652 O O   . CYS E 5 160 ? -17.12635 48.39668  50.59137  1.000 218.41816 ? 140 CYS E O   1 
ATOM   8653 C CB  . CYS E 5 160 ? -19.30087 49.71140  52.15786  1.000 228.73242 ? 140 CYS E CB  1 
ATOM   8654 S SG  . CYS E 5 160 ? -20.90973 50.05676  52.91287  1.000 233.61551 ? 140 CYS E SG  1 
ATOM   8655 N N   . PHE E 5 161 ? -17.86827 49.77773  48.96324  1.000 232.47022 ? 141 PHE E N   1 
ATOM   8656 C CA  . PHE E 5 161 ? -16.64615 49.72370  48.16613  1.000 225.69388 ? 141 PHE E CA  1 
ATOM   8657 C C   . PHE E 5 161 ? -15.68385 50.81447  48.62341  1.000 224.04443 ? 141 PHE E C   1 
ATOM   8658 O O   . PHE E 5 161 ? -15.90064 51.99922  48.35024  1.000 218.72622 ? 141 PHE E O   1 
ATOM   8659 C CB  . PHE E 5 161 ? -16.96621 49.87586  46.68136  1.000 216.62522 ? 141 PHE E CB  1 
ATOM   8660 C CG  . PHE E 5 161 ? -17.40444 48.60207  46.01974  1.000 216.71156 ? 141 PHE E CG  1 
ATOM   8661 C CD1 . PHE E 5 161 ? -16.82367 47.39203  46.36066  1.000 219.99467 ? 141 PHE E CD1 1 
ATOM   8662 C CD2 . PHE E 5 161 ? -18.39804 48.61484  45.05637  1.000 212.79399 ? 141 PHE E CD2 1 
ATOM   8663 C CE1 . PHE E 5 161 ? -17.22517 46.21876  45.75106  1.000 219.99280 ? 141 PHE E CE1 1 
ATOM   8664 C CE2 . PHE E 5 161 ? -18.80449 47.44603  44.44599  1.000 213.47519 ? 141 PHE E CE2 1 
ATOM   8665 C CZ  . PHE E 5 161 ? -18.21765 46.24633  44.79266  1.000 217.21751 ? 141 PHE E CZ  1 
ATOM   8666 N N   . LEU E 5 162 ? -14.61929 50.41195  49.31087  1.000 213.27330 ? 142 LEU E N   1 
ATOM   8667 C CA  . LEU E 5 162 ? -13.50404 51.28978  49.63942  1.000 212.47288 ? 142 LEU E CA  1 
ATOM   8668 C C   . LEU E 5 162 ? -12.36076 50.99720  48.67875  1.000 203.06588 ? 142 LEU E C   1 
ATOM   8669 O O   . LEU E 5 162 ? -11.97108 49.83677  48.51313  1.000 199.24017 ? 142 LEU E O   1 
ATOM   8670 C CB  . LEU E 5 162 ? -13.03418 51.07771  51.07992  1.000 221.22883 ? 142 LEU E CB  1 
ATOM   8671 C CG  . LEU E 5 162 ? -13.85856 51.55493  52.27591  1.000 228.68150 ? 142 LEU E CG  1 
ATOM   8672 C CD1 . LEU E 5 162 ? -15.14288 50.75789  52.44524  1.000 233.70166 ? 142 LEU E CD1 1 
ATOM   8673 C CD2 . LEU E 5 162 ? -13.00343 51.45290  53.52178  1.000 235.36169 ? 142 LEU E CD2 1 
ATOM   8674 N N   . ASN E 5 163 ? -11.82048 52.03779  48.04921  1.000 219.61577 ? 143 ASN E N   1 
ATOM   8675 C CA  . ASN E 5 163 ? -10.75403 51.79444  47.08800  1.000 212.63173 ? 143 ASN E CA  1 
ATOM   8676 C C   . ASN E 5 163 ? -9.89249  53.03585  46.91511  1.000 211.17998 ? 143 ASN E C   1 
ATOM   8677 O O   . ASN E 5 163 ? -10.34174 54.16299  47.14250  1.000 213.37766 ? 143 ASN E O   1 
ATOM   8678 C CB  . ASN E 5 163 ? -11.31764 51.34244  45.73470  1.000 205.56486 ? 143 ASN E CB  1 
ATOM   8679 C CG  . ASN E 5 163 ? -12.28738 52.33902  45.13902  1.000 208.75253 ? 143 ASN E CG  1 
ATOM   8680 O OD1 . ASN E 5 163 ? -12.76360 53.24473  45.82041  1.000 210.89233 ? 143 ASN E OD1 1 
ATOM   8681 N ND2 . ASN E 5 163 ? -12.59258 52.17009  43.85691  1.000 205.04044 ? 143 ASN E ND2 1 
ATOM   8682 N N   . ASN E 5 164 ? -8.64353  52.79809  46.50989  1.000 213.26154 ? 144 ASN E N   1 
ATOM   8683 C CA  . ASN E 5 164 ? -7.66360  53.83748  46.19604  1.000 214.43208 ? 144 ASN E CA  1 
ATOM   8684 C C   . ASN E 5 164 ? -7.41786  54.74459  47.40569  1.000 218.93159 ? 144 ASN E C   1 
ATOM   8685 O O   . ASN E 5 164 ? -7.80010  55.91511  47.44898  1.000 219.39602 ? 144 ASN E O   1 
ATOM   8686 C CB  . ASN E 5 164 ? -8.09227  54.63734  44.96158  1.000 207.45476 ? 144 ASN E CB  1 
ATOM   8687 C CG  . ASN E 5 164 ? -7.95710  53.83624  43.68028  1.000 202.60184 ? 144 ASN E CG  1 
ATOM   8688 O OD1 . ASN E 5 164 ? -8.81704  53.89349  42.80245  1.000 197.56391 ? 144 ASN E OD1 1 
ATOM   8689 N ND2 . ASN E 5 164 ? -6.87694  53.06884  43.57569  1.000 202.68689 ? 144 ASN E ND2 1 
ATOM   8690 N N   . PHE E 5 165 ? -6.74169  54.15380  48.38736  1.000 198.08734 ? 145 PHE E N   1 
ATOM   8691 C CA  . PHE E 5 165 ? -6.31762  54.85179  49.58958  1.000 203.07022 ? 145 PHE E CA  1 
ATOM   8692 C C   . PHE E 5 165 ? -4.95251  54.32613  50.00629  1.000 207.04131 ? 145 PHE E C   1 
ATOM   8693 O O   . PHE E 5 165 ? -4.46773  53.31430  49.49505  1.000 206.50133 ? 145 PHE E O   1 
ATOM   8694 C CB  . PHE E 5 165 ? -7.32710  54.68184  50.73136  1.000 210.42542 ? 145 PHE E CB  1 
ATOM   8695 C CG  . PHE E 5 165 ? -7.77743  53.26295  50.94018  1.000 211.63458 ? 145 PHE E CG  1 
ATOM   8696 C CD1 . PHE E 5 165 ? -7.07122  52.41099  51.77354  1.000 217.23869 ? 145 PHE E CD1 1 
ATOM   8697 C CD2 . PHE E 5 165 ? -8.91221  52.78321  50.30628  1.000 206.68269 ? 145 PHE E CD2 1 
ATOM   8698 C CE1 . PHE E 5 165 ? -7.48575  51.10634  51.96636  1.000 216.34394 ? 145 PHE E CE1 1 
ATOM   8699 C CE2 . PHE E 5 165 ? -9.33187  51.48110  50.49595  1.000 206.06736 ? 145 PHE E CE2 1 
ATOM   8700 C CZ  . PHE E 5 165 ? -8.61777  50.64151  51.32677  1.000 211.80010 ? 145 PHE E CZ  1 
ATOM   8701 N N   . TYR E 5 166 ? -4.32870  55.02920  50.95055  1.000 211.29675 ? 146 TYR E N   1 
ATOM   8702 C CA  . TYR E 5 166 ? -3.06125  54.60593  51.49895  1.000 215.30648 ? 146 TYR E CA  1 
ATOM   8703 C C   . TYR E 5 166 ? -3.01748  55.04532  52.95812  1.000 221.76007 ? 146 TYR E C   1 
ATOM   8704 O O   . TYR E 5 166 ? -3.33943  56.20811  53.25221  1.000 221.63292 ? 146 TYR E O   1 
ATOM   8705 C CB  . TYR E 5 166 ? -1.86745  55.18415  50.73599  1.000 212.10528 ? 146 TYR E CB  1 
ATOM   8706 C CG  . TYR E 5 166 ? -0.54578  54.66169  51.23688  1.000 215.06506 ? 146 TYR E CG  1 
ATOM   8707 C CD1 . TYR E 5 166 ? -0.09305  53.40356  50.86471  1.000 213.32212 ? 146 TYR E CD1 1 
ATOM   8708 C CD2 . TYR E 5 166 ? 0.24244   55.41596  52.09530  1.000 219.23764 ? 146 TYR E CD2 1 
ATOM   8709 C CE1 . TYR E 5 166 ? 1.11245   52.91411  51.32566  1.000 216.76755 ? 146 TYR E CE1 1 
ATOM   8710 C CE2 . TYR E 5 166 ? 1.44889   54.93296  52.56195  1.000 222.58645 ? 146 TYR E CE2 1 
ATOM   8711 C CZ  . TYR E 5 166 ? 1.88008   53.68411  52.17295  1.000 221.48858 ? 146 TYR E CZ  1 
ATOM   8712 O OH  . TYR E 5 166 ? 3.08310   53.20807  52.64140  1.000 225.76310 ? 146 TYR E OH  1 
ATOM   8713 N N   . PRO E 5 167 ? -2.61759  54.16054  53.88718  1.000 222.62650 ? 147 PRO E N   1 
ATOM   8714 C CA  . PRO E 5 167 ? -2.15565  52.79119  53.63216  1.000 223.42983 ? 147 PRO E CA  1 
ATOM   8715 C C   . PRO E 5 167 ? -3.26303  51.73806  53.65604  1.000 225.26562 ? 147 PRO E C   1 
ATOM   8716 O O   . PRO E 5 167 ? -4.44848  52.07101  53.65010  1.000 224.77412 ? 147 PRO E O   1 
ATOM   8717 C CB  . PRO E 5 167 ? -1.17439  52.55263  54.77732  1.000 229.18443 ? 147 PRO E CB  1 
ATOM   8718 C CG  . PRO E 5 167 ? -1.77494  53.31305  55.91008  1.000 233.54463 ? 147 PRO E CG  1 
ATOM   8719 C CD  . PRO E 5 167 ? -2.45044  54.53118  55.30388  1.000 228.59146 ? 147 PRO E CD  1 
ATOM   8720 N N   . LYS E 5 168 ? -2.85696  50.46615  53.69167  1.000 223.93840 ? 148 LYS E N   1 
ATOM   8721 C CA  . LYS E 5 168 ? -3.82185  49.37221  53.70606  1.000 227.15074 ? 148 LYS E CA  1 
ATOM   8722 C C   . LYS E 5 168 ? -4.49219  49.23103  55.06600  1.000 235.95942 ? 148 LYS E C   1 
ATOM   8723 O O   . LYS E 5 168 ? -5.62214  48.73597  55.14985  1.000 237.41587 ? 148 LYS E O   1 
ATOM   8724 C CB  . LYS E 5 168 ? -3.12974  48.06508  53.31893  1.000 224.90029 ? 148 LYS E CB  1 
ATOM   8725 C CG  . LYS E 5 168 ? -4.07276  46.94219  52.92237  1.000 225.98465 ? 148 LYS E CG  1 
ATOM   8726 C CD  . LYS E 5 168 ? -3.30121  45.67041  52.60992  1.000 227.20974 ? 148 LYS E CD  1 
ATOM   8727 C CE  . LYS E 5 168 ? -4.12687  44.72227  51.76017  1.000 219.14988 ? 148 LYS E CE  1 
ATOM   8728 N NZ  . LYS E 5 168 ? -3.44349  43.41755  51.53440  1.000 226.98926 ? 148 LYS E NZ  1 
ATOM   8729 N N   . ASP E 5 169 ? -3.81678  49.65643  56.13366  1.000 227.47202 ? 149 ASP E N   1 
ATOM   8730 C CA  . ASP E 5 169 ? -4.33636  49.52250  57.48907  1.000 235.22881 ? 149 ASP E CA  1 
ATOM   8731 C C   . ASP E 5 169 ? -5.62629  50.31584  57.65721  1.000 234.56509 ? 149 ASP E C   1 
ATOM   8732 O O   . ASP E 5 169 ? -5.60842  51.55089  57.65207  1.000 230.96325 ? 149 ASP E O   1 
ATOM   8733 C CB  . ASP E 5 169 ? -3.28608  49.98137  58.50438  1.000 238.16428 ? 149 ASP E CB  1 
ATOM   8734 C CG  . ASP E 5 169 ? -3.53983  49.43519  59.89577  1.000 246.27889 ? 149 ASP E CG  1 
ATOM   8735 O OD1 . ASP E 5 169 ? -3.55564  48.19598  60.05242  1.000 250.76027 ? 149 ASP E OD1 1 
ATOM   8736 O OD2 . ASP E 5 169 ? -3.71445  50.24252  60.83324  1.000 248.05960 ? 149 ASP E OD2 1 
ATOM   8737 N N   . ILE E 5 170 ? -6.74986  49.61342  57.80254  1.000 230.32467 ? 150 ILE E N   1 
ATOM   8738 C CA  . ILE E 5 170 ? -8.05386  50.25259  57.94196  1.000 229.58921 ? 150 ILE E CA  1 
ATOM   8739 C C   . ILE E 5 170 ? -9.00017  49.23965  58.56795  1.000 236.48244 ? 150 ILE E C   1 
ATOM   8740 O O   . ILE E 5 170 ? -8.76261  48.03129  58.51736  1.000 239.14084 ? 150 ILE E O   1 
ATOM   8741 C CB  . ILE E 5 170 ? -8.57968  50.76243  56.57466  1.000 220.10214 ? 150 ILE E CB  1 
ATOM   8742 C CG1 . ILE E 5 170 ? -9.60590  51.87942  56.77147  1.000 219.27270 ? 150 ILE E CG1 1 
ATOM   8743 C CG2 . ILE E 5 170 ? -9.18286  49.62051  55.76929  1.000 219.31459 ? 150 ILE E CG2 1 
ATOM   8744 C CD1 . ILE E 5 170 ? -10.02524 52.55607  55.48721  1.000 210.95997 ? 150 ILE E CD1 1 
ATOM   8745 N N   . ASN E 5 171 ? -10.07783 49.73453  59.17368  1.000 221.82302 ? 151 ASN E N   1 
ATOM   8746 C CA  . ASN E 5 171 ? -11.07383 48.87567  59.80002  1.000 223.10430 ? 151 ASN E CA  1 
ATOM   8747 C C   . ASN E 5 171 ? -12.46039 49.37398  59.42461  1.000 222.95150 ? 151 ASN E C   1 
ATOM   8748 O O   . ASN E 5 171 ? -12.74363 50.56996  59.53823  1.000 224.38789 ? 151 ASN E O   1 
ATOM   8749 C CB  . ASN E 5 171 ? -10.90857 48.85102  61.32464  1.000 227.39495 ? 151 ASN E CB  1 
ATOM   8750 C CG  . ASN E 5 171 ? -11.34296 47.53363  61.93687  1.000 232.19943 ? 151 ASN E CG  1 
ATOM   8751 O OD1 . ASN E 5 171 ? -11.20697 46.47556  61.32242  1.000 232.78146 ? 151 ASN E OD1 1 
ATOM   8752 N ND2 . ASN E 5 171 ? -11.87060 47.59185  63.15439  1.000 236.70461 ? 151 ASN E ND2 1 
ATOM   8753 N N   . VAL E 5 172 ? -13.31688 48.46012  58.97645  1.000 230.24602 ? 152 VAL E N   1 
ATOM   8754 C CA  . VAL E 5 172 ? -14.66761 48.78659  58.53222  1.000 228.88211 ? 152 VAL E CA  1 
ATOM   8755 C C   . VAL E 5 172 ? -15.65378 48.22826  59.54842  1.000 235.48621 ? 152 VAL E C   1 
ATOM   8756 O O   . VAL E 5 172 ? -15.66304 47.02073  59.81885  1.000 240.39363 ? 152 VAL E O   1 
ATOM   8757 C CB  . VAL E 5 172 ? -14.95170 48.23440  57.12690  1.000 225.14632 ? 152 VAL E CB  1 
ATOM   8758 C CG1 . VAL E 5 172 ? -16.42123 48.41081  56.77428  1.000 224.96508 ? 152 VAL E CG1 1 
ATOM   8759 C CG2 . VAL E 5 172 ? -14.06786 48.92360  56.09845  1.000 217.59511 ? 152 VAL E CG2 1 
ATOM   8760 N N   . LYS E 5 173 ? -16.48376 49.10437  60.10675  1.000 241.33086 ? 153 LYS E N   1 
ATOM   8761 C CA  . LYS E 5 173 ? -17.51947 48.72241  61.05475  1.000 247.31871 ? 153 LYS E CA  1 
ATOM   8762 C C   . LYS E 5 173 ? -18.88454 48.84336  60.39082  1.000 246.28617 ? 153 LYS E C   1 
ATOM   8763 O O   . LYS E 5 173 ? -19.14460 49.80135  59.65586  1.000 240.64740 ? 153 LYS E O   1 
ATOM   8764 C CB  . LYS E 5 173 ? -17.47083 49.59889  62.30885  1.000 249.07226 ? 153 LYS E CB  1 
ATOM   8765 C CG  . LYS E 5 173 ? -16.08046 49.80403  62.88670  1.000 248.88589 ? 153 LYS E CG  1 
ATOM   8766 C CD  . LYS E 5 173 ? -16.11035 50.82999  64.00876  1.000 249.87885 ? 153 LYS E CD  1 
ATOM   8767 C CE  . LYS E 5 173 ? -14.78597 50.88848  64.75067  1.000 251.40436 ? 153 LYS E CE  1 
ATOM   8768 N NZ  . LYS E 5 173 ? -14.86652 51.78967  65.93380  1.000 253.45330 ? 153 LYS E NZ  1 
ATOM   8769 N N   . TRP E 5 174 ? -19.75408 47.87217  60.65295  1.000 253.72130 ? 154 TRP E N   1 
ATOM   8770 C CA  . TRP E 5 174 ? -21.08255 47.81737  60.05510  1.000 253.51020 ? 154 TRP E CA  1 
ATOM   8771 C C   . TRP E 5 174 ? -22.12915 48.12680  61.11698  1.000 258.56146 ? 154 TRP E C   1 
ATOM   8772 O O   . TRP E 5 174 ? -22.24113 47.40364  62.11295  1.000 265.61400 ? 154 TRP E O   1 
ATOM   8773 C CB  . TRP E 5 174 ? -21.34193 46.44869  59.42688  1.000 256.18321 ? 154 TRP E CB  1 
ATOM   8774 C CG  . TRP E 5 174 ? -20.75689 46.29561  58.05846  1.000 249.95004 ? 154 TRP E CG  1 
ATOM   8775 C CD1 . TRP E 5 174 ? -19.52398 45.80526  57.74097  1.000 248.76391 ? 154 TRP E CD1 1 
ATOM   8776 C CD2 . TRP E 5 174 ? -21.38587 46.63463  56.81802  1.000 244.12569 ? 154 TRP E CD2 1 
ATOM   8777 N NE1 . TRP E 5 174 ? -19.34670 45.81783  56.37804  1.000 242.62784 ? 154 TRP E NE1 1 
ATOM   8778 C CE2 . TRP E 5 174 ? -20.47601 46.32291  55.78890  1.000 239.47681 ? 154 TRP E CE2 1 
ATOM   8779 C CE3 . TRP E 5 174 ? -22.63028 47.17301  56.47816  1.000 242.21802 ? 154 TRP E CE3 1 
ATOM   8780 C CZ2 . TRP E 5 174 ? -20.77190 46.53107  54.44364  1.000 232.82163 ? 154 TRP E CZ2 1 
ATOM   8781 C CZ3 . TRP E 5 174 ? -22.92233 47.37798  55.14369  1.000 235.57415 ? 154 TRP E CZ3 1 
ATOM   8782 C CH2 . TRP E 5 174 ? -21.99815 47.05689  54.14268  1.000 230.79280 ? 154 TRP E CH2 1 
ATOM   8783 N N   . LYS E 5 175 ? -22.89490 49.19223  60.89754  1.000 252.10905 ? 155 LYS E N   1 
ATOM   8784 C CA  . LYS E 5 175 ? -23.95095 49.61491  61.80738  1.000 256.32615 ? 155 LYS E CA  1 
ATOM   8785 C C   . LYS E 5 175 ? -25.30789 49.34248  61.17245  1.000 257.06629 ? 155 LYS E C   1 
ATOM   8786 O O   . LYS E 5 175 ? -25.52806 49.67237  60.00215  1.000 251.09578 ? 155 LYS E O   1 
ATOM   8787 C CB  . LYS E 5 175 ? -23.81352 51.10003  62.15374  1.000 252.48766 ? 155 LYS E CB  1 
ATOM   8788 C CG  . LYS E 5 175 ? -22.53034 51.44598  62.89399  1.000 252.24199 ? 155 LYS E CG  1 
ATOM   8789 C CD  . LYS E 5 175 ? -22.47692 52.91844  63.27503  1.000 249.24126 ? 155 LYS E CD  1 
ATOM   8790 C CE  . LYS E 5 175 ? -22.38426 53.81129  62.04868  1.000 241.23982 ? 155 LYS E CE  1 
ATOM   8791 N NZ  . LYS E 5 175 ? -22.24405 55.24697  62.42026  1.000 238.64848 ? 155 LYS E NZ  1 
ATOM   8792 N N   . ILE E 5 176 ? -26.20996 48.73964  61.94384  1.000 253.77752 ? 156 ILE E N   1 
ATOM   8793 C CA  . ILE E 5 176 ? -27.56065 48.41643  61.49396  1.000 255.52240 ? 156 ILE E CA  1 
ATOM   8794 C C   . ILE E 5 176 ? -28.53177 49.02438  62.49653  1.000 259.78091 ? 156 ILE E C   1 
ATOM   8795 O O   . ILE E 5 176 ? -28.61579 48.56129  63.64126  1.000 266.51028 ? 156 ILE E O   1 
ATOM   8796 C CB  . ILE E 5 176 ? -27.78684 46.90358  61.36570  1.000 260.85300 ? 156 ILE E CB  1 
ATOM   8797 C CG1 . ILE E 5 176 ? -26.80100 46.29457  60.36668  1.000 256.76018 ? 156 ILE E CG1 1 
ATOM   8798 C CG2 . ILE E 5 176 ? -29.21981 46.61299  60.94697  1.000 262.73520 ? 156 ILE E CG2 1 
ATOM   8799 C CD1 . ILE E 5 176 ? -26.91488 44.79119  60.24049  1.000 261.78844 ? 156 ILE E CD1 1 
ATOM   8800 N N   . ASP E 5 177 ? -29.26859 50.05043  62.06779  1.000 259.06253 ? 157 ASP E N   1 
ATOM   8801 C CA  . ASP E 5 177 ? -30.19424 50.78548  62.93154  1.000 262.39316 ? 157 ASP E CA  1 
ATOM   8802 C C   . ASP E 5 177 ? -29.49621 51.26396  64.20295  1.000 264.91747 ? 157 ASP E C   1 
ATOM   8803 O O   . ASP E 5 177 ? -29.98569 51.08651  65.32065  1.000 271.68264 ? 157 ASP E O   1 
ATOM   8804 C CB  . ASP E 5 177 ? -31.42849 49.94497  63.26559  1.000 269.49512 ? 157 ASP E CB  1 
ATOM   8805 C CG  . ASP E 5 177 ? -32.59026 50.21954  62.33125  1.000 266.84216 ? 157 ASP E CG  1 
ATOM   8806 O OD1 . ASP E 5 177 ? -32.37051 50.84971  61.27569  1.000 259.47949 ? 157 ASP E OD1 1 
ATOM   8807 O OD2 . ASP E 5 177 ? -33.72560 49.81089  62.65475  1.000 272.14678 ? 157 ASP E OD2 1 
ATOM   8808 N N   . GLY E 5 178 ? -28.32929 51.87582  64.02031  1.000 258.04899 ? 158 GLY E N   1 
ATOM   8809 C CA  . GLY E 5 178 ? -27.56786 52.39864  65.13663  1.000 260.88471 ? 158 GLY E CA  1 
ATOM   8810 C C   . GLY E 5 178 ? -26.63525 51.38218  65.76141  1.000 263.13857 ? 158 GLY E C   1 
ATOM   8811 O O   . GLY E 5 178 ? -25.42155 51.60025  65.82339  1.000 260.10893 ? 158 GLY E O   1 
ATOM   8812 N N   . SER E 5 179 ? -27.19089 50.26590  66.22512  1.000 263.06872 ? 159 SER E N   1 
ATOM   8813 C CA  . SER E 5 179 ? -26.39340 49.24738  66.89202  1.000 267.63087 ? 159 SER E CA  1 
ATOM   8814 C C   . SER E 5 179 ? -25.43609 48.57393  65.91397  1.000 263.74453 ? 159 SER E C   1 
ATOM   8815 O O   . SER E 5 179 ? -25.70751 48.46409  64.71526  1.000 259.66320 ? 159 SER E O   1 
ATOM   8816 C CB  . SER E 5 179 ? -27.30082 48.20070  67.53894  1.000 275.96277 ? 159 SER E CB  1 
ATOM   8817 O OG  . SER E 5 179 ? -28.19762 47.64716  66.59147  1.000 275.74389 ? 159 SER E OG  1 
ATOM   8818 N N   . GLU E 5 180 ? -24.30291 48.12312  66.44220  1.000 277.59993 ? 160 GLU E N   1 
ATOM   8819 C CA  . GLU E 5 180 ? -23.30094 47.42187  65.65552  1.000 274.65609 ? 160 GLU E CA  1 
ATOM   8820 C C   . GLU E 5 180 ? -23.55064 45.91666  65.69114  1.000 280.59553 ? 160 GLU E C   1 
ATOM   8821 O O   . GLU E 5 180 ? -24.28130 45.40106  66.54051  1.000 287.46434 ? 160 GLU E O   1 
ATOM   8822 C CB  . GLU E 5 180 ? -21.89432 47.73242  66.17141  1.000 272.80172 ? 160 GLU E CB  1 
ATOM   8823 C CG  . GLU E 5 180 ? -21.51166 49.20326  66.10463  1.000 266.92356 ? 160 GLU E CG  1 
ATOM   8824 C CD  . GLU E 5 180 ? -20.14210 49.47559  66.69728  1.000 265.68780 ? 160 GLU E CD  1 
ATOM   8825 O OE1 . GLU E 5 180 ? -19.48851 48.51380  67.15302  1.000 269.13804 ? 160 GLU E OE1 1 
ATOM   8826 O OE2 . GLU E 5 180 ? -19.71933 50.65093  66.70894  1.000 261.40240 ? 160 GLU E OE2 1 
ATOM   8827 N N   . ARG E 5 181 ? -22.92655 45.21248  64.74945  1.000 263.45631 ? 161 ARG E N   1 
ATOM   8828 C CA  . ARG E 5 181 ? -23.06429 43.76579  64.65794  1.000 268.10751 ? 161 ARG E CA  1 
ATOM   8829 C C   . ARG E 5 181 ? -21.85228 43.20521  63.92610  1.000 264.27499 ? 161 ARG E C   1 
ATOM   8830 O O   . ARG E 5 181 ? -21.28036 43.86383  63.05367  1.000 258.47216 ? 161 ARG E O   1 
ATOM   8831 C CB  . ARG E 5 181 ? -24.36546 43.37254  63.94512  1.000 267.51531 ? 161 ARG E CB  1 
ATOM   8832 C CG  . ARG E 5 181 ? -24.67010 41.88291  63.97121  1.000 269.49576 ? 161 ARG E CG  1 
ATOM   8833 C CD  . ARG E 5 181 ? -26.00455 41.56586  63.31296  1.000 268.81409 ? 161 ARG E CD  1 
ATOM   8834 N NE  . ARG E 5 181 ? -27.13896 41.98078  64.12983  1.000 273.50289 ? 161 ARG E NE  1 
ATOM   8835 C CZ  . ARG E 5 181 ? -28.40864 41.78860  63.79864  1.000 274.06018 ? 161 ARG E CZ  1 
ATOM   8836 N NH1 . ARG E 5 181 ? -28.74492 41.19444  62.66535  1.000 269.93609 ? 161 ARG E NH1 1 
ATOM   8837 N NH2 . ARG E 5 181 ? -29.36497 42.20185  64.62549  1.000 278.77822 ? 161 ARG E NH2 1 
ATOM   8838 N N   . GLN E 5 182 ? -21.46466 41.98571  64.29679  1.000 255.15591 ? 162 GLN E N   1 
ATOM   8839 C CA  . GLN E 5 182 ? -20.29718 41.30996  63.73842  1.000 252.27041 ? 162 GLN E CA  1 
ATOM   8840 C C   . GLN E 5 182 ? -20.63062 39.87827  63.34531  1.000 252.55767 ? 162 GLN E C   1 
ATOM   8841 O O   . GLN E 5 182 ? -19.83410 38.95799  63.55246  1.000 253.38304 ? 162 GLN E O   1 
ATOM   8842 C CB  . GLN E 5 182 ? -19.13190 41.32197  64.72463  1.000 254.53175 ? 162 GLN E CB  1 
ATOM   8843 C CG  . GLN E 5 182 ? -18.26794 42.56552  64.67711  1.000 251.62973 ? 162 GLN E CG  1 
ATOM   8844 C CD  . GLN E 5 182 ? -16.97238 42.39092  65.44690  1.000 252.23908 ? 162 GLN E CD  1 
ATOM   8845 O OE1 . GLN E 5 182 ? -16.94444 41.75633  66.50196  1.000 257.52312 ? 162 GLN E OE1 1 
ATOM   8846 N NE2 . GLN E 5 182 ? -15.88803 42.94289  64.91441  1.000 246.41384 ? 162 GLN E NE2 1 
ATOM   8847 N N   . ASN E 5 183 ? -21.80918 39.66258  62.76928  1.000 253.22504 ? 163 ASN E N   1 
ATOM   8848 C CA  . ASN E 5 183 ? -22.29035 38.32223  62.44039  1.000 253.13156 ? 163 ASN E CA  1 
ATOM   8849 C C   . ASN E 5 183 ? -22.29585 38.15542  60.92350  1.000 246.45148 ? 163 ASN E C   1 
ATOM   8850 O O   . ASN E 5 183 ? -23.19039 38.65782  60.23693  1.000 244.06030 ? 163 ASN E O   1 
ATOM   8851 C CB  . ASN E 5 183 ? -23.67851 38.08570  63.02699  1.000 257.25080 ? 163 ASN E CB  1 
ATOM   8852 C CG  . ASN E 5 183 ? -23.79352 38.55465  64.46488  1.000 263.45717 ? 163 ASN E CG  1 
ATOM   8853 O OD1 . ASN E 5 183 ? -22.79124 38.81094  65.13201  1.000 264.84212 ? 163 ASN E OD1 1 
ATOM   8854 N ND2 . ASN E 5 183 ? -25.02371 38.66625  64.95097  1.000 267.02158 ? 163 ASN E ND2 1 
ATOM   8855 N N   . GLY E 5 184 ? -21.29818 37.44108  60.40756  1.000 249.67489 ? 164 GLY E N   1 
ATOM   8856 C CA  . GLY E 5 184 ? -21.23400 37.12506  58.99380  1.000 243.27061 ? 164 GLY E CA  1 
ATOM   8857 C C   . GLY E 5 184 ? -20.93421 38.31352  58.10430  1.000 239.09892 ? 164 GLY E C   1 
ATOM   8858 O O   . GLY E 5 184 ? -21.82602 38.82156  57.41629  1.000 236.54724 ? 164 GLY E O   1 
ATOM   8859 N N   . VAL E 5 185 ? -19.67872 38.75521  58.09795  1.000 239.18518 ? 165 VAL E N   1 
ATOM   8860 C CA  . VAL E 5 185 ? -19.24575 39.90737  57.31568  1.000 235.26444 ? 165 VAL E CA  1 
ATOM   8861 C C   . VAL E 5 185 ? -17.99320 39.52635  56.53715  1.000 231.47078 ? 165 VAL E C   1 
ATOM   8862 O O   . VAL E 5 185 ? -17.02411 39.02234  57.11627  1.000 233.57831 ? 165 VAL E O   1 
ATOM   8863 C CB  . VAL E 5 185 ? -18.99017 41.13821  58.21209  1.000 238.16637 ? 165 VAL E CB  1 
ATOM   8864 C CG1 . VAL E 5 185 ? -18.16777 40.75862  59.43461  1.000 242.67299 ? 165 VAL E CG1 1 
ATOM   8865 C CG2 . VAL E 5 185 ? -18.30877 42.23754  57.41694  1.000 233.75911 ? 165 VAL E CG2 1 
ATOM   8866 N N   . LEU E 5 186 ? -18.01743 39.75795  55.22834  1.000 233.60036 ? 166 LEU E N   1 
ATOM   8867 C CA  . LEU E 5 186 ? -16.89455 39.41814  54.36358  1.000 229.69538 ? 166 LEU E CA  1 
ATOM   8868 C C   . LEU E 5 186 ? -15.89947 40.56969  54.29969  1.000 228.66836 ? 166 LEU E C   1 
ATOM   8869 O O   . LEU E 5 186 ? -16.24764 41.73284  54.52698  1.000 229.09186 ? 166 LEU E O   1 
ATOM   8870 C CB  . LEU E 5 186 ? -17.37872 39.07000  52.95747  1.000 224.04388 ? 166 LEU E CB  1 
ATOM   8871 C CG  . LEU E 5 186 ? -18.47918 38.01115  52.85987  1.000 223.77123 ? 166 LEU E CG  1 
ATOM   8872 C CD1 . LEU E 5 186 ? -18.74332 37.64631  51.40893  1.000 217.47247 ? 166 LEU E CD1 1 
ATOM   8873 C CD2 . LEU E 5 186 ? -18.12596 36.77739  53.67211  1.000 226.92971 ? 166 LEU E CD2 1 
ATOM   8874 N N   . ASN E 5 187 ? -14.64625 40.23473  54.00192  1.000 235.53257 ? 167 ASN E N   1 
ATOM   8875 C CA  . ASN E 5 187 ? -13.59209 41.24421  53.94800  1.000 234.30369 ? 167 ASN E CA  1 
ATOM   8876 C C   . ASN E 5 187 ? -12.60813 40.87073  52.84921  1.000 227.86925 ? 167 ASN E C   1 
ATOM   8877 O O   . ASN E 5 187 ? -11.96136 39.82282  52.92887  1.000 230.57956 ? 167 ASN E O   1 
ATOM   8878 C CB  . ASN E 5 187 ? -12.86950 41.40399  55.31488  1.000 238.71157 ? 167 ASN E CB  1 
ATOM   8879 C CG  . ASN E 5 187 ? -12.46522 40.05302  55.97947  1.000 236.88286 ? 167 ASN E CG  1 
ATOM   8880 O OD1 . ASN E 5 187 ? -12.81160 39.78545  57.14137  1.000 239.72626 ? 167 ASN E OD1 1 
ATOM   8881 N ND2 . ASN E 5 187 ? -11.79735 39.18528  55.21469  1.000 231.85864 ? 167 ASN E ND2 1 
ATOM   8882 N N   . SER E 5 188 ? -12.49593 41.70579  51.81710  1.000 226.29789 ? 168 SER E N   1 
ATOM   8883 C CA  . SER E 5 188 ? -11.60056 41.42166  50.70001  1.000 217.94099 ? 168 SER E CA  1 
ATOM   8884 C C   . SER E 5 188 ? -10.59049 42.55181  50.55411  1.000 210.24777 ? 168 SER E C   1 
ATOM   8885 O O   . SER E 5 188 ? -10.97095 43.70932  50.35630  1.000 209.85496 ? 168 SER E O   1 
ATOM   8886 C CB  . SER E 5 188 ? -12.38827 41.20882  49.40491  1.000 211.31595 ? 168 SER E CB  1 
ATOM   8887 O OG  . SER E 5 188 ? -13.21640 40.05922  49.49942  1.000 217.61872 ? 168 SER E OG  1 
ATOM   8888 N N   . TRP E 5 189 ? -9.30760  42.21700  50.65876  1.000 215.06838 ? 169 TRP E N   1 
ATOM   8889 C CA  . TRP E 5 189 ? -8.23150  43.18779  50.51522  1.000 208.74311 ? 169 TRP E CA  1 
ATOM   8890 C C   . TRP E 5 189 ? -7.48438  42.94353  49.21156  1.000 195.72256 ? 169 TRP E C   1 
ATOM   8891 O O   . TRP E 5 189 ? -7.18247  41.79784  48.86403  1.000 196.41141 ? 169 TRP E O   1 
ATOM   8892 C CB  . TRP E 5 189 ? -7.25451  43.12245  51.69303  1.000 217.27975 ? 169 TRP E CB  1 
ATOM   8893 C CG  . TRP E 5 189 ? -7.66080  43.94743  52.87613  1.000 224.26628 ? 169 TRP E CG  1 
ATOM   8894 C CD1 . TRP E 5 189 ? -7.40067  45.27239  53.08580  1.000 222.86293 ? 169 TRP E CD1 1 
ATOM   8895 C CD2 . TRP E 5 189 ? -8.39182  43.49677  54.01932  1.000 238.28380 ? 169 TRP E CD2 1 
ATOM   8896 N NE1 . TRP E 5 189 ? -7.93171  45.67362  54.28787  1.000 232.49527 ? 169 TRP E NE1 1 
ATOM   8897 C CE2 . TRP E 5 189 ? -8.54549  44.60138  54.88028  1.000 240.13603 ? 169 TRP E CE2 1 
ATOM   8898 C CE3 . TRP E 5 189 ? -8.93486  42.26619  54.39738  1.000 247.09247 ? 169 TRP E CE3 1 
ATOM   8899 C CZ2 . TRP E 5 189 ? -9.21978  44.51126  56.09529  1.000 249.62351 ? 169 TRP E CZ2 1 
ATOM   8900 C CZ3 . TRP E 5 189 ? -9.60008  42.17851  55.60381  1.000 257.61100 ? 169 TRP E CZ3 1 
ATOM   8901 C CH2 . TRP E 5 189 ? -9.73984  43.29404  56.43771  1.000 257.74241 ? 169 TRP E CH2 1 
ATOM   8902 N N   . THR E 5 190 ? -7.17593  44.02462  48.50015  1.000 214.64032 ? 170 THR E N   1 
ATOM   8903 C CA  . THR E 5 190 ? -6.56742  43.93947  47.18336  1.000 206.49250 ? 170 THR E CA  1 
ATOM   8904 C C   . THR E 5 190 ? -5.06023  44.17469  47.27225  1.000 206.15146 ? 170 THR E C   1 
ATOM   8905 O O   . THR E 5 190 ? -4.48391  44.29122  48.35805  1.000 212.15361 ? 170 THR E O   1 
ATOM   8906 C CB  . THR E 5 190 ? -7.22133  44.94097  46.22818  1.000 199.34360 ? 170 THR E CB  1 
ATOM   8907 O OG1 . THR E 5 190 ? -6.72723  46.25864  46.50081  1.000 196.62446 ? 170 THR E OG1 1 
ATOM   8908 C CG2 . THR E 5 190 ? -8.72912  44.92849  46.39664  1.000 200.86659 ? 170 THR E CG2 1 
ATOM   8909 N N   . ASP E 5 191 ? -4.41426  44.24588  46.11281  1.000 209.55294 ? 171 ASP E N   1 
ATOM   8910 C CA  . ASP E 5 191 ? -2.99024  44.51500  45.99058  1.000 214.56641 ? 171 ASP E CA  1 
ATOM   8911 C C   . ASP E 5 191 ? -2.77874  45.93424  45.47762  1.000 212.07184 ? 171 ASP E C   1 
ATOM   8912 O O   . ASP E 5 191 ? -3.71179  46.60492  45.02794  1.000 205.92752 ? 171 ASP E O   1 
ATOM   8913 C CB  . ASP E 5 191 ? -2.32739  43.50206  45.04944  1.000 213.45883 ? 171 ASP E CB  1 
ATOM   8914 C CG  . ASP E 5 191 ? -2.85537  42.09251  45.24346  1.000 216.47978 ? 171 ASP E CG  1 
ATOM   8915 O OD1 . ASP E 5 191 ? -2.99557  41.65966  46.40730  1.000 222.52260 ? 171 ASP E OD1 1 
ATOM   8916 O OD2 . ASP E 5 191 ? -3.13849  41.42033  44.22884  1.000 213.09324 ? 171 ASP E OD2 1 
ATOM   8917 N N   . GLN E 5 192 ? -1.53011  46.38748  45.54422  1.000 214.34742 ? 172 GLN E N   1 
ATOM   8918 C CA  . GLN E 5 192 ? -1.20099  47.72785  45.08288  1.000 211.92102 ? 172 GLN E CA  1 
ATOM   8919 C C   . GLN E 5 192 ? -1.38481  47.84245  43.57399  1.000 205.21268 ? 172 GLN E C   1 
ATOM   8920 O O   . GLN E 5 192 ? -1.21903  46.87432  42.82729  1.000 202.10787 ? 172 GLN E O   1 
ATOM   8921 C CB  . GLN E 5 192 ? 0.23497   48.08859  45.45897  1.000 214.55177 ? 172 GLN E CB  1 
ATOM   8922 C CG  . GLN E 5 192 ? 0.46095   48.26735  46.94463  1.000 221.73736 ? 172 GLN E CG  1 
ATOM   8923 C CD  . GLN E 5 192 ? 1.90656   48.56896  47.28309  1.000 222.72795 ? 172 GLN E CD  1 
ATOM   8924 O OE1 . GLN E 5 192 ? 2.20563   49.11288  48.34586  1.000 227.41489 ? 172 GLN E OE1 1 
ATOM   8925 N NE2 . GLN E 5 192 ? 2.81327   48.21582  46.37884  1.000 218.50455 ? 172 GLN E NE2 1 
ATOM   8926 N N   . ASP E 5 193 ? -1.73479  49.04409  43.13038  1.000 202.53150 ? 173 ASP E N   1 
ATOM   8927 C CA  . ASP E 5 193 ? -1.90280  49.32441  41.71416  1.000 196.89707 ? 173 ASP E CA  1 
ATOM   8928 C C   . ASP E 5 193 ? -0.57604  49.74242  41.08949  1.000 197.13042 ? 173 ASP E C   1 
ATOM   8929 O O   . ASP E 5 193 ? 0.36594   50.14634  41.77498  1.000 201.58305 ? 173 ASP E O   1 
ATOM   8930 C CB  . ASP E 5 193 ? -2.95184  50.41605  41.49980  1.000 193.76387 ? 173 ASP E CB  1 
ATOM   8931 C CG  . ASP E 5 193 ? -4.32378  49.85326  41.18279  1.000 191.14624 ? 173 ASP E CG  1 
ATOM   8932 O OD1 . ASP E 5 193 ? -4.78587  48.95770  41.92077  1.000 194.02837 ? 173 ASP E OD1 1 
ATOM   8933 O OD2 . ASP E 5 193 ? -4.94227  50.31198  40.19829  1.000 188.34424 ? 173 ASP E OD2 1 
ATOM   8934 N N   . SER E 5 194 ? -0.51352  49.63671  39.76393  1.000 205.19771 ? 174 SER E N   1 
ATOM   8935 C CA  . SER E 5 194 ? 0.68886   50.00143  39.02940  1.000 207.13490 ? 174 SER E CA  1 
ATOM   8936 C C   . SER E 5 194 ? 0.72941   51.47373  38.64921  1.000 207.84182 ? 174 SER E C   1 
ATOM   8937 O O   . SER E 5 194 ? 1.82085   52.01362  38.43527  1.000 211.40191 ? 174 SER E O   1 
ATOM   8938 C CB  . SER E 5 194 ? 0.81304   49.14802  37.76355  1.000 204.56210 ? 174 SER E CB  1 
ATOM   8939 O OG  . SER E 5 194 ? 0.78283   47.76699  38.07803  1.000 204.92458 ? 174 SER E OG  1 
ATOM   8940 N N   . LYS E 5 195 ? -0.42429  52.13366  38.56449  1.000 210.74569 ? 175 LYS E N   1 
ATOM   8941 C CA  . LYS E 5 195 ? -0.49132  53.53717  38.17784  1.000 210.51699 ? 175 LYS E CA  1 
ATOM   8942 C C   . LYS E 5 195 ? -0.75546  54.46598  39.35562  1.000 212.83745 ? 175 LYS E C   1 
ATOM   8943 O O   . LYS E 5 195 ? -0.11951  55.51913  39.45888  1.000 217.35494 ? 175 LYS E O   1 
ATOM   8944 C CB  . LYS E 5 195 ? -1.57304  53.73859  37.11088  1.000 204.45196 ? 175 LYS E CB  1 
ATOM   8945 C CG  . LYS E 5 195 ? -1.27539  54.86179  36.12821  1.000 203.59876 ? 175 LYS E CG  1 
ATOM   8946 C CD  . LYS E 5 195 ? -2.39129  55.01801  35.10500  1.000 198.75759 ? 175 LYS E CD  1 
ATOM   8947 C CE  . LYS E 5 195 ? -2.60869  53.73912  34.30892  1.000 193.33492 ? 175 LYS E CE  1 
ATOM   8948 N NZ  . LYS E 5 195 ? -1.41780  53.37133  33.49403  1.000 194.55299 ? 175 LYS E NZ  1 
ATOM   8949 N N   . ASP E 5 196 ? -1.67703  54.10421  40.25061  1.000 204.21121 ? 176 ASP E N   1 
ATOM   8950 C CA  . ASP E 5 196 ? -1.95004  54.91148  41.43288  1.000 207.34114 ? 176 ASP E CA  1 
ATOM   8951 C C   . ASP E 5 196 ? -1.26191  54.39637  42.68949  1.000 212.62379 ? 176 ASP E C   1 
ATOM   8952 O O   . ASP E 5 196 ? -1.10269  55.16607  43.64369  1.000 216.12193 ? 176 ASP E O   1 
ATOM   8953 C CB  . ASP E 5 196 ? -3.46067  55.00017  41.68964  1.000 204.97677 ? 176 ASP E CB  1 
ATOM   8954 C CG  . ASP E 5 196 ? -4.16249  53.66773  41.52178  1.000 203.60979 ? 176 ASP E CG  1 
ATOM   8955 O OD1 . ASP E 5 196 ? -4.23323  53.17277  40.37678  1.000 199.59648 ? 176 ASP E OD1 1 
ATOM   8956 O OD2 . ASP E 5 196 ? -4.63567  53.11119  42.53560  1.000 206.98163 ? 176 ASP E OD2 1 
ATOM   8957 N N   . SER E 5 197 ? -0.86191  53.12253  42.71347  1.000 196.44912 ? 177 SER E N   1 
ATOM   8958 C CA  . SER E 5 197 ? -0.10459  52.54353  43.82549  1.000 200.85257 ? 177 SER E CA  1 
ATOM   8959 C C   . SER E 5 197 ? -0.87457  52.64900  45.14175  1.000 203.77840 ? 177 SER E C   1 
ATOM   8960 O O   . SER E 5 197 ? -0.37244  53.15881  46.14558  1.000 208.01658 ? 177 SER E O   1 
ATOM   8961 C CB  . SER E 5 197 ? 1.27573   53.19453  43.94156  1.000 204.62424 ? 177 SER E CB  1 
ATOM   8962 O OG  . SER E 5 197 ? 2.05359   52.94870  42.78295  1.000 203.54322 ? 177 SER E OG  1 
ATOM   8963 N N   . THR E 5 198 ? -2.10854  52.15118  45.13232  1.000 205.52537 ? 178 THR E N   1 
ATOM   8964 C CA  . THR E 5 198 ? -2.99618  52.22971  46.28249  1.000 208.68612 ? 178 THR E CA  1 
ATOM   8965 C C   . THR E 5 198 ? -3.60153  50.86024  46.56285  1.000 206.08261 ? 178 THR E C   1 
ATOM   8966 O O   . THR E 5 198 ? -3.47281  49.92224  45.77211  1.000 200.34779 ? 178 THR E O   1 
ATOM   8967 C CB  . THR E 5 198 ? -4.11355  53.25734  46.05758  1.000 205.26258 ? 178 THR E CB  1 
ATOM   8968 O OG1 . THR E 5 198 ? -4.87422  52.88945  44.89990  1.000 199.94993 ? 178 THR E OG1 1 
ATOM   8969 C CG2 . THR E 5 198 ? -3.53520  54.65094  45.85690  1.000 204.63387 ? 178 THR E CG2 1 
ATOM   8970 N N   . TYR E 5 199 ? -4.27428  50.75668  47.70464  1.000 204.48253 ? 179 TYR E N   1 
ATOM   8971 C CA  . TYR E 5 199 ? -4.98466  49.55190  48.10691  1.000 204.91747 ? 179 TYR E CA  1 
ATOM   8972 C C   . TYR E 5 199 ? -6.48901  49.76840  47.98715  1.000 203.56952 ? 179 TYR E C   1 
ATOM   8973 O O   . TYR E 5 199 ? -6.96597  50.87282  47.71262  1.000 202.63848 ? 179 TYR E O   1 
ATOM   8974 C CB  . TYR E 5 199 ? -4.61912  49.15211  49.54181  1.000 213.72538 ? 179 TYR E CB  1 
ATOM   8975 C CG  . TYR E 5 199 ? -3.15830  48.81780  49.75233  1.000 219.76906 ? 179 TYR E CG  1 
ATOM   8976 C CD1 . TYR E 5 199 ? -2.24568  49.80078  50.11258  1.000 224.44832 ? 179 TYR E CD1 1 
ATOM   8977 C CD2 . TYR E 5 199 ? -2.69501  47.51665  49.60477  1.000 219.76676 ? 179 TYR E CD2 1 
ATOM   8978 C CE1 . TYR E 5 199 ? -0.91187  49.49910  50.31246  1.000 226.15427 ? 179 TYR E CE1 1 
ATOM   8979 C CE2 . TYR E 5 199 ? -1.36323  47.20519  49.80366  1.000 226.64477 ? 179 TYR E CE2 1 
ATOM   8980 C CZ  . TYR E 5 199 ? -0.47692  48.19995  50.15889  1.000 227.09528 ? 179 TYR E CZ  1 
ATOM   8981 O OH  . TYR E 5 199 ? 0.85051   47.89542  50.35497  1.000 228.47903 ? 179 TYR E OH  1 
ATOM   8982 N N   . SER E 5 200 ? -7.23824  48.68827  48.20212  1.000 202.01153 ? 180 SER E N   1 
ATOM   8983 C CA  . SER E 5 200 ? -8.69186  48.72698  48.12867  1.000 201.74292 ? 180 SER E CA  1 
ATOM   8984 C C   . SER E 5 200 ? -9.25885  47.63734  49.02706  1.000 208.52262 ? 180 SER E C   1 
ATOM   8985 O O   . SER E 5 200 ? -8.55556  46.70127  49.41643  1.000 210.45125 ? 180 SER E O   1 
ATOM   8986 C CB  . SER E 5 200 ? -9.18645  48.55062  46.68781  1.000 193.31362 ? 180 SER E CB  1 
ATOM   8987 O OG  . SER E 5 200 ? -8.64623  49.54674  45.83621  1.000 191.00382 ? 180 SER E OG  1 
ATOM   8988 N N   . MET E 5 201 ? -10.54497 47.76457  49.35263  1.000 199.32965 ? 181 MET E N   1 
ATOM   8989 C CA  . MET E 5 201 ? -11.18697 46.79233  50.22665  1.000 202.95211 ? 181 MET E CA  1 
ATOM   8990 C C   . MET E 5 201 ? -12.69746 46.83172  50.03653  1.000 203.54799 ? 181 MET E C   1 
ATOM   8991 O O   . MET E 5 201 ? -13.28066 47.90333  49.85923  1.000 201.25328 ? 181 MET E O   1 
ATOM   8992 C CB  . MET E 5 201 ? -10.84158 47.04721  51.69896  1.000 211.87909 ? 181 MET E CB  1 
ATOM   8993 C CG  . MET E 5 201 ? -11.42178 46.00695  52.64258  1.000 221.55246 ? 181 MET E CG  1 
ATOM   8994 S SD  . MET E 5 201 ? -11.66128 46.60715  54.32190  1.000 238.98747 ? 181 MET E SD  1 
ATOM   8995 C CE  . MET E 5 201 ? -13.00228 45.54420  54.85078  1.000 252.14510 ? 181 MET E CE  1 
ATOM   8996 N N   . SER E 5 202 ? -13.32102 45.65642  50.08669  1.000 208.03464 ? 182 SER E N   1 
ATOM   8997 C CA  . SER E 5 202 ? -14.76928 45.53073  50.03853  1.000 211.61263 ? 182 SER E CA  1 
ATOM   8998 C C   . SER E 5 202 ? -15.24790 44.74836  51.25477  1.000 230.41113 ? 182 SER E C   1 
ATOM   8999 O O   . SER E 5 202 ? -14.46617 44.08480  51.93948  1.000 235.55167 ? 182 SER E O   1 
ATOM   9000 C CB  . SER E 5 202 ? -15.23490 44.84004  48.74986  1.000 205.76408 ? 182 SER E CB  1 
ATOM   9001 O OG  . SER E 5 202 ? -14.72274 43.52189  48.66553  1.000 209.05565 ? 182 SER E OG  1 
ATOM   9002 N N   . SER E 5 203 ? -16.54980 44.83204  51.51720  1.000 215.03327 ? 183 SER E N   1 
ATOM   9003 C CA  . SER E 5 203 ? -17.14765 44.14949  52.65493  1.000 225.22223 ? 183 SER E CA  1 
ATOM   9004 C C   . SER E 5 203 ? -18.59912 43.83670  52.32717  1.000 226.59782 ? 183 SER E C   1 
ATOM   9005 O O   . SER E 5 203 ? -19.26860 44.61214  51.64308  1.000 221.07584 ? 183 SER E O   1 
ATOM   9006 C CB  . SER E 5 203 ? -17.05310 44.99834  53.92769  1.000 227.68477 ? 183 SER E CB  1 
ATOM   9007 O OG  . SER E 5 203 ? -17.36681 44.23406  55.07604  1.000 236.04683 ? 183 SER E OG  1 
ATOM   9008 N N   . THR E 5 204 ? -19.08319 42.69867  52.82428  1.000 228.19471 ? 184 THR E N   1 
ATOM   9009 C CA  . THR E 5 204 ? -20.41825 42.21071  52.49734  1.000 228.55098 ? 184 THR E CA  1 
ATOM   9010 C C   . THR E 5 204 ? -21.19488 41.95786  53.78039  1.000 234.39259 ? 184 THR E C   1 
ATOM   9011 O O   . THR E 5 204 ? -20.76064 41.17003  54.62651  1.000 237.92138 ? 184 THR E O   1 
ATOM   9012 C CB  . THR E 5 204 ? -20.34719 40.93271  51.65745  1.000 225.24491 ? 184 THR E CB  1 
ATOM   9013 O OG1 . THR E 5 204 ? -19.53916 41.16529  50.49746  1.000 220.15097 ? 184 THR E OG1 1 
ATOM   9014 C CG2 . THR E 5 204 ? -21.73474 40.50430  51.22235  1.000 223.85754 ? 184 THR E CG2 1 
ATOM   9015 N N   . LEU E 5 205 ? -22.34262 42.62468  53.92077  1.000 233.51820 ? 185 LEU E N   1 
ATOM   9016 C CA  . LEU E 5 205 ? -23.21513 42.45143  55.08241  1.000 239.11831 ? 185 LEU E CA  1 
ATOM   9017 C C   . LEU E 5 205 ? -24.28134 41.41562  54.73408  1.000 238.69011 ? 185 LEU E C   1 
ATOM   9018 O O   . LEU E 5 205 ? -25.41207 41.73368  54.35874  1.000 237.82176 ? 185 LEU E O   1 
ATOM   9019 C CB  . LEU E 5 205 ? -23.83135 43.78342  55.49138  1.000 240.18946 ? 185 LEU E CB  1 
ATOM   9020 C CG  . LEU E 5 205 ? -24.61087 43.82137  56.80647  1.000 247.04355 ? 185 LEU E CG  1 
ATOM   9021 C CD1 . LEU E 5 205 ? -23.66581 43.73266  57.99502  1.000 251.12031 ? 185 LEU E CD1 1 
ATOM   9022 C CD2 . LEU E 5 205 ? -25.46784 45.07515  56.88664  1.000 244.44579 ? 185 LEU E CD2 1 
ATOM   9023 N N   . THR E 5 206 ? -23.90212 40.14623  54.86685  1.000 238.87464 ? 186 THR E N   1 
ATOM   9024 C CA  . THR E 5 206 ? -24.80606 39.05071  54.54065  1.000 238.01198 ? 186 THR E CA  1 
ATOM   9025 C C   . THR E 5 206 ? -25.95320 38.99424  55.54255  1.000 243.48924 ? 186 THR E C   1 
ATOM   9026 O O   . THR E 5 206 ? -25.73333 39.01972  56.75736  1.000 248.87270 ? 186 THR E O   1 
ATOM   9027 C CB  . THR E 5 206 ? -24.04876 37.72315  54.52808  1.000 237.19499 ? 186 THR E CB  1 
ATOM   9028 O OG1 . THR E 5 206 ? -23.55848 37.43618  55.84391  1.000 242.80043 ? 186 THR E OG1 1 
ATOM   9029 C CG2 . THR E 5 206 ? -22.87445 37.79008  53.56164  1.000 232.17122 ? 186 THR E CG2 1 
ATOM   9030 N N   . LEU E 5 207 ? -27.17987 38.91214  55.03071  1.000 247.59720 ? 187 LEU E N   1 
ATOM   9031 C CA  . LEU E 5 207 ? -28.36379 38.93079  55.87627  1.000 252.73003 ? 187 LEU E CA  1 
ATOM   9032 C C   . LEU E 5 207 ? -29.49194 38.16877  55.19860  1.000 250.65735 ? 187 LEU E C   1 
ATOM   9033 O O   . LEU E 5 207 ? -29.53321 38.04910  53.97110  1.000 244.81608 ? 187 LEU E O   1 
ATOM   9034 C CB  . LEU E 5 207 ? -28.81127 40.36515  56.18177  1.000 254.65192 ? 187 LEU E CB  1 
ATOM   9035 C CG  . LEU E 5 207 ? -28.23248 41.01244  57.43943  1.000 259.73903 ? 187 LEU E CG  1 
ATOM   9036 C CD1 . LEU E 5 207 ? -28.47434 42.51198  57.42820  1.000 259.55078 ? 187 LEU E CD1 1 
ATOM   9037 C CD2 . LEU E 5 207 ? -28.84294 40.38123  58.67940  1.000 266.21145 ? 187 LEU E CD2 1 
ATOM   9038 N N   . THR E 5 208 ? -30.40768 37.65659  56.01561  1.000 252.39834 ? 188 THR E N   1 
ATOM   9039 C CA  . THR E 5 208 ? -31.59472 36.99405  55.50408  1.000 251.32072 ? 188 THR E CA  1 
ATOM   9040 C C   . THR E 5 208 ? -32.60292 38.02949  55.01386  1.000 250.54808 ? 188 THR E C   1 
ATOM   9041 O O   . THR E 5 208 ? -32.52853 39.21492  55.34903  1.000 252.25481 ? 188 THR E O   1 
ATOM   9042 C CB  . THR E 5 208 ? -32.23331 36.11501  56.58088  1.000 257.27273 ? 188 THR E CB  1 
ATOM   9043 O OG1 . THR E 5 208 ? -33.10219 36.91089  57.39607  1.000 262.71548 ? 188 THR E OG1 1 
ATOM   9044 C CG2 . THR E 5 208 ? -31.16094 35.49092  57.46439  1.000 259.95568 ? 188 THR E CG2 1 
ATOM   9045 N N   . LYS E 5 209 ? -33.56062 37.56444  54.20839  1.000 257.79835 ? 189 LYS E N   1 
ATOM   9046 C CA  . LYS E 5 209 ? -34.57478 38.47252  53.68185  1.000 256.89953 ? 189 LYS E CA  1 
ATOM   9047 C C   . LYS E 5 209 ? -35.50090 38.96969  54.78543  1.000 263.87395 ? 189 LYS E C   1 
ATOM   9048 O O   . LYS E 5 209 ? -35.85900 40.15307  54.81473  1.000 264.70618 ? 189 LYS E O   1 
ATOM   9049 C CB  . LYS E 5 209 ? -35.37665 37.78817  52.57539  1.000 252.53390 ? 189 LYS E CB  1 
ATOM   9050 C CG  . LYS E 5 209 ? -36.42791 38.68566  51.94206  1.000 251.22858 ? 189 LYS E CG  1 
ATOM   9051 C CD  . LYS E 5 209 ? -37.19722 37.96512  50.84853  1.000 246.86108 ? 189 LYS E CD  1 
ATOM   9052 C CE  . LYS E 5 209 ? -38.26831 38.86342  50.25067  1.000 245.90984 ? 189 LYS E CE  1 
ATOM   9053 N NZ  . LYS E 5 209 ? -39.04797 38.17317  49.18757  1.000 241.79071 ? 189 LYS E NZ  1 
ATOM   9054 N N   . ASP E 5 210 ? -35.89693 38.08340  55.70303  1.000 255.72680 ? 190 ASP E N   1 
ATOM   9055 C CA  . ASP E 5 210 ? -36.76916 38.49526  56.79897  1.000 262.74264 ? 190 ASP E CA  1 
ATOM   9056 C C   . ASP E 5 210 ? -36.06418 39.47790  57.72619  1.000 266.03510 ? 190 ASP E C   1 
ATOM   9057 O O   . ASP E 5 210 ? -36.68900 40.41373  58.23868  1.000 269.52870 ? 190 ASP E O   1 
ATOM   9058 C CB  . ASP E 5 210 ? -37.25162 37.26934  57.57643  1.000 267.48907 ? 190 ASP E CB  1 
ATOM   9059 C CG  . ASP E 5 210 ? -36.12921 36.56912  58.32046  1.000 269.10109 ? 190 ASP E CG  1 
ATOM   9060 O OD1 . ASP E 5 210 ? -35.82264 36.97936  59.46013  1.000 274.30686 ? 190 ASP E OD1 1 
ATOM   9061 O OD2 . ASP E 5 210 ? -35.54791 35.61430  57.76319  1.000 265.09489 ? 190 ASP E OD2 1 
ATOM   9062 N N   . GLU E 5 211 ? -34.76256 39.28245  57.95068  1.000 266.85937 ? 191 GLU E N   1 
ATOM   9063 C CA  . GLU E 5 211 ? -34.00285 40.20601  58.78547  1.000 269.59396 ? 191 GLU E CA  1 
ATOM   9064 C C   . GLU E 5 211 ? -33.80060 41.54752  58.09488  1.000 265.69662 ? 191 GLU E C   1 
ATOM   9065 O O   . GLU E 5 211 ? -33.77350 42.58912  58.76019  1.000 268.42723 ? 191 GLU E O   1 
ATOM   9066 C CB  . GLU E 5 211 ? -32.65112 39.58896  59.14460  1.000 269.28953 ? 191 GLU E CB  1 
ATOM   9067 C CG  . GLU E 5 211 ? -32.36176 39.51446  60.63207  1.000 275.97928 ? 191 GLU E CG  1 
ATOM   9068 C CD  . GLU E 5 211 ? -31.07502 38.77021  60.93008  1.000 275.59711 ? 191 GLU E CD  1 
ATOM   9069 O OE1 . GLU E 5 211 ? -30.70304 37.88202  60.13392  1.000 271.30459 ? 191 GLU E OE1 1 
ATOM   9070 O OE2 . GLU E 5 211 ? -30.43173 39.07771  61.95505  1.000 279.44127 ? 191 GLU E OE2 1 
ATOM   9071 N N   . TYR E 5 212 ? -33.65906 41.54042  56.76763  1.000 277.49255 ? 192 TYR E N   1 
ATOM   9072 C CA  . TYR E 5 212 ? -33.40907 42.77433  56.03149  1.000 273.34197 ? 192 TYR E CA  1 
ATOM   9073 C C   . TYR E 5 212 ? -34.63227 43.68136  56.01102  1.000 274.89164 ? 192 TYR E C   1 
ATOM   9074 O O   . TYR E 5 212 ? -34.49016 44.90888  55.97286  1.000 274.13976 ? 192 TYR E O   1 
ATOM   9075 C CB  . TYR E 5 212 ? -32.96505 42.43920  54.60717  1.000 266.03923 ? 192 TYR E CB  1 
ATOM   9076 C CG  . TYR E 5 212 ? -32.71067 43.63783  53.72219  1.000 261.29743 ? 192 TYR E CG  1 
ATOM   9077 C CD1 . TYR E 5 212 ? -31.69988 44.54226  54.01800  1.000 260.20852 ? 192 TYR E CD1 1 
ATOM   9078 C CD2 . TYR E 5 212 ? -33.46616 43.85087  52.57612  1.000 256.87331 ? 192 TYR E CD2 1 
ATOM   9079 C CE1 . TYR E 5 212 ? -31.45880 45.63447  53.20643  1.000 251.72272 ? 192 TYR E CE1 1 
ATOM   9080 C CE2 . TYR E 5 212 ? -33.23172 44.93899  51.75775  1.000 248.86061 ? 192 TYR E CE2 1 
ATOM   9081 C CZ  . TYR E 5 212 ? -32.22689 45.82710  52.07730  1.000 246.07454 ? 192 TYR E CZ  1 
ATOM   9082 O OH  . TYR E 5 212 ? -31.99024 46.91212  51.26506  1.000 237.47902 ? 192 TYR E OH  1 
ATOM   9083 N N   . GLU E 5 213 ? -35.83524 43.10430  56.04534  1.000 269.65965 ? 193 GLU E N   1 
ATOM   9084 C CA  . GLU E 5 213 ? -37.07316 43.86845  55.94910  1.000 271.07660 ? 193 GLU E CA  1 
ATOM   9085 C C   . GLU E 5 213 ? -37.60599 44.30820  57.30867  1.000 278.34118 ? 193 GLU E C   1 
ATOM   9086 O O   . GLU E 5 213 ? -38.81647 44.52442  57.45729  1.000 281.24117 ? 193 GLU E O   1 
ATOM   9087 C CB  . GLU E 5 213 ? -38.12579 43.05954  55.19047  1.000 269.54958 ? 193 GLU E CB  1 
ATOM   9088 C CG  . GLU E 5 213 ? -37.68931 42.68432  53.78265  1.000 262.08059 ? 193 GLU E CG  1 
ATOM   9089 C CD  . GLU E 5 213 ? -38.82201 42.14199  52.93589  1.000 259.88220 ? 193 GLU E CD  1 
ATOM   9090 O OE1 . GLU E 5 213 ? -39.39425 41.09265  53.29866  1.000 262.65415 ? 193 GLU E OE1 1 
ATOM   9091 O OE2 . GLU E 5 213 ? -39.14307 42.77301  51.90686  1.000 255.38663 ? 193 GLU E OE2 1 
ATOM   9092 N N   . ARG E 5 214 ? -36.73280 44.44779  58.30550  1.000 267.81450 ? 194 ARG E N   1 
ATOM   9093 C CA  . ARG E 5 214 ? -37.10024 44.99627  59.60441  1.000 274.27560 ? 194 ARG E CA  1 
ATOM   9094 C C   . ARG E 5 214 ? -36.53628 46.39783  59.79540  1.000 272.62967 ? 194 ARG E C   1 
ATOM   9095 O O   . ARG E 5 214 ? -37.28660 47.34309  60.05430  1.000 272.61339 ? 194 ARG E O   1 
ATOM   9096 C CB  . ARG E 5 214 ? -36.61574 44.07257  60.73032  1.000 279.10645 ? 194 ARG E CB  1 
ATOM   9097 C CG  . ARG E 5 214 ? -37.24362 42.69177  60.72770  1.000 281.04276 ? 194 ARG E CG  1 
ATOM   9098 C CD  . ARG E 5 214 ? -36.65512 41.82895  61.83183  1.000 285.57642 ? 194 ARG E CD  1 
ATOM   9099 N NE  . ARG E 5 214 ? -37.24598 40.49673  61.86336  1.000 287.47211 ? 194 ARG E NE  1 
ATOM   9100 C CZ  . ARG E 5 214 ? -36.85886 39.52628  62.67975  1.000 291.04799 ? 194 ARG E CZ  1 
ATOM   9101 N NH1 . ARG E 5 214 ? -35.87449 39.70327  63.54581  1.000 293.28135 ? 194 ARG E NH1 1 
ATOM   9102 N NH2 . ARG E 5 214 ? -37.47390 38.34837  62.62513  1.000 292.36022 ? 194 ARG E NH2 1 
ATOM   9103 N N   . HIS E 5 215 ? -35.22203 46.55244  59.67088  1.000 269.57885 ? 195 HIS E N   1 
ATOM   9104 C CA  . HIS E 5 215 ? -34.58206 47.84964  59.79468  1.000 264.47125 ? 195 HIS E CA  1 
ATOM   9105 C C   . HIS E 5 215 ? -34.69338 48.62362  58.48401  1.000 255.41447 ? 195 HIS E C   1 
ATOM   9106 O O   . HIS E 5 215 ? -34.99985 48.06747  57.42613  1.000 252.57579 ? 195 HIS E O   1 
ATOM   9107 C CB  . HIS E 5 215 ? -33.11410 47.68257  60.18706  1.000 263.92563 ? 195 HIS E CB  1 
ATOM   9108 C CG  . HIS E 5 215 ? -32.89557 46.71245  61.30654  1.000 272.17925 ? 195 HIS E CG  1 
ATOM   9109 N ND1 . HIS E 5 215 ? -33.08027 47.04784  62.63062  1.000 277.70437 ? 195 HIS E ND1 1 
ATOM   9110 C CD2 . HIS E 5 215 ? -32.50886 45.41477  61.29804  1.000 274.54684 ? 195 HIS E CD2 1 
ATOM   9111 C CE1 . HIS E 5 215 ? -32.81577 45.99922  63.38946  1.000 283.70131 ? 195 HIS E CE1 1 
ATOM   9112 N NE2 . HIS E 5 215 ? -32.46675 44.99520  62.60545  1.000 280.51225 ? 195 HIS E NE2 1 
ATOM   9113 N N   . ASN E 5 216 ? -34.44102 49.92895  58.56545  1.000 271.34055 ? 196 ASN E N   1 
ATOM   9114 C CA  . ASN E 5 216 ? -34.48934 50.79366  57.39277  1.000 262.55162 ? 196 ASN E CA  1 
ATOM   9115 C C   . ASN E 5 216 ? -33.22576 51.60708  57.16067  1.000 255.86424 ? 196 ASN E C   1 
ATOM   9116 O O   . ASN E 5 216 ? -33.02284 52.07392  56.03371  1.000 248.26451 ? 196 ASN E O   1 
ATOM   9117 C CB  . ASN E 5 216 ? -35.68652 51.75303  57.47891  1.000 262.46097 ? 196 ASN E CB  1 
ATOM   9118 C CG  . ASN E 5 216 ? -36.93166 51.18980  56.82057  1.000 263.92035 ? 196 ASN E CG  1 
ATOM   9119 O OD1 . ASN E 5 216 ? -37.31648 51.61451  55.73107  1.000 257.64661 ? 196 ASN E OD1 1 
ATOM   9120 N ND2 . ASN E 5 216 ? -37.56202 50.22097  57.47453  1.000 272.16484 ? 196 ASN E ND2 1 
ATOM   9121 N N   . SER E 5 217 ? -32.37448 51.79102  58.16512  1.000 258.33912 ? 197 SER E N   1 
ATOM   9122 C CA  . SER E 5 217 ? -31.12232 52.52011  58.01666  1.000 252.55580 ? 197 SER E CA  1 
ATOM   9123 C C   . SER E 5 217 ? -29.95596 51.54744  58.12438  1.000 254.08578 ? 197 SER E C   1 
ATOM   9124 O O   . SER E 5 217 ? -29.85549 50.79735  59.10111  1.000 261.20598 ? 197 SER E O   1 
ATOM   9125 C CB  . SER E 5 217 ? -30.99998 53.62284  59.07137  1.000 253.92205 ? 197 SER E CB  1 
ATOM   9126 O OG  . SER E 5 217 ? -31.20265 53.11033  60.37662  1.000 262.41262 ? 197 SER E OG  1 
ATOM   9127 N N   . TYR E 5 218 ? -29.08112 51.56112  57.12014  1.000 250.23324 ? 198 TYR E N   1 
ATOM   9128 C CA  . TYR E 5 218 ? -27.92869 50.66883  57.06237  1.000 251.02744 ? 198 TYR E CA  1 
ATOM   9129 C C   . TYR E 5 218 ? -26.69002 51.49370  56.74931  1.000 244.68290 ? 198 TYR E C   1 
ATOM   9130 O O   . TYR E 5 218 ? -26.64397 52.18036  55.72368  1.000 237.48014 ? 198 TYR E O   1 
ATOM   9131 C CB  . TYR E 5 218 ? -28.13281 49.57411  56.01122  1.000 250.01007 ? 198 TYR E CB  1 
ATOM   9132 C CG  . TYR E 5 218 ? -29.30127 48.65773  56.30018  1.000 256.81439 ? 198 TYR E CG  1 
ATOM   9133 C CD1 . TYR E 5 218 ? -29.13000 47.49849  57.04431  1.000 264.35839 ? 198 TYR E CD1 1 
ATOM   9134 C CD2 . TYR E 5 218 ? -30.57477 48.95127  55.82886  1.000 255.76335 ? 198 TYR E CD2 1 
ATOM   9135 C CE1 . TYR E 5 218 ? -30.19291 46.65675  57.31149  1.000 270.66337 ? 198 TYR E CE1 1 
ATOM   9136 C CE2 . TYR E 5 218 ? -31.64456 48.11508  56.09093  1.000 262.09517 ? 198 TYR E CE2 1 
ATOM   9137 C CZ  . TYR E 5 218 ? -31.44762 46.96942  56.83266  1.000 269.53064 ? 198 TYR E CZ  1 
ATOM   9138 O OH  . TYR E 5 218 ? -32.50827 46.13324  57.09699  1.000 275.78356 ? 198 TYR E OH  1 
ATOM   9139 N N   . THR E 5 219 ? -25.68746 51.41874  57.62388  1.000 250.71686 ? 199 THR E N   1 
ATOM   9140 C CA  . THR E 5 219 ? -24.50702 52.26539  57.53623  1.000 245.78764 ? 199 THR E CA  1 
ATOM   9141 C C   . THR E 5 219 ? -23.24371 51.42533  57.67188  1.000 247.26956 ? 199 THR E C   1 
ATOM   9142 O O   . THR E 5 219 ? -23.23449 50.38995  58.34321  1.000 253.62388 ? 199 THR E O   1 
ATOM   9143 C CB  . THR E 5 219 ? -24.52582 53.35354  58.62580  1.000 247.32643 ? 199 THR E CB  1 
ATOM   9144 O OG1 . THR E 5 219 ? -25.83739 53.92449  58.71038  1.000 247.88505 ? 199 THR E OG1 1 
ATOM   9145 C CG2 . THR E 5 219 ? -23.52498 54.45575  58.31176  1.000 241.27959 ? 199 THR E CG2 1 
ATOM   9146 N N   . CYS E 5 220 ? -22.17569 51.88269  57.01908  1.000 252.43549 ? 200 CYS E N   1 
ATOM   9147 C CA  . CYS E 5 220 ? -20.84879 51.29467  57.14864  1.000 253.32307 ? 200 CYS E CA  1 
ATOM   9148 C C   . CYS E 5 220 ? -19.84971 52.41004  57.41726  1.000 249.70520 ? 200 CYS E C   1 
ATOM   9149 O O   . CYS E 5 220 ? -19.81695 53.40612  56.68752  1.000 243.46793 ? 200 CYS E O   1 
ATOM   9150 C CB  . CYS E 5 220 ? -20.45869 50.50896  55.88875  1.000 249.79136 ? 200 CYS E CB  1 
ATOM   9151 S SG  . CYS E 5 220 ? -20.55410 51.45315  54.34622  1.000 239.49896 ? 200 CYS E SG  1 
ATOM   9152 N N   . GLU E 5 221 ? -19.04687 52.24995  58.46653  1.000 237.10368 ? 201 GLU E N   1 
ATOM   9153 C CA  . GLU E 5 221 ? -18.06834 53.25252  58.86617  1.000 234.93835 ? 201 GLU E CA  1 
ATOM   9154 C C   . GLU E 5 221 ? -16.66851 52.66040  58.80517  1.000 234.93877 ? 201 GLU E C   1 
ATOM   9155 O O   . GLU E 5 221 ? -16.42332 51.57397  59.34044  1.000 239.88859 ? 201 GLU E O   1 
ATOM   9156 C CB  . GLU E 5 221 ? -18.35921 53.78411  60.27393  1.000 239.62989 ? 201 GLU E CB  1 
ATOM   9157 C CG  . GLU E 5 221 ? -18.68491 52.71722  61.30020  1.000 247.25406 ? 201 GLU E CG  1 
ATOM   9158 C CD  . GLU E 5 221 ? -18.87995 53.28644  62.69215  1.000 251.58607 ? 201 GLU E CD  1 
ATOM   9159 O OE1 . GLU E 5 221 ? -18.76032 54.51925  62.85474  1.000 248.89900 ? 201 GLU E OE1 1 
ATOM   9160 O OE2 . GLU E 5 221 ? -19.15246 52.50039  63.62394  1.000 257.85820 ? 201 GLU E OE2 1 
ATOM   9161 N N   . ALA E 5 222 ? -15.75774 53.37746  58.15473  1.000 228.21766 ? 202 ALA E N   1 
ATOM   9162 C CA  . ALA E 5 222 ? -14.36253 52.98342  58.05483  1.000 226.82921 ? 202 ALA E CA  1 
ATOM   9163 C C   . ALA E 5 222 ? -13.48762 53.96980  58.81601  1.000 229.48574 ? 202 ALA E C   1 
ATOM   9164 O O   . ALA E 5 222 ? -13.79914 55.16071  58.90876  1.000 231.13499 ? 202 ALA E O   1 
ATOM   9165 C CB  . ALA E 5 222 ? -13.91189 52.90696  56.59556  1.000 222.74039 ? 202 ALA E CB  1 
ATOM   9166 N N   . THR E 5 223 ? -12.38522 53.46177  59.35720  1.000 226.46122 ? 203 THR E N   1 
ATOM   9167 C CA  . THR E 5 223 ? -11.47948 54.24020  60.19827  1.000 227.64157 ? 203 THR E CA  1 
ATOM   9168 C C   . THR E 5 223 ? -10.14207 54.37041  59.47739  1.000 222.83216 ? 203 THR E C   1 
ATOM   9169 O O   . THR E 5 223 ? -9.30671  53.46314  59.52738  1.000 223.90113 ? 203 THR E O   1 
ATOM   9170 C CB  . THR E 5 223 ? -11.31240 53.58509  61.56618  1.000 237.35999 ? 203 THR E CB  1 
ATOM   9171 O OG1 . THR E 5 223 ? -10.79166 52.25988  61.40272  1.000 239.50705 ? 203 THR E OG1 1 
ATOM   9172 C CG2 . THR E 5 223 ? -12.65168 53.51269  62.28601  1.000 240.73737 ? 203 THR E CG2 1 
ATOM   9173 N N   . HIS E 5 224 ? -9.94010  55.50421  58.81430  1.000 244.71170 ? 204 HIS E N   1 
ATOM   9174 C CA  . HIS E 5 224 ? -8.71506  55.77891  58.07947  1.000 240.09036 ? 204 HIS E CA  1 
ATOM   9175 C C   . HIS E 5 224 ? -7.93719  56.89674  58.76289  1.000 241.67669 ? 204 HIS E C   1 
ATOM   9176 O O   . HIS E 5 224 ? -8.51676  57.76642  59.41849  1.000 242.57912 ? 204 HIS E O   1 
ATOM   9177 C CB  . HIS E 5 224 ? -9.01968  56.16291  56.62786  1.000 231.67822 ? 204 HIS E CB  1 
ATOM   9178 C CG  . HIS E 5 224 ? -7.84431  56.03487  55.70887  1.000 227.32319 ? 204 HIS E CG  1 
ATOM   9179 N ND1 . HIS E 5 224 ? -6.87261  57.00643  55.60211  1.000 224.77157 ? 204 HIS E ND1 1 
ATOM   9180 C CD2 . HIS E 5 224 ? -7.48586  55.04930  54.85194  1.000 225.49113 ? 204 HIS E CD2 1 
ATOM   9181 C CE1 . HIS E 5 224 ? -5.96520  56.62415  54.72143  1.000 221.63933 ? 204 HIS E CE1 1 
ATOM   9182 N NE2 . HIS E 5 224 ? -6.31403  55.44035  54.25089  1.000 221.77221 ? 204 HIS E NE2 1 
ATOM   9183 N N   . LYS E 5 225 ? -6.61286  56.87019  58.59405  1.000 241.25439 ? 205 LYS E N   1 
ATOM   9184 C CA  . LYS E 5 225 ? -5.74094  57.81738  59.28259  1.000 242.32586 ? 205 LYS E CA  1 
ATOM   9185 C C   . LYS E 5 225 ? -5.92819  59.25400  58.80932  1.000 237.87899 ? 205 LYS E C   1 
ATOM   9186 O O   . LYS E 5 225 ? -5.59857  60.18465  59.55343  1.000 240.14818 ? 205 LYS E O   1 
ATOM   9187 C CB  . LYS E 5 225 ? -4.28061  57.40073  59.09704  1.000 241.61272 ? 205 LYS E CB  1 
ATOM   9188 C CG  . LYS E 5 225 ? -3.97543  55.99537  59.58336  1.000 245.98245 ? 205 LYS E CG  1 
ATOM   9189 C CD  . LYS E 5 225 ? -2.59933  55.53775  59.13937  1.000 244.42097 ? 205 LYS E CD  1 
ATOM   9190 C CE  . LYS E 5 225 ? -2.37948  54.07469  59.49001  1.000 248.34236 ? 205 LYS E CE  1 
ATOM   9191 N NZ  . LYS E 5 225 ? -1.02784  53.59258  59.09069  1.000 246.43515 ? 205 LYS E NZ  1 
ATOM   9192 N N   . THR E 5 226 ? -6.44627  59.45781  57.59671  1.000 238.56302 ? 206 THR E N   1 
ATOM   9193 C CA  . THR E 5 226 ? -6.56138  60.80992  57.05855  1.000 234.34361 ? 206 THR E CA  1 
ATOM   9194 C C   . THR E 5 226 ? -7.50839  61.66199  57.89532  1.000 236.91397 ? 206 THR E C   1 
ATOM   9195 O O   . THR E 5 226 ? -7.18517  62.80060  58.25091  1.000 237.39124 ? 206 THR E O   1 
ATOM   9196 C CB  . THR E 5 226 ? -7.02974  60.75718  55.60412  1.000 227.94895 ? 206 THR E CB  1 
ATOM   9197 O OG1 . THR E 5 226 ? -8.21160  59.95265  55.50819  1.000 228.50023 ? 206 THR E OG1 1 
ATOM   9198 C CG2 . THR E 5 226 ? -5.94819  60.17177  54.71345  1.000 224.95823 ? 206 THR E CG2 1 
ATOM   9199 N N   . SER E 5 227 ? -8.68438  61.13153  58.21399  1.000 246.12729 ? 207 SER E N   1 
ATOM   9200 C CA  . SER E 5 227 ? -9.69444  61.86127  58.96315  1.000 248.68621 ? 207 SER E CA  1 
ATOM   9201 C C   . SER E 5 227 ? -9.87811  61.25029  60.34631  1.000 256.10143 ? 207 SER E C   1 
ATOM   9202 O O   . SER E 5 227 ? -9.58319  60.07489  60.57769  1.000 259.19884 ? 207 SER E O   1 
ATOM   9203 C CB  . SER E 5 227 ? -11.03095 61.86789  58.21325  1.000 245.46714 ? 207 SER E CB  1 
ATOM   9204 O OG  . SER E 5 227 ? -11.98208 62.68222  58.87448  1.000 244.59393 ? 207 SER E OG  1 
ATOM   9205 N N   . THR E 5 228 ? -10.36984 62.07303  61.27274  1.000 245.75266 ? 208 THR E N   1 
ATOM   9206 C CA  . THR E 5 228 ? -10.68575 61.60240  62.61389  1.000 253.11342 ? 208 THR E CA  1 
ATOM   9207 C C   . THR E 5 228 ? -12.10889 61.07882  62.73333  1.000 256.25099 ? 208 THR E C   1 
ATOM   9208 O O   . THR E 5 228 ? -12.39577 60.30830  63.65608  1.000 264.06206 ? 208 THR E O   1 
ATOM   9209 C CB  . THR E 5 228 ? -10.47164 62.71980  63.64099  1.000 256.04098 ? 208 THR E CB  1 
ATOM   9210 O OG1 . THR E 5 228 ? -10.74644 62.22011  64.95546  1.000 264.72900 ? 208 THR E OG1 1 
ATOM   9211 C CG2 . THR E 5 228 ? -11.39101 63.89295  63.35331  1.000 252.55518 ? 208 THR E CG2 1 
ATOM   9212 N N   . SER E 5 229 ? -13.00057 61.47399  61.82807  1.000 249.37974 ? 209 SER E N   1 
ATOM   9213 C CA  . SER E 5 229 ? -14.35703 60.94284  61.83965  1.000 252.54752 ? 209 SER E CA  1 
ATOM   9214 C C   . SER E 5 229 ? -14.41730 59.63743  61.05537  1.000 251.42612 ? 209 SER E C   1 
ATOM   9215 O O   . SER E 5 229 ? -13.74611 59.50065  60.02810  1.000 244.56899 ? 209 SER E O   1 
ATOM   9216 C CB  . SER E 5 229 ? -15.33666 61.93880  61.22978  1.000 247.87164 ? 209 SER E CB  1 
ATOM   9217 O OG  . SER E 5 229 ? -15.00728 62.20965  59.87752  1.000 239.59198 ? 209 SER E OG  1 
ATOM   9218 N N   . PRO E 5 230 ? -15.19506 58.66315  61.51994  1.000 243.59013 ? 210 PRO E N   1 
ATOM   9219 C CA  . PRO E 5 230 ? -15.39131 57.44212  60.72654  1.000 242.83252 ? 210 PRO E CA  1 
ATOM   9220 C C   . PRO E 5 230 ? -16.09939 57.76310  59.41836  1.000 236.27689 ? 210 PRO E C   1 
ATOM   9221 O O   . PRO E 5 230 ? -17.25726 58.18322  59.42298  1.000 236.33928 ? 210 PRO E O   1 
ATOM   9222 C CB  . PRO E 5 230 ? -16.24933 56.56084  61.64039  1.000 248.70576 ? 210 PRO E CB  1 
ATOM   9223 C CG  . PRO E 5 230 ? -16.93061 57.52333  62.56680  1.000 250.85452 ? 210 PRO E CG  1 
ATOM   9224 C CD  . PRO E 5 230 ? -15.95848 58.64404  62.77825  1.000 248.89158 ? 210 PRO E CD  1 
ATOM   9225 N N   . ILE E 5 231 ? -15.39823 57.59131  58.29660  1.000 242.65725 ? 211 ILE E N   1 
ATOM   9226 C CA  . ILE E 5 231 ? -15.95804 57.94690  56.99809  1.000 235.21940 ? 211 ILE E CA  1 
ATOM   9227 C C   . ILE E 5 231 ? -17.18231 57.07368  56.73204  1.000 238.43215 ? 211 ILE E C   1 
ATOM   9228 O O   . ILE E 5 231 ? -17.07840 55.84968  56.58329  1.000 240.89952 ? 211 ILE E O   1 
ATOM   9229 C CB  . ILE E 5 231 ? -14.89360 57.83795  55.88549  1.000 228.24236 ? 211 ILE E CB  1 
ATOM   9230 C CG1 . ILE E 5 231 ? -15.46751 58.28276  54.53740  1.000 220.94732 ? 211 ILE E CG1 1 
ATOM   9231 C CG2 . ILE E 5 231 ? -14.25718 56.44903  55.83593  1.000 230.29591 ? 211 ILE E CG2 1 
ATOM   9232 C CD1 . ILE E 5 231 ? -15.75310 59.76816  54.46785  1.000 221.32011 ? 211 ILE E CD1 1 
ATOM   9233 N N   . VAL E 5 232 ? -18.35711 57.69920  56.69336  1.000 233.86356 ? 212 VAL E N   1 
ATOM   9234 C CA  . VAL E 5 232 ? -19.63235 56.99427  56.74674  1.000 237.58014 ? 212 VAL E CA  1 
ATOM   9235 C C   . VAL E 5 232 ? -20.41105 57.24776  55.46315  1.000 230.83624 ? 212 VAL E C   1 
ATOM   9236 O O   . VAL E 5 232 ? -20.40330 58.36162  54.92763  1.000 225.30725 ? 212 VAL E O   1 
ATOM   9237 C CB  . VAL E 5 232 ? -20.45034 57.42254  57.98758  1.000 242.84190 ? 212 VAL E CB  1 
ATOM   9238 C CG1 . VAL E 5 232 ? -21.88934 57.77627  57.61981  1.000 241.51385 ? 212 VAL E CG1 1 
ATOM   9239 C CG2 . VAL E 5 232 ? -20.42993 56.33043  59.04372  1.000 250.14033 ? 212 VAL E CG2 1 
ATOM   9240 N N   . LYS E 5 233 ? -21.06478 56.19992  54.96313  1.000 244.27229 ? 213 LYS E N   1 
ATOM   9241 C CA  . LYS E 5 233 ? -22.03024 56.30405  53.87731  1.000 239.03982 ? 213 LYS E CA  1 
ATOM   9242 C C   . LYS E 5 233 ? -23.14582 55.30608  54.14781  1.000 244.66973 ? 213 LYS E C   1 
ATOM   9243 O O   . LYS E 5 233 ? -22.87403 54.13924  54.44577  1.000 249.08742 ? 213 LYS E O   1 
ATOM   9244 C CB  . LYS E 5 233 ? -21.38368 56.03858  52.51156  1.000 232.10072 ? 213 LYS E CB  1 
ATOM   9245 C CG  . LYS E 5 233 ? -20.58670 57.21230  51.95362  1.000 222.25240 ? 213 LYS E CG  1 
ATOM   9246 C CD  . LYS E 5 233 ? -20.36879 57.05773  50.45650  1.000 212.97749 ? 213 LYS E CD  1 
ATOM   9247 C CE  . LYS E 5 233 ? -19.78090 58.31631  49.83215  1.000 212.52420 ? 213 LYS E CE  1 
ATOM   9248 N NZ  . LYS E 5 233 ? -18.32967 58.48094  50.12160  1.000 212.38614 ? 213 LYS E NZ  1 
ATOM   9249 N N   . SER E 5 234 ? -24.39338 55.76379  54.05377  1.000 248.59174 ? 214 SER E N   1 
ATOM   9250 C CA  . SER E 5 234 ? -25.54123 54.96432  54.45610  1.000 254.23050 ? 214 SER E CA  1 
ATOM   9251 C C   . SER E 5 234 ? -26.65795 55.10816  53.43158  1.000 250.42133 ? 214 SER E C   1 
ATOM   9252 O O   . SER E 5 234 ? -26.58892 55.92926  52.51322  1.000 243.34379 ? 214 SER E O   1 
ATOM   9253 C CB  . SER E 5 234 ? -26.04054 55.37487  55.84740  1.000 260.37203 ? 214 SER E CB  1 
ATOM   9254 O OG  . SER E 5 234 ? -27.19461 54.64140  56.21778  1.000 266.32764 ? 214 SER E OG  1 
ATOM   9255 N N   . PHE E 5 235 ? -27.69871 54.29072  53.59887  1.000 251.96575 ? 215 PHE E N   1 
ATOM   9256 C CA  . PHE E 5 235 ? -28.89961 54.38458  52.78156  1.000 249.41451 ? 215 PHE E CA  1 
ATOM   9257 C C   . PHE E 5 235 ? -30.11877 54.09374  53.64453  1.000 256.92543 ? 215 PHE E C   1 
ATOM   9258 O O   . PHE E 5 235 ? -30.03824 53.36886  54.64015  1.000 264.23597 ? 215 PHE E O   1 
ATOM   9259 C CB  . PHE E 5 235 ? -28.85688 53.43019  51.56892  1.000 246.10479 ? 215 PHE E CB  1 
ATOM   9260 C CG  . PHE E 5 235 ? -29.15762 51.98743  51.89781  1.000 253.46460 ? 215 PHE E CG  1 
ATOM   9261 C CD1 . PHE E 5 235 ? -30.46189 51.51063  51.87966  1.000 257.09973 ? 215 PHE E CD1 1 
ATOM   9262 C CD2 . PHE E 5 235 ? -28.13362 51.10073  52.18800  1.000 256.27893 ? 215 PHE E CD2 1 
ATOM   9263 C CE1 . PHE E 5 235 ? -30.73898 50.18780  52.17269  1.000 263.53414 ? 215 PHE E CE1 1 
ATOM   9264 C CE2 . PHE E 5 235 ? -28.40492 49.77368  52.47628  1.000 262.63928 ? 215 PHE E CE2 1 
ATOM   9265 C CZ  . PHE E 5 235 ? -29.70906 49.31783  52.46876  1.000 266.24884 ? 215 PHE E CZ  1 
ATOM   9266 N N   . ASN E 5 236 ? -31.25161 54.66815  53.24731  1.000 254.21873 ? 216 ASN E N   1 
ATOM   9267 C CA  . ASN E 5 236 ? -32.52325 54.48349  53.93275  1.000 260.66140 ? 216 ASN E CA  1 
ATOM   9268 C C   . ASN E 5 236 ? -33.55323 53.97293  52.93576  1.000 259.11431 ? 216 ASN E C   1 
ATOM   9269 O O   . ASN E 5 236 ? -33.77237 54.59578  51.89116  1.000 251.91586 ? 216 ASN E O   1 
ATOM   9270 C CB  . ASN E 5 236 ? -33.00083 55.79229  54.57143  1.000 260.89941 ? 216 ASN E CB  1 
ATOM   9271 C CG  . ASN E 5 236 ? -34.20212 55.59674  55.47906  1.000 257.62701 ? 216 ASN E CG  1 
ATOM   9272 O OD1 . ASN E 5 236 ? -34.36478 54.54345  56.09427  1.000 257.12354 ? 216 ASN E OD1 1 
ATOM   9273 N ND2 . ASN E 5 236 ? -35.05049 56.61567  55.56723  1.000 255.78820 ? 216 ASN E ND2 1 
ATOM   9274 N N   . ARG E 5 237 ? -34.17623 52.84279  53.25651  1.000 243.37174 ? 217 ARG E N   1 
ATOM   9275 C CA  . ARG E 5 237 ? -35.19522 52.25360  52.39266  1.000 242.98046 ? 217 ARG E CA  1 
ATOM   9276 C C   . ARG E 5 237 ? -36.41793 53.15843  52.27972  1.000 242.29613 ? 217 ARG E C   1 
ATOM   9277 O O   . ARG E 5 237 ? -36.96105 53.35070  51.19170  1.000 236.27657 ? 217 ARG E O   1 
ATOM   9278 C CB  . ARG E 5 237 ? -35.61064 50.87557  52.91379  1.000 251.32940 ? 217 ARG E CB  1 
ATOM   9279 C CG  . ARG E 5 237 ? -34.73650 49.72815  52.43119  1.000 250.57388 ? 217 ARG E CG  1 
ATOM   9280 C CD  . ARG E 5 237 ? -34.28459 48.85561  53.59124  1.000 259.41034 ? 217 ARG E CD  1 
ATOM   9281 N NE  . ARG E 5 237 ? -35.36053 48.60826  54.54401  1.000 267.48545 ? 217 ARG E NE  1 
ATOM   9282 C CZ  . ARG E 5 237 ? -36.14270 47.53746  54.53597  1.000 272.59542 ? 217 ARG E CZ  1 
ATOM   9283 N NH1 . ARG E 5 237 ? -35.99748 46.58136  53.63318  1.000 270.53180 ? 217 ARG E NH1 1 
ATOM   9284 N NH2 . ARG E 5 237 ? -37.09302 47.42178  55.45935  1.000 279.90096 ? 217 ARG E NH2 1 
HETATM 9285 C C1  . NAG F 6 .   ? 34.18073  23.99268  29.70359  1.000 236.10723 ? 1   NAG F C1  1 
HETATM 9286 C C2  . NAG F 6 .   ? 35.43638  24.83106  29.74880  1.000 240.36070 ? 1   NAG F C2  1 
HETATM 9287 C C3  . NAG F 6 .   ? 35.24949  25.96093  30.74853  1.000 242.26057 ? 1   NAG F C3  1 
HETATM 9288 C C4  . NAG F 6 .   ? 33.99230  26.76445  30.41514  1.000 239.46599 ? 1   NAG F C4  1 
HETATM 9289 C C5  . NAG F 6 .   ? 32.78334  25.87531  30.06657  1.000 234.87125 ? 1   NAG F C5  1 
HETATM 9290 C C6  . NAG F 6 .   ? 31.69198  26.63803  29.35241  1.000 232.11575 ? 1   NAG F C6  1 
HETATM 9291 C C7  . NAG F 6 .   ? 36.79801  23.28068  31.12744  1.000 245.66580 ? 1   NAG F C7  1 
HETATM 9292 C C8  . NAG F 6 .   ? 38.11579  22.57205  31.22605  1.000 249.27303 ? 1   NAG F C8  1 
HETATM 9293 N N2  . NAG F 6 .   ? 36.63120  24.05074  30.04442  1.000 243.49964 ? 1   NAG F N2  1 
HETATM 9294 O O3  . NAG F 6 .   ? 36.40441  26.79238  30.71411  1.000 245.71441 ? 1   NAG F O3  1 
HETATM 9295 O O4  . NAG F 6 .   ? 33.59955  27.53870  31.54613  1.000 240.80157 ? 1   NAG F O4  1 
HETATM 9296 O O5  . NAG F 6 .   ? 33.12515  24.77076  29.20886  1.000 233.18461 ? 1   NAG F O5  1 
HETATM 9297 O O6  . NAG F 6 .   ? 32.12315  27.06866  28.06817  1.000 231.63829 ? 1   NAG F O6  1 
HETATM 9298 O O7  . NAG F 6 .   ? 35.93316  23.16261  31.98958  1.000 244.87111 ? 1   NAG F O7  1 
HETATM 9299 C C1  . NAG F 6 .   ? 34.34315  28.76847  31.73261  1.000 246.92421 ? 2   NAG F C1  1 
HETATM 9300 C C2  . NAG F 6 .   ? 33.34350  29.92170  31.74329  1.000 245.97133 ? 2   NAG F C2  1 
HETATM 9301 C C3  . NAG F 6 .   ? 33.99189  31.24756  32.20066  1.000 249.46224 ? 2   NAG F C3  1 
HETATM 9302 C C4  . NAG F 6 .   ? 35.21641  31.11806  33.11292  1.000 253.23882 ? 2   NAG F C4  1 
HETATM 9303 C C5  . NAG F 6 .   ? 35.93148  29.77232  33.03137  1.000 253.31289 ? 2   NAG F C5  1 
HETATM 9304 C C6  . NAG F 6 .   ? 36.79824  29.48244  34.23451  1.000 256.78448 ? 2   NAG F C6  1 
HETATM 9305 C C7  . NAG F 6 .   ? 31.70604  30.86492  30.16093  1.000 241.43542 ? 2   NAG F C7  1 
HETATM 9306 C C8  . NAG F 6 .   ? 31.26710  30.91916  28.72850  1.000 238.62082 ? 2   NAG F C8  1 
HETATM 9307 N N2  . NAG F 6 .   ? 32.76250  30.08587  30.41925  1.000 243.19128 ? 2   NAG F N2  1 
HETATM 9308 O O3  . NAG F 6 .   ? 32.99328  32.00322  32.87908  1.000 249.31059 ? 2   NAG F O3  1 
HETATM 9309 O O4  . NAG F 6 .   ? 36.17458  32.06509  32.66321  1.000 255.89752 ? 2   NAG F O4  1 
HETATM 9310 O O5  . NAG F 6 .   ? 34.98465  28.70969  32.93845  1.000 250.00645 ? 2   NAG F O5  1 
HETATM 9311 O O6  . NAG F 6 .   ? 37.14540  28.10582  34.29966  1.000 256.93293 ? 2   NAG F O6  1 
HETATM 9312 O O7  . NAG F 6 .   ? 31.12383  31.48880  31.04306  1.000 242.11878 ? 2   NAG F O7  1 
HETATM 9313 C C1  . BMA F 6 .   ? 36.45457  33.33320  33.36493  1.000 248.25614 ? 3   BMA F C1  1 
HETATM 9314 C C2  . BMA F 6 .   ? 35.16636  34.07820  33.88631  1.000 247.62668 ? 3   BMA F C2  1 
HETATM 9315 C C3  . BMA F 6 .   ? 35.62967  35.47158  34.28607  1.000 251.91219 ? 3   BMA F C3  1 
HETATM 9316 C C4  . BMA F 6 .   ? 36.77879  35.40531  35.33561  1.000 255.53893 ? 3   BMA F C4  1 
HETATM 9317 C C5  . BMA F 6 .   ? 37.89894  34.39521  34.92144  1.000 255.88933 ? 3   BMA F C5  1 
HETATM 9318 C C6  . BMA F 6 .   ? 38.90848  34.13413  36.02663  1.000 259.18105 ? 3   BMA F C6  1 
HETATM 9319 O O2  . BMA F 6 .   ? 34.65119  33.48350  35.06007  1.000 247.58743 ? 3   BMA F O2  1 
HETATM 9320 O O3  . BMA F 6 .   ? 34.55479  36.26940  34.77904  1.000 252.88221 ? 3   BMA F O3  1 
HETATM 9321 O O4  . BMA F 6 .   ? 37.35133  36.69361  35.50125  1.000 258.85630 ? 3   BMA F O4  1 
HETATM 9322 O O5  . BMA F 6 .   ? 37.30880  33.13439  34.52190  1.000 252.46630 ? 3   BMA F O5  1 
HETATM 9323 O O6  . BMA F 6 .   ? 39.52891  35.37084  36.36224  1.000 262.48345 ? 3   BMA F O6  1 
HETATM 9324 C C1  . MAN F 6 .   ? 34.37489  37.42932  33.93581  1.000 256.97533 ? 4   MAN F C1  1 
HETATM 9325 C C2  . MAN F 6 .   ? 33.55205  38.46348  34.75266  1.000 262.21835 ? 4   MAN F C2  1 
HETATM 9326 C C3  . MAN F 6 .   ? 32.54294  39.18013  33.86296  1.000 263.43899 ? 4   MAN F C3  1 
HETATM 9327 C C4  . MAN F 6 .   ? 33.14385  39.45781  32.49183  1.000 262.04522 ? 4   MAN F C4  1 
HETATM 9328 C C5  . MAN F 6 .   ? 33.38053  38.12220  31.76899  1.000 255.95525 ? 4   MAN F C5  1 
HETATM 9329 C C6  . MAN F 6 .   ? 34.44625  38.19258  30.67896  1.000 254.40113 ? 4   MAN F C6  1 
HETATM 9330 O O2  . MAN F 6 .   ? 34.38998  39.48612  35.28626  1.000 266.81515 ? 4   MAN F O2  1 
HETATM 9331 O O3  . MAN F 6 .   ? 32.08290  40.38785  34.45631  1.000 269.16590 ? 4   MAN F O3  1 
HETATM 9332 O O4  . MAN F 6 .   ? 32.25018  40.25239  31.72536  1.000 264.04790 ? 4   MAN F O4  1 
HETATM 9333 O O5  . MAN F 6 .   ? 33.74307  37.06045  32.71328  1.000 253.67001 ? 4   MAN F O5  1 
HETATM 9334 O O6  . MAN F 6 .   ? 35.63957  38.72420  31.24109  1.000 257.00629 ? 4   MAN F O6  1 
HETATM 9335 C C1  . NAG G 6 .   ? 38.65773  20.63003  25.46301  1.000 216.14505 ? 1   NAG G C1  1 
HETATM 9336 C C2  . NAG G 6 .   ? 39.35452  21.16151  26.68721  1.000 246.66676 ? 1   NAG G C2  1 
HETATM 9337 C C3  . NAG G 6 .   ? 38.97334  22.63048  26.84877  1.000 261.21444 ? 1   NAG G C3  1 
HETATM 9338 C C4  . NAG G 6 .   ? 39.12551  23.38043  25.51908  1.000 264.31625 ? 1   NAG G C4  1 
HETATM 9339 C C5  . NAG G 6 .   ? 38.75431  22.54473  24.27055  1.000 241.01598 ? 1   NAG G C5  1 
HETATM 9340 C C6  . NAG G 6 .   ? 39.32758  23.07044  22.97311  1.000 245.30547 ? 1   NAG G C6  1 
HETATM 9341 C C7  . NAG G 6 .   ? 37.86362  20.14516  28.39136  1.000 229.75634 ? 1   NAG G C7  1 
HETATM 9342 C C8  . NAG G 6 .   ? 37.83241  19.33474  29.65141  1.000 235.36959 ? 1   NAG G C8  1 
HETATM 9343 N N2  . NAG G 6 .   ? 39.08054  20.39764  27.89658  1.000 245.95717 ? 1   NAG G N2  1 
HETATM 9344 O O3  . NAG G 6 .   ? 39.75489  23.24600  27.86825  1.000 277.13035 ? 1   NAG G O3  1 
HETATM 9345 O O4  . NAG G 6 .   ? 38.28097  24.52865  25.54432  1.000 270.27278 ? 1   NAG G O4  1 
HETATM 9346 O O5  . NAG G 6 .   ? 39.20132  21.18692  24.37282  1.000 221.52823 ? 1   NAG G O5  1 
HETATM 9347 O O6  . NAG G 6 .   ? 40.65498  23.54898  23.13782  1.000 266.47243 ? 1   NAG G O6  1 
HETATM 9348 O O7  . NAG G 6 .   ? 36.83698  20.54490  27.85045  1.000 216.91164 ? 1   NAG G O7  1 
HETATM 9349 C C1  . NAG G 6 .   ? 39.06999  25.62821  25.02701  1.000 256.24279 ? 2   NAG G C1  1 
HETATM 9350 C C2  . NAG G 6 .   ? 38.18481  26.82957  24.69136  1.000 257.51514 ? 2   NAG G C2  1 
HETATM 9351 C C3  . NAG G 6 .   ? 39.05007  27.95598  24.14155  1.000 261.95664 ? 2   NAG G C3  1 
HETATM 9352 C C4  . NAG G 6 .   ? 40.18504  28.27600  25.11118  1.000 268.14692 ? 2   NAG G C4  1 
HETATM 9353 C C5  . NAG G 6 .   ? 40.93493  27.01390  25.54704  1.000 268.39859 ? 2   NAG G C5  1 
HETATM 9354 C C6  . NAG G 6 .   ? 41.91027  27.26996  26.67206  1.000 274.39254 ? 2   NAG G C6  1 
HETATM 9355 C C7  . NAG G 6 .   ? 37.29977  26.05236  22.50703  1.000 240.23243 ? 2   NAG G C7  1 
HETATM 9356 C C8  . NAG G 6 .   ? 36.05204  25.76189  21.72984  1.000 226.08308 ? 2   NAG G C8  1 
HETATM 9357 N N2  . NAG G 6 .   ? 37.11636  26.48445  23.76215  1.000 249.71868 ? 2   NAG G N2  1 
HETATM 9358 O O3  . NAG G 6 .   ? 38.23726  29.10159  23.91194  1.000 262.34843 ? 2   NAG G O3  1 
HETATM 9359 O O4  . NAG G 6 .   ? 41.13258  29.12743  24.48185  1.000 271.31443 ? 2   NAG G O4  1 
HETATM 9360 O O5  . NAG G 6 .   ? 40.02311  26.01381  26.02145  1.000 264.28410 ? 2   NAG G O5  1 
HETATM 9361 O O6  . NAG G 6 .   ? 43.23566  27.42859  26.18564  1.000 277.59761 ? 2   NAG G O6  1 
HETATM 9362 O O7  . NAG G 6 .   ? 38.41617  25.89680  22.02097  1.000 241.49140 ? 2   NAG G O7  1 
HETATM 9363 C C1  . BMA G 6 .   ? 40.85247  30.49632  24.78240  1.000 257.62284 ? 3   BMA G C1  1 
HETATM 9364 C C2  . BMA G 6 .   ? 42.11308  31.13346  25.38765  1.000 263.50736 ? 3   BMA G C2  1 
HETATM 9365 C C3  . BMA G 6 .   ? 41.97395  32.65883  25.46675  1.000 266.39392 ? 3   BMA G C3  1 
HETATM 9366 C C4  . BMA G 6 .   ? 41.36797  33.25885  24.17899  1.000 264.35152 ? 3   BMA G C4  1 
HETATM 9367 C C5  . BMA G 6 .   ? 40.09037  32.50707  23.78847  1.000 258.55096 ? 3   BMA G C5  1 
HETATM 9368 C C6  . BMA G 6 .   ? 39.48406  32.99748  22.48723  1.000 256.52347 ? 3   BMA G C6  1 
HETATM 9369 O O2  . BMA G 6 .   ? 43.25022  30.86378  24.57153  1.000 264.82845 ? 3   BMA G O2  1 
HETATM 9370 O O3  . BMA G 6 .   ? 43.23279  33.26318  25.73130  1.000 270.95950 ? 3   BMA G O3  1 
HETATM 9371 O O4  . BMA G 6 .   ? 41.06156  34.63069  24.37762  1.000 266.51471 ? 3   BMA G O4  1 
HETATM 9372 O O5  . BMA G 6 .   ? 40.43415  31.14416  23.61018  1.000 255.91393 ? 3   BMA G O5  1 
HETATM 9373 O O6  . BMA G 6 .   ? 39.20322  31.86024  21.67626  1.000 251.00277 ? 3   BMA G O6  1 
HETATM 9374 C C1  . MAN G 6 .   ? 43.11983  34.15144  26.86543  1.000 261.33765 ? 4   MAN G C1  1 
HETATM 9375 C C2  . MAN G 6 .   ? 43.96977  35.39862  26.53752  1.000 264.78059 ? 4   MAN G C2  1 
HETATM 9376 C C3  . MAN G 6 .   ? 45.44404  35.01273  26.47164  1.000 267.50404 ? 4   MAN G C3  1 
HETATM 9377 C C4  . MAN G 6 .   ? 45.87850  34.27249  27.74812  1.000 269.50407 ? 4   MAN G C4  1 
HETATM 9378 C C5  . MAN G 6 .   ? 44.95707  33.06717  28.00503  1.000 265.99045 ? 4   MAN G C5  1 
HETATM 9379 C C6  . MAN G 6 .   ? 45.24938  32.37953  29.32619  1.000 267.87719 ? 4   MAN G C6  1 
HETATM 9380 O O2  . MAN G 6 .   ? 43.87055  36.37879  27.57232  1.000 267.65240 ? 4   MAN G O2  1 
HETATM 9381 O O3  . MAN G 6 .   ? 46.27739  36.14741  26.25454  1.000 270.91843 ? 4   MAN G O3  1 
HETATM 9382 O O4  . MAN G 6 .   ? 47.21630  33.81658  27.60867  1.000 271.95054 ? 4   MAN G O4  1 
HETATM 9383 O O5  . MAN G 6 .   ? 43.58221  33.51113  28.04067  1.000 263.33696 ? 4   MAN G O5  1 
HETATM 9384 O O6  . MAN G 6 .   ? 45.04671  30.98061  29.15688  1.000 264.78848 ? 4   MAN G O6  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ILE A 45  ? 2.80994 2.65462 3.45314 0.33668  -0.25682 -0.18184 43  ILE A N   
2    C CA  . ILE A 45  ? 2.80534 2.67893 3.47207 0.34288  -0.23747 -0.20594 43  ILE A CA  
3    C C   . ILE A 45  ? 2.77463 2.65596 3.39529 0.33418  -0.22183 -0.20937 43  ILE A C   
4    O O   . ILE A 45  ? 2.76372 2.62210 3.33751 0.32612  -0.22483 -0.19541 43  ILE A O   
5    C CB  . ILE A 45  ? 2.74985 2.62182 3.44031 0.35423  -0.22959 -0.22330 43  ILE A CB  
6    C CG1 . ILE A 45  ? 2.68087 2.52717 3.31793 0.35186  -0.22531 -0.21985 43  ILE A CG1 
7    C CG2 . ILE A 45  ? 2.80624 2.66879 3.55102 0.36329  -0.24561 -0.21724 43  ILE A CG2 
8    C CD1 . ILE A 45  ? 2.63539 2.48988 3.28429 0.35944  -0.21008 -0.24255 43  ILE A CD1 
9    N N   . GLY A 46  ? 2.94124 2.85752 3.57886 0.33497  -0.20508 -0.22792 44  GLY A N   
10   C CA  . GLY A 46  ? 2.95629 2.88608 3.55662 0.32611  -0.19067 -0.22798 44  GLY A CA  
11   C C   . GLY A 46  ? 2.95082 2.92589 3.57371 0.32690  -0.17192 -0.25144 44  GLY A C   
12   O O   . GLY A 46  ? 2.92833 2.92094 3.59534 0.33520  -0.16814 -0.27210 44  GLY A O   
13   N N   . TYR A 47  ? 3.14219 3.13853 3.73701 0.31679  -0.15993 -0.24808 45  TYR A N   
14   C CA  . TYR A 47  ? 3.14460 3.19300 3.75410 0.31273  -0.14148 -0.26846 45  TYR A CA  
15   C C   . TYR A 47  ? 3.15601 3.24292 3.81560 0.31143  -0.13923 -0.28513 45  TYR A C   
16   O O   . TYR A 47  ? 3.15788 3.23559 3.82912 0.30970  -0.15057 -0.27409 45  TYR A O   
17   C CB  . TYR A 47  ? 2.75194 2.81594 3.32029 0.30012  -0.13202 -0.25372 45  TYR A CB  
18   C CG  . TYR A 47  ? 2.64436 2.66854 3.16607 0.30147  -0.13544 -0.23439 45  TYR A CG  
19   C CD1 . TYR A 47  ? 2.60114 2.63112 3.10688 0.30512  -0.12668 -0.24196 45  TYR A CD1 
20   C CD2 . TYR A 47  ? 2.63943 2.62305 3.13546 0.29823  -0.14652 -0.21093 45  TYR A CD2 
21   C CE1 . TYR A 47  ? 2.55620 2.55212 3.02201 0.30687  -0.12970 -0.22515 45  TYR A CE1 
22   C CE2 . TYR A 47  ? 2.59341 2.54268 3.05196 0.29957  -0.14860 -0.19656 45  TYR A CE2 
23   C CZ  . TYR A 47  ? 2.55215 2.50752 2.99588 0.30455  -0.14057 -0.20296 45  TYR A CZ  
24   O OH  . TYR A 47  ? 2.50872 2.43210 2.91765 0.30639  -0.14255 -0.18941 45  TYR A OH  
25   N N   . LYS A 48  ? 3.35548 3.48961 4.04622 0.31120  -0.12364 -0.31401 46  LYS A N   
26   C CA  . LYS A 48  ? 3.35627 3.53211 4.10157 0.31070  -0.11919 -0.33618 46  LYS A CA  
27   C C   . LYS A 48  ? 3.36300 3.60452 4.11969 0.30057  -0.09687 -0.36423 46  LYS A C   
28   O O   . LYS A 48  ? 3.35483 3.60700 4.09376 0.29910  -0.08575 -0.37400 46  LYS A O   
29   C CB  . LYS A 48  ? 2.37652 2.53358 3.17796 0.32693  -0.12842 -0.35011 46  LYS A CB  
30   C CG  . LYS A 48  ? 2.36896 2.56407 3.23392 0.32877  -0.12661 -0.37065 46  LYS A CG  
31   C CD  . LYS A 48  ? 2.35331 2.52278 3.27662 0.34585  -0.14005 -0.37496 46  LYS A CD  
32   C CE  . LYS A 48  ? 2.34773 2.52367 3.30992 0.35527  -0.12842 -0.40529 46  LYS A CE  
33   N NZ  . LYS A 48  ? 2.33393 2.49408 3.37000 0.37160  -0.13970 -0.41198 46  LYS A NZ  
34   N N   . CYS A 49  ? 3.08107 3.37117 3.86663 0.29168  -0.09023 -0.37747 47  CYS A N   
35   C CA  . CYS A 49  ? 3.08887 3.45229 3.89385 0.27946  -0.06872 -0.40899 47  CYS A CA  
36   C C   . CYS A 49  ? 3.07671 3.47876 3.94473 0.28020  -0.06563 -0.43561 47  CYS A C   
37   O O   . CYS A 49  ? 3.10070 3.49429 3.97318 0.27872  -0.07672 -0.41927 47  CYS A O   
38   C CB  . CYS A 49  ? 3.13913 3.53670 3.89325 0.25879  -0.06063 -0.38968 47  CYS A CB  
39   S SG  . CYS A 49  ? 3.15291 3.53827 3.85085 0.25595  -0.05491 -0.37477 47  CYS A SG  
40   N N   . ASN A 50  ? 2.99767 3.44300 3.91699 0.28222  -0.04998 -0.47839 48  ASN A N   
41   C CA  . ASN A 50  ? 2.97863 3.45407 3.97251 0.28824  -0.04699 -0.50967 48  ASN A CA  
42   C C   . ASN A 50  ? 2.98361 3.54837 3.99801 0.26902  -0.02354 -0.54641 48  ASN A C   
43   O O   . ASN A 50  ? 2.96767 3.57150 3.96895 0.25827  -0.00589 -0.56715 48  ASN A O   
44   C CB  . ASN A 50  ? 2.92699 3.37257 3.97886 0.30907  -0.04911 -0.53218 48  ASN A CB  
45   C CG  . ASN A 50  ? 2.91517 3.35989 4.04285 0.32261  -0.05769 -0.54461 48  ASN A CG  
46   O OD1 . ASN A 50  ? 2.91706 3.41791 4.08354 0.31511  -0.04764 -0.56938 48  ASN A OD1 
47   N ND2 . ASN A 50  ? 2.90315 3.28704 4.05388 0.34194  -0.07696 -0.52614 48  ASN A ND2 
48   N N   . PHE A 51  ? 2.91345 3.51514 3.96027 0.26311  -0.02315 -0.55532 49  PHE A N   
49   C CA  . PHE A 51  ? 2.92070 3.61329 3.98650 0.24184  -0.00165 -0.58949 49  PHE A CA  
50   C C   . PHE A 51  ? 2.89780 3.62518 4.04714 0.24870  0.00274  -0.62710 49  PHE A C   
51   O O   . PHE A 51  ? 2.91784 3.71124 4.08019 0.23141  0.01294  -0.64349 49  PHE A O   
52   C CB  . PHE A 51  ? 2.97872 3.69782 3.98454 0.21868  -0.00291 -0.55748 49  PHE A CB  
53   C CG  . PHE A 51  ? 3.00450 3.69092 3.93449 0.21227  -0.00770 -0.51825 49  PHE A CG  
54   C CD1 . PHE A 51  ? 2.99737 3.72843 3.90190 0.19785  0.00873  -0.52967 49  PHE A CD1 
55   C CD2 . PHE A 51  ? 3.02317 3.63788 3.91013 0.21981  -0.02817 -0.47114 49  PHE A CD2 
56   C CE1 . PHE A 51  ? 3.01989 3.72253 3.85935 0.19309  0.00369  -0.49211 49  PHE A CE1 
57   C CE2 . PHE A 51  ? 3.03617 3.62103 3.86007 0.21493  -0.03190 -0.43703 49  PHE A CE2 
58   C CZ  . PHE A 51  ? 3.04912 3.67695 3.85024 0.20256  -0.01653 -0.44620 49  PHE A CZ  
59   N N   . SER A 52  ? 2.91760 3.60337 4.12706 0.27334  -0.00511 -0.64017 50  SER A N   
60   C CA  . SER A 52  ? 2.89330 3.61055 4.19231 0.28257  -0.00121 -0.67628 50  SER A CA  
61   C C   . SER A 52  ? 2.83825 3.54157 4.21056 0.30166  0.00581  -0.71292 50  SER A C   
62   O O   . SER A 52  ? 2.80990 3.56918 4.25635 0.30068  0.02434  -0.76495 50  SER A O   
63   C CB  . SER A 52  ? 2.91269 3.58887 4.22305 0.29484  -0.02565 -0.64238 50  SER A CB  
64   O OG  . SER A 52  ? 2.89760 3.49221 4.20482 0.31631  -0.04726 -0.61059 50  SER A OG  
65   N N   . ASN A 53  ? 2.91002 3.54013 4.26509 0.31810  -0.00826 -0.68739 51  ASN A N   
66   C CA  . ASN A 53  ? 2.86256 3.47125 4.28480 0.33591  -0.00319 -0.71671 51  ASN A CA  
67   C C   . ASN A 53  ? 2.83874 3.49620 4.25715 0.32156  0.02483  -0.76026 51  ASN A C   
68   O O   . ASN A 53  ? 2.80394 3.51002 4.29796 0.32115  0.04526  -0.81514 51  ASN A O   
69   C CB  . ASN A 53  ? 2.86057 3.37938 4.25925 0.35453  -0.02734 -0.67313 51  ASN A CB  
70   C CG  . ASN A 53  ? 2.88093 3.35632 4.28758 0.36722  -0.05531 -0.63142 51  ASN A CG  
71   O OD1 . ASN A 53  ? 2.88773 3.39489 4.34297 0.36868  -0.05692 -0.64149 51  ASN A OD1 
72   N ND2 . ASN A 53  ? 2.89046 3.29715 4.24977 0.37511  -0.07721 -0.58540 51  ASN A ND2 
73   N N   . ILE A 69  ? 2.93114 4.03002 3.74591 0.09138  0.10686  -0.62438 71  ILE A N   
74   C CA  . ILE A 69  ? 2.93547 3.93527 3.72111 0.11712  0.09029  -0.59234 71  ILE A CA  
75   C C   . ILE A 69  ? 2.99291 3.93827 3.72571 0.11968  0.06869  -0.52657 71  ILE A C   
76   O O   . ILE A 69  ? 3.03019 3.99872 3.76008 0.10718  0.06461  -0.50912 71  ILE A O   
77   C CB  . ILE A 69  ? 2.90703 3.83291 3.74508 0.14828  0.08381  -0.61797 71  ILE A CB  
78   C CG1 . ILE A 69  ? 2.85499 3.84311 3.76585 0.14372  0.10537  -0.68607 71  ILE A CG1 
79   C CG2 . ILE A 69  ? 2.88711 3.74206 3.70320 0.16774  0.07626  -0.60555 71  ILE A CG2 
80   C CD1 . ILE A 69  ? 2.82739 3.74833 3.80129 0.17374  0.09850  -0.70952 71  ILE A CD1 
81   N N   . PHE A 70  ? 2.96968 3.84376 3.66322 0.13504  0.05569  -0.49197 72  PHE A N   
82   C CA  . PHE A 70  ? 3.01898 3.83948 3.66542 0.13770  0.03695  -0.43245 72  PHE A CA  
83   C C   . PHE A 70  ? 3.02053 3.73292 3.65993 0.16746  0.01912  -0.41489 72  PHE A C   
84   O O   . PHE A 70  ? 2.98092 3.66490 3.62299 0.18110  0.02103  -0.43092 72  PHE A O   
85   C CB  . PHE A 70  ? 3.02167 3.88396 3.61832 0.11845  0.04030  -0.39947 72  PHE A CB  
86   C CG  . PHE A 70  ? 3.01244 3.98904 3.61134 0.08504  0.05667  -0.41152 72  PHE A CG  
87   C CD1 . PHE A 70  ? 3.05105 4.05931 3.64023 0.06636  0.05226  -0.38234 72  PHE A CD1 
88   C CD2 . PHE A 70  ? 2.96032 4.01628 3.57189 0.07015  0.07698  -0.45322 72  PHE A CD2 
89   C CE1 . PHE A 70  ? 3.03640 4.15538 3.62662 0.03283  0.06674  -0.39194 72  PHE A CE1 
90   C CE2 . PHE A 70  ? 2.94511 4.11465 3.55798 0.03603  0.09252  -0.46587 72  PHE A CE2 
91   C CZ  . PHE A 70  ? 2.98293 4.18502 3.58427 0.01706  0.08687  -0.43399 72  PHE A CZ  
92   N N   . CYS A 71  ? 3.05578 3.71176 3.68615 0.17526  0.00220  -0.38258 73  CYS A N   
93   C CA  . CYS A 71  ? 3.05304 3.61204 3.67674 0.19989  -0.01578 -0.36469 73  CYS A CA  
94   C C   . CYS A 71  ? 3.08214 3.60048 3.65257 0.19909  -0.02610 -0.31640 73  CYS A C   
95   O O   . CYS A 71  ? 3.10996 3.59835 3.66493 0.19661  -0.03712 -0.28394 73  CYS A O   
96   C CB  . CYS A 71  ? 3.07003 3.59938 3.72467 0.20777  -0.02663 -0.36614 73  CYS A CB  
97   S SG  . CYS A 71  ? 3.02441 3.44605 3.66506 0.23023  -0.05079 -0.33573 73  CYS A SG  
98   N N   . THR A 72  ? 3.03959 3.55868 3.58507 0.20086  -0.02158 -0.31336 74  THR A N   
99   C CA  . THR A 72  ? 3.05984 3.54694 3.56010 0.20064  -0.02959 -0.27020 74  THR A CA  
100  C C   . THR A 72  ? 3.05243 3.44595 3.54151 0.22286  -0.04536 -0.25676 74  THR A C   
101  O O   . THR A 72  ? 3.00685 3.37110 3.50836 0.23772  -0.04632 -0.28007 74  THR A O   
102  C CB  . THR A 72  ? 3.01063 3.54614 3.48972 0.19176  -0.01793 -0.27234 74  THR A CB  
103  O OG1 . THR A 72  ? 3.04163 3.66906 3.52259 0.16603  -0.00532 -0.27373 74  THR A OG1 
104  C CG2 . THR A 72  ? 2.99505 3.48595 3.43395 0.19774  -0.02753 -0.23099 74  THR A CG2 
105  N N   . ILE A 73  ? 3.06057 3.40951 3.52813 0.22352  -0.05727 -0.21977 75  ILE A N   
106  C CA  . ILE A 73  ? 3.04136 3.30734 3.49784 0.24081  -0.07186 -0.20761 75  ILE A CA  
107  C C   . ILE A 73  ? 3.04875 3.28402 3.47479 0.23743  -0.07849 -0.16679 75  ILE A C   
108  O O   . ILE A 73  ? 3.05644 3.31448 3.48124 0.22346  -0.07767 -0.14480 75  ILE A O   
109  C CB  . ILE A 73  ? 2.91391 3.14880 3.39798 0.24754  -0.08132 -0.21883 75  ILE A CB  
110  C CG1 . ILE A 73  ? 2.71600 2.87282 3.18524 0.26069  -0.09675 -0.20341 75  ILE A CG1 
111  C CG2 . ILE A 73  ? 3.02985 3.29645 3.52518 0.23242  -0.08024 -0.20887 75  ILE A CG2 
112  C CD1 . ILE A 73  ? 2.72301 2.85286 3.21819 0.26641  -0.10753 -0.21211 75  ILE A CD1 
113  N N   . HIS A 74  ? 3.13348 3.31745 3.53820 0.24986  -0.08477 -0.15725 76  HIS A N   
114  C CA  . HIS A 74  ? 3.12597 3.27151 3.50873 0.24986  -0.09130 -0.12257 76  HIS A CA  
115  C C   . HIS A 74  ? 3.08842 3.17183 3.45583 0.26587  -0.09925 -0.12528 76  HIS A C   
116  O O   . HIS A 74  ? 3.06644 3.15536 3.42573 0.27321  -0.09558 -0.14024 76  HIS A O   
117  C CB  . HIS A 74  ? 2.81222 3.00377 3.18063 0.23895  -0.08359 -0.09857 76  HIS A CB  
118  C CG  . HIS A 74  ? 2.77510 2.99688 3.13145 0.24242  -0.07573 -0.11201 76  HIS A CG  
119  N ND1 . HIS A 74  ? 2.93929 3.22050 3.30763 0.23617  -0.06453 -0.14205 76  HIS A ND1 
120  C CD2 . HIS A 74  ? 2.70083 2.90384 3.03594 0.25056  -0.07659 -0.10149 76  HIS A CD2 
121  C CE1 . HIS A 74  ? 2.93282 3.23028 3.28643 0.23949  -0.05867 -0.14944 76  HIS A CE1 
122  N NE2 . HIS A 74  ? 2.72817 2.97916 3.06038 0.24854  -0.06631 -0.12407 76  HIS A NE2 
123  N N   . SER A 75  ? 2.97905 3.00702 3.34291 0.26937  -0.10939 -0.11256 77  SER A N   
124  C CA  . SER A 75  ? 2.89613 2.86787 3.24546 0.28157  -0.11739 -0.11590 77  SER A CA  
125  C C   . SER A 75  ? 2.90187 2.82615 3.25008 0.27921  -0.12567 -0.10034 77  SER A C   
126  O O   . SER A 75  ? 2.96788 2.90000 3.32869 0.26923  -0.12572 -0.08958 77  SER A O   
127  C CB  . SER A 75  ? 2.86277 2.82380 3.22185 0.29038  -0.12185 -0.14367 77  SER A CB  
128  O OG  . SER A 75  ? 2.82504 2.73452 3.16910 0.29895  -0.13093 -0.14441 77  SER A OG  
129  N N   . TYR A 76  ? 3.15917 3.03652 3.49284 0.28695  -0.13185 -0.10122 78  TYR A N   
130  C CA  . TYR A 76  ? 3.15869 2.99085 3.49289 0.28395  -0.13939 -0.09566 78  TYR A CA  
131  C C   . TYR A 76  ? 3.15735 2.97810 3.50052 0.28425  -0.14851 -0.11367 78  TYR A C   
132  O O   . TYR A 76  ? 3.13440 2.94632 3.47201 0.29203  -0.15332 -0.12797 78  TYR A O   
133  C CB  . TYR A 76  ? 2.55546 2.34899 2.87225 0.28995  -0.14094 -0.09105 78  TYR A CB  
134  C CG  . TYR A 76  ? 2.49497 2.27719 2.79546 0.29976  -0.14442 -0.10770 78  TYR A CG  
135  C CD1 . TYR A 76  ? 2.46405 2.27301 2.75546 0.30629  -0.13824 -0.11098 78  TYR A CD1 
136  C CD2 . TYR A 76  ? 2.47398 2.22185 2.76797 0.30035  -0.15386 -0.11949 78  TYR A CD2 
137  C CE1 . TYR A 76  ? 2.41018 2.20777 2.68778 0.31413  -0.14109 -0.12598 78  TYR A CE1 
138  C CE2 . TYR A 76  ? 2.42359 2.16207 2.70312 0.30749  -0.15778 -0.13203 78  TYR A CE2 
139  C CZ  . TYR A 76  ? 2.38981 2.15090 2.66172 0.31488  -0.15123 -0.13534 78  TYR A CZ  
140  O OH  . TYR A 76  ? 2.34246 2.09322 2.60101 0.32098  -0.15480 -0.14775 78  TYR A OH  
141  N N   . PHE A 77  ? 3.07784 2.90127 3.43682 0.27517  -0.15135 -0.11119 79  PHE A N   
142  C CA  . PHE A 77  ? 3.08495 2.91033 3.45884 0.27455  -0.15995 -0.12513 79  PHE A CA  
143  C C   . PHE A 77  ? 3.08977 2.87537 3.45677 0.27022  -0.17006 -0.12567 79  PHE A C   
144  O O   . PHE A 77  ? 3.11508 2.88629 3.48344 0.26019  -0.16938 -0.11735 79  PHE A O   
145  C CB  . PHE A 77  ? 2.59239 2.45301 2.98885 0.26615  -0.15672 -0.12409 79  PHE A CB  
146  C CG  . PHE A 77  ? 2.62737 2.53593 3.03105 0.26664  -0.14582 -0.12620 79  PHE A CG  
147  C CD1 . PHE A 77  ? 2.57719 2.50809 2.98935 0.27547  -0.14370 -0.14483 79  PHE A CD1 
148  C CD2 . PHE A 77  ? 2.78085 2.71502 3.18483 0.25646  -0.13742 -0.10976 79  PHE A CD2 
149  C CE1 . PHE A 77  ? 2.61227 2.59333 3.03186 0.27320  -0.13204 -0.15111 79  PHE A CE1 
150  C CE2 . PHE A 77  ? 2.84492 2.83175 3.25393 0.25345  -0.12733 -0.11196 79  PHE A CE2 
151  C CZ  . PHE A 77  ? 2.74451 2.75640 3.16069 0.26136  -0.12396 -0.13470 79  PHE A CZ  
152  N N   . ILE A 78  ? 3.01333 2.78409 3.37442 0.27597  -0.17914 -0.13580 80  ILE A N   
153  C CA  . ILE A 78  ? 3.02516 2.76682 3.37778 0.26938  -0.18951 -0.13772 80  ILE A CA  
154  C C   . ILE A 78  ? 3.05320 2.80823 3.42618 0.26478  -0.20035 -0.14159 80  ILE A C   
155  O O   . ILE A 78  ? 3.04687 2.80284 3.42506 0.26974  -0.21044 -0.14641 80  ILE A O   
156  C CB  . ILE A 78  ? 2.40259 2.12322 2.73447 0.27568  -0.19409 -0.14305 80  ILE A CB  
157  C CG1 . ILE A 78  ? 2.36331 2.07848 2.67896 0.28281  -0.18307 -0.13948 80  ILE A CG1 
158  C CG2 . ILE A 78  ? 2.42379 2.11975 2.74367 0.26485  -0.20274 -0.14547 80  ILE A CG2 
159  C CD1 . ILE A 78  ? 2.39039 2.09000 2.70275 0.27640  -0.17563 -0.13013 80  ILE A CD1 
160  N N   . TYR A 79  ? 3.03213 2.79861 3.41912 0.25496  -0.19879 -0.13780 81  TYR A N   
161  C CA  . TYR A 79  ? 3.03689 2.82086 3.44600 0.24984  -0.20863 -0.14020 81  TYR A CA  
162  C C   . TYR A 79  ? 3.01846 2.82794 3.45142 0.26202  -0.21174 -0.14675 81  TYR A C   
163  O O   . TYR A 79  ? 3.01799 2.83232 3.46781 0.26368  -0.22439 -0.14828 81  TYR A O   
164  C CB  . TYR A 79  ? 2.53776 2.30428 2.93817 0.24023  -0.22166 -0.14056 81  TYR A CB  
165  C CG  . TYR A 79  ? 2.59275 2.34529 2.98425 0.22367  -0.21839 -0.13936 81  TYR A CG  
166  C CD1 . TYR A 79  ? 2.87345 2.64181 3.28153 0.21368  -0.21572 -0.13713 81  TYR A CD1 
167  C CD2 . TYR A 79  ? 2.58091 2.30572 2.95031 0.21709  -0.21711 -0.14277 81  TYR A CD2 
168  C CE1 . TYR A 79  ? 3.04521 2.79978 3.44878 0.19744  -0.21163 -0.13784 81  TYR A CE1 
169  C CE2 . TYR A 79  ? 2.74519 2.45716 3.11257 0.20122  -0.21234 -0.14570 81  TYR A CE2 
170  C CZ  . TYR A 79  ? 3.03188 2.75763 3.41674 0.19137  -0.20954 -0.14297 81  TYR A CZ  
171  O OH  . TYR A 79  ? 3.12792 2.83986 3.51412 0.17452  -0.20375 -0.14752 81  TYR A OH  
172  N N   . ASP A 80  ? 3.20625 3.03473 3.64396 0.26971  -0.19991 -0.15063 82  ASP A N   
173  C CA  . ASP A 80  ? 3.19247 3.04853 3.65792 0.28024  -0.19900 -0.16208 82  ASP A CA  
174  C C   . ASP A 80  ? 3.18804 3.08089 3.68353 0.27566  -0.19531 -0.16638 82  ASP A C   
175  O O   . ASP A 80  ? 3.19441 3.09443 3.68401 0.26455  -0.19013 -0.15904 82  ASP A O   
176  C CB  . ASP A 80  ? 2.65902 2.52347 3.11414 0.28856  -0.18690 -0.16830 82  ASP A CB  
177  C CG  . ASP A 80  ? 2.60479 2.43557 3.03097 0.29339  -0.19008 -0.16531 82  ASP A CG  
178  O OD1 . ASP A 80  ? 2.59156 2.39823 3.01374 0.29286  -0.20313 -0.16269 82  ASP A OD1 
179  O OD2 . ASP A 80  ? 2.58046 2.41278 2.98798 0.29647  -0.17983 -0.16492 82  ASP A OD2 
180  N N   . LYS A 81  ? 3.05731 2.97400 3.58861 0.28406  -0.19772 -0.17901 83  LYS A N   
181  C CA  . LYS A 81  ? 3.05242 3.00706 3.61889 0.28085  -0.19545 -0.18663 83  LYS A CA  
182  C C   . LYS A 81  ? 3.04868 3.04256 3.63492 0.28592  -0.18047 -0.20461 83  LYS A C   
183  O O   . LYS A 81  ? 3.04222 3.04140 3.65162 0.29753  -0.17996 -0.21920 83  LYS A O   
184  C CB  . LYS A 81  ? 3.04707 3.00217 3.64829 0.28553  -0.21117 -0.18762 83  LYS A CB  
185  C CG  . LYS A 81  ? 3.04323 3.03372 3.67807 0.28006  -0.21143 -0.19224 83  LYS A CG  
186  C CD  . LYS A 81  ? 3.03195 3.05149 3.72156 0.29258  -0.21204 -0.20961 83  LYS A CD  
187  C CE  . LYS A 81  ? 3.02962 3.02891 3.74349 0.30198  -0.23081 -0.20199 83  LYS A CE  
188  N NZ  . LYS A 81  ? 3.01871 3.04439 3.79594 0.31541  -0.23125 -0.21861 83  LYS A NZ  
189  N N   . ILE A 82  ? 2.97280 2.99658 3.55163 0.27545  -0.16801 -0.20384 84  ILE A N   
190  C CA  . ILE A 82  ? 2.97669 3.04906 3.57266 0.27521  -0.15257 -0.22185 84  ILE A CA  
191  C C   . ILE A 82  ? 2.96989 3.08123 3.61497 0.27578  -0.15226 -0.24024 84  ILE A C   
192  O O   . ILE A 82  ? 2.97008 3.09445 3.62227 0.26617  -0.15504 -0.23387 84  ILE A O   
193  C CB  . ILE A 82  ? 2.99223 3.08642 3.56016 0.26121  -0.14055 -0.20956 84  ILE A CB  
194  C CG1 . ILE A 82  ? 2.99908 3.05560 3.52523 0.26271  -0.14074 -0.19168 84  ILE A CG1 
195  C CG2 . ILE A 82  ? 3.00218 3.15824 3.58812 0.25662  -0.12460 -0.22898 84  ILE A CG2 
196  C CD1 . ILE A 82  ? 2.93288 3.00762 3.43582 0.24971  -0.13109 -0.17345 84  ILE A CD1 
197  N N   . ARG A 83  ? 2.97098 3.10171 3.65320 0.28676  -0.14820 -0.26440 85  ARG A N   
198  C CA  . ARG A 83  ? 2.96292 3.12824 3.70174 0.29056  -0.14823 -0.28501 85  ARG A CA  
199  C C   . ARG A 83  ? 2.97296 3.20252 3.73077 0.28211  -0.12846 -0.31003 85  ARG A C   
200  O O   . ARG A 83  ? 2.98198 3.22914 3.72988 0.28152  -0.11546 -0.32287 85  ARG A O   
201  C CB  . ARG A 83  ? 2.95005 3.09547 3.72935 0.30828  -0.15682 -0.29679 85  ARG A CB  
202  C CG  . ARG A 83  ? 2.94475 3.03466 3.70831 0.31454  -0.17753 -0.27193 85  ARG A CG  
203  C CD  . ARG A 83  ? 2.94055 3.00380 3.71617 0.32841  -0.18125 -0.27771 85  ARG A CD  
204  N NE  . ARG A 83  ? 2.93690 2.96216 3.72091 0.33491  -0.20280 -0.25812 85  ARG A NE  
205  C CZ  . ARG A 83  ? 2.94322 2.92893 3.68074 0.33038  -0.21416 -0.23446 85  ARG A CZ  
206  N NH1 . ARG A 83  ? 2.92938 2.90291 3.61177 0.32136  -0.20642 -0.22691 85  ARG A NH1 
207  N NH2 . ARG A 83  ? 2.94465 2.90549 3.69415 0.33413  -0.23386 -0.21773 85  ARG A NH2 
208  N N   . LEU A 84  ? 2.91250 3.18137 3.69700 0.27380  -0.12600 -0.31764 86  LEU A N   
209  C CA  . LEU A 84  ? 2.92307 3.26161 3.73410 0.26406  -0.10776 -0.34559 86  LEU A CA  
210  C C   . LEU A 84  ? 2.91014 3.27629 3.78744 0.27120  -0.10977 -0.36975 86  LEU A C   
211  O O   . LEU A 84  ? 2.89744 3.23665 3.78971 0.27745  -0.12590 -0.35590 86  LEU A O   
212  C CB  . LEU A 84  ? 2.94131 3.31252 3.71706 0.24190  -0.10020 -0.33009 86  LEU A CB  
213  C CG  . LEU A 84  ? 2.96125 3.34018 3.68824 0.23092  -0.09020 -0.31630 86  LEU A CG  
214  C CD1 . LEU A 84  ? 2.95694 3.26634 3.63886 0.23759  -0.10220 -0.28464 86  LEU A CD1 
215  C CD2 . LEU A 84  ? 2.97975 3.40956 3.69042 0.20739  -0.08115 -0.30596 86  LEU A CD2 
216  N N   . ILE A 85  ? 2.86442 3.28808 3.78396 0.26945  -0.09296 -0.40700 87  ILE A N   
217  C CA  . ILE A 85  ? 2.85078 3.30396 3.84438 0.27849  -0.09236 -0.43616 87  ILE A CA  
218  C C   . ILE A 85  ? 2.86410 3.39818 3.87752 0.26065  -0.07332 -0.46453 87  ILE A C   
219  O O   . ILE A 85  ? 2.87826 3.45631 3.88290 0.24970  -0.05469 -0.48579 87  ILE A O   
220  C CB  . ILE A 85  ? 2.83693 3.27662 3.88158 0.29787  -0.09023 -0.46209 87  ILE A CB  
221  C CG1 . ILE A 85  ? 2.82847 3.19203 3.84792 0.31248  -0.10874 -0.43225 87  ILE A CG1 
222  C CG2 . ILE A 85  ? 2.82095 3.28704 3.95071 0.30913  -0.09114 -0.48949 87  ILE A CG2 
223  C CD1 . ILE A 85  ? 2.81685 3.14124 3.84420 0.32011  -0.13237 -0.40314 87  ILE A CD1 
224  N N   . ILE A 86  ? 2.70103 3.25937 3.74091 0.25606  -0.07787 -0.46536 88  ILE A N   
225  C CA  . ILE A 86  ? 2.71265 3.35228 3.77872 0.23879  -0.06056 -0.49504 88  ILE A CA  
226  C C   . ILE A 86  ? 2.69537 3.35712 3.83753 0.24975  -0.06449 -0.51865 88  ILE A C   
227  O O   . ILE A 86  ? 2.68595 3.32173 3.83128 0.25408  -0.08151 -0.49547 88  ILE A O   
228  C CB  . ILE A 86  ? 2.73246 3.39293 3.74123 0.21368  -0.05933 -0.46772 88  ILE A CB  
229  C CG1 . ILE A 86  ? 2.75395 3.41805 3.70260 0.19993  -0.04986 -0.45309 88  ILE A CG1 
230  C CG2 . ILE A 86  ? 2.74088 3.48229 3.78328 0.19636  -0.04652 -0.49450 88  ILE A CG2 
231  C CD1 . ILE A 86  ? 2.76780 3.50406 3.73584 0.18925  -0.02699 -0.49227 88  ILE A CD1 
232  N N   . ILE A 97  ? 2.59606 3.52860 3.42875 0.06948  -0.00858 -0.40658 99  ILE A N   
233  C CA  . ILE A 97  ? 2.59361 3.44250 3.37885 0.07865  -0.02332 -0.35969 99  ILE A CA  
234  C C   . ILE A 97  ? 2.59872 3.45305 3.34534 0.05420  -0.02741 -0.31626 99  ILE A C   
235  O O   . ILE A 97  ? 2.59382 3.45288 3.35031 0.04550  -0.03217 -0.31052 99  ILE A O   
236  C CB  . ILE A 97  ? 2.57466 3.33833 3.37516 0.10735  -0.04019 -0.35641 99  ILE A CB  
237  C CG1 . ILE A 97  ? 2.56340 3.34258 3.40315 0.10729  -0.04471 -0.37120 99  ILE A CG1 
238  C CG2 . ILE A 97  ? 2.56703 3.30670 3.39270 0.13213  -0.03882 -0.38411 99  ILE A CG2 
239  C CD1 . ILE A 97  ? 2.53988 3.24364 3.39276 0.13121  -0.06292 -0.36243 99  ILE A CD1 
240  N N   . LEU A 98  ? 2.70212 3.55692 3.40760 0.04278  -0.02561 -0.28487 100 LEU A N   
241  C CA  . LEU A 98  ? 2.70672 3.56878 3.37927 0.01866  -0.02886 -0.23985 100 LEU A CA  
242  C C   . LEU A 98  ? 2.70871 3.50289 3.34285 0.02745  -0.03757 -0.19881 100 LEU A C   
243  O O   . LEU A 98  ? 2.71026 3.48573 3.33754 0.04326  -0.03587 -0.20769 100 LEU A O   
244  C CB  . LEU A 98  ? 2.71473 3.68272 3.38395 -0.01436 -0.01433 -0.24281 100 LEU A CB  
245  C CG  . LEU A 98  ? 2.71328 3.76680 3.42184 -0.02772 -0.00186 -0.28861 100 LEU A CG  
246  C CD1 . LEU A 98  ? 2.71273 3.80691 3.45135 -0.01668 0.01156  -0.34082 100 LEU A CD1 
247  C CD2 . LEU A 98  ? 2.71572 3.85790 3.41103 -0.06715 0.00616  -0.27167 100 LEU A CD2 
248  N N   . PRO A 99  ? 2.71313 3.46983 3.32477 0.01723  -0.04635 -0.15469 101 PRO A N   
249  C CA  . PRO A 99  ? 2.71221 3.48418 3.32820 -0.00341 -0.04890 -0.13819 101 PRO A CA  
250  C C   . PRO A 99  ? 2.69853 3.41882 3.33390 0.01061  -0.05820 -0.15193 101 PRO A C   
251  O O   . PRO A 99  ? 2.68958 3.33234 3.32002 0.03329  -0.06807 -0.14858 101 PRO A O   
252  C CB  . PRO A 99  ? 2.71987 3.45645 3.30589 -0.01511 -0.05505 -0.08347 101 PRO A CB  
253  C CG  . PRO A 99  ? 2.72588 3.45222 3.29247 -0.00474 -0.05344 -0.07304 101 PRO A CG  
254  C CD  . PRO A 99  ? 2.71765 3.41974 3.29774 0.02291  -0.05273 -0.11523 101 PRO A CD  
255  N N   . GLU A 100 ? 2.71423 3.48254 3.37069 -0.00493 -0.05507 -0.16625 102 GLU A N   
256  C CA  . GLU A 100 ? 2.70039 3.43496 3.37704 0.00343  -0.06350 -0.17783 102 GLU A CA  
257  C C   . GLU A 100 ? 2.68690 3.36881 3.38086 0.03581  -0.07090 -0.20274 102 GLU A C   
258  O O   . GLU A 100 ? 2.68741 3.39913 3.40455 0.04853  -0.06478 -0.23638 102 GLU A O   
259  C CB  . GLU A 100 ? 2.69869 3.37758 3.35435 -0.00674 -0.07269 -0.13797 102 GLU A CB  
260  C CG  . GLU A 100 ? 2.71012 3.43624 3.35433 -0.04016 -0.06747 -0.10914 102 GLU A CG  
261  C CD  . GLU A 100 ? 2.72423 3.44086 3.34029 -0.04903 -0.06631 -0.06944 102 GLU A CD  
262  O OE1 . GLU A 100 ? 2.72457 3.36504 3.32547 -0.03985 -0.07425 -0.04165 102 GLU A OE1 
263  O OE2 . GLU A 100 ? 2.73497 3.52395 3.34630 -0.06596 -0.05731 -0.06654 102 GLU A OE2 
264  N N   . LYS A 101 ? 2.70364 3.30982 3.38866 0.04758  -0.08381 -0.18663 103 LYS A N   
265  C CA  . LYS A 101 ? 2.68892 3.24075 3.38519 0.07581  -0.09335 -0.20173 103 LYS A CA  
266  C C   . LYS A 101 ? 2.69156 3.18059 3.35444 0.08648  -0.09762 -0.17828 103 LYS A C   
267  O O   . LYS A 101 ? 2.69348 3.13649 3.33217 0.07939  -0.10289 -0.14835 103 LYS A O   
268  C CB  . LYS A 101 ? 2.67349 3.19307 3.38354 0.07923  -0.10512 -0.20202 103 LYS A CB  
269  C CG  . LYS A 101 ? 2.66898 3.24889 3.41446 0.06973  -0.10210 -0.22457 103 LYS A CG  
270  C CD  . LYS A 101 ? 2.65366 3.20024 3.41055 0.07340  -0.11510 -0.22198 103 LYS A CD  
271  C CE  . LYS A 101 ? 2.64794 3.25534 3.44269 0.06509  -0.11284 -0.24428 103 LYS A CE  
272  N NZ  . LYS A 101 ? 2.63397 3.21333 3.44004 0.06809  -0.12628 -0.24064 103 LYS A NZ  
273  N N   . CYS A 102 ? 2.78625 3.27383 3.45086 0.10314  -0.09467 -0.19361 104 CYS A N   
274  C CA  . CYS A 102 ? 2.78945 3.22464 3.42294 0.11284  -0.09762 -0.17332 104 CYS A CA  
275  C C   . CYS A 102 ? 2.77540 3.13285 3.40085 0.12730  -0.11164 -0.16407 104 CYS A C   
276  O O   . CYS A 102 ? 2.76296 3.10949 3.40783 0.13127  -0.11972 -0.17437 104 CYS A O   
277  C CB  . CYS A 102 ? 2.79391 3.24849 3.43218 0.12631  -0.09074 -0.19465 104 CYS A CB  
278  S SG  . CYS A 102 ? 2.80154 3.21086 3.39936 0.13312  -0.09128 -0.16809 104 CYS A SG  
279  N N   . PHE A 103 ? 2.79612 3.10388 3.39296 0.13370  -0.11432 -0.14420 105 PHE A N   
280  C CA  . PHE A 103 ? 2.78787 3.02397 3.37138 0.14412  -0.12578 -0.13419 105 PHE A CA  
281  C C   . PHE A 103 ? 2.79238 3.00558 3.37033 0.12803  -0.12951 -0.11504 105 PHE A C   
282  O O   . PHE A 103 ? 2.79360 2.95058 3.35796 0.13085  -0.13637 -0.10442 105 PHE A O   
283  C CB  . PHE A 103 ? 2.77101 2.99143 3.37461 0.16264  -0.13508 -0.15754 105 PHE A CB  
284  C CG  . PHE A 103 ? 2.76774 2.99441 3.37632 0.17987  -0.13218 -0.17451 105 PHE A CG  
285  C CD1 . PHE A 103 ? 2.78016 3.01635 3.36818 0.17903  -0.12295 -0.16740 105 PHE A CD1 
286  C CD2 . PHE A 103 ? 2.75361 2.97762 3.38991 0.19617  -0.13896 -0.19620 105 PHE A CD2 
287  C CE1 . PHE A 103 ? 2.77920 3.02278 3.37169 0.19314  -0.11922 -0.18486 105 PHE A CE1 
288  C CE2 . PHE A 103 ? 2.75138 2.97925 3.39562 0.21100  -0.13548 -0.21251 105 PHE A CE2 
289  C CZ  . PHE A 103 ? 2.76454 3.00227 3.38553 0.20903  -0.12498 -0.20845 105 PHE A CZ  
290  N N   . GLN A 104 ? 2.72314 2.98121 3.31219 0.10946  -0.12413 -0.11193 106 GLN A N   
291  C CA  . GLN A 104 ? 2.73348 2.97422 3.31446 0.09021  -0.12400 -0.08790 106 GLN A CA  
292  C C   . GLN A 104 ? 2.74824 3.03229 3.32419 0.07088  -0.11424 -0.06705 106 GLN A C   
293  O O   . GLN A 104 ? 2.76039 3.02078 3.32780 0.05687  -0.11354 -0.03911 106 GLN A O   
294  C CB  . GLN A 104 ? 2.72913 2.97720 3.32802 0.08159  -0.12919 -0.09873 106 GLN A CB  
295  C CG  . GLN A 104 ? 2.74905 2.96642 3.34036 0.06264  -0.12963 -0.07680 106 GLN A CG  
296  C CD  . GLN A 104 ? 2.75601 2.98717 3.36379 0.05110  -0.13375 -0.08748 106 GLN A CD  
297  O OE1 . GLN A 104 ? 2.74227 2.99646 3.36761 0.06066  -0.13902 -0.11020 106 GLN A OE1 
298  N NE2 . GLN A 104 ? 2.77836 2.99591 3.38365 0.03018  -0.13142 -0.07032 106 GLN A NE2 
299  N N   . LYS A 105 ? 2.75621 3.10440 3.33944 0.06878  -0.10659 -0.07961 107 LYS A N   
300  C CA  . LYS A 105 ? 2.77110 3.16973 3.34656 0.04998  -0.09762 -0.05916 107 LYS A CA  
301  C C   . LYS A 105 ? 2.77661 3.18591 3.33962 0.06162  -0.09325 -0.06057 107 LYS A C   
302  O O   . LYS A 105 ? 2.76798 3.17630 3.33771 0.08048  -0.09342 -0.08932 107 LYS A O   
303  C CB  . LYS A 105 ? 2.77190 3.25042 3.36592 0.03212  -0.09054 -0.07519 107 LYS A CB  
304  C CG  . LYS A 105 ? 2.76512 3.23798 3.37328 0.02158  -0.09486 -0.07832 107 LYS A CG  
305  C CD  . LYS A 105 ? 2.77708 3.22379 3.37359 0.00124  -0.09623 -0.04028 107 LYS A CD  
306  C CE  . LYS A 105 ? 2.77219 3.22602 3.38322 -0.01342 -0.09850 -0.04574 107 LYS A CE  
307  N NZ  . LYS A 105 ? 2.76953 3.30804 3.39752 -0.02757 -0.09159 -0.06551 107 LYS A NZ  
308  N N   . VAL A 106 ? 2.77120 3.19040 3.31819 0.05006  -0.08982 -0.02794 108 VAL A N   
309  C CA  . VAL A 106 ? 2.77744 3.19497 3.30897 0.06138  -0.08733 -0.02276 108 VAL A CA  
310  C C   . VAL A 106 ? 2.79330 3.27912 3.31713 0.03977  -0.07969 0.00186  108 VAL A C   
311  O O   . VAL A 106 ? 2.80234 3.30523 3.32705 0.01794  -0.07983 0.03294  108 VAL A O   
312  C CB  . VAL A 106 ? 2.77739 3.11037 3.29525 0.07680  -0.09511 -0.00302 108 VAL A CB  
313  C CG1 . VAL A 106 ? 2.79119 3.12920 3.29309 0.07683  -0.09256 0.02458  108 VAL A CG1 
314  C CG2 . VAL A 106 ? 2.76172 3.04776 3.28096 0.10145  -0.10083 -0.03387 108 VAL A CG2 
315  N N   . TYR A 107 ? 2.82974 3.35707 3.34684 0.04449  -0.07315 -0.01162 109 TYR A N   
316  C CA  . TYR A 107 ? 2.84254 3.44680 3.35081 0.02335  -0.06544 0.00776  109 TYR A CA  
317  C C   . TYR A 107 ? 2.85168 3.42266 3.34129 0.02890  -0.06956 0.04626  109 TYR A C   
318  O O   . TYR A 107 ? 2.85379 3.44597 3.33219 0.03593  -0.06554 0.04040  109 TYR A O   
319  C CB  . TYR A 107 ? 2.83993 3.51551 3.35546 0.02331  -0.05428 -0.03515 109 TYR A CB  
320  C CG  . TYR A 107 ? 2.84694 3.62242 3.35603 -0.00285 -0.04387 -0.02738 109 TYR A CG  
321  C CD1 . TYR A 107 ? 2.85051 3.68410 3.36026 -0.03357 -0.04216 -0.00090 109 TYR A CD1 
322  C CD2 . TYR A 107 ? 2.84640 3.66414 3.34976 0.00106  -0.03515 -0.04937 109 TYR A CD2 
323  C CE1 . TYR A 107 ? 2.84917 3.78302 3.35214 -0.06065 -0.03292 0.00626  109 TYR A CE1 
324  C CE2 . TYR A 107 ? 2.84576 3.76319 3.34281 -0.02556 -0.02489 -0.04521 109 TYR A CE2 
325  C CZ  . TYR A 107 ? 2.84516 3.82258 3.34145 -0.05693 -0.02410 -0.01678 109 TYR A CZ  
326  O OH  . TYR A 107 ? 2.83775 3.92240 3.32646 -0.08671 -0.01432 -0.01127 109 TYR A OH  
327  N N   . THR A 108 ? 2.73215 3.24904 3.22192 0.02584  -0.07740 0.08496  110 THR A N   
328  C CA  . THR A 108 ? 2.74538 3.21970 3.22561 0.03345  -0.08237 0.12257  110 THR A CA  
329  C C   . THR A 108 ? 2.75217 3.30036 3.22331 0.01631  -0.07827 0.15230  110 THR A C   
330  O O   . THR A 108 ? 2.74004 3.30306 3.19853 0.02678  -0.07552 0.14482  110 THR A O   
331  C CB  . THR A 108 ? 2.77147 3.18242 3.26289 0.02929  -0.08968 0.15748  110 THR A CB  
332  O OG1 . THR A 108 ? 2.78333 3.22786 3.28672 0.00589  -0.08844 0.16376  110 THR A OG1 
333  C CG2 . THR A 108 ? 2.76682 3.08643 3.26042 0.05300  -0.09514 0.13651  110 THR A CG2 
334  N N   . ASP A 109 ? 2.85176 3.44907 3.32917 -0.01153 -0.07825 0.18772  111 ASP A N   
335  C CA  . ASP A 109 ? 2.84774 3.52762 3.31712 -0.03299 -0.07538 0.22031  111 ASP A CA  
336  C C   . ASP A 109 ? 2.84084 3.61807 3.30499 -0.04826 -0.06407 0.18110  111 ASP A C   
337  O O   . ASP A 109 ? 2.83828 3.66528 3.31084 -0.06973 -0.06025 0.17294  111 ASP A O   
338  C CB  . ASP A 109 ? 2.84878 3.54213 3.32970 -0.05820 -0.08112 0.27798  111 ASP A CB  
339  C CG  . ASP A 109 ? 2.84426 3.59995 3.31917 -0.07498 -0.08283 0.32657  111 ASP A CG  
340  O OD1 . ASP A 109 ? 2.83596 3.67103 3.29546 -0.08291 -0.07565 0.30958  111 ASP A OD1 
341  O OD2 . ASP A 109 ? 2.84840 3.57513 3.33695 -0.08080 -0.09132 0.38202  111 ASP A OD2 
342  N N   . TYR A 110 ? 2.85685 3.66241 3.30935 -0.03773 -0.05776 0.15406  112 TYR A N   
343  C CA  . TYR A 110 ? 2.84877 3.74149 3.30204 -0.04952 -0.04487 0.10741  112 TYR A CA  
344  C C   . TYR A 110 ? 2.83929 3.84534 3.28906 -0.08858 -0.03926 0.13129  112 TYR A C   
345  O O   . TYR A 110 ? 2.83293 3.91174 3.29121 -0.10728 -0.02952 0.09856  112 TYR A O   
346  C CB  . TYR A 110 ? 2.84554 3.74012 3.28908 -0.03056 -0.03885 0.07490  112 TYR A CB  
347  C CG  . TYR A 110 ? 2.83884 3.79283 3.26494 -0.04416 -0.03700 0.10662  112 TYR A CG  
348  C CD1 . TYR A 110 ? 2.84229 3.74834 3.25993 -0.03663 -0.04792 0.15941  112 TYR A CD1 
349  C CD2 . TYR A 110 ? 2.82664 3.88880 3.24772 -0.06565 -0.02399 0.08315  112 TYR A CD2 
350  C CE1 . TYR A 110 ? 2.83400 3.79799 3.23810 -0.04905 -0.04749 0.19174  112 TYR A CE1 
351  C CE2 . TYR A 110 ? 2.81692 3.94062 3.22115 -0.08039 -0.02271 0.11337  112 TYR A CE2 
352  C CZ  . TYR A 110 ? 2.82093 3.89518 3.21641 -0.07152 -0.03528 0.16960  112 TYR A CZ  
353  O OH  . TYR A 110 ? 2.80994 3.94867 3.19092 -0.08597 -0.03519 0.20263  112 TYR A OH  
354  N N   . GLU A 111 ? 2.80945 3.83537 3.24913 -0.10230 -0.04555 0.18892  113 GLU A N   
355  C CA  . GLU A 111 ? 2.79688 3.93925 3.23109 -0.14190 -0.04136 0.21634  113 GLU A CA  
356  C C   . GLU A 111 ? 2.79859 3.95868 3.24478 -0.16674 -0.04485 0.24006  113 GLU A C   
357  O O   . GLU A 111 ? 2.78930 4.04685 3.23641 -0.19715 -0.03624 0.22517  113 GLU A O   
358  C CB  . GLU A 111 ? 2.79207 3.95143 3.21490 -0.14827 -0.04882 0.27518  113 GLU A CB  
359  C CG  . GLU A 111 ? 2.77433 4.07062 3.18561 -0.18686 -0.04237 0.29230  113 GLU A CG  
360  C CD  . GLU A 111 ? 2.76298 4.13148 3.16477 -0.18900 -0.02592 0.22865  113 GLU A CD  
361  O OE1 . GLU A 111 ? 2.75889 4.17045 3.16942 -0.19891 -0.01437 0.17720  113 GLU A OE1 
362  O OE2 . GLU A 111 ? 2.75770 4.14007 3.14635 -0.18076 -0.02400 0.22873  113 GLU A OE2 
363  N N   . ASN A 112 ? 2.85521 3.92386 3.31201 -0.15554 -0.05656 0.27488  114 ASN A N   
364  C CA  . ASN A 112 ? 2.85851 3.93230 3.32831 -0.17726 -0.05987 0.29521  114 ASN A CA  
365  C C   . ASN A 112 ? 2.86120 3.92537 3.34047 -0.17121 -0.05295 0.23656  114 ASN A C   
366  O O   . ASN A 112 ? 2.86229 3.94462 3.35139 -0.19177 -0.05365 0.24509  114 ASN A O   
367  C CB  . ASN A 112 ? 2.86948 3.84544 3.35227 -0.16684 -0.07310 0.34676  114 ASN A CB  
368  C CG  . ASN A 112 ? 2.86685 3.86433 3.35003 -0.17966 -0.08130 0.41554  114 ASN A CG  
369  O OD1 . ASN A 112 ? 2.86137 3.87251 3.33322 -0.16899 -0.08116 0.42036  114 ASN A OD1 
370  N ND2 . ASN A 112 ? 2.87111 3.87195 3.36995 -0.20286 -0.08897 0.47074  114 ASN A ND2 
371  N N   . ARG A 113 ? 2.79884 3.83701 3.27771 -0.14427 -0.04681 0.17960  115 ARG A N   
372  C CA  . ARG A 113 ? 2.80058 3.82840 3.29377 -0.13452 -0.04112 0.12298  115 ARG A CA  
373  C C   . ARG A 113 ? 2.80933 3.76401 3.31468 -0.13105 -0.04981 0.13769  115 ARG A C   
374  O O   . ARG A 113 ? 2.80847 3.80203 3.32362 -0.15270 -0.04767 0.13488  115 ARG A O   
375  C CB  . ARG A 113 ? 2.78981 3.93691 3.28858 -0.16301 -0.02786 0.08980  115 ARG A CB  
376  C CG  . ARG A 113 ? 2.78946 3.93340 3.30922 -0.14853 -0.02034 0.02401  115 ARG A CG  
377  C CD  . ARG A 113 ? 2.77725 4.04313 3.30742 -0.17517 -0.00482 -0.01576 115 ARG A CD  
378  N NE  . ARG A 113 ? 2.77694 4.03749 3.33553 -0.16061 0.00157  -0.07587 115 ARG A NE  
379  C CZ  . ARG A 113 ? 2.76817 4.12110 3.34666 -0.17574 0.01654  -0.12537 115 ARG A CZ  
380  N NH1 . ARG A 113 ? 2.75674 4.22051 3.32652 -0.20829 0.02784  -0.12581 115 ARG A NH1 
381  N NH2 . ARG A 113 ? 2.76859 4.10572 3.37923 -0.15863 0.02041  -0.17609 115 ARG A NH2 
382  N N   . VAL A 114 ? 2.80909 3.65900 3.31384 -0.10442 -0.05904 0.15179  116 VAL A N   
383  C CA  . VAL A 114 ? 2.81534 3.58828 3.33152 -0.09990 -0.06688 0.16514  116 VAL A CA  
384  C C   . VAL A 114 ? 2.81396 3.52412 3.33712 -0.07082 -0.06772 0.11595  116 VAL A C   
385  O O   . VAL A 114 ? 2.80487 3.51957 3.32528 -0.05174 -0.06372 0.07828  116 VAL A O   
386  C CB  . VAL A 114 ? 2.81980 3.52296 3.33590 -0.09543 -0.07634 0.21922  116 VAL A CB  
387  C CG1 . VAL A 114 ? 2.81839 3.58816 3.33094 -0.12327 -0.07716 0.27242  116 VAL A CG1 
388  C CG2 . VAL A 114 ? 2.82075 3.45470 3.32911 -0.06235 -0.07939 0.20828  116 VAL A CG2 
389  N N   . GLU A 115 ? 2.80638 3.45895 3.34037 -0.06897 -0.07331 0.11798  117 GLU A N   
390  C CA  . GLU A 115 ? 2.79049 3.39315 3.33350 -0.04699 -0.07558 0.07574  117 GLU A CA  
391  C C   . GLU A 115 ? 2.78977 3.29426 3.33438 -0.03533 -0.08441 0.09474  117 GLU A C   
392  O O   . GLU A 115 ? 2.78813 3.27065 3.34333 -0.04509 -0.08700 0.09754  117 GLU A O   
393  C CB  . GLU A 115 ? 2.78317 3.43903 3.34166 -0.06188 -0.07129 0.04772  117 GLU A CB  
394  C CG  . GLU A 115 ? 2.78464 3.54521 3.34639 -0.07732 -0.06050 0.02491  117 GLU A CG  
395  C CD  . GLU A 115 ? 2.79810 3.63042 3.35230 -0.11227 -0.05683 0.06325  117 GLU A CD  
396  O OE1 . GLU A 115 ? 2.80867 3.60652 3.35932 -0.12433 -0.06334 0.10939  117 GLU A OE1 
397  O OE2 . GLU A 115 ? 2.79619 3.72168 3.35039 -0.12898 -0.04725 0.04714  117 GLU A OE2 
398  N N   . THR A 116 ? 2.82829 3.27645 3.36344 -0.01553 -0.08814 0.10538  118 THR A N   
399  C CA  . THR A 116 ? 2.82879 3.18619 3.36742 -0.00410 -0.09486 0.11772  118 THR A CA  
400  C C   . THR A 116 ? 2.81155 3.12578 3.35214 0.01601  -0.09840 0.07630  118 THR A C   
401  O O   . THR A 116 ? 2.80027 3.12352 3.33525 0.03394  -0.09787 0.04662  118 THR A O   
402  C CB  . THR A 116 ? 2.83717 3.15525 3.36758 0.00881  -0.09711 0.14377  118 THR A CB  
403  O OG1 . THR A 116 ? 2.85078 3.21515 3.38208 -0.01077 -0.09533 0.18682  118 THR A OG1 
404  C CG2 . THR A 116 ? 2.84074 3.06860 3.37950 0.01848  -0.10227 0.15342  118 THR A CG2 
405  N N   . ASP A 117 ? 2.84211 3.11167 3.39237 0.01170  -0.10218 0.07531  119 ASP A N   
406  C CA  . ASP A 117 ? 2.82635 3.05948 3.37888 0.02781  -0.10703 0.04051  119 ASP A CA  
407  C C   . ASP A 117 ? 2.82419 2.99366 3.36599 0.05080  -0.11135 0.03627  119 ASP A C   
408  O O   . ASP A 117 ? 2.83720 2.97411 3.37436 0.05264  -0.11088 0.06210  119 ASP A O   
409  C CB  . ASP A 117 ? 2.82925 3.03756 3.39389 0.01390  -0.10944 0.04057  119 ASP A CB  
410  C CG  . ASP A 117 ? 2.82696 3.10020 3.40246 -0.00715 -0.10584 0.03664  119 ASP A CG  
411  O OD1 . ASP A 117 ? 2.82930 3.16651 3.40320 -0.01622 -0.10047 0.04268  119 ASP A OD1 
412  O OD2 . ASP A 117 ? 2.82412 3.08842 3.40967 -0.01592 -0.10804 0.02610  119 ASP A OD2 
413  N N   . ILE A 118 ? 2.81538 2.96925 3.35575 0.06808  -0.11604 0.00408  120 ILE A N   
414  C CA  . ILE A 118 ? 2.81264 2.90996 3.34176 0.08824  -0.12075 -0.00277 120 ILE A CA  
415  C C   . ILE A 118 ? 2.82512 2.85827 3.35594 0.08432  -0.12370 0.00690  120 ILE A C   
416  O O   . ILE A 118 ? 2.82833 2.81428 3.35031 0.09733  -0.12600 0.00617  120 ILE A O   
417  C CB  . ILE A 118 ? 2.79312 2.89273 3.32312 0.10565  -0.12629 -0.03663 120 ILE A CB  
418  C CG1 . ILE A 118 ? 2.78959 2.85321 3.30433 0.12596  -0.12892 -0.04100 120 ILE A CG1 
419  C CG2 . ILE A 118 ? 2.78868 2.86419 3.32774 0.10214  -0.13328 -0.05031 120 ILE A CG2 
420  C CD1 . ILE A 118 ? 2.77255 2.82755 3.28953 0.14268  -0.13618 -0.06890 120 ILE A CD1 
421  N N   . SER A 119 ? 2.87985 2.91209 3.42333 0.06540  -0.12271 0.01386  121 SER A N   
422  C CA  . SER A 119 ? 2.89818 2.87212 3.44786 0.05886  -0.12334 0.01956  121 SER A CA  
423  C C   . SER A 119 ? 2.91781 2.86190 3.47248 0.05624  -0.11875 0.05095  121 SER A C   
424  O O   . SER A 119 ? 2.93122 2.81998 3.48893 0.06180  -0.11877 0.05054  121 SER A O   
425  C CB  . SER A 119 ? 2.90554 2.89015 3.46938 0.03776  -0.12262 0.01700  121 SER A CB  
426  O OG  . SER A 119 ? 2.90825 2.93893 3.48000 0.02085  -0.11774 0.03811  121 SER A OG  
427  N N   . GLU A 120 ? 2.88880 2.87206 3.44712 0.04695  -0.11490 0.07864  122 GLU A N   
428  C CA  . GLU A 120 ? 2.90738 2.86888 3.47623 0.04316  -0.11191 0.11525  122 GLU A CA  
429  C C   . GLU A 120 ? 2.90109 2.86844 3.45548 0.06173  -0.11247 0.12175  122 GLU A C   
430  O O   . GLU A 120 ? 2.90547 2.90951 3.45970 0.05711  -0.11061 0.15016  122 GLU A O   
431  C CB  . GLU A 120 ? 2.91734 2.92138 3.49948 0.01943  -0.10881 0.14744  122 GLU A CB  
432  C CG  . GLU A 120 ? 2.93882 2.91408 3.54248 0.01142  -0.10706 0.19038  122 GLU A CG  
433  C CD  . GLU A 120 ? 2.93895 2.97140 3.54012 0.00387  -0.10672 0.22717  122 GLU A CD  
434  O OE1 . GLU A 120 ? 2.92625 3.02585 3.51002 -0.00030 -0.10599 0.21682  122 GLU A OE1 
435  O OE2 . GLU A 120 ? 2.95249 2.96572 3.57178 0.00132  -0.10708 0.26621  122 GLU A OE2 
436  N N   . LEU A 121 ? 2.86052 2.79432 3.40210 0.08144  -0.11539 0.09529  123 LEU A N   
437  C CA  . LEU A 121 ? 2.85417 2.78859 3.38057 0.10002  -0.11597 0.09600  123 LEU A CA  
438  C C   . LEU A 121 ? 2.86037 2.72802 3.38762 0.11358  -0.11749 0.08782  123 LEU A C   
439  O O   . LEU A 121 ? 2.86974 2.69546 3.40784 0.10843  -0.11781 0.07612  123 LEU A O   
440  C CB  . LEU A 121 ? 2.83308 2.80862 3.34109 0.11080  -0.11759 0.06722  123 LEU A CB  
441  C CG  . LEU A 121 ? 2.82881 2.87836 3.33805 0.09784  -0.11414 0.06995  123 LEU A CG  
442  C CD1 . LEU A 121 ? 2.81088 2.89537 3.31035 0.11009  -0.11449 0.03698  123 LEU A CD1 
443  C CD2 . LEU A 121 ? 2.84261 2.92837 3.35265 0.08823  -0.11006 0.10636  123 LEU A CD2 
444  N N   . GLY A 122 ? 2.86884 2.73078 3.38480 0.12957  -0.11770 0.09207  124 GLY A N   
445  C CA  . GLY A 122 ? 2.87643 2.68130 3.39558 0.14166  -0.11795 0.08865  124 GLY A CA  
446  C C   . GLY A 122 ? 2.86482 2.64300 3.36615 0.15474  -0.12187 0.05224  124 GLY A C   
447  O O   . GLY A 122 ? 2.86248 2.59654 3.36558 0.16319  -0.12154 0.04610  124 GLY A O   
448  N N   . LEU A 123 ? 2.83328 2.63849 3.32034 0.15610  -0.12581 0.02851  125 LEU A N   
449  C CA  . LEU A 123 ? 2.82252 2.60647 3.29441 0.16707  -0.13138 -0.00162 125 LEU A CA  
450  C C   . LEU A 123 ? 2.83582 2.58420 3.31679 0.15674  -0.13321 -0.01659 125 LEU A C   
451  O O   . LEU A 123 ? 2.84499 2.59999 3.34089 0.14097  -0.13155 -0.01240 125 LEU A O   
452  C CB  . LEU A 123 ? 2.80090 2.62719 3.26217 0.17241  -0.13552 -0.01902 125 LEU A CB  
453  C CG  . LEU A 123 ? 2.78811 2.59983 3.23715 0.18305  -0.14331 -0.04596 125 LEU A CG  
454  C CD1 . LEU A 123 ? 2.78734 2.57270 3.22043 0.19762  -0.14378 -0.04851 125 LEU A CD1 
455  C CD2 . LEU A 123 ? 2.76860 2.62409 3.21903 0.18750  -0.14651 -0.05963 125 LEU A CD2 
456  N N   . ILE A 124 ? 2.85187 2.56624 3.32326 0.16374  -0.13623 -0.03509 126 ILE A N   
457  C CA  . ILE A 124 ? 2.87155 2.55645 3.35041 0.15163  -0.13702 -0.05229 126 ILE A CA  
458  C C   . ILE A 124 ? 2.86367 2.57311 3.33613 0.14555  -0.14497 -0.07025 126 ILE A C   
459  O O   . ILE A 124 ? 2.87517 2.59124 3.36050 0.12962  -0.14426 -0.07235 126 ILE A O   
460  C CB  . ILE A 124 ? 2.88301 2.52932 3.35457 0.15838  -0.13674 -0.06672 126 ILE A CB  
461  C CG1 . ILE A 124 ? 2.88196 2.49733 3.37342 0.15973  -0.12768 -0.05026 126 ILE A CG1 
462  C CG2 . ILE A 124 ? 2.90348 2.53496 3.37474 0.14506  -0.13967 -0.09216 126 ILE A CG2 
463  C CD1 . ILE A 124 ? 2.87814 2.45505 3.37014 0.16312  -0.12518 -0.06853 126 ILE A CD1 
464  N N   . GLU A 125 ? 2.86529 2.58910 3.32072 0.15790  -0.15297 -0.08230 127 GLU A N   
465  C CA  . GLU A 125 ? 2.85935 2.60487 3.31314 0.15421  -0.16252 -0.09735 127 GLU A CA  
466  C C   . GLU A 125 ? 2.82985 2.61344 3.28258 0.16705  -0.16649 -0.09631 127 GLU A C   
467  O O   . GLU A 125 ? 2.81665 2.60009 3.25828 0.18213  -0.16680 -0.09619 127 GLU A O   
468  C CB  . GLU A 125 ? 2.87291 2.59774 3.31347 0.15415  -0.17011 -0.11482 127 GLU A CB  
469  C CG  . GLU A 125 ? 2.86857 2.61894 3.30867 0.15219  -0.18268 -0.12540 127 GLU A CG  
470  C CD  . GLU A 125 ? 2.89146 2.62677 3.31803 0.14725  -0.19081 -0.13914 127 GLU A CD  
471  O OE1 . GLU A 125 ? 2.91939 2.62727 3.34197 0.13716  -0.18481 -0.14647 127 GLU A OE1 
472  O OE2 . GLU A 125 ? 2.88416 2.63714 3.30680 0.15253  -0.20308 -0.14256 127 GLU A OE2 
473  N N   . TYR A 126 ? 2.82531 2.64279 3.29209 0.16042  -0.16865 -0.09774 128 TYR A N   
474  C CA  . TYR A 126 ? 2.80060 2.65771 3.27450 0.17111  -0.17130 -0.10185 128 TYR A CA  
475  C C   . TYR A 126 ? 2.79585 2.67649 3.28523 0.16600  -0.18041 -0.11273 128 TYR A C   
476  O O   . TYR A 126 ? 2.81242 2.68593 3.30559 0.15127  -0.18300 -0.11426 128 TYR A O   
477  C CB  . TYR A 126 ? 2.79452 2.68339 3.27583 0.16876  -0.16119 -0.08962 128 TYR A CB  
478  C CG  . TYR A 126 ? 2.80240 2.71016 3.29826 0.15055  -0.15734 -0.08229 128 TYR A CG  
479  C CD1 . TYR A 126 ? 2.82333 2.70461 3.31972 0.13687  -0.15175 -0.06792 128 TYR A CD1 
480  C CD2 . TYR A 126 ? 2.79005 2.74272 3.30263 0.14680  -0.15875 -0.09030 128 TYR A CD2 
481  C CE1 . TYR A 126 ? 2.83170 2.72967 3.34215 0.11884  -0.14808 -0.06039 128 TYR A CE1 
482  C CE2 . TYR A 126 ? 2.79691 2.76933 3.32168 0.12896  -0.15511 -0.08391 128 TYR A CE2 
483  C CZ  . TYR A 126 ? 2.81775 2.76230 3.33998 0.11448  -0.14993 -0.06822 128 TYR A CZ  
484  O OH  . TYR A 126 ? 2.82568 2.78922 3.36077 0.09537  -0.14621 -0.06111 128 TYR A OH  
485  N N   . GLU A 127 ? 2.89747 2.80797 3.39912 0.17812  -0.18493 -0.12097 129 GLU A N   
486  C CA  . GLU A 127 ? 2.89046 2.82807 3.41417 0.17632  -0.19438 -0.12976 129 GLU A CA  
487  C C   . GLU A 127 ? 2.86985 2.85085 3.41644 0.18591  -0.19058 -0.13717 129 GLU A C   
488  O O   . GLU A 127 ? 2.85917 2.84302 3.40849 0.20136  -0.19082 -0.14369 129 GLU A O   
489  C CB  . GLU A 127 ? 2.89478 2.81567 3.41598 0.18238  -0.20865 -0.13478 129 GLU A CB  
490  C CG  . GLU A 127 ? 2.89186 2.84097 3.43883 0.17982  -0.22079 -0.13926 129 GLU A CG  
491  C CD  . GLU A 127 ? 2.86822 2.84636 3.44461 0.19700  -0.22469 -0.14641 129 GLU A CD  
492  O OE1 . GLU A 127 ? 2.86020 2.82630 3.43230 0.21162  -0.22428 -0.14891 129 GLU A OE1 
493  O OE2 . GLU A 127 ? 2.85908 2.87269 3.46578 0.19561  -0.22748 -0.15104 129 GLU A OE2 
494  N N   . ILE A 128 ? 2.82651 2.84295 3.39096 0.17556  -0.18621 -0.13835 130 ILE A N   
495  C CA  . ILE A 128 ? 2.81264 2.87767 3.40203 0.18107  -0.18036 -0.14922 130 ILE A CA  
496  C C   . ILE A 128 ? 2.80206 2.89303 3.42528 0.18485  -0.19048 -0.16125 130 ILE A C   
497  O O   . ILE A 128 ? 2.80759 2.89665 3.43471 0.17403  -0.19787 -0.15747 130 ILE A O   
498  C CB  . ILE A 128 ? 2.81922 2.91340 3.40659 0.16543  -0.16765 -0.14181 130 ILE A CB  
499  C CG1 . ILE A 128 ? 2.82761 2.92089 3.41742 0.14679  -0.16996 -0.13473 130 ILE A CG1 
500  C CG2 . ILE A 128 ? 2.83069 2.90227 3.39051 0.16379  -0.15917 -0.12628 130 ILE A CG2 
501  C CD1 . ILE A 128 ? 2.83779 2.95102 3.42292 0.12857  -0.15864 -0.12169 130 ILE A CD1 
502  N N   . GLU A 129 ? 2.86268 2.97912 3.51379 0.19998  -0.19071 -0.17617 131 GLU A N   
503  C CA  . GLU A 129 ? 2.85221 2.98992 3.54339 0.20786  -0.20182 -0.18624 131 GLU A CA  
504  C C   . GLU A 129 ? 2.84258 3.03361 3.57325 0.21282  -0.19258 -0.20628 131 GLU A C   
505  O O   . GLU A 129 ? 2.84326 3.04863 3.57324 0.21799  -0.18058 -0.21662 131 GLU A O   
506  C CB  . GLU A 129 ? 2.84883 2.95676 3.54511 0.22399  -0.21486 -0.18489 131 GLU A CB  
507  C CG  . GLU A 129 ? 2.84386 2.96429 3.57771 0.22910  -0.23139 -0.18474 131 GLU A CG  
508  C CD  . GLU A 129 ? 2.82883 2.97941 3.61600 0.24652  -0.23148 -0.20153 131 GLU A CD  
509  O OE1 . GLU A 129 ? 2.82449 2.98303 3.61553 0.25457  -0.21855 -0.21568 131 GLU A OE1 
510  O OE2 . GLU A 129 ? 2.82333 2.99152 3.65166 0.25166  -0.24428 -0.20104 131 GLU A OE2 
511  N N   . GLU A 130 ? 2.84174 3.06586 3.60803 0.20997  -0.19770 -0.21328 132 GLU A N   
512  C CA  . GLU A 130 ? 2.83401 3.11318 3.64641 0.21429  -0.18960 -0.23624 132 GLU A CA  
513  C C   . GLU A 130 ? 2.82199 3.11008 3.68600 0.22904  -0.20392 -0.24332 132 GLU A C   
514  O O   . GLU A 130 ? 2.82124 3.10737 3.69154 0.22352  -0.21690 -0.23184 132 GLU A O   
515  C CB  . GLU A 130 ? 2.83902 3.15904 3.64978 0.19417  -0.18022 -0.23797 132 GLU A CB  
516  C CG  . GLU A 130 ? 2.83105 3.21103 3.69652 0.19609  -0.17672 -0.26150 132 GLU A CG  
517  C CD  . GLU A 130 ? 2.83289 3.25183 3.72484 0.20373  -0.16172 -0.28821 132 GLU A CD  
518  O OE1 . GLU A 130 ? 2.82664 3.23112 3.74163 0.22294  -0.16430 -0.29899 132 GLU A OE1 
519  O OE2 . GLU A 130 ? 2.84268 3.30950 3.73313 0.18866  -0.14693 -0.29895 132 GLU A OE2 
520  N N   . ASN A 131 ? 2.83973 3.13889 3.74331 0.24702  -0.20168 -0.26144 133 ASN A N   
521  C CA  . ASN A 131 ? 2.82834 3.13453 3.79041 0.26351  -0.21546 -0.26648 133 ASN A CA  
522  C C   . ASN A 131 ? 2.82103 3.18506 3.84445 0.26862  -0.20460 -0.29683 133 ASN A C   
523  O O   . ASN A 131 ? 2.82380 3.21015 3.85664 0.27106  -0.18750 -0.32049 133 ASN A O   
524  C CB  . ASN A 131 ? 2.82556 3.09275 3.79341 0.28127  -0.22323 -0.26236 133 ASN A CB  
525  C CG  . ASN A 131 ? 2.81498 3.08782 3.84893 0.29844  -0.23903 -0.26267 133 ASN A CG  
526  O OD1 . ASN A 131 ? 2.81669 3.07130 3.85053 0.29817  -0.25886 -0.23878 133 ASN A OD1 
527  N ND2 . ASN A 131 ? 2.80608 3.10697 3.90015 0.31250  -0.23022 -0.28968 133 ASN A ND2 
528  N N   . ASP A 132 ? 3.17647 3.56856 4.24266 0.26905  -0.21406 -0.29753 134 ASP A N   
529  C CA  . ASP A 132 ? 3.16823 3.61602 4.30368 0.27596  -0.20602 -0.32752 134 ASP A CA  
530  C C   . ASP A 132 ? 3.15483 3.60170 4.36152 0.29694  -0.22298 -0.32651 134 ASP A C   
531  O O   . ASP A 132 ? 3.14633 3.63678 4.42301 0.30628  -0.21759 -0.35261 134 ASP A O   
532  C CB  . ASP A 132 ? 2.18267 2.67604 3.31414 0.25671  -0.20012 -0.33193 134 ASP A CB  
533  C CG  . ASP A 132 ? 2.17932 2.73838 3.37079 0.25861  -0.18479 -0.36953 134 ASP A CG  
534  O OD1 . ASP A 132 ? 2.17672 2.74609 3.40697 0.27256  -0.17508 -0.39516 134 ASP A OD1 
535  O OD2 . ASP A 132 ? 2.17989 2.78205 3.38103 0.24502  -0.18170 -0.37542 134 ASP A OD2 
536  N N   . THR A 133 ? 2.82299 3.22390 4.01659 0.30379  -0.24341 -0.29665 135 THR A N   
537  C CA  . THR A 133 ? 2.81289 3.21340 4.07379 0.32184  -0.26297 -0.28713 135 THR A CA  
538  C C   . THR A 133 ? 2.80339 3.21147 4.13397 0.34351  -0.25541 -0.31353 135 THR A C   
539  O O   . THR A 133 ? 2.79215 3.22252 4.20352 0.35874  -0.26404 -0.31941 135 THR A O   
540  C CB  . THR A 133 ? 2.82043 3.17213 4.04571 0.32152  -0.28504 -0.24914 135 THR A CB  
541  O OG1 . THR A 133 ? 2.82502 3.13539 4.02586 0.32943  -0.28082 -0.24916 135 THR A OG1 
542  C CG2 . THR A 133 ? 2.83310 3.17390 3.98452 0.29787  -0.28787 -0.22927 135 THR A CG2 
543  N N   . ASN A 134 ? 2.87781 3.26907 4.18242 0.34492  -0.23916 -0.33006 136 ASN A N   
544  C CA  . ASN A 134 ? 2.87010 3.26925 4.23995 0.36316  -0.22910 -0.35966 136 ASN A CA  
545  C C   . ASN A 134 ? 2.86445 3.32752 4.29565 0.36337  -0.21139 -0.40049 136 ASN A C   
546  O O   . ASN A 134 ? 2.87236 3.37024 4.26686 0.34507  -0.19577 -0.41445 136 ASN A O   
547  C CB  . ASN A 134 ? 2.87800 3.25053 4.19901 0.36093  -0.21423 -0.36927 136 ASN A CB  
548  C CG  . ASN A 134 ? 2.87076 3.24676 4.25758 0.37859  -0.20404 -0.39980 136 ASN A CG  
549  O OD1 . ASN A 134 ? 2.87035 3.29042 4.28900 0.37691  -0.18176 -0.44058 136 ASN A OD1 
550  N ND2 . ASN A 134 ? 2.86666 3.19858 4.27568 0.39388  -0.21983 -0.38104 136 ASN A ND2 
551  N N   . PRO A 135 ? 2.68588 3.16781 4.21309 0.38270  -0.21313 -0.42036 137 PRO A N   
552  C CA  . PRO A 135 ? 2.68004 3.22712 4.27329 0.38292  -0.19608 -0.46270 137 PRO A CA  
553  C C   . PRO A 135 ? 2.68503 3.26345 4.28591 0.37847  -0.16629 -0.51039 137 PRO A C   
554  O O   . PRO A 135 ? 2.68117 3.31793 4.34350 0.37828  -0.15009 -0.55145 137 PRO A O   
555  C CB  . PRO A 135 ? 2.66363 3.21168 4.36311 0.40756  -0.21147 -0.46233 137 PRO A CB  
556  C CG  . PRO A 135 ? 2.66300 3.14998 4.35990 0.42140  -0.22478 -0.43832 137 PRO A CG  
557  C CD  . PRO A 135 ? 2.67685 3.12191 4.26114 0.40476  -0.23240 -0.40231 137 PRO A CD  
558  N N   . ASN A 136 ? 2.78910 3.33567 4.33120 0.37366  -0.15817 -0.50769 138 ASN A N   
559  C CA  . ASN A 136 ? 2.79398 3.37446 4.33931 0.36703  -0.13012 -0.55158 138 ASN A CA  
560  C C   . ASN A 136 ? 2.81570 3.40640 4.26453 0.34224  -0.11697 -0.54559 138 ASN A C   
561  O O   . ASN A 136 ? 2.82554 3.47173 4.27601 0.32855  -0.09308 -0.58199 138 ASN A O   
562  C CB  . ASN A 136 ? 2.75784 3.30051 4.33466 0.38429  -0.12833 -0.56164 138 ASN A CB  
563  C CG  . ASN A 136 ? 2.71911 3.26895 4.41269 0.40750  -0.13183 -0.58402 138 ASN A CG  
564  O OD1 . ASN A 136 ? 2.71193 3.31210 4.47131 0.40939  -0.12604 -0.60987 138 ASN A OD1 
565  N ND2 . ASN A 136 ? 2.69429 3.19431 4.41767 0.42516  -0.14125 -0.57401 138 ASN A ND2 
566  N N   . TYR A 137 ? 2.82196 3.36429 4.19039 0.33508  -0.13155 -0.50114 139 TYR A N   
567  C CA  . TYR A 137 ? 2.84040 3.38689 4.12294 0.31347  -0.12034 -0.49155 139 TYR A CA  
568  C C   . TYR A 137 ? 2.84518 3.36550 4.06525 0.30118  -0.13582 -0.44937 139 TYR A C   
569  O O   . TYR A 137 ? 2.83546 3.31588 4.05922 0.31043  -0.15746 -0.42105 139 TYR A O   
570  C CB  . TYR A 137 ? 2.84514 3.35232 4.08845 0.31742  -0.11590 -0.48728 139 TYR A CB  
571  C CG  . TYR A 137 ? 2.83407 3.27180 4.07972 0.33623  -0.13691 -0.45972 139 TYR A CG  
572  C CD1 . TYR A 137 ? 2.83567 3.22417 4.02496 0.33318  -0.15673 -0.41560 139 TYR A CD1 
573  C CD2 . TYR A 137 ? 2.82374 3.24751 4.12882 0.35507  -0.13614 -0.47877 139 TYR A CD2 
574  C CE1 . TYR A 137 ? 2.82927 3.16140 4.01876 0.34716  -0.17585 -0.39055 139 TYR A CE1 
575  C CE2 . TYR A 137 ? 2.81001 3.17344 4.11685 0.37003  -0.15605 -0.45089 139 TYR A CE2 
576  C CZ  . TYR A 137 ? 2.82079 3.14087 4.06797 0.36535  -0.17612 -0.40644 139 TYR A CZ  
577  O OH  . TYR A 137 ? 2.81759 3.08437 4.06497 0.37725  -0.19598 -0.37876 139 TYR A OH  
578  N N   . ASN A 138 ? 2.71522 3.26163 3.87999 0.27853  -0.12412 -0.44558 140 ASN A N   
579  C CA  . ASN A 138 ? 2.72159 3.24158 3.82175 0.26367  -0.13458 -0.40780 140 ASN A CA  
580  C C   . ASN A 138 ? 2.73226 3.20941 3.76341 0.25904  -0.13257 -0.38687 140 ASN A C   
581  O O   . ASN A 138 ? 2.74909 3.25065 3.74152 0.24250  -0.11806 -0.38826 140 ASN A O   
582  C CB  . ASN A 138 ? 2.73302 3.31011 3.82460 0.24114  -0.12377 -0.41484 140 ASN A CB  
583  C CG  . ASN A 138 ? 2.72086 3.32826 3.86741 0.24408  -0.13145 -0.42372 140 ASN A CG  
584  O OD1 . ASN A 138 ? 2.72185 3.32969 3.84534 0.23117  -0.13927 -0.40342 140 ASN A OD1 
585  N ND2 . ASN A 138 ? 2.70857 3.34186 3.93163 0.26107  -0.12902 -0.45463 140 ASN A ND2 
586  N N   . GLU A 139 ? 2.81043 3.22641 3.82792 0.27305  -0.14780 -0.36610 141 GLU A N   
587  C CA  . GLU A 139 ? 2.81847 3.19337 3.77897 0.27203  -0.14598 -0.35012 141 GLU A CA  
588  C C   . GLU A 139 ? 2.82626 3.17156 3.72209 0.25656  -0.15207 -0.31655 141 GLU A C   
589  O O   . GLU A 139 ? 2.82183 3.15870 3.71599 0.25095  -0.16371 -0.30068 141 GLU A O   
590  C CB  . GLU A 139 ? 2.80783 3.13261 3.78203 0.29213  -0.15886 -0.34387 141 GLU A CB  
591  C CG  . GLU A 139 ? 2.79986 3.08362 3.77333 0.29752  -0.18235 -0.31566 141 GLU A CG  
592  C CD  . GLU A 139 ? 2.79468 3.03076 3.77303 0.31358  -0.19496 -0.30534 141 GLU A CD  
593  O OE1 . GLU A 139 ? 2.79773 3.02158 3.76145 0.31830  -0.18531 -0.31492 141 GLU A OE1 
594  O OE2 . GLU A 139 ? 2.78959 3.00380 3.78633 0.32004  -0.21482 -0.28669 141 GLU A OE2 
595  N N   . ARG A 140 ? 2.77322 3.10427 3.61888 0.24928  -0.14359 -0.30657 142 ARG A N   
596  C CA  . ARG A 140 ? 2.78129 3.08264 3.57031 0.23517  -0.14685 -0.27634 142 ARG A CA  
597  C C   . ARG A 140 ? 2.78259 3.02917 3.53310 0.24332  -0.15161 -0.26067 142 ARG A C   
598  O O   . ARG A 140 ? 2.78637 3.03764 3.53429 0.25008  -0.14280 -0.27225 142 ARG A O   
599  C CB  . ARG A 140 ? 2.79805 3.14364 3.56604 0.21501  -0.13104 -0.27561 142 ARG A CB  
600  C CG  . ARG A 140 ? 2.80170 3.14140 3.54485 0.19697  -0.13484 -0.25210 142 ARG A CG  
601  C CD  . ARG A 140 ? 2.79280 3.16021 3.57382 0.19384  -0.14036 -0.26209 142 ARG A CD  
602  N NE  . ARG A 140 ? 2.79676 3.15882 3.55469 0.17503  -0.14322 -0.24116 142 ARG A NE  
603  C CZ  . ARG A 140 ? 2.80746 3.21296 3.55988 0.15490  -0.13264 -0.23925 142 ARG A CZ  
604  N NH1 . ARG A 140 ? 2.81789 3.28102 3.58363 0.14918  -0.11825 -0.25731 142 ARG A NH1 
605  N NH2 . ARG A 140 ? 2.80997 3.20356 3.54386 0.13820  -0.13620 -0.21930 142 ARG A NH2 
606  N N   . THR A 141 ? 2.78863 2.98682 3.51032 0.24139  -0.16471 -0.23666 143 THR A N   
607  C CA  . THR A 141 ? 2.79012 2.93637 3.47665 0.24828  -0.17027 -0.22273 143 THR A CA  
608  C C   . THR A 141 ? 2.79939 2.91360 3.44238 0.23467  -0.17262 -0.19841 143 THR A C   
609  O O   . THR A 141 ? 2.80263 2.92796 3.44594 0.22107  -0.17329 -0.19121 143 THR A O   
610  C CB  . THR A 141 ? 2.78024 2.89602 3.48646 0.26303  -0.18648 -0.22261 143 THR A CB  
611  O OG1 . THR A 141 ? 2.77776 2.89324 3.49937 0.25794  -0.19957 -0.21416 143 THR A OG1 
612  C CG2 . THR A 141 ? 2.77165 2.91138 3.52529 0.27825  -0.18313 -0.24636 143 THR A CG2 
613  N N   . ILE A 142 ? 2.80840 2.88284 3.41689 0.23818  -0.17320 -0.18728 144 ILE A N   
614  C CA  . ILE A 142 ? 2.81920 2.85997 3.39157 0.22677  -0.17378 -0.16685 144 ILE A CA  
615  C C   . ILE A 142 ? 2.82138 2.81462 3.36773 0.23553  -0.17980 -0.16064 144 ILE A C   
616  O O   . ILE A 142 ? 2.81761 2.80912 3.36090 0.24721  -0.17668 -0.16764 144 ILE A O   
617  C CB  . ILE A 142 ? 2.83005 2.89294 3.38749 0.21488  -0.15958 -0.15749 144 ILE A CB  
618  C CG1 . ILE A 142 ? 2.84258 2.86550 3.37059 0.20489  -0.15992 -0.13581 144 ILE A CG1 
619  C CG2 . ILE A 142 ? 2.83280 2.91663 3.38577 0.22261  -0.14935 -0.16487 144 ILE A CG2 
620  C CD1 . ILE A 142 ? 2.85497 2.89744 3.37263 0.19264  -0.14817 -0.11997 144 ILE A CD1 
621  N N   . THR A 143 ? 2.88423 2.84179 3.41266 0.22827  -0.18768 -0.14959 145 THR A N   
622  C CA  . THR A 143 ? 2.89091 2.80536 3.39306 0.23283  -0.19288 -0.14450 145 THR A CA  
623  C C   . THR A 143 ? 2.90442 2.79580 3.38041 0.22433  -0.18411 -0.13191 145 THR A C   
624  O O   . THR A 143 ? 2.91431 2.80628 3.39159 0.21052  -0.18092 -0.12433 145 THR A O   
625  C CB  . THR A 143 ? 2.89862 2.79436 3.40231 0.22893  -0.20804 -0.14373 145 THR A CB  
626  O OG1 . THR A 143 ? 2.88693 2.80545 3.42193 0.23757  -0.21756 -0.15118 145 THR A OG1 
627  C CG2 . THR A 143 ? 2.90918 2.76638 3.38546 0.23173  -0.21290 -0.14085 145 THR A CG2 
628  N N   . ILE A 144 ? 2.83471 2.70593 3.29051 0.23255  -0.18026 -0.12932 146 ILE A N   
629  C CA  . ILE A 144 ? 2.84726 2.69805 3.28442 0.22764  -0.17179 -0.11600 146 ILE A CA  
630  C C   . ILE A 144 ? 2.85704 2.66399 3.27457 0.22934  -0.17713 -0.11675 146 ILE A C   
631  O O   . ILE A 144 ? 2.85089 2.64787 3.25717 0.24048  -0.18041 -0.12271 146 ILE A O   
632  C CB  . ILE A 144 ? 2.84411 2.71664 3.27599 0.23452  -0.16141 -0.11122 146 ILE A CB  
633  C CG1 . ILE A 144 ? 2.83996 2.76420 3.29164 0.22990  -0.15509 -0.11402 146 ILE A CG1 
634  C CG2 . ILE A 144 ? 2.85874 2.71021 3.27646 0.23024  -0.15450 -0.09294 146 ILE A CG2 
635  C CD1 . ILE A 144 ? 2.84959 2.78497 3.30938 0.21365  -0.15151 -0.10100 146 ILE A CD1 
636  N N   . SER A 145 ? 2.78723 2.56997 3.20201 0.21703  -0.17705 -0.11255 147 SER A N   
637  C CA  . SER A 145 ? 2.80232 2.54747 3.20051 0.21612  -0.17935 -0.11622 147 SER A CA  
638  C C   . SER A 145 ? 2.79654 2.52659 3.18310 0.22483  -0.17066 -0.10802 147 SER A C   
639  O O   . SER A 145 ? 2.79313 2.53575 3.18651 0.22470  -0.16202 -0.09419 147 SER A O   
640  C CB  . SER A 145 ? 2.82715 2.55337 3.23048 0.19899  -0.17859 -0.11761 147 SER A CB  
641  O OG  . SER A 145 ? 2.83578 2.55315 3.24783 0.19356  -0.16752 -0.10488 147 SER A OG  
642  N N   . PRO A 146 ? 2.74191 2.44866 3.11149 0.23140  -0.17329 -0.11482 148 PRO A N   
643  C CA  . PRO A 146 ? 2.71495 2.40721 3.07532 0.23960  -0.16530 -0.10693 148 PRO A CA  
644  C C   . PRO A 146 ? 2.72854 2.40027 3.10078 0.23159  -0.15700 -0.09579 148 PRO A C   
645  O O   . PRO A 146 ? 2.71366 2.37975 3.08633 0.23828  -0.15014 -0.08300 148 PRO A O   
646  C CB  . PRO A 146 ? 2.69706 2.36797 3.03823 0.24469  -0.17106 -0.12003 148 PRO A CB  
647  C CG  . PRO A 146 ? 2.72675 2.39500 3.06862 0.23363  -0.18118 -0.13193 148 PRO A CG  
648  C CD  . PRO A 146 ? 2.74565 2.44266 3.10440 0.23077  -0.18434 -0.12833 148 PRO A CD  
649  N N   . PHE A 147 ? 2.74997 2.41153 3.13506 0.21708  -0.15744 -0.09954 149 PHE A N   
650  C CA  . PHE A 147 ? 2.76652 2.40611 3.17021 0.20801  -0.14897 -0.09008 149 PHE A CA  
651  C C   . PHE A 147 ? 2.76922 2.43199 3.18713 0.20740  -0.14332 -0.06609 149 PHE A C   
652  O O   . PHE A 147 ? 2.78925 2.47353 3.21684 0.19770  -0.14415 -0.06283 149 PHE A O   
653  C CB  . PHE A 147 ? 2.78679 2.41386 3.20077 0.19039  -0.15039 -0.10380 149 PHE A CB  
654  C CG  . PHE A 147 ? 2.78941 2.40292 3.18873 0.18637  -0.15645 -0.12697 149 PHE A CG  
655  C CD1 . PHE A 147 ? 2.71395 2.31313 3.09738 0.19672  -0.15700 -0.13387 149 PHE A CD1 
656  C CD2 . PHE A 147 ? 2.85064 2.47057 3.25158 0.17029  -0.16188 -0.14117 149 PHE A CD2 
657  C CE1 . PHE A 147 ? 2.70570 2.29792 3.07449 0.19015  -0.16290 -0.15432 149 PHE A CE1 
658  C CE2 . PHE A 147 ? 2.86733 2.48256 3.25386 0.16331  -0.16819 -0.16049 149 PHE A CE2 
659  C CZ  . PHE A 147 ? 2.79125 2.39291 3.16139 0.17273  -0.16871 -0.16699 149 PHE A CZ  
660  N N   . SER A 148 ? 2.79719 2.45985 3.21662 0.21641  -0.13789 -0.04823 150 SER A N   
661  C CA  . SER A 148 ? 2.80460 2.49428 3.23714 0.21330  -0.13296 -0.02143 150 SER A CA  
662  C C   . SER A 148 ? 2.79948 2.46942 3.24649 0.21735  -0.12702 0.00102  150 SER A C   
663  O O   . SER A 148 ? 2.77769 2.44897 3.21320 0.23034  -0.12655 0.00441  150 SER A O   
664  C CB  . SER A 148 ? 2.77539 2.51202 3.19308 0.22056  -0.13432 -0.01988 150 SER A CB  
665  O OG  . SER A 148 ? 2.79724 2.56909 3.22622 0.21350  -0.12956 0.00491  150 SER A OG  
666  N N   . PRO A 149 ? 2.77284 2.42436 3.24830 0.20657  -0.12256 0.01746  151 PRO A N   
667  C CA  . PRO A 149 ? 2.76961 2.40054 3.26786 0.21123  -0.11765 0.04185  151 PRO A CA  
668  C C   . PRO A 149 ? 2.76690 2.43781 3.26871 0.21277  -0.11678 0.07817  151 PRO A C   
669  O O   . PRO A 149 ? 2.76141 2.42185 3.28139 0.21886  -0.11446 0.10235  151 PRO A O   
670  C CB  . PRO A 149 ? 2.79662 2.39305 3.32945 0.19713  -0.11321 0.04429  151 PRO A CB  
671  C CG  . PRO A 149 ? 2.81629 2.43677 3.34342 0.18262  -0.11550 0.03806  151 PRO A CG  
672  C CD  . PRO A 149 ? 2.80134 2.44663 3.29300 0.18951  -0.12189 0.01299  151 PRO A CD  
673  N N   . LYS A 150 ? 2.85474 2.57464 3.34244 0.20643  -0.11846 0.08276  152 LYS A N   
674  C CA  . LYS A 150 ? 2.85676 2.62608 3.34464 0.20406  -0.11726 0.11462  152 LYS A CA  
675  C C   . LYS A 150 ? 2.84675 2.66424 3.30418 0.20929  -0.11839 0.09760  152 LYS A C   
676  O O   . LYS A 150 ? 2.84151 2.65505 3.28341 0.21277  -0.12089 0.06530  152 LYS A O   
677  C CB  . LYS A 150 ? 2.88036 2.67231 3.38954 0.18500  -0.11590 0.14082  152 LYS A CB  
678  C CG  . LYS A 150 ? 2.89257 2.63654 3.43787 0.17702  -0.11392 0.15588  152 LYS A CG  
679  C CD  . LYS A 150 ? 2.91523 2.68765 3.47946 0.15681  -0.11305 0.18448  152 LYS A CD  
680  C CE  . LYS A 150 ? 2.92898 2.65544 3.52192 0.14490  -0.11064 0.17938  152 LYS A CE  
681  N NZ  . LYS A 150 ? 2.95096 2.70887 3.55737 0.12353  -0.11010 0.20243  152 LYS A NZ  
682  N N   . ASP A 151 ? 2.90800 2.77376 3.36031 0.20870  -0.11642 0.12028  153 ASP A N   
683  C CA  . ASP A 151 ? 2.90476 2.82420 3.33372 0.21075  -0.11502 0.10415  153 ASP A CA  
684  C C   . ASP A 151 ? 2.92662 2.89837 3.36156 0.19298  -0.11292 0.10985  153 ASP A C   
685  O O   . ASP A 151 ? 2.94071 2.95697 3.38297 0.18062  -0.11061 0.14103  153 ASP A O   
686  C CB  . ASP A 151 ? 2.89905 2.84842 3.31794 0.21764  -0.11291 0.12134  153 ASP A CB  
687  C CG  . ASP A 151 ? 2.87305 2.84714 3.26650 0.22740  -0.11124 0.09046  153 ASP A CG  
688  O OD1 . ASP A 151 ? 2.88493 2.89942 3.27309 0.22096  -0.10888 0.07117  153 ASP A OD1 
689  O OD2 . ASP A 151 ? 2.79678 2.74938 3.17850 0.24134  -0.11186 0.08423  153 ASP A OD2 
690  N N   . ILE A 152 ? 2.89337 2.86319 3.32643 0.19072  -0.11418 0.08069  154 ILE A N   
691  C CA  . ILE A 152 ? 2.91375 2.92726 3.35581 0.17389  -0.11227 0.08109  154 ILE A CA  
692  C C   . ILE A 152 ? 2.91638 2.99586 3.34765 0.17286  -0.10778 0.06299  154 ILE A C   
693  O O   . ILE A 152 ? 2.90014 2.97595 3.31964 0.18684  -0.10787 0.03532  154 ILE A O   
694  C CB  . ILE A 152 ? 2.91199 2.89037 3.36215 0.17173  -0.11613 0.05913  154 ILE A CB  
695  C CG1 . ILE A 152 ? 2.90841 2.93623 3.36730 0.15626  -0.11414 0.05300  154 ILE A CG1 
696  C CG2 . ILE A 152 ? 2.89640 2.84340 3.33406 0.18835  -0.12044 0.02526  154 ILE A CG2 
697  C CD1 . ILE A 152 ? 2.89693 2.89842 3.36310 0.15518  -0.11860 0.02922  154 ILE A CD1 
698  N N   . GLU A 153 ? 2.89843 3.04069 3.33587 0.15474  -0.10324 0.07781  155 GLU A N   
699  C CA  . GLU A 153 ? 2.89833 3.11361 3.33001 0.14934  -0.09653 0.05920  155 GLU A CA  
700  C C   . GLU A 153 ? 2.89681 3.15436 3.34233 0.13224  -0.09394 0.04978  155 GLU A C   
701  O O   . GLU A 153 ? 2.90816 3.19385 3.36117 0.11287  -0.09300 0.07890  155 GLU A O   
702  C CB  . GLU A 153 ? 2.91330 3.18172 3.33657 0.14073  -0.09203 0.08709  155 GLU A CB  
703  C CG  . GLU A 153 ? 2.90483 3.13540 3.31644 0.15717  -0.09463 0.09923  155 GLU A CG  
704  C CD  . GLU A 153 ? 2.91082 3.20197 3.31473 0.14793  -0.09080 0.12731  155 GLU A CD  
705  O OE1 . GLU A 153 ? 2.92489 3.27451 3.33549 0.12621  -0.08865 0.15311  155 GLU A OE1 
706  O OE2 . GLU A 153 ? 2.89954 3.18360 3.29034 0.16096  -0.09025 0.12442  155 GLU A OE2 
707  N N   . PHE A 154 ? 2.89185 3.15543 3.34344 0.13898  -0.09312 0.01049  156 PHE A N   
708  C CA  . PHE A 154 ? 2.88813 3.18743 3.35639 0.12549  -0.09116 -0.00344 156 PHE A CA  
709  C C   . PHE A 154 ? 2.88583 3.24736 3.36223 0.12582  -0.08319 -0.04024 156 PHE A C   
710  O O   . PHE A 154 ? 2.87773 3.22076 3.35485 0.14386  -0.08360 -0.06838 156 PHE A O   
711  C CB  . PHE A 154 ? 2.87437 3.11395 3.35214 0.13286  -0.09931 -0.01481 156 PHE A CB  
712  C CG  . PHE A 154 ? 2.85808 3.06736 3.33788 0.15342  -0.10351 -0.04886 156 PHE A CG  
713  C CD1 . PHE A 154 ? 2.85321 3.00773 3.31870 0.17059  -0.10843 -0.04860 156 PHE A CD1 
714  C CD2 . PHE A 154 ? 2.84769 3.08432 3.34688 0.15499  -0.10307 -0.07976 156 PHE A CD2 
715  C CE1 . PHE A 154 ? 2.83790 2.96664 3.30586 0.18740  -0.11342 -0.07620 156 PHE A CE1 
716  C CE2 . PHE A 154 ? 2.83258 3.04158 3.33871 0.17349  -0.10839 -0.10635 156 PHE A CE2 
717  C CZ  . PHE A 154 ? 2.82743 2.98262 3.31670 0.18893  -0.11394 -0.10333 156 PHE A CZ  
718  N N   . PHE A 155 ? 2.87767 3.31449 3.36283 0.10474  -0.07544 -0.04083 157 PHE A N   
719  C CA  . PHE A 155 ? 2.87881 3.38600 3.37582 0.10115  -0.06490 -0.07737 157 PHE A CA  
720  C C   . PHE A 155 ? 2.87250 3.40833 3.39588 0.09388  -0.06301 -0.10336 157 PHE A C   
721  O O   . PHE A 155 ? 2.86987 3.39040 3.39751 0.08424  -0.06826 -0.08634 157 PHE A O   
722  C CB  . PHE A 155 ? 2.89148 3.48091 3.37794 0.07959  -0.05502 -0.06239 157 PHE A CB  
723  C CG  . PHE A 155 ? 2.89711 3.47554 3.36140 0.08736  -0.05498 -0.04455 157 PHE A CG  
724  C CD1 . PHE A 155 ? 2.89317 3.38782 3.34660 0.11048  -0.06379 -0.03641 157 PHE A CD1 
725  C CD2 . PHE A 155 ? 2.90358 3.56158 3.35814 0.06982  -0.04584 -0.03684 157 PHE A CD2 
726  C CE1 . PHE A 155 ? 2.89877 3.38597 3.33327 0.11758  -0.06358 -0.02088 157 PHE A CE1 
727  C CE2 . PHE A 155 ? 2.90714 3.55950 3.34213 0.07646  -0.04608 -0.01976 157 PHE A CE2 
728  C CZ  . PHE A 155 ? 2.90649 3.47179 3.33205 0.10124  -0.05498 -0.01190 157 PHE A CZ  
729  N N   . CYS A 156 ? 2.89690 3.47582 3.44132 0.09843  -0.05478 -0.14622 158 CYS A N   
730  C CA  . CYS A 156 ? 2.89191 3.50667 3.46881 0.09370  -0.05138 -0.17750 158 CYS A CA  
731  C C   . CYS A 156 ? 2.89521 3.57278 3.49679 0.09505  -0.03804 -0.22327 158 CYS A C   
732  O O   . CYS A 156 ? 2.89106 3.53802 3.50096 0.11586  -0.03840 -0.24558 158 CYS A O   
733  C CB  . CYS A 156 ? 2.87526 3.41956 3.46721 0.11324  -0.06371 -0.18592 158 CYS A CB  
734  S SG  . CYS A 156 ? 2.86799 3.36078 3.44869 0.10486  -0.07581 -0.14948 158 CYS A SG  
735  N N   . PHE A 157 ? 2.78728 3.55313 3.40364 0.07231  -0.02572 -0.23982 159 PHE A N   
736  C CA  . PHE A 157 ? 2.78917 3.62278 3.43179 0.07011  -0.01014 -0.28693 159 PHE A CA  
737  C C   . PHE A 157 ? 2.78477 3.65512 3.47440 0.06895  -0.00494 -0.32707 159 PHE A C   
738  O O   . PHE A 157 ? 2.78051 3.62840 3.47863 0.06841  -0.01374 -0.31618 159 PHE A O   
739  C CB  . PHE A 157 ? 2.79416 3.71595 3.41697 0.04193  0.00301  -0.27936 159 PHE A CB  
740  C CG  . PHE A 157 ? 2.79322 3.79734 3.42346 0.01095  0.01017  -0.27814 159 PHE A CG  
741  C CD1 . PHE A 157 ? 2.79530 3.77950 3.40895 -0.00119 -0.00019 -0.23544 159 PHE A CD1 
742  C CD2 . PHE A 157 ? 2.78785 3.89201 3.44306 -0.00784 0.02815  -0.32121 159 PHE A CD2 
743  C CE1 . PHE A 157 ? 2.79400 3.85551 3.41365 -0.03145 0.00607  -0.23283 159 PHE A CE1 
744  C CE2 . PHE A 157 ? 2.78417 3.96969 3.44515 -0.03868 0.03500  -0.32094 159 PHE A CE2 
745  C CZ  . PHE A 157 ? 2.78819 3.95198 3.43011 -0.05055 0.02337  -0.27511 159 PHE A CZ  
746  N N   . CYS A 158 ? 2.70729 3.63631 3.43064 0.06831  0.01025  -0.37566 160 CYS A N   
747  C CA  . CYS A 158 ? 2.70254 3.67517 3.47950 0.06780  0.01781  -0.42015 160 CYS A CA  
748  C C   . CYS A 158 ? 2.70140 3.77921 3.50226 0.04771  0.04056  -0.46512 160 CYS A C   
749  O O   . CYS A 158 ? 2.69929 3.78974 3.50166 0.05216  0.05019  -0.48630 160 CYS A O   
750  C CB  . CYS A 158 ? 2.69151 3.59612 3.50783 0.10103  0.00919  -0.44300 160 CYS A CB  
751  S SG  . CYS A 158 ? 2.68024 3.63138 3.57330 0.10523  0.01648  -0.49593 160 CYS A SG  
752  N N   . MET A 174 ? 2.88070 3.78989 3.57324 0.09553  0.02839  -0.40979 174 MET A N   
753  C CA  . MET A 174 ? 2.89560 3.75955 3.53785 0.09281  0.01428  -0.35098 174 MET A CA  
754  C C   . MET A 174 ? 2.89348 3.65162 3.52113 0.12200  -0.00144 -0.33219 174 MET A C   
755  O O   . MET A 174 ? 2.89087 3.62722 3.52378 0.13734  0.00142  -0.35256 174 MET A O   
756  C CB  . MET A 174 ? 2.89739 3.82380 3.50384 0.06968  0.02285  -0.33018 174 MET A CB  
757  C CG  . MET A 174 ? 2.90220 3.76957 3.46318 0.07487  0.00898  -0.27394 174 MET A CG  
758  S SD  . MET A 174 ? 2.90496 3.71692 3.45292 0.07269  -0.00821 -0.22426 174 MET A SD  
759  C CE  . MET A 174 ? 2.90513 3.81755 3.43663 0.03281  -0.00078 -0.19411 174 MET A CE  
760  N N   . VAL A 175 ? 2.96329 3.65858 3.57345 0.12776  -0.01737 -0.29472 175 VAL A N   
761  C CA  . VAL A 175 ? 2.95416 3.55237 3.55092 0.15235  -0.03282 -0.27714 175 VAL A CA  
762  C C   . VAL A 175 ? 2.95797 3.52138 3.51364 0.14576  -0.04210 -0.22582 175 VAL A C   
763  O O   . VAL A 175 ? 2.95410 3.49499 3.50749 0.14019  -0.05034 -0.20320 175 VAL A O   
764  C CB  . VAL A 175 ? 2.93740 3.48909 3.56507 0.16788  -0.04348 -0.28997 175 VAL A CB  
765  C CG1 . VAL A 175 ? 2.92196 3.38536 3.53777 0.19142  -0.05775 -0.27844 175 VAL A CG1 
766  C CG2 . VAL A 175 ? 2.93304 3.53237 3.61219 0.17046  -0.03330 -0.33855 175 VAL A CG2 
767  N N   . HIS A 176 ? 2.99367 3.55195 3.52018 0.14652  -0.04059 -0.20777 176 HIS A N   
768  C CA  . HIS A 176 ? 2.99642 3.51737 3.49085 0.14333  -0.04927 -0.15972 176 HIS A CA  
769  C C   . HIS A 176 ? 2.98721 3.41894 3.46809 0.16720  -0.06070 -0.15186 176 HIS A C   
770  O O   . HIS A 176 ? 2.98405 3.40135 3.46551 0.18176  -0.05884 -0.17429 176 HIS A O   
771  C CB  . HIS A 176 ? 3.00749 3.58824 3.48046 0.12641  -0.04101 -0.13922 176 HIS A CB  
772  C CG  . HIS A 176 ? 3.00955 3.60059 3.47379 0.13578  -0.03431 -0.15857 176 HIS A CG  
773  N ND1 . HIS A 176 ? 3.00883 3.53627 3.45257 0.15393  -0.04178 -0.14398 176 HIS A ND1 
774  C CD2 . HIS A 176 ? 3.01078 3.67048 3.48521 0.12817  -0.01989 -0.19355 176 HIS A CD2 
775  C CE1 . HIS A 176 ? 3.01112 3.56628 3.45108 0.15738  -0.03294 -0.16719 176 HIS A CE1 
776  N NE2 . HIS A 176 ? 3.01180 3.64661 3.47079 0.14179  -0.01924 -0.19809 176 HIS A NE2 
777  N N   . VAL A 177 ? 2.93702 3.31096 3.40740 0.16960  -0.07187 -0.12173 177 VAL A N   
778  C CA  . VAL A 177 ? 2.92506 3.21683 3.38378 0.18905  -0.08280 -0.11550 177 VAL A CA  
779  C C   . VAL A 177 ? 2.93146 3.18999 3.36957 0.18498  -0.08766 -0.07405 177 VAL A C   
780  O O   . VAL A 177 ? 2.93394 3.19087 3.37651 0.17237  -0.09012 -0.05162 177 VAL A O   
781  C CB  . VAL A 177 ? 2.90661 3.15462 3.38304 0.19765  -0.09226 -0.12971 177 VAL A CB  
782  C CG1 . VAL A 177 ? 2.89317 3.06816 3.35744 0.21604  -0.10253 -0.12937 177 VAL A CG1 
783  C CG2 . VAL A 177 ? 2.90124 3.19028 3.40898 0.19910  -0.08745 -0.16660 177 VAL A CG2 
784  N N   . ARG A 178 ? 2.93998 3.17137 3.35920 0.19565  -0.08885 -0.06437 178 ARG A N   
785  C CA  . ARG A 178 ? 2.94499 3.13398 3.35140 0.19638  -0.09417 -0.02851 178 ARG A CA  
786  C C   . ARG A 178 ? 2.92312 3.03718 3.32168 0.21504  -0.10244 -0.03765 178 ARG A C   
787  O O   . ARG A 178 ? 2.90565 3.01029 3.29336 0.22777  -0.10192 -0.05348 178 ARG A O   
788  C CB  . ARG A 178 ? 2.95310 3.18118 3.34630 0.19073  -0.08869 -0.00457 178 ARG A CB  
789  C CG  . ARG A 178 ? 2.96004 3.21402 3.34154 0.19928  -0.08272 -0.02703 178 ARG A CG  
790  C CD  . ARG A 178 ? 2.96173 3.24991 3.32902 0.19353  -0.07921 0.00215  178 ARG A CD  
791  N NE  . ARG A 178 ? 2.91291 3.21450 3.26642 0.20321  -0.07427 -0.01847 178 ARG A NE  
792  C CZ  . ARG A 178 ? 2.79043 3.12838 3.13026 0.19941  -0.07050 0.00005  178 ARG A CZ  
793  N NH1 . ARG A 178 ? 2.85455 3.22076 3.19446 0.18656  -0.07201 0.04267  178 ARG A NH1 
794  N NH2 . ARG A 178 ? 2.65947 3.00716 2.98711 0.20801  -0.06554 -0.02313 178 ARG A NH2 
795  N N   . VAL A 179 ? 2.90102 2.96556 3.30533 0.21460  -0.10956 -0.02917 179 VAL A N   
796  C CA  . VAL A 179 ? 2.87712 2.87603 3.27428 0.22807  -0.11734 -0.03830 179 VAL A CA  
797  C C   . VAL A 179 ? 2.86446 2.83294 3.24965 0.23345  -0.11732 -0.01621 179 VAL A C   
798  O O   . VAL A 179 ? 2.87537 2.83527 3.26817 0.22543  -0.11660 0.01152  179 VAL A O   
799  C CB  . VAL A 179 ? 2.88369 2.84856 3.29268 0.22260  -0.12378 -0.04061 179 VAL A CB  
800  C CG1 . VAL A 179 ? 2.86369 2.76761 3.26387 0.23262  -0.13124 -0.04913 179 VAL A CG1 
801  C CG2 . VAL A 179 ? 2.87710 2.87357 3.30130 0.21894  -0.12467 -0.06246 179 VAL A CG2 
802  N N   . LEU A 180 ? 2.95125 2.90378 3.32115 0.24698  -0.11810 -0.02807 180 LEU A N   
803  C CA  . LEU A 180 ? 2.93786 2.86257 3.29813 0.25381  -0.11810 -0.01052 180 LEU A CA  
804  C C   . LEU A 180 ? 2.92454 2.78472 3.28683 0.25794  -0.12423 -0.01340 180 LEU A C   
805  O O   . LEU A 180 ? 2.92103 2.75900 3.28518 0.25745  -0.12954 -0.03274 180 LEU A O   
806  C CB  . LEU A 180 ? 2.91277 2.85007 3.25499 0.26514  -0.11573 -0.02337 180 LEU A CB  
807  C CG  . LEU A 180 ? 2.93498 2.93384 3.27235 0.26043  -0.10778 -0.01150 180 LEU A CG  
808  C CD1 . LEU A 180 ? 2.95801 3.01543 3.30497 0.24892  -0.10239 -0.02343 180 LEU A CD1 
809  C CD2 . LEU A 180 ? 2.88988 2.89068 3.20876 0.27196  -0.10569 -0.02489 180 LEU A CD2 
810  N N   . LYS A 181 ? 3.17438 3.00825 3.53896 0.26109  -0.12324 0.00580  181 LYS A N   
811  C CA  . LYS A 181 ? 3.16523 2.94166 3.53490 0.26371  -0.12661 0.00046  181 LYS A CA  
812  C C   . LYS A 181 ? 3.13568 2.88869 3.48590 0.27662  -0.12890 -0.01798 181 LYS A C   
813  O O   . LYS A 181 ? 3.12323 2.89612 3.46114 0.28472  -0.12631 -0.01391 181 LYS A O   
814  C CB  . LYS A 181 ? 2.30827 2.06667 2.70006 0.25993  -0.12343 0.02957  181 LYS A CB  
815  C CG  . LYS A 181 ? 2.31506 2.01664 2.71998 0.25963  -0.12444 0.02012  181 LYS A CG  
816  C CD  . LYS A 181 ? 2.33335 2.01648 2.76979 0.25634  -0.12040 0.04914  181 LYS A CD  
817  C CE  . LYS A 181 ? 2.34399 1.97370 2.80029 0.25257  -0.11912 0.03429  181 LYS A CE  
818  N NZ  . LYS A 181 ? 2.33874 1.94129 2.77884 0.26224  -0.12027 0.00627  181 LYS A NZ  
819  N N   . TYR A 182 ? 2.68694 2.40168 3.03386 0.27654  -0.13374 -0.03817 182 TYR A N   
820  C CA  . TYR A 182 ? 2.65910 2.35228 2.98690 0.28585  -0.13677 -0.05637 182 TYR A CA  
821  C C   . TYR A 182 ? 2.65162 2.32080 2.98449 0.29173  -0.13264 -0.04601 182 TYR A C   
822  O O   . TYR A 182 ? 2.66712 2.30691 3.01985 0.28647  -0.13076 -0.04193 182 TYR A O   
823  C CB  . TYR A 182 ? 2.66136 2.32857 2.98494 0.28024  -0.14386 -0.07883 182 TYR A CB  
824  C CG  . TYR A 182 ? 2.63410 2.28889 2.93550 0.28688  -0.14898 -0.09779 182 TYR A CG  
825  C CD1 . TYR A 182 ? 2.60819 2.28160 2.89385 0.29740  -0.14792 -0.09906 182 TYR A CD1 
826  C CD2 . TYR A 182 ? 2.63922 2.26718 2.93542 0.28040  -0.15466 -0.11455 182 TYR A CD2 
827  C CE1 . TYR A 182 ? 2.58213 2.24384 2.84816 0.30216  -0.15280 -0.11499 182 TYR A CE1 
828  C CE2 . TYR A 182 ? 2.61776 2.23792 2.89314 0.28403  -0.16013 -0.12943 182 TYR A CE2 
829  C CZ  . TYR A 182 ? 2.58698 2.22208 2.84766 0.29537  -0.15940 -0.12884 182 TYR A CZ  
830  O OH  . TYR A 182 ? 2.56550 2.19245 2.80603 0.29776  -0.16504 -0.14239 182 TYR A OH  
831  N N   . PRO A 183 ? 2.67077 2.35218 2.98985 0.30230  -0.13058 -0.04276 183 PRO A N   
832  C CA  . PRO A 183 ? 2.66585 2.32823 2.99501 0.30904  -0.12669 -0.03069 183 PRO A CA  
833  C C   . PRO A 183 ? 2.65301 2.27268 2.98111 0.31015  -0.12799 -0.05247 183 PRO A C   
834  O O   . PRO A 183 ? 2.65552 2.25394 3.00255 0.31412  -0.12384 -0.04537 183 PRO A O   
835  C CB  . PRO A 183 ? 2.64934 2.34425 2.96006 0.31875  -0.12472 -0.02451 183 PRO A CB  
836  C CG  . PRO A 183 ? 2.63280 2.34556 2.91993 0.31834  -0.12811 -0.04658 183 PRO A CG  
837  C CD  . PRO A 183 ? 2.65379 2.37079 2.95223 0.30800  -0.13063 -0.04904 183 PRO A CD  
838  N N   . HIS A 184 ? 2.67596 2.28551 2.98570 0.30584  -0.13359 -0.07819 184 HIS A N   
839  C CA  . HIS A 184 ? 2.66797 2.24692 2.97155 0.30418  -0.13499 -0.10076 184 HIS A CA  
840  C C   . HIS A 184 ? 2.69703 2.24929 3.02338 0.29167  -0.13347 -0.10917 184 HIS A C   
841  O O   . HIS A 184 ? 2.72099 2.27774 3.06143 0.28320  -0.13382 -0.10128 184 HIS A O   
842  C CB  . HIS A 184 ? 2.65002 2.23511 2.92351 0.30296  -0.14293 -0.12140 184 HIS A CB  
843  C CG  . HIS A 184 ? 2.62103 2.22863 2.87365 0.31403  -0.14325 -0.11867 184 HIS A CG  
844  N ND1 . HIS A 184 ? 2.60809 2.22701 2.84008 0.31417  -0.14999 -0.13109 184 HIS A ND1 
845  C CD2 . HIS A 184 ? 2.60889 2.23135 2.86046 0.32437  -0.13748 -0.10494 184 HIS A CD2 
846  C CE1 . HIS A 184 ? 2.55610 2.19421 2.77510 0.32370  -0.14714 -0.12796 184 HIS A CE1 
847  N NE2 . HIS A 184 ? 2.55658 2.19949 2.78506 0.32956  -0.13964 -0.11231 184 HIS A NE2 
848  N N   . ASN A 185 ? 2.69390 2.22077 3.02460 0.28928  -0.13087 -0.12777 185 ASN A N   
849  C CA  . ASN A 185 ? 2.72400 2.22783 3.07559 0.27490  -0.12805 -0.14352 185 ASN A CA  
850  C C   . ASN A 185 ? 2.74004 2.25268 3.07139 0.26108  -0.13659 -0.16103 185 ASN A C   
851  O O   . ASN A 185 ? 2.72056 2.24848 3.02243 0.26321  -0.14480 -0.16720 185 ASN A O   
852  C CB  . ASN A 185 ? 2.27748 1.75770 2.64073 0.27478  -0.12166 -0.16375 185 ASN A CB  
853  C CG  . ASN A 185 ? 2.29094 1.76182 2.68168 0.28932  -0.11388 -0.14492 185 ASN A CG  
854  O OD1 . ASN A 185 ? 2.27597 1.76191 2.67227 0.29866  -0.11418 -0.11452 185 ASN A OD1 
855  N ND2 . ASN A 185 ? 2.33287 1.78281 2.74300 0.29038  -0.10697 -0.16291 185 ASN A ND2 
856  N N   . ILE A 186 ? 2.44370 1.94764 2.79391 0.24621  -0.13489 -0.16777 186 ILE A N   
857  C CA  . ILE A 186 ? 2.46843 1.98427 2.80456 0.23117  -0.14331 -0.18156 186 ILE A CA  
858  C C   . ILE A 186 ? 2.49942 2.00028 2.84555 0.21320  -0.13924 -0.20893 186 ILE A C   
859  O O   . ILE A 186 ? 2.51554 1.99650 2.89384 0.20780  -0.12880 -0.21256 186 ILE A O   
860  C CB  . ILE A 186 ? 2.48888 2.01863 2.83645 0.22700  -0.14550 -0.16526 186 ILE A CB  
861  C CG1 . ILE A 186 ? 2.45925 2.01202 2.79577 0.24202  -0.14901 -0.14404 186 ILE A CG1 
862  C CG2 . ILE A 186 ? 2.52307 2.06525 2.86210 0.21032  -0.15401 -0.17948 186 ILE A CG2 
863  C CD1 . ILE A 186 ? 2.47615 2.04909 2.82295 0.23751  -0.15112 -0.13085 186 ILE A CD1 
864  N N   . LEU A 187 ? 2.42826 1.94111 2.74930 0.20249  -0.14724 -0.22818 187 LEU A N   
865  C CA  . LEU A 187 ? 2.46171 1.97108 2.78689 0.18154  -0.14388 -0.25802 187 LEU A CA  
866  C C   . LEU A 187 ? 2.51050 2.04255 2.82602 0.16253  -0.15376 -0.26257 187 LEU A C   
867  O O   . LEU A 187 ? 2.51549 2.06951 2.80386 0.15956  -0.16704 -0.26075 187 LEU A O   
868  C CB  . LEU A 187 ? 2.44454 1.95669 2.74769 0.18121  -0.14529 -0.27618 187 LEU A CB  
869  C CG  . LEU A 187 ? 2.39591 1.89400 2.70023 0.20333  -0.13953 -0.26688 187 LEU A CG  
870  C CD1 . LEU A 187 ? 2.38072 1.88634 2.65915 0.20075  -0.14233 -0.28574 187 LEU A CD1 
871  C CD2 . LEU A 187 ? 2.39241 1.86405 2.73850 0.20913  -0.12457 -0.26693 187 LEU A CD2 
872  N N   . PHE A 188 ? 2.52783 2.05538 2.86819 0.14932  -0.14762 -0.26706 188 PHE A N   
873  C CA  . PHE A 188 ? 2.57065 2.12198 2.90612 0.13074  -0.15613 -0.26999 188 PHE A CA  
874  C C   . PHE A 188 ? 2.60959 2.17123 2.94367 0.10364  -0.15341 -0.30261 188 PHE A C   
875  O O   . PHE A 188 ? 2.61763 2.16111 2.97759 0.09408  -0.13870 -0.32342 188 PHE A O   
876  C CB  . PHE A 188 ? 2.58594 2.13127 2.94794 0.12995  -0.15089 -0.25622 188 PHE A CB  
877  C CG  . PHE A 188 ? 2.62734 2.20037 2.98470 0.11417  -0.16063 -0.25503 188 PHE A CG  
878  C CD1 . PHE A 188 ? 2.63977 2.24170 2.97135 0.11165  -0.17680 -0.25153 188 PHE A CD1 
879  C CD2 . PHE A 188 ? 2.65662 2.22757 3.03836 0.10149  -0.15402 -0.25604 188 PHE A CD2 
880  C CE1 . PHE A 188 ? 2.68146 2.31142 3.01306 0.09791  -0.18674 -0.24816 188 PHE A CE1 
881  C CE2 . PHE A 188 ? 2.69580 2.29530 3.07405 0.08683  -0.16308 -0.25501 188 PHE A CE2 
882  C CZ  . PHE A 188 ? 2.70861 2.33853 3.06244 0.08556  -0.17973 -0.25067 188 PHE A CZ  
883  N N   . THR A 189 ? 2.51690 2.11023 2.82398 0.09013  -0.16739 -0.30695 189 THR A N   
884  C CA  . THR A 189 ? 2.55612 2.17230 2.85639 0.06017  -0.16709 -0.33665 189 THR A CA  
885  C C   . THR A 189 ? 2.60685 2.25363 2.90708 0.04082  -0.17651 -0.33244 189 THR A C   
886  O O   . THR A 189 ? 2.62922 2.30783 2.90764 0.03491  -0.19395 -0.32025 189 THR A O   
887  C CB  . THR A 189 ? 2.54870 2.18392 2.81704 0.05641  -0.17690 -0.34272 189 THR A CB  
888  O OG1 . THR A 189 ? 2.49949 2.10720 2.76801 0.07687  -0.16857 -0.34410 189 THR A OG1 
889  C CG2 . THR A 189 ? 2.58227 2.24689 2.84412 0.02219  -0.17464 -0.37605 189 THR A CG2 
890  N N   . ASN A 190 ? 2.74676 2.38448 3.07445 0.03053  -0.16516 -0.34153 190 ASN A N   
891  C CA  . ASN A 190 ? 2.79180 2.45718 3.12310 0.01366  -0.17243 -0.33653 190 ASN A CA  
892  C C   . ASN A 190 ? 2.83152 2.53291 3.15484 -0.02211 -0.17297 -0.36617 190 ASN A C   
893  O O   . ASN A 190 ? 2.83217 2.52538 3.17403 -0.03999 -0.15629 -0.39821 190 ASN A O   
894  C CB  . ASN A 190 ? 2.79489 2.43548 3.15848 0.01832  -0.16001 -0.33107 190 ASN A CB  
895  C CG  . ASN A 190 ? 2.83653 2.49919 3.21356 -0.01046 -0.15694 -0.34665 190 ASN A CG  
896  O OD1 . ASN A 190 ? 2.87157 2.57329 3.23476 -0.02428 -0.17069 -0.34101 190 ASN A OD1 
897  N ND2 . ASN A 190 ? 2.83175 2.46852 3.23987 -0.01930 -0.13824 -0.36587 190 ASN A ND2 
898  N N   . LEU A 191 ? 2.77401 2.51786 3.07235 -0.03326 -0.19216 -0.35527 191 LEU A N   
899  C CA  . LEU A 191 ? 2.80991 2.60077 3.09582 -0.06981 -0.19653 -0.37765 191 LEU A CA  
900  C C   . LEU A 191 ? 2.85417 2.68423 3.13999 -0.08332 -0.21105 -0.36070 191 LEU A C   
901  O O   . LEU A 191 ? 2.87584 2.75253 3.14177 -0.09984 -0.22896 -0.35168 191 LEU A O   
902  C CB  . LEU A 191 ? 2.80132 2.61529 3.05650 -0.07475 -0.20841 -0.37757 191 LEU A CB  
903  C CG  . LEU A 191 ? 2.75596 2.53686 3.00822 -0.06106 -0.19609 -0.39348 191 LEU A CG  
904  C CD1 . LEU A 191 ? 2.74886 2.55420 2.96812 -0.06322 -0.21145 -0.38491 191 LEU A CD1 
905  C CD2 . LEU A 191 ? 2.75135 2.52736 3.02272 -0.08312 -0.17396 -0.43842 191 LEU A CD2 
906  N N   . THR A 192 ? 2.97045 2.78411 3.27986 -0.07658 -0.20432 -0.35394 192 THR A N   
907  C CA  . THR A 192 ? 2.98732 2.83660 3.30059 -0.08683 -0.21699 -0.33769 192 THR A CA  
908  C C   . THR A 192 ? 3.00182 2.84671 3.33982 -0.10512 -0.20053 -0.35861 192 THR A C   
909  O O   . THR A 192 ? 2.99438 2.80053 3.35152 -0.10340 -0.18000 -0.37922 192 THR A O   
910  C CB  . THR A 192 ? 2.96416 2.80268 3.28125 -0.05491 -0.22978 -0.29980 192 THR A CB  
911  O OG1 . THR A 192 ? 2.98206 2.85980 3.30594 -0.06560 -0.24288 -0.28536 192 THR A OG1 
912  C CG2 . THR A 192 ? 2.93142 2.72058 3.26872 -0.03050 -0.21403 -0.29549 192 THR A CG2 
913  N N   . ASN A 193 ? 3.09303 2.97875 3.43363 -0.12282 -0.21013 -0.35189 193 ASN A N   
914  C CA  . ASN A 193 ? 3.11050 2.99886 3.47328 -0.14433 -0.19560 -0.37235 193 ASN A CA  
915  C C   . ASN A 193 ? 3.09138 2.93230 3.47919 -0.12056 -0.18408 -0.35972 193 ASN A C   
916  O O   . ASN A 193 ? 3.09743 2.91455 3.50908 -0.13159 -0.16484 -0.38062 193 ASN A O   
917  C CB  . ASN A 193 ? 3.13279 3.08151 3.49083 -0.16826 -0.21055 -0.36501 193 ASN A CB  
918  C CG  . ASN A 193 ? 3.11961 3.08218 3.47470 -0.14421 -0.23228 -0.32360 193 ASN A CG  
919  O OD1 . ASN A 193 ? 3.10552 3.06523 3.44677 -0.12422 -0.24593 -0.30289 193 ASN A OD1 
920  N ND2 . ASN A 193 ? 3.12427 3.10175 3.49564 -0.14611 -0.23467 -0.31294 193 ASN A ND2 
921  N N   . ASP A 194 ? 3.11107 2.94030 3.49621 -0.08964 -0.19527 -0.32599 194 ASP A N   
922  C CA  . ASP A 194 ? 3.08533 2.88100 3.49185 -0.06991 -0.18639 -0.31082 194 ASP A CA  
923  C C   . ASP A 194 ? 3.06585 2.80843 3.48697 -0.05898 -0.16703 -0.32157 194 ASP A C   
924  O O   . ASP A 194 ? 3.04424 2.76573 3.45450 -0.04068 -0.16748 -0.31790 194 ASP A O   
925  C CB  . ASP A 194 ? 3.05069 2.85079 3.45111 -0.04039 -0.20158 -0.27681 194 ASP A CB  
926  C CG  . ASP A 194 ? 3.06799 2.91745 3.46681 -0.04832 -0.21959 -0.26301 194 ASP A CG  
927  O OD1 . ASP A 194 ? 3.10229 2.97897 3.50819 -0.07471 -0.21793 -0.27546 194 ASP A OD1 
928  O OD2 . ASP A 194 ? 3.04401 2.90588 3.43775 -0.02832 -0.23511 -0.24012 194 ASP A OD2 
929  N N   . LEU A 195 ? 3.06218 2.78395 3.51075 -0.07054 -0.15036 -0.33369 195 LEU A N   
930  C CA  . LEU A 195 ? 3.04697 2.71764 3.51951 -0.06057 -0.13206 -0.34001 195 LEU A CA  
931  C C   . LEU A 195 ? 3.00202 2.64883 3.47547 -0.02734 -0.13546 -0.30526 195 LEU A C   
932  O O   . LEU A 195 ? 2.98856 2.63481 3.47478 -0.02235 -0.13505 -0.28558 195 LEU A O   
933  C CB  . LEU A 195 ? 3.07020 2.72660 3.57698 -0.08244 -0.11484 -0.35791 195 LEU A CB  
934  C CG  . LEU A 195 ? 3.11077 2.79522 3.62063 -0.11958 -0.10846 -0.39681 195 LEU A CG  
935  C CD1 . LEU A 195 ? 3.12854 2.79346 3.67736 -0.13891 -0.08998 -0.41287 195 LEU A CD1 
936  C CD2 . LEU A 195 ? 3.11426 2.79565 3.61752 -0.12679 -0.10260 -0.42668 195 LEU A CD2 
937  N N   . PHE A 196 ? 3.03044 2.66166 3.48974 -0.00628 -0.13845 -0.29858 196 PHE A N   
938  C CA  . PHE A 196 ? 2.98547 2.60132 3.44217 0.02385  -0.14197 -0.26763 196 PHE A CA  
939  C C   . PHE A 196 ? 2.97533 2.54786 3.46118 0.03250  -0.12564 -0.26336 196 PHE A C   
940  O O   . PHE A 196 ? 2.95073 2.49904 3.43782 0.04492  -0.12047 -0.26671 196 PHE A O   
941  C CB  . PHE A 196 ? 2.96542 2.59015 3.39264 0.04100  -0.15407 -0.26158 196 PHE A CB  
942  C CG  . PHE A 196 ? 2.96835 2.63415 3.37440 0.03864  -0.17249 -0.25375 196 PHE A CG  
943  C CD1 . PHE A 196 ? 2.96727 2.65701 3.38172 0.03429  -0.17826 -0.24161 196 PHE A CD1 
944  C CD2 . PHE A 196 ? 2.97347 2.65505 3.35463 0.04038  -0.18442 -0.25726 196 PHE A CD2 
945  C CE1 . PHE A 196 ? 2.97001 2.69772 3.37232 0.03353  -0.19569 -0.23292 196 PHE A CE1 
946  C CE2 . PHE A 196 ? 2.97947 2.69805 3.34792 0.03866  -0.20252 -0.24610 196 PHE A CE2 
947  C CZ  . PHE A 196 ? 2.97754 2.71880 3.35855 0.03601  -0.20820 -0.23393 196 PHE A CZ  
948  N N   . THR A 197 ? 2.97940 2.54384 3.49136 0.02540  -0.11806 -0.25377 197 THR A N   
949  C CA  . THR A 197 ? 2.97679 2.50185 3.52431 0.03000  -0.10335 -0.24535 197 THR A CA  
950  C C   . THR A 197 ? 2.93615 2.45489 3.48341 0.05509  -0.10631 -0.20824 197 THR A C   
951  O O   . THR A 197 ? 2.92916 2.42093 3.50746 0.05889  -0.09650 -0.19234 197 THR A O   
952  C CB  . THR A 197 ? 3.00450 2.52436 3.58306 0.00722  -0.09350 -0.25158 197 THR A CB  
953  O OG1 . THR A 197 ? 2.99063 2.53818 3.56051 0.00736  -0.10187 -0.22876 197 THR A OG1 
954  C CG2 . THR A 197 ? 3.04479 2.57808 3.62341 -0.02091 -0.08958 -0.29088 197 THR A CG2 
955  N N   . TYR A 198 ? 2.99841 2.54376 3.51439 0.07094  -0.11940 -0.19381 198 TYR A N   
956  C CA  . TYR A 198 ? 2.96308 2.51001 3.47813 0.09190  -0.12106 -0.16193 198 TYR A CA  
957  C C   . TYR A 198 ? 2.93263 2.45116 3.45325 0.10851  -0.11541 -0.15643 198 TYR A C   
958  O O   . TYR A 198 ? 2.91702 2.42297 3.45733 0.11757  -0.10987 -0.13138 198 TYR A O   
959  C CB  . TYR A 198 ? 2.93301 2.51729 3.41860 0.10331  -0.13475 -0.15280 198 TYR A CB  
960  C CG  . TYR A 198 ? 2.93707 2.53576 3.39595 0.10313  -0.14539 -0.17237 198 TYR A CG  
961  C CD1 . TYR A 198 ? 2.93133 2.51596 3.37502 0.11416  -0.14643 -0.18030 198 TYR A CD1 
962  C CD2 . TYR A 198 ? 2.94563 2.57526 3.39568 0.09161  -0.15542 -0.18009 198 TYR A CD2 
963  C CE1 . TYR A 198 ? 2.93875 2.53889 3.35832 0.11199  -0.15707 -0.19486 198 TYR A CE1 
964  C CE2 . TYR A 198 ? 2.95364 2.59951 3.38199 0.09031  -0.16693 -0.19253 198 TYR A CE2 
965  C CZ  . TYR A 198 ? 2.95107 2.58192 3.36364 0.09990  -0.16778 -0.19936 198 TYR A CZ  
966  O OH  . TYR A 198 ? 2.96237 2.61129 3.35356 0.09662  -0.18003 -0.20885 198 TYR A OH  
967  N N   . LEU A 199 ? 2.96373 2.47525 3.46822 0.11159  -0.11719 -0.17813 199 LEU A N   
968  C CA  . LEU A 199 ? 2.93549 2.42062 3.44738 0.12568  -0.11112 -0.17786 199 LEU A CA  
969  C C   . LEU A 199 ? 2.95816 2.41481 3.49767 0.11093  -0.09921 -0.20665 199 LEU A C   
970  O O   . LEU A 199 ? 2.98127 2.44819 3.50842 0.09451  -0.10056 -0.23712 199 LEU A O   
971  C CB  . LEU A 199 ? 2.90224 2.40130 3.37754 0.14001  -0.12060 -0.18255 199 LEU A CB  
972  C CG  . LEU A 199 ? 2.86257 2.38056 3.31980 0.16044  -0.12762 -0.15491 199 LEU A CG  
973  C CD1 . LEU A 199 ? 2.82310 2.34570 3.25106 0.17394  -0.13387 -0.16249 199 LEU A CD1 
974  C CD2 . LEU A 199 ? 2.84736 2.35303 3.32997 0.17028  -0.11982 -0.12667 199 LEU A CD2 
975  N N   . PRO A 200 ? 2.88605 2.30995 3.46603 0.11496  -0.08736 -0.19850 200 PRO A N   
976  C CA  . PRO A 200 ? 2.90754 2.30306 3.52364 0.10033  -0.07366 -0.22967 200 PRO A CA  
977  C C   . PRO A 200 ? 2.89725 2.29381 3.49649 0.09903  -0.07273 -0.26411 200 PRO A C   
978  O O   . PRO A 200 ? 2.92725 2.33544 3.52030 0.07735  -0.07051 -0.29880 200 PRO A O   
979  C CB  . PRO A 200 ? 2.89331 2.25455 3.55771 0.11239  -0.06396 -0.20510 200 PRO A CB  
980  C CG  . PRO A 200 ? 2.88534 2.26331 3.54139 0.12129  -0.07177 -0.16145 200 PRO A CG  
981  C CD  . PRO A 200 ? 2.86549 2.28079 3.46582 0.12991  -0.08585 -0.15874 200 PRO A CD  
982  N N   . LYS A 201 ? 2.88140 2.27053 3.47227 0.12002  -0.07442 -0.25525 201 LYS A N   
983  C CA  . LYS A 201 ? 2.86950 2.25962 3.44697 0.11841  -0.07249 -0.28774 201 LYS A CA  
984  C C   . LYS A 201 ? 2.87783 2.30515 3.40171 0.11048  -0.08640 -0.29920 201 LYS A C   
985  O O   . LYS A 201 ? 2.86299 2.31037 3.35543 0.12192  -0.09938 -0.27374 201 LYS A O   
986  C CB  . LYS A 201 ? 2.82575 2.20053 3.40814 0.14351  -0.07127 -0.27257 201 LYS A CB  
987  C CG  . LYS A 201 ? 2.82163 2.15899 3.46470 0.15043  -0.05715 -0.26660 201 LYS A CG  
988  C CD  . LYS A 201 ? 2.78474 2.11161 3.43270 0.17162  -0.05535 -0.26294 201 LYS A CD  
989  C CE  . LYS A 201 ? 2.78584 2.07515 3.50272 0.17652  -0.04054 -0.26468 201 LYS A CE  
990  N NZ  . LYS A 201 ? 2.75397 2.03596 3.47799 0.19413  -0.03763 -0.27123 201 LYS A NZ  
991  N N   . THR A 202 ? 2.76989 2.20891 3.28655 0.08978  -0.08355 -0.33762 202 THR A N   
992  C CA  . THR A 202 ? 2.78130 2.25815 3.25107 0.07917  -0.09768 -0.34687 202 THR A CA  
993  C C   . THR A 202 ? 2.78590 2.27281 3.25033 0.06143  -0.09218 -0.38783 202 THR A C   
994  O O   . THR A 202 ? 2.78738 2.25417 3.28847 0.05311  -0.07574 -0.41542 202 THR A O   
995  C CB  . THR A 202 ? 2.82337 2.32584 3.28477 0.06078  -0.10499 -0.34376 202 THR A CB  
996  O OG1 . THR A 202 ? 2.83148 2.37150 3.25040 0.05451  -0.12157 -0.34378 202 THR A OG1 
997  C CG2 . THR A 202 ? 2.86492 2.36562 3.35602 0.03221  -0.09163 -0.37734 202 THR A CG2 
998  N N   . TYR A 203 ? 2.75305 2.27338 3.17406 0.05503  -0.10610 -0.39145 203 TYR A N   
999  C CA  . TYR A 203 ? 2.75587 2.29738 3.16245 0.03540  -0.10412 -0.42723 203 TYR A CA  
1000 C C   . TYR A 203 ? 2.80070 2.38736 3.18303 0.00564  -0.11454 -0.43879 203 TYR A C   
1001 O O   . TYR A 203 ? 2.81430 2.41986 3.17474 0.00920  -0.13054 -0.41125 203 TYR A O   
1002 C CB  . TYR A 203 ? 2.71156 2.25705 3.08647 0.05258  -0.11283 -0.41830 203 TYR A CB  
1003 C CG  . TYR A 203 ? 2.67909 2.18728 3.07430 0.08175  -0.10420 -0.40528 203 TYR A CG  
1004 C CD1 . TYR A 203 ? 2.65562 2.14818 3.07390 0.08166  -0.08988 -0.43328 203 TYR A CD1 
1005 C CD2 . TYR A 203 ? 2.66878 2.16215 3.06181 0.10833  -0.11031 -0.36553 203 TYR A CD2 
1006 C CE1 . TYR A 203 ? 2.62738 2.08914 3.06706 0.10855  -0.08314 -0.41862 203 TYR A CE1 
1007 C CE2 . TYR A 203 ? 2.63473 2.10080 3.04586 0.13300  -0.10333 -0.35113 203 TYR A CE2 
1008 C CZ  . TYR A 203 ? 2.61674 2.06653 3.05144 0.13360  -0.09044 -0.37609 203 TYR A CZ  
1009 O OH  . TYR A 203 ? 2.59055 2.01629 3.04608 0.15824  -0.08456 -0.35942 203 TYR A OH  
1010 N N   . ASN A 204 ? 2.70000 2.30801 3.08837 -0.02456 -0.10551 -0.47992 204 ASN A N   
1011 C CA  . ASN A 204 ? 2.74322 2.40208 3.10867 -0.05663 -0.11556 -0.49105 204 ASN A CA  
1012 C C   . ASN A 204 ? 2.74222 2.43561 3.09141 -0.08265 -0.11263 -0.52853 204 ASN A C   
1013 O O   . ASN A 204 ? 2.70725 2.38613 3.05548 -0.07167 -0.10674 -0.53988 204 ASN A O   
1014 C CB  . ASN A 204 ? 2.78022 2.44030 3.17457 -0.07501 -0.10675 -0.50101 204 ASN A CB  
1015 C CG  . ASN A 204 ? 2.78272 2.43320 3.21702 -0.09747 -0.08264 -0.54910 204 ASN A CG  
1016 O OD1 . ASN A 204 ? 2.76954 2.43268 3.20383 -0.11134 -0.07410 -0.58406 204 ASN A OD1 
1017 N ND2 . ASN A 204 ? 2.79898 2.42807 3.27063 -0.10223 -0.07085 -0.55239 204 ASN A ND2 
1018 N N   . GLU A 205 ? 2.74894 2.49320 3.08517 -0.11901 -0.11688 -0.54786 205 GLU A N   
1019 C CA  . GLU A 205 ? 2.74597 2.53992 3.05440 -0.14732 -0.12094 -0.57387 205 GLU A CA  
1020 C C   . GLU A 205 ? 2.71934 2.50595 3.05361 -0.16040 -0.09744 -0.62521 205 GLU A C   
1021 O O   . GLU A 205 ? 2.70253 2.52193 3.01408 -0.17599 -0.09921 -0.64546 205 GLU A O   
1022 C CB  . GLU A 205 ? 2.78298 2.63989 3.07396 -0.18594 -0.13114 -0.58053 205 GLU A CB  
1023 C CG  . GLU A 205 ? 2.80800 2.66228 3.13267 -0.20275 -0.11736 -0.59924 205 GLU A CG  
1024 C CD  . GLU A 205 ? 2.83686 2.68124 3.16081 -0.18620 -0.13122 -0.55618 205 GLU A CD  
1025 O OE1 . GLU A 205 ? 2.86463 2.75869 3.16503 -0.20419 -0.14922 -0.53975 205 GLU A OE1 
1026 O OE2 . GLU A 205 ? 2.82963 2.61990 3.17800 -0.15585 -0.12452 -0.53792 205 GLU A OE2 
1027 N N   . SER A 206 ? 2.79349 2.53954 3.17778 -0.15541 -0.07541 -0.64709 206 SER A N   
1028 C CA  . SER A 206 ? 2.76976 2.50686 3.18847 -0.16642 -0.05174 -0.69819 206 SER A CA  
1029 C C   . SER A 206 ? 2.72938 2.44205 3.14148 -0.13922 -0.05181 -0.69224 206 SER A C   
1030 O O   . SER A 206 ? 2.71164 2.43956 3.13252 -0.15349 -0.03916 -0.73396 206 SER A O   
1031 C CB  . SER A 206 ? 2.77622 2.46729 3.25761 -0.16200 -0.02928 -0.71601 206 SER A CB  
1032 O OG  . SER A 206 ? 2.80628 2.48533 3.32956 -0.16976 -0.00577 -0.76572 206 SER A OG  
1033 N N   . ASN A 207 ? 2.69815 2.37713 3.09518 -0.10159 -0.06533 -0.64293 207 ASN A N   
1034 C CA  . ASN A 207 ? 2.65811 2.31658 3.04544 -0.07515 -0.06689 -0.63336 207 ASN A CA  
1035 C C   . ASN A 207 ? 2.65586 2.36199 2.99035 -0.08946 -0.08225 -0.63457 207 ASN A C   
1036 O O   . ASN A 207 ? 2.62635 2.32394 2.95184 -0.07485 -0.08130 -0.63696 207 ASN A O   
1037 C CB  . ASN A 207 ? 2.63870 2.25355 3.02524 -0.03404 -0.07629 -0.58118 207 ASN A CB  
1038 C CG  . ASN A 207 ? 2.64906 2.22199 3.08424 -0.02202 -0.06421 -0.57231 207 ASN A CG  
1039 O OD1 . ASN A 207 ? 2.68226 2.26284 3.11921 -0.03294 -0.06822 -0.56185 207 ASN A OD1 
1040 N ND2 . ASN A 207 ? 2.61891 2.14908 3.09599 -0.00028 -0.04973 -0.57518 207 ASN A ND2 
1041 N N   . PHE A 208 ? 2.59574 2.35335 2.89678 -0.11823 -0.09680 -0.63120 208 PHE A N   
1042 C CA  . PHE A 208 ? 2.59825 2.40516 2.85158 -0.13559 -0.11262 -0.62940 208 PHE A CA  
1043 C C   . PHE A 208 ? 2.58296 2.42251 2.84221 -0.16517 -0.09675 -0.68474 208 PHE A C   
1044 O O   . PHE A 208 ? 2.58923 2.42858 2.88767 -0.18307 -0.07512 -0.72909 208 PHE A O   
1045 C CB  . PHE A 208 ? 2.64027 2.49715 2.86250 -0.15993 -0.13330 -0.60779 208 PHE A CB  
1046 C CG  . PHE A 208 ? 2.65081 2.49317 2.84994 -0.13229 -0.15623 -0.55073 208 PHE A CG  
1047 C CD1 . PHE A 208 ? 2.65166 2.44741 2.87307 -0.10180 -0.15506 -0.52317 208 PHE A CD1 
1048 C CD2 . PHE A 208 ? 2.66014 2.53766 2.81831 -0.13824 -0.17859 -0.52544 208 PHE A CD2 
1049 C CE1 . PHE A 208 ? 2.65813 2.44433 2.86209 -0.07772 -0.17431 -0.47580 208 PHE A CE1 
1050 C CE2 . PHE A 208 ? 2.67065 2.53401 2.81482 -0.11283 -0.19824 -0.47638 208 PHE A CE2 
1051 C CZ  . PHE A 208 ? 2.66820 2.48680 2.83565 -0.08258 -0.19539 -0.45372 208 PHE A CZ  
1052 N N   . VAL A 209 ? 2.65422 2.52309 2.87628 -0.17098 -0.10704 -0.68328 209 VAL A N   
1053 C CA  . VAL A 209 ? 2.63547 2.54176 2.85715 -0.19890 -0.09379 -0.73416 209 VAL A CA  
1054 C C   . VAL A 209 ? 2.65337 2.63502 2.82428 -0.23681 -0.11335 -0.72893 209 VAL A C   
1055 O O   . VAL A 209 ? 2.64948 2.64156 2.78134 -0.22847 -0.13219 -0.69729 209 VAL A O   
1056 C CB  . VAL A 209 ? 2.59458 2.46723 2.82138 -0.17063 -0.08649 -0.73851 209 VAL A CB  
1057 C CG1 . VAL A 209 ? 2.57152 2.48668 2.80177 -0.20119 -0.07120 -0.79581 209 VAL A CG1 
1058 C CG2 . VAL A 209 ? 2.57298 2.37333 2.85060 -0.13155 -0.07083 -0.73303 209 VAL A CG2 
1059 N N   . SER A 210 ? 2.64225 2.67887 2.81508 -0.27991 -0.10911 -0.75889 210 SER A N   
1060 C CA  . SER A 210 ? 2.65871 2.77564 2.78625 -0.32071 -0.12891 -0.75055 210 SER A CA  
1061 C C   . SER A 210 ? 2.68432 2.79680 2.78043 -0.30253 -0.15961 -0.68240 210 SER A C   
1062 O O   . SER A 210 ? 2.68572 2.83426 2.74207 -0.31172 -0.18101 -0.65479 210 SER A O   
1063 C CB  . SER A 210 ? 2.63203 2.79391 2.73330 -0.34287 -0.12788 -0.77673 210 SER A CB  
1064 O OG  . SER A 210 ? 2.60505 2.76075 2.74330 -0.35131 -0.09783 -0.84000 210 SER A OG  
1065 N N   . ASN A 211 ? 2.63102 2.69854 2.74922 -0.27662 -0.16110 -0.65582 211 ASN A N   
1066 C CA  . ASN A 211 ? 2.65632 2.71104 2.75642 -0.25392 -0.18679 -0.59457 211 ASN A CA  
1067 C C   . ASN A 211 ? 2.63942 2.65634 2.72177 -0.21790 -0.19732 -0.56177 211 ASN A C   
1068 O O   . ASN A 211 ? 2.65496 2.69271 2.70757 -0.21693 -0.22136 -0.52227 211 ASN A O   
1069 C CB  . ASN A 211 ? 2.68398 2.81331 2.75478 -0.29091 -0.20990 -0.57436 211 ASN A CB  
1070 C CG  . ASN A 211 ? 2.71275 2.86613 2.80276 -0.31298 -0.20574 -0.58503 211 ASN A CG  
1071 O OD1 . ASN A 211 ? 2.72141 2.82498 2.84343 -0.29041 -0.19348 -0.58654 211 ASN A OD1 
1072 N ND2 . ASN A 211 ? 2.72628 2.95975 2.79639 -0.35881 -0.21651 -0.59086 211 ASN A ND2 
1073 N N   . VAL A 212 ? 2.60619 2.56767 2.71043 -0.18840 -0.17897 -0.57783 212 VAL A N   
1074 C CA  . VAL A 212 ? 2.58236 2.50476 2.67391 -0.15250 -0.18529 -0.55071 212 VAL A CA  
1075 C C   . VAL A 212 ? 2.55642 2.41003 2.68508 -0.11381 -0.16762 -0.55220 212 VAL A C   
1076 O O   . VAL A 212 ? 2.54196 2.37997 2.70461 -0.11778 -0.14517 -0.59056 212 VAL A O   
1077 C CB  . VAL A 212 ? 2.55658 2.50679 2.62399 -0.16747 -0.18350 -0.57352 212 VAL A CB  
1078 C CG1 . VAL A 212 ? 2.51428 2.41139 2.58874 -0.12899 -0.17485 -0.56963 212 VAL A CG1 
1079 C CG2 . VAL A 212 ? 2.57878 2.58073 2.60280 -0.18873 -0.20994 -0.54367 212 VAL A CG2 
1080 N N   . LEU A 213 ? 2.52773 2.34283 2.65298 -0.07764 -0.17772 -0.51010 213 LEU A N   
1081 C CA  . LEU A 213 ? 2.49707 2.25286 2.65350 -0.04082 -0.16422 -0.50306 213 LEU A CA  
1082 C C   . LEU A 213 ? 2.46031 2.19277 2.59876 -0.01087 -0.17057 -0.47904 213 LEU A C   
1083 O O   . LEU A 213 ? 2.46899 2.21005 2.58123 -0.00340 -0.18960 -0.44499 213 LEU A O   
1084 C CB  . LEU A 213 ? 2.51899 2.25470 2.69387 -0.02798 -0.16805 -0.47618 213 LEU A CB  
1085 C CG  . LEU A 213 ? 2.48686 2.16756 2.69032 0.00923  -0.15782 -0.45939 213 LEU A CG  
1086 C CD1 . LEU A 213 ? 2.46190 2.11617 2.70279 0.01155  -0.13407 -0.49352 213 LEU A CD1 
1087 C CD2 . LEU A 213 ? 2.51106 2.18192 2.72929 0.01610  -0.16266 -0.43442 213 LEU A CD2 
1088 N N   . GLU A 214 ? 2.50492 2.20881 2.66107 0.00603  -0.15439 -0.49699 214 GLU A N   
1089 C CA  . GLU A 214 ? 2.46374 2.14898 2.60414 0.03225  -0.15750 -0.48031 214 GLU A CA  
1090 C C   . GLU A 214 ? 2.42862 2.06556 2.59846 0.06839  -0.14876 -0.46021 214 GLU A C   
1091 O O   . GLU A 214 ? 2.40051 2.01300 2.60336 0.07879  -0.13138 -0.47861 214 GLU A O   
1092 C CB  . GLU A 214 ? 2.43601 2.13559 2.57177 0.02098  -0.14706 -0.51628 214 GLU A CB  
1093 C CG  . GLU A 214 ? 2.46348 2.21778 2.56321 -0.01557 -0.15801 -0.53100 214 GLU A CG  
1094 C CD  . GLU A 214 ? 2.44205 2.21856 2.54798 -0.03603 -0.14243 -0.57980 214 GLU A CD  
1095 O OE1 . GLU A 214 ? 2.45269 2.23973 2.58740 -0.05631 -0.12738 -0.61677 214 GLU A OE1 
1096 O OE2 . GLU A 214 ? 2.41535 2.19996 2.49955 -0.03247 -0.14431 -0.58326 214 GLU A OE2 
1097 N N   . VAL A 215 ? 2.49742 2.12384 2.65787 0.08660  -0.16109 -0.42181 215 VAL A N   
1098 C CA  . VAL A 215 ? 2.46365 2.05363 2.64839 0.11726  -0.15481 -0.39886 215 VAL A CA  
1099 C C   . VAL A 215 ? 2.41310 1.99131 2.58304 0.14212  -0.15614 -0.38375 215 VAL A C   
1100 O O   . VAL A 215 ? 2.40926 2.00361 2.54594 0.14184  -0.16940 -0.37150 215 VAL A O   
1101 C CB  . VAL A 215 ? 2.48945 2.07990 2.67499 0.12159  -0.16559 -0.36944 215 VAL A CB  
1102 C CG1 . VAL A 215 ? 2.45066 2.01109 2.65762 0.15095  -0.15965 -0.34476 215 VAL A CG1 
1103 C CG2 . VAL A 215 ? 2.53895 2.14229 2.74034 0.09675  -0.16338 -0.38469 215 VAL A CG2 
1104 N N   . GLU A 216 ? 2.49312 2.04459 2.69007 0.16285  -0.14266 -0.38344 216 GLU A N   
1105 C CA  . GLU A 216 ? 2.44559 1.98711 2.63278 0.18822  -0.14289 -0.36542 216 GLU A CA  
1106 C C   . GLU A 216 ? 2.42967 1.95820 2.62595 0.20929  -0.14572 -0.33070 216 GLU A C   
1107 O O   . GLU A 216 ? 2.44672 1.96310 2.67125 0.20993  -0.14081 -0.32373 216 GLU A O   
1108 C CB  . GLU A 216 ? 2.41866 1.94491 2.63175 0.19841  -0.12746 -0.38307 216 GLU A CB  
1109 C CG  . GLU A 216 ? 2.41345 1.95765 2.60889 0.18415  -0.12537 -0.41440 216 GLU A CG  
1110 C CD  . GLU A 216 ? 2.37262 1.90562 2.58181 0.20375  -0.11527 -0.41909 216 GLU A CD  
1111 O OE1 . GLU A 216 ? 2.34639 1.86261 2.56877 0.22891  -0.11357 -0.39160 216 GLU A OE1 
1112 O OE2 . GLU A 216 ? 2.36800 1.91307 2.57547 0.19297  -0.10910 -0.45022 216 GLU A OE2 
1113 N N   . LEU A 217 ? 2.53672 2.07047 2.70982 0.22479  -0.15289 -0.31059 217 LEU A N   
1114 C CA  . LEU A 217 ? 2.51904 2.04885 2.69774 0.24282  -0.15521 -0.28068 217 LEU A CA  
1115 C C   . LEU A 217 ? 2.48055 2.00682 2.65797 0.26459  -0.14955 -0.26893 217 LEU A C   
1116 O O   . LEU A 217 ? 2.45871 1.99221 2.61343 0.26641  -0.15123 -0.27728 217 LEU A O   
1117 C CB  . LEU A 217 ? 2.52846 2.07469 2.68372 0.23866  -0.16998 -0.26747 217 LEU A CB  
1118 C CG  . LEU A 217 ? 2.57733 2.13192 2.73695 0.21937  -0.17750 -0.27080 217 LEU A CG  
1119 C CD1 . LEU A 217 ? 2.58733 2.15889 2.72838 0.21728  -0.19324 -0.25627 217 LEU A CD1 
1120 C CD2 . LEU A 217 ? 2.58804 2.13128 2.77905 0.22240  -0.17018 -0.26244 217 LEU A CD2 
1121 N N   . ASN A 218 ? 2.70712 2.22603 2.90849 0.27942  -0.14325 -0.24840 218 ASN A N   
1122 C CA  . ASN A 218 ? 2.66722 2.18964 2.86906 0.29886  -0.13839 -0.23315 218 ASN A CA  
1123 C C   . ASN A 218 ? 2.61176 2.15335 2.78470 0.30548  -0.14627 -0.22007 218 ASN A C   
1124 O O   . ASN A 218 ? 2.62345 2.17224 2.77890 0.29616  -0.15591 -0.22326 218 ASN A O   
1125 C CB  . ASN A 218 ? 2.68252 2.19628 2.92138 0.30935  -0.13011 -0.21245 218 ASN A CB  
1126 C CG  . ASN A 218 ? 2.65980 2.17147 2.91408 0.32449  -0.12212 -0.20559 218 ASN A CG  
1127 O OD1 . ASN A 218 ? 2.59910 2.12297 2.82993 0.33158  -0.12331 -0.20858 218 ASN A OD1 
1128 N ND2 . ASN A 218 ? 2.67423 2.17097 2.97093 0.32926  -0.11421 -0.19525 218 ASN A ND2 
1129 N N   . ASP A 219 ? 2.78949 2.34144 2.96091 0.32118  -0.14189 -0.20530 219 ASP A N   
1130 C CA  . ASP A 219 ? 2.75083 2.32287 2.89794 0.32719  -0.14653 -0.19758 219 ASP A CA  
1131 C C   . ASP A 219 ? 2.76704 2.34713 2.91541 0.32251  -0.15302 -0.18959 219 ASP A C   
1132 O O   . ASP A 219 ? 2.75747 2.34300 2.88832 0.31713  -0.16154 -0.19606 219 ASP A O   
1133 C CB  . ASP A 219 ? 2.71954 2.30766 2.87152 0.34254  -0.13911 -0.18050 219 ASP A CB  
1134 C CG  . ASP A 219 ? 2.68962 2.27776 2.83158 0.34854  -0.13511 -0.18973 219 ASP A CG  
1135 O OD1 . ASP A 219 ? 2.68259 2.26489 2.80316 0.34094  -0.13927 -0.20996 219 ASP A OD1 
1136 O OD2 . ASP A 219 ? 2.67692 2.27404 2.83312 0.36001  -0.12833 -0.17545 219 ASP A OD2 
1137 N N   . GLY A 220 ? 2.52731 2.10914 2.69950 0.32424  -0.14937 -0.17459 220 GLY A N   
1138 C CA  . GLY A 220 ? 2.54929 2.13917 2.72747 0.31876  -0.15475 -0.16913 220 GLY A CA  
1139 C C   . GLY A 220 ? 2.60614 2.18234 2.80867 0.31035  -0.15316 -0.16624 220 GLY A C   
1140 O O   . GLY A 220 ? 2.63453 2.20532 2.85850 0.31447  -0.14531 -0.15455 220 GLY A O   
1141 N N   . GLU A 221 ? 2.49216 2.06388 2.69396 0.29782  -0.16074 -0.17542 221 GLU A N   
1142 C CA  . GLU A 221 ? 2.52756 2.08729 2.75135 0.28714  -0.15889 -0.17630 221 GLU A CA  
1143 C C   . GLU A 221 ? 2.55286 2.12152 2.77420 0.27597  -0.16899 -0.17950 221 GLU A C   
1144 O O   . GLU A 221 ? 2.54082 2.12422 2.74980 0.27904  -0.17682 -0.17751 221 GLU A O   
1145 C CB  . GLU A 221 ? 2.54015 2.07901 2.76982 0.27927  -0.15417 -0.19376 221 GLU A CB  
1146 C CG  . GLU A 221 ? 2.54498 2.06930 2.80407 0.28619  -0.14251 -0.18509 221 GLU A CG  
1147 C CD  . GLU A 221 ? 2.54608 2.05170 2.81444 0.28195  -0.13616 -0.20603 221 GLU A CD  
1148 O OE1 . GLU A 221 ? 2.54882 2.05626 2.79691 0.27096  -0.14065 -0.22859 221 GLU A OE1 
1149 O OE2 . GLU A 221 ? 2.54663 2.03806 2.84525 0.28893  -0.12671 -0.19962 221 GLU A OE2 
1150 N N   . LEU A 222 ? 2.39386 1.95431 2.63069 0.26274  -0.16860 -0.18460 222 LEU A N   
1151 C CA  . LEU A 222 ? 2.42481 1.99690 2.66396 0.25149  -0.17790 -0.18511 222 LEU A CA  
1152 C C   . LEU A 222 ? 2.46856 2.03160 2.71325 0.23214  -0.17809 -0.20146 222 LEU A C   
1153 O O   . LEU A 222 ? 2.48548 2.03375 2.75067 0.22799  -0.16811 -0.20463 222 LEU A O   
1154 C CB  . LEU A 222 ? 2.43020 2.01348 2.68875 0.25598  -0.17520 -0.16863 222 LEU A CB  
1155 C CG  . LEU A 222 ? 2.44873 2.05160 2.71093 0.25107  -0.18531 -0.16562 222 LEU A CG  
1156 C CD1 . LEU A 222 ? 2.41827 2.03591 2.66877 0.26184  -0.19229 -0.16335 222 LEU A CD1 
1157 C CD2 . LEU A 222 ? 2.46383 2.07692 2.74812 0.25092  -0.18023 -0.15334 222 LEU A CD2 
1158 N N   . PHE A 223 ? 2.34632 1.92054 2.57530 0.21901  -0.18926 -0.21143 223 PHE A N   
1159 C CA  . PHE A 223 ? 2.39961 1.97543 2.63066 0.19651  -0.19036 -0.22908 223 PHE A CA  
1160 C C   . PHE A 223 ? 2.44175 2.03642 2.67970 0.18530  -0.20030 -0.22234 223 PHE A C   
1161 O O   . PHE A 223 ? 2.44262 2.05387 2.67280 0.18920  -0.21292 -0.21067 223 PHE A O   
1162 C CB  . PHE A 223 ? 2.40856 1.99138 2.61531 0.18550  -0.19621 -0.24497 223 PHE A CB  
1163 C CG  . PHE A 223 ? 2.45949 2.05301 2.66640 0.15865  -0.19692 -0.26602 223 PHE A CG  
1164 C CD1 . PHE A 223 ? 2.46252 2.04245 2.68236 0.14992  -0.18276 -0.28918 223 PHE A CD1 
1165 C CD2 . PHE A 223 ? 2.50617 2.12659 2.70358 0.14117  -0.21148 -0.26321 223 PHE A CD2 
1166 C CE1 . PHE A 223 ? 2.50716 2.10185 2.72862 0.12262  -0.18153 -0.31319 223 PHE A CE1 
1167 C CE2 . PHE A 223 ? 2.55503 2.19302 2.75114 0.11343  -0.21187 -0.28321 223 PHE A CE2 
1168 C CZ  . PHE A 223 ? 2.55297 2.17901 2.76010 0.10330  -0.19611 -0.31027 223 PHE A CZ  
1169 N N   . VAL A 224 ? 2.42044 2.01285 2.67648 0.17141  -0.19442 -0.22991 224 VAL A N   
1170 C CA  . VAL A 224 ? 2.46283 2.07494 2.72771 0.15954  -0.20261 -0.22439 224 VAL A CA  
1171 C C   . VAL A 224 ? 2.51599 2.14006 2.77849 0.13186  -0.20393 -0.24512 224 VAL A C   
1172 O O   . VAL A 224 ? 2.51659 2.12781 2.78185 0.12229  -0.19289 -0.26611 224 VAL A O   
1173 C CB  . VAL A 224 ? 2.45898 2.06399 2.74883 0.16617  -0.19416 -0.21283 224 VAL A CB  
1174 C CG1 . VAL A 224 ? 2.49444 2.12417 2.79237 0.15845  -0.20427 -0.20420 224 VAL A CG1 
1175 C CG2 . VAL A 224 ? 2.40906 2.00473 2.70136 0.19019  -0.18879 -0.19620 224 VAL A CG2 
1176 N N   . LEU A 225 ? 2.50708 2.15950 2.76703 0.11816  -0.21733 -0.24006 225 LEU A N   
1177 C CA  . LEU A 225 ? 2.52498 2.19916 2.78241 0.08849  -0.21976 -0.25808 225 LEU A CA  
1178 C C   . LEU A 225 ? 2.52269 2.22440 2.78978 0.07961  -0.23128 -0.24504 225 LEU A C   
1179 O O   . LEU A 225 ? 2.50626 2.21457 2.77787 0.09575  -0.24131 -0.22292 225 LEU A O   
1180 C CB  . LEU A 225 ? 2.52929 2.22245 2.76082 0.07456  -0.22890 -0.26780 225 LEU A CB  
1181 C CG  . LEU A 225 ? 2.51540 2.23021 2.73224 0.08030  -0.24955 -0.24465 225 LEU A CG  
1182 C CD1 . LEU A 225 ? 2.53095 2.28800 2.74466 0.05434  -0.26521 -0.24080 225 LEU A CD1 
1183 C CD2 . LEU A 225 ? 2.51171 2.22069 2.70561 0.08590  -0.25216 -0.24698 225 LEU A CD2 
1184 N N   . ALA A 226 ? 2.65798 2.37823 2.93080 0.05307  -0.22914 -0.26085 226 ALA A N   
1185 C CA  . ALA A 226 ? 2.69470 2.44371 2.97884 0.04234  -0.23878 -0.25030 226 ALA A CA  
1186 C C   . ALA A 226 ? 2.74512 2.53473 3.01796 0.00885  -0.24726 -0.26378 226 ALA A C   
1187 O O   . ALA A 226 ? 2.76541 2.55879 3.04341 -0.01398 -0.23513 -0.28959 226 ALA A O   
1188 C CB  . ALA A 226 ? 2.68329 2.41519 2.99210 0.04378  -0.22458 -0.25361 226 ALA A CB  
1189 N N   . CYS A 227 ? 2.80093 2.62324 3.06118 0.00476  -0.26793 -0.24596 227 CYS A N   
1190 C CA  . CYS A 227 ? 2.83885 2.71040 3.08742 -0.02842 -0.27999 -0.25139 227 CYS A CA  
1191 C C   . CYS A 227 ? 2.84656 2.74884 3.09493 -0.02309 -0.30541 -0.21771 227 CYS A C   
1192 O O   . CYS A 227 ? 2.83029 2.71464 3.09261 0.00520  -0.31083 -0.19563 227 CYS A O   
1193 C CB  . CYS A 227 ? 2.84526 2.72286 3.07146 -0.04790 -0.27391 -0.27666 227 CYS A CB  
1194 S SG  . CYS A 227 ? 2.81720 2.67452 3.02263 -0.02579 -0.28104 -0.26342 227 CYS A SG  
1195 N N   . GLU A 228 ? 2.78415 2.73555 3.01988 -0.05138 -0.32098 -0.21368 228 GLU A N   
1196 C CA  . GLU A 228 ? 2.78361 2.76913 3.02459 -0.05007 -0.34721 -0.17857 228 GLU A CA  
1197 C C   . GLU A 228 ? 2.78579 2.79250 3.00183 -0.06377 -0.36008 -0.17197 228 GLU A C   
1198 O O   . GLU A 228 ? 2.79781 2.83437 2.99268 -0.09574 -0.35711 -0.19259 228 GLU A O   
1199 C CB  . GLU A 228 ? 2.79201 2.82819 3.04591 -0.07365 -0.35862 -0.17024 228 GLU A CB  
1200 C CG  . GLU A 228 ? 2.78886 2.80981 3.06927 -0.06046 -0.34901 -0.17207 228 GLU A CG  
1201 C CD  . GLU A 228 ? 2.80185 2.80431 3.07950 -0.07390 -0.32405 -0.20823 228 GLU A CD  
1202 O OE1 . GLU A 228 ? 2.81105 2.81761 3.06931 -0.09566 -0.31433 -0.23452 228 GLU A OE1 
1203 O OE2 . GLU A 228 ? 2.80015 2.78488 3.09790 -0.06335 -0.31385 -0.21084 228 GLU A OE2 
1204 N N   . LEU A 229 ? 2.83078 2.82482 3.05107 -0.04136 -0.37389 -0.14442 229 LEU A N   
1205 C CA  . LEU A 229 ? 2.83143 2.83537 3.02853 -0.04941 -0.38432 -0.13687 229 LEU A CA  
1206 C C   . LEU A 229 ? 2.83654 2.90367 3.02968 -0.07951 -0.40999 -0.11201 229 LEU A C   
1207 O O   . LEU A 229 ? 2.83197 2.93046 3.04741 -0.08470 -0.42420 -0.09065 229 LEU A O   
1208 C CB  . LEU A 229 ? 2.81389 2.77869 3.02027 -0.01433 -0.38834 -0.11730 229 LEU A CB  
1209 C CG  . LEU A 229 ? 2.80496 2.71315 3.01448 0.01583  -0.36534 -0.13632 229 LEU A CG  
1210 C CD1 . LEU A 229 ? 2.76899 2.64991 2.99385 0.04803  -0.37142 -0.11488 229 LEU A CD1 
1211 C CD2 . LEU A 229 ? 2.80612 2.69843 2.98668 0.00616  -0.34846 -0.16689 229 LEU A CD2 
1212 N N   . ILE A 230 ? 2.89610 2.98509 3.06112 -0.10028 -0.41637 -0.11362 230 ILE A N   
1213 C CA  . ILE A 230 ? 2.89656 3.04682 3.05554 -0.12873 -0.44323 -0.08352 230 ILE A CA  
1214 C C   . ILE A 230 ? 2.88363 3.01620 3.05725 -0.10461 -0.46212 -0.04429 230 ILE A C   
1215 O O   . ILE A 230 ? 2.88287 2.98110 3.04170 -0.09057 -0.45580 -0.05034 230 ILE A O   
1216 C CB  . ILE A 230 ? 2.90610 3.09665 3.02688 -0.16827 -0.44009 -0.10674 230 ILE A CB  
1217 C CG1 . ILE A 230 ? 2.90700 3.09090 3.01733 -0.18251 -0.41211 -0.15801 230 ILE A CG1 
1218 C CG2 . ILE A 230 ? 2.90433 3.17439 3.01980 -0.20674 -0.46666 -0.07789 230 ILE A CG2 
1219 C CD1 . ILE A 230 ? 2.89237 3.11422 2.96959 -0.22031 -0.40479 -0.18927 230 ILE A CD1 
1220 N N   . ASN A 231 ? 2.86582 3.02125 3.07231 -0.09927 -0.48465 -0.00496 231 ASN A N   
1221 C CA  . ASN A 231 ? 2.84719 2.98646 3.08077 -0.07551 -0.50346 0.03413  231 ASN A CA  
1222 C C   . ASN A 231 ? 2.83039 2.89998 3.07857 -0.03248 -0.48652 0.02219  231 ASN A C   
1223 O O   . ASN A 231 ? 2.81028 2.86014 3.08170 -0.01126 -0.49782 0.04752  231 ASN A O   
1224 C CB  . ASN A 231 ? 2.85450 3.02216 3.06564 -0.09770 -0.52131 0.05536  231 ASN A CB  
1225 C CG  . ASN A 231 ? 2.86031 3.10692 3.06272 -0.14114 -0.54314 0.07709  231 ASN A CG  
1226 O OD1 . ASN A 231 ? 2.86473 3.14560 3.06496 -0.16067 -0.53887 0.06297  231 ASN A OD1 
1227 N ND2 . ASN A 231 ? 2.85911 3.13817 3.05686 -0.15828 -0.56687 0.11252  231 ASN A ND2 
1228 N N   . LYS A 232 ? 2.86271 2.89719 3.09989 -0.02065 -0.45966 -0.01536 232 LYS A N   
1229 C CA  . LYS A 232 ? 2.83827 2.81563 3.09170 0.01788  -0.44257 -0.02683 232 LYS A CA  
1230 C C   . LYS A 232 ? 2.82737 2.77190 3.06989 0.03441  -0.44101 -0.02425 232 LYS A C   
1231 O O   . LYS A 232 ? 2.78979 2.70063 3.05684 0.06516  -0.43756 -0.01812 232 LYS A O   
1232 C CB  . LYS A 232 ? 2.80093 2.77623 3.10270 0.04044  -0.45056 -0.00608 232 LYS A CB  
1233 C CG  . LYS A 232 ? 2.80958 2.82630 3.12614 0.02230  -0.45778 -0.00083 232 LYS A CG  
1234 C CD  . LYS A 232 ? 2.83649 2.85075 3.12788 0.00743  -0.43584 -0.03727 232 LYS A CD  
1235 C CE  . LYS A 232 ? 2.81130 2.78404 3.11875 0.03493  -0.41461 -0.05587 232 LYS A CE  
1236 N NZ  . LYS A 232 ? 2.79100 2.78392 3.13384 0.03932  -0.42047 -0.04454 232 LYS A NZ  
1237 N N   . LYS A 233 ? 2.89212 2.84900 3.09828 0.01290  -0.44249 -0.03121 233 LYS A N   
1238 C CA  . LYS A 233 ? 2.85706 2.78427 3.04700 0.02541  -0.43867 -0.03338 233 LYS A CA  
1239 C C   . LYS A 233 ? 2.64014 2.54208 2.79802 0.02571  -0.41256 -0.07399 233 LYS A C   
1240 O O   . LYS A 233 ? 2.81814 2.74351 2.94525 -0.00183 -0.40947 -0.09149 233 LYS A O   
1241 C CB  . LYS A 233 ? 2.88604 2.84831 3.06116 0.00066  -0.46100 -0.00843 233 LYS A CB  
1242 C CG  . LYS A 233 ? 2.88643 2.88614 3.09470 -0.00810 -0.48947 0.03477  233 LYS A CG  
1243 C CD  . LYS A 233 ? 2.87460 2.88892 3.08175 -0.01792 -0.51143 0.06788  233 LYS A CD  
1244 C CE  . LYS A 233 ? 2.86959 2.92090 3.11777 -0.02508 -0.54112 0.11551  233 LYS A CE  
1245 N NZ  . LYS A 233 ? 2.85158 2.90304 3.11394 -0.02499 -0.56202 0.15263  233 LYS A NZ  
1246 N N   . CYS A 234 ? 2.86806 2.72559 3.03604 0.05590  -0.39372 -0.08905 234 CYS A N   
1247 C CA  . CYS A 234 ? 2.79274 2.62548 2.93990 0.05893  -0.36918 -0.12386 234 CYS A CA  
1248 C C   . CYS A 234 ? 2.62225 2.41074 2.77361 0.09156  -0.35511 -0.12958 234 CYS A C   
1249 O O   . CYS A 234 ? 2.57330 2.34742 2.75145 0.11475  -0.35760 -0.11467 234 CYS A O   
1250 C CB  . CYS A 234 ? 2.82200 2.65775 2.98024 0.05349  -0.35724 -0.14043 234 CYS A CB  
1251 S SG  . CYS A 234 ? 2.91569 2.70719 3.07418 0.07303  -0.32739 -0.17097 234 CYS A SG  
1252 N N   . PHE A 235 ? 2.83073 2.60194 2.95718 0.09165  -0.33961 -0.15315 235 PHE A N   
1253 C CA  . PHE A 235 ? 2.75153 2.48498 2.87778 0.11860  -0.32187 -0.16463 235 PHE A CA  
1254 C C   . PHE A 235 ? 2.71502 2.43488 2.84632 0.13841  -0.32837 -0.14792 235 PHE A C   
1255 O O   . PHE A 235 ? 2.64845 2.34308 2.78717 0.16255  -0.31568 -0.15248 235 PHE A O   
1256 C CB  . PHE A 235 ? 2.71649 2.43255 2.86537 0.13457  -0.30772 -0.17082 235 PHE A CB  
1257 C CG  . PHE A 235 ? 2.70628 2.41240 2.84779 0.12707  -0.28958 -0.19662 235 PHE A CG  
1258 C CD1 . PHE A 235 ? 2.72553 2.44116 2.84431 0.10647  -0.28621 -0.21622 235 PHE A CD1 
1259 C CD2 . PHE A 235 ? 2.67443 2.36248 2.83503 0.14017  -0.27537 -0.20176 235 PHE A CD2 
1260 C CE1 . PHE A 235 ? 2.71147 2.41603 2.83161 0.10051  -0.26832 -0.24234 235 PHE A CE1 
1261 C CE2 . PHE A 235 ? 2.66773 2.34340 2.82847 0.13382  -0.25870 -0.22376 235 PHE A CE2 
1262 C CZ  . PHE A 235 ? 2.68578 2.36828 2.82864 0.11480  -0.25487 -0.24494 235 PHE A CZ  
1263 N N   . GLN A 236 ? 2.83026 2.56843 2.95945 0.12741  -0.34776 -0.12821 236 GLN A N   
1264 C CA  . GLN A 236 ? 2.80036 2.52427 2.93453 0.14320  -0.35304 -0.11510 236 GLN A CA  
1265 C C   . GLN A 236 ? 2.84055 2.57387 2.94431 0.12666  -0.36058 -0.11407 236 GLN A C   
1266 O O   . GLN A 236 ? 2.79895 2.51400 2.89636 0.13983  -0.35675 -0.11470 236 GLN A O   
1267 C CB  . GLN A 236 ? 2.82869 2.56105 3.00093 0.15019  -0.37063 -0.08685 236 GLN A CB  
1268 C CG  . GLN A 236 ? 2.80302 2.53034 3.00857 0.16649  -0.36414 -0.08750 236 GLN A CG  
1269 C CD  . GLN A 236 ? 2.86637 2.61991 3.10303 0.15766  -0.38410 -0.06323 236 GLN A CD  
1270 O OE1 . GLN A 236 ? 2.85749 2.60978 3.13050 0.17082  -0.39461 -0.04453 236 GLN A OE1 
1271 N NE2 . GLN A 236 ? 2.92525 2.70472 3.15097 0.13471  -0.38915 -0.06420 236 GLN A NE2 
1272 N N   . GLU A 237 ? 2.69089 2.45596 2.77523 0.09634  -0.37056 -0.11379 237 GLU A N   
1273 C CA  . GLU A 237 ? 2.79732 2.58110 2.85287 0.07515  -0.38034 -0.11031 237 GLU A CA  
1274 C C   . GLU A 237 ? 2.73981 2.51715 2.76255 0.06964  -0.36147 -0.14431 237 GLU A C   
1275 O O   . GLU A 237 ? 2.64116 2.39890 2.66655 0.08202  -0.34195 -0.16793 237 GLU A O   
1276 C CB  . GLU A 237 ? 3.02193 2.85268 3.07438 0.04189  -0.40158 -0.09162 237 GLU A CB  
1277 C CG  . GLU A 237 ? 3.05186 2.90348 3.10800 0.02731  -0.39661 -0.10547 237 GLU A CG  
1278 C CD  . GLU A 237 ? 3.03084 2.87865 3.12595 0.04215  -0.40310 -0.08653 237 GLU A CD  
1279 O OE1 . GLU A 237 ? 3.10791 2.97994 3.22235 0.03414  -0.42560 -0.05379 237 GLU A OE1 
1280 O OE2 . GLU A 237 ? 2.84677 2.66904 2.95532 0.06154  -0.38610 -0.10316 237 GLU A OE2 
1281 N N   . GLY A 238 ? 2.81604 2.61136 2.81054 0.05051  -0.36779 -0.14561 238 GLY A N   
1282 C CA  . GLY A 238 ? 2.78906 2.58437 2.75462 0.04258  -0.35143 -0.17851 238 GLY A CA  
1283 C C   . GLY A 238 ? 2.94642 2.78006 2.88237 0.01004  -0.36429 -0.17575 238 GLY A C   
1284 O O   . GLY A 238 ? 3.02815 2.87302 2.96374 0.00357  -0.38365 -0.14550 238 GLY A O   
1285 N N   . LYS A 239 ? 2.77570 2.63140 2.68957 -0.01176 -0.35324 -0.20784 239 LYS A N   
1286 C CA  . LYS A 239 ? 3.03614 2.93973 2.92061 -0.04918 -0.36460 -0.20927 239 LYS A CA  
1287 C C   . LYS A 239 ? 3.00527 2.90432 2.86296 -0.04956 -0.35503 -0.22917 239 LYS A C   
1288 O O   . LYS A 239 ? 3.01969 2.95805 2.85159 -0.07939 -0.36629 -0.22558 239 LYS A O   
1289 C CB  . LYS A 239 ? 3.04473 2.99111 2.92324 -0.08203 -0.36050 -0.23387 239 LYS A CB  
1290 C CG  . LYS A 239 ? 3.07863 3.08802 2.93927 -0.12416 -0.38332 -0.21391 239 LYS A CG  
1291 C CD  . LYS A 239 ? 3.07504 3.13450 2.91241 -0.16282 -0.37378 -0.25276 239 LYS A CD  
1292 C CE  . LYS A 239 ? 3.09031 3.21893 2.90460 -0.20708 -0.39752 -0.23003 239 LYS A CE  
1293 N NZ  . LYS A 239 ? 3.07033 3.25528 2.85956 -0.24816 -0.38717 -0.27169 239 LYS A NZ  
1294 N N   . GLU A 240 ? 3.14766 3.00411 3.01074 -0.01879 -0.33530 -0.24855 240 GLU A N   
1295 C CA  . GLU A 240 ? 3.11963 2.97043 2.95986 -0.01562 -0.32693 -0.26435 240 GLU A CA  
1296 C C   . GLU A 240 ? 3.13179 2.96700 2.96762 -0.00304 -0.33992 -0.23325 240 GLU A C   
1297 O O   . GLU A 240 ? 3.09623 2.91334 2.92004 0.01105  -0.33023 -0.24385 240 GLU A O   
1298 C CB  . GLU A 240 ? 2.98282 2.79854 2.83346 0.01154  -0.30138 -0.29521 240 GLU A CB  
1299 C CG  . GLU A 240 ? 3.03110 2.86687 2.86483 -0.00495 -0.28672 -0.33505 240 GLU A CG  
1300 C CD  . GLU A 240 ? 2.96747 2.76821 2.81895 0.02343  -0.26305 -0.36070 240 GLU A CD  
1301 O OE1 . GLU A 240 ? 2.76714 2.53544 2.64502 0.04876  -0.25696 -0.35163 240 GLU A OE1 
1302 O OE2 . GLU A 240 ? 2.94124 2.74930 2.78207 0.01987  -0.25096 -0.38874 240 GLU A OE2 
1303 N N   . LYS A 241 ? 3.13231 2.97479 2.98124 -0.00796 -0.36124 -0.19566 241 LYS A N   
1304 C CA  . LYS A 241 ? 3.15361 2.97604 3.01100 0.00651  -0.37338 -0.16463 241 LYS A CA  
1305 C C   . LYS A 241 ? 2.83928 2.61327 2.71402 0.04662  -0.35683 -0.17210 241 LYS A C   
1306 O O   . LYS A 241 ? 2.83631 2.59149 2.71483 0.06014  -0.35997 -0.15828 241 LYS A O   
1307 C CB  . LYS A 241 ? 3.16931 3.01456 2.99611 -0.01583 -0.38266 -0.15937 241 LYS A CB  
1308 C CG  . LYS A 241 ? 3.20159 3.10259 3.01136 -0.05899 -0.40242 -0.14491 241 LYS A CG  
1309 C CD  . LYS A 241 ? 3.24133 3.15157 3.08018 -0.06353 -0.42582 -0.10187 241 LYS A CD  
1310 C CE  . LYS A 241 ? 3.26310 3.23488 3.08460 -0.10856 -0.44849 -0.08013 241 LYS A CE  
1311 N NZ  . LYS A 241 ? 3.25465 3.26992 3.05496 -0.13686 -0.43985 -0.11225 241 LYS A NZ  
1312 N N   . ALA A 242 ? 2.98905 2.74544 2.87604 0.06407  -0.33919 -0.19340 242 ALA A N   
1313 C CA  . ALA A 242 ? 2.80464 2.52292 2.70814 0.09939  -0.32293 -0.20027 242 ALA A CA  
1314 C C   . ALA A 242 ? 2.76677 2.47451 2.69933 0.11176  -0.31848 -0.19863 242 ALA A C   
1315 O O   . ALA A 242 ? 2.75242 2.46271 2.68494 0.10838  -0.30671 -0.21961 242 ALA A O   
1316 C CB  . ALA A 242 ? 2.72683 2.43692 2.61132 0.10739  -0.30298 -0.23071 242 ALA A CB  
1317 N N   . LEU A 243 ? 2.81385 2.51021 2.77418 0.12555  -0.32736 -0.17485 243 LEU A N   
1318 C CA  . LEU A 243 ? 2.80039 2.49277 2.78897 0.13361  -0.32655 -0.16975 243 LEU A CA  
1319 C C   . LEU A 243 ? 2.69845 2.36488 2.69909 0.16061  -0.30569 -0.18524 243 LEU A C   
1320 O O   . LEU A 243 ? 2.63429 2.28314 2.64025 0.18140  -0.29843 -0.18427 243 LEU A O   
1321 C CB  . LEU A 243 ? 2.83160 2.52513 2.85009 0.13784  -0.34414 -0.13924 243 LEU A CB  
1322 C CG  . LEU A 243 ? 2.89273 2.61825 2.91424 0.11065  -0.36671 -0.11734 243 LEU A CG  
1323 C CD1 . LEU A 243 ? 2.95791 2.70789 2.94684 0.08340  -0.37738 -0.11435 243 LEU A CD1 
1324 C CD2 . LEU A 243 ? 2.90162 2.62383 2.96290 0.12064  -0.38269 -0.08648 243 LEU A CD2 
1325 N N   . TYR A 244 ? 2.73097 2.39795 2.73712 0.15838  -0.29611 -0.19898 244 TYR A N   
1326 C CA  . TYR A 244 ? 2.64906 2.29501 2.67109 0.18131  -0.27851 -0.20807 244 TYR A CA  
1327 C C   . TYR A 244 ? 2.61997 2.26035 2.67256 0.19615  -0.28293 -0.19012 244 TYR A C   
1328 O O   . TYR A 244 ? 2.65660 2.30824 2.72473 0.18664  -0.29252 -0.18058 244 TYR A O   
1329 C CB  . TYR A 244 ? 2.66462 2.31241 2.68789 0.17185  -0.26790 -0.22698 244 TYR A CB  
1330 C CG  . TYR A 244 ? 2.59664 2.22347 2.63325 0.19236  -0.24877 -0.23700 244 TYR A CG  
1331 C CD1 . TYR A 244 ? 2.52464 2.13784 2.56738 0.21642  -0.24166 -0.22946 244 TYR A CD1 
1332 C CD2 . TYR A 244 ? 2.61250 2.23598 2.65817 0.18593  -0.23786 -0.25341 244 TYR A CD2 
1333 C CE1 . TYR A 244 ? 2.47588 2.07591 2.53123 0.23287  -0.22580 -0.23412 244 TYR A CE1 
1334 C CE2 . TYR A 244 ? 2.56438 2.16912 2.62658 0.20382  -0.22192 -0.25781 244 TYR A CE2 
1335 C CZ  . TYR A 244 ? 2.49846 2.09310 2.56438 0.22698  -0.21675 -0.24615 244 TYR A CZ  
1336 O OH  . TYR A 244 ? 2.46336 2.04498 2.54607 0.24280  -0.20241 -0.24615 244 TYR A OH  
1337 N N   . LYS A 245 ? 2.59780 2.22487 2.66010 0.21817  -0.27550 -0.18715 245 LYS A N   
1338 C CA  . LYS A 245 ? 2.56658 2.19166 2.66034 0.23246  -0.27783 -0.17437 245 LYS A CA  
1339 C C   . LYS A 245 ? 2.50527 2.12258 2.61135 0.24959  -0.26049 -0.18194 245 LYS A C   
1340 O O   . LYS A 245 ? 2.46884 2.07906 2.56057 0.25636  -0.24679 -0.19321 245 LYS A O   
1341 C CB  . LYS A 245 ? 2.54319 2.16514 2.64424 0.24129  -0.28332 -0.16591 245 LYS A CB  
1342 C CG  . LYS A 245 ? 2.62075 2.25177 2.71923 0.22416  -0.30375 -0.15043 245 LYS A CG  
1343 C CD  . LYS A 245 ? 2.61020 2.23500 2.69695 0.22638  -0.30526 -0.14958 245 LYS A CD  
1344 C CE  . LYS A 245 ? 2.64818 2.26934 2.77105 0.23467  -0.31519 -0.13347 245 LYS A CE  
1345 N NZ  . LYS A 245 ? 2.59003 2.20464 2.74280 0.25693  -0.30151 -0.14164 245 LYS A NZ  
1346 N N   . SER A 246 ? 2.48453 2.10614 2.61919 0.25583  -0.26179 -0.17406 246 SER A N   
1347 C CA  . SER A 246 ? 2.44717 2.06702 2.59502 0.26730  -0.24749 -0.17799 246 SER A CA  
1348 C C   . SER A 246 ? 2.40419 2.03078 2.57768 0.28307  -0.24377 -0.17384 246 SER A C   
1349 O O   . SER A 246 ? 2.41902 2.04954 2.60829 0.28506  -0.25334 -0.16801 246 SER A O   
1350 C CB  . SER A 246 ? 2.50759 2.13128 2.66652 0.25655  -0.24990 -0.17628 246 SER A CB  
1351 O OG  . SER A 246 ? 2.53345 2.16800 2.72052 0.25858  -0.25819 -0.16574 246 SER A OG  
1352 N N   . ASN A 247 ? 2.48340 2.11357 2.66415 0.29320  -0.22937 -0.17708 247 ASN A N   
1353 C CA  . ASN A 247 ? 2.46648 2.11080 2.67301 0.30520  -0.22361 -0.17668 247 ASN A CA  
1354 C C   . ASN A 247 ? 2.51217 2.16574 2.74915 0.30225  -0.23225 -0.17028 247 ASN A C   
1355 O O   . ASN A 247 ? 2.50961 2.17477 2.77434 0.30980  -0.23323 -0.17116 247 ASN A O   
1356 C CB  . ASN A 247 ? 2.43517 2.08797 2.63967 0.31314  -0.20691 -0.17906 247 ASN A CB  
1357 C CG  . ASN A 247 ? 2.42011 2.06847 2.59903 0.31775  -0.19829 -0.18385 247 ASN A CG  
1358 O OD1 . ASN A 247 ? 2.41418 2.06113 2.58334 0.32016  -0.20035 -0.18903 247 ASN A OD1 
1359 N ND2 . ASN A 247 ? 2.42455 2.07093 2.59526 0.31886  -0.18884 -0.18119 247 ASN A ND2 
1360 N N   . LYS A 248 ? 2.43182 2.08231 2.66692 0.29093  -0.23781 -0.16568 248 LYS A N   
1361 C CA  . LYS A 248 ? 2.50007 2.16211 2.76289 0.28680  -0.24615 -0.15907 248 LYS A CA  
1362 C C   . LYS A 248 ? 2.58666 2.24552 2.83956 0.26960  -0.25466 -0.15550 248 LYS A C   
1363 O O   . LYS A 248 ? 2.61055 2.26197 2.84979 0.26400  -0.24585 -0.16058 248 LYS A O   
1364 C CB  . LYS A 248 ? 2.34880 2.02482 2.63161 0.29473  -0.23380 -0.16125 248 LYS A CB  
1365 C CG  . LYS A 248 ? 2.52940 2.22115 2.84431 0.29221  -0.24093 -0.15645 248 LYS A CG  
1366 C CD  . LYS A 248 ? 2.54064 2.25083 2.87347 0.29879  -0.22753 -0.16019 248 LYS A CD  
1367 C CE  . LYS A 248 ? 2.59837 2.32714 2.96504 0.29656  -0.23388 -0.15743 248 LYS A CE  
1368 N NZ  . LYS A 248 ? 2.62405 2.37608 3.00784 0.30063  -0.22060 -0.16217 248 LYS A NZ  
1369 N N   . ILE A 249 ? 2.56716 2.23384 2.82983 0.26016  -0.27161 -0.14665 249 ILE A N   
1370 C CA  . ILE A 249 ? 2.62734 2.30074 2.88441 0.24111  -0.28053 -0.14353 249 ILE A CA  
1371 C C   . ILE A 249 ? 2.65032 2.34060 2.94041 0.24181  -0.28536 -0.13622 249 ILE A C   
1372 O O   . ILE A 249 ? 2.66519 2.36823 2.97988 0.24326  -0.29936 -0.12465 249 ILE A O   
1373 C CB  . ILE A 249 ? 2.67505 2.35376 2.91793 0.22634  -0.29735 -0.13612 249 ILE A CB  
1374 C CG1 . ILE A 249 ? 2.64886 2.31336 2.86617 0.23054  -0.29338 -0.14202 249 ILE A CG1 
1375 C CG2 . ILE A 249 ? 2.74598 2.43415 2.97235 0.20300  -0.30112 -0.14033 249 ILE A CG2 
1376 C CD1 . ILE A 249 ? 2.68877 2.36111 2.89371 0.21637  -0.31062 -0.13203 249 ILE A CD1 
1377 N N   . ILE A 250 ? 2.59866 2.28956 2.89255 0.24093  -0.27389 -0.14203 250 ILE A N   
1378 C CA  . ILE A 250 ? 2.61762 2.32569 2.94222 0.24300  -0.27493 -0.13765 250 ILE A CA  
1379 C C   . ILE A 250 ? 2.68733 2.40667 3.01137 0.22303  -0.28341 -0.13484 250 ILE A C   
1380 O O   . ILE A 250 ? 2.70281 2.41315 3.00584 0.21000  -0.27696 -0.14326 250 ILE A O   
1381 C CB  . ILE A 250 ? 2.58121 2.28776 2.91159 0.25307  -0.25687 -0.14403 250 ILE A CB  
1382 C CG1 . ILE A 250 ? 2.61329 2.33832 2.96874 0.24874  -0.25668 -0.14142 250 ILE A CG1 
1383 C CG2 . ILE A 250 ? 2.56587 2.25268 2.86904 0.24920  -0.24417 -0.15077 250 ILE A CG2 
1384 C CD1 . ILE A 250 ? 2.61267 2.35932 3.00406 0.25814  -0.26444 -0.13736 250 ILE A CD1 
1385 N N   . TYR A 251 ? 2.74419 2.48519 3.09456 0.22012  -0.29750 -0.12398 251 TYR A N   
1386 C CA  . TYR A 251 ? 2.78001 2.54000 3.13215 0.19968  -0.30817 -0.11921 251 TYR A CA  
1387 C C   . TYR A 251 ? 2.76408 2.54252 3.14774 0.20260  -0.30707 -0.11665 251 TYR A C   
1388 O O   . TYR A 251 ? 2.75835 2.55709 3.17284 0.20690  -0.32023 -0.10485 251 TYR A O   
1389 C CB  . TYR A 251 ? 2.80684 2.58333 3.16165 0.18996  -0.33004 -0.10364 251 TYR A CB  
1390 C CG  . TYR A 251 ? 2.83661 2.60344 3.15685 0.17913  -0.33312 -0.10621 251 TYR A CG  
1391 C CD1 . TYR A 251 ? 2.88510 2.66047 3.17901 0.15463  -0.33336 -0.11461 251 TYR A CD1 
1392 C CD2 . TYR A 251 ? 2.82007 2.57246 3.13562 0.19169  -0.33529 -0.10227 251 TYR A CD2 
1393 C CE1 . TYR A 251 ? 2.91594 2.68763 3.17935 0.14302  -0.33557 -0.11957 251 TYR A CE1 
1394 C CE2 . TYR A 251 ? 2.84795 2.59450 3.13142 0.18056  -0.33826 -0.10489 251 TYR A CE2 
1395 C CZ  . TYR A 251 ? 2.89578 2.65308 3.15309 0.15622  -0.33845 -0.11371 251 TYR A CZ  
1396 O OH  . TYR A 251 ? 2.91897 2.67512 3.14521 0.14360  -0.34057 -0.11905 251 TYR A OH  
1397 N N   . HIS A 252 ? 2.80914 2.58155 3.18807 0.19972  -0.29180 -0.12679 252 HIS A N   
1398 C CA  . HIS A 252 ? 2.80113 2.59346 3.20535 0.19735  -0.29039 -0.12545 252 HIS A CA  
1399 C C   . HIS A 252 ? 2.83881 2.63558 3.23068 0.17421  -0.28851 -0.13103 252 HIS A C   
1400 O O   . HIS A 252 ? 2.86404 2.64241 3.23012 0.16366  -0.28109 -0.14076 252 HIS A O   
1401 C CB  . HIS A 252 ? 2.76502 2.55300 3.18020 0.21200  -0.27381 -0.13105 252 HIS A CB  
1402 C CG  . HIS A 252 ? 2.75258 2.56656 3.19797 0.21149  -0.27363 -0.12944 252 HIS A CG  
1403 N ND1 . HIS A 252 ? 2.73942 2.57796 3.21904 0.21924  -0.28545 -0.12339 252 HIS A ND1 
1404 C CD2 . HIS A 252 ? 2.75207 2.57233 3.20120 0.20360  -0.26321 -0.13298 252 HIS A CD2 
1405 C CE1 . HIS A 252 ? 2.73027 2.59105 3.23201 0.21642  -0.28186 -0.12511 252 HIS A CE1 
1406 N NE2 . HIS A 252 ? 2.73809 2.58853 3.22001 0.20619  -0.26853 -0.13042 252 HIS A NE2 
1407 N N   . LYS A 253 ? 2.75429 2.57724 3.16784 0.16599  -0.29463 -0.12670 253 LYS A N   
1408 C CA  . LYS A 253 ? 2.79221 2.62514 3.19912 0.14228  -0.29263 -0.13329 253 LYS A CA  
1409 C C   . LYS A 253 ? 2.84259 2.68117 3.22699 0.12305  -0.30299 -0.13480 253 LYS A C   
1410 O O   . LYS A 253 ? 2.84797 2.70357 3.23660 0.12385  -0.32049 -0.12136 253 LYS A O   
1411 C CB  . LYS A 253 ? 2.78654 2.59587 3.18572 0.14102  -0.27193 -0.14512 253 LYS A CB  
1412 C CG  . LYS A 253 ? 2.81785 2.63701 3.22080 0.11899  -0.26672 -0.15284 253 LYS A CG  
1413 C CD  . LYS A 253 ? 2.82736 2.61475 3.21918 0.11348  -0.24786 -0.16505 253 LYS A CD  
1414 C CE  . LYS A 253 ? 2.78176 2.54970 3.17824 0.13469  -0.23603 -0.15909 253 LYS A CE  
1415 N NZ  . LYS A 253 ? 2.79048 2.52670 3.18063 0.13085  -0.21953 -0.16619 253 LYS A NZ  
1416 N N   . ASN A 254 ? 2.66496 2.49232 3.02840 0.10466  -0.29286 -0.15075 254 ASN A N   
1417 C CA  . ASN A 254 ? 2.71927 2.55514 3.05943 0.08429  -0.29964 -0.15733 254 ASN A CA  
1418 C C   . ASN A 254 ? 2.71837 2.51964 3.03605 0.08862  -0.28589 -0.17213 254 ASN A C   
1419 O O   . ASN A 254 ? 2.76094 2.56250 3.06141 0.06843  -0.28118 -0.18910 254 ASN A O   
1420 C CB  . ASN A 254 ? 2.77545 2.63748 3.11466 0.05408  -0.29957 -0.16847 254 ASN A CB  
1421 C CG  . ASN A 254 ? 2.83854 2.72992 3.15854 0.02915  -0.31234 -0.17051 254 ASN A CG  
1422 O OD1 . ASN A 254 ? 2.85503 2.75303 3.16123 0.00418  -0.30397 -0.19206 254 ASN A OD1 
1423 N ND2 . ASN A 254 ? 2.86150 2.77311 3.18306 0.03432  -0.33248 -0.14833 254 ASN A ND2 
1424 N N   . LEU A 255 ? 2.66617 2.44102 2.98595 0.11424  -0.27886 -0.16722 255 LEU A N   
1425 C CA  . LEU A 255 ? 2.65295 2.39464 2.95669 0.12212  -0.26426 -0.17904 255 LEU A CA  
1426 C C   . LEU A 255 ? 2.63105 2.36530 2.92244 0.13803  -0.27128 -0.17096 255 LEU A C   
1427 O O   . LEU A 255 ? 2.58973 2.32360 2.89385 0.15813  -0.27448 -0.15834 255 LEU A O   
1428 C CB  . LEU A 255 ? 2.61616 2.33568 2.93352 0.13609  -0.24741 -0.17974 255 LEU A CB  
1429 C CG  . LEU A 255 ? 2.63750 2.34647 2.96266 0.12077  -0.23337 -0.19303 255 LEU A CG  
1430 C CD1 . LEU A 255 ? 2.66843 2.40550 3.00555 0.10109  -0.23986 -0.19403 255 LEU A CD1 
1431 C CD2 . LEU A 255 ? 2.60073 2.28825 2.93927 0.13643  -0.21882 -0.18694 255 LEU A CD2 
1432 N N   . THR A 256 ? 2.61313 2.34336 2.88129 0.12775  -0.27262 -0.18045 256 THR A N   
1433 C CA  . THR A 256 ? 2.58372 2.30450 2.83709 0.14050  -0.27737 -0.17517 256 THR A CA  
1434 C C   . THR A 256 ? 2.52233 2.21122 2.76833 0.15628  -0.25969 -0.18490 256 THR A C   
1435 O O   . THR A 256 ? 2.52178 2.19693 2.76344 0.14780  -0.24678 -0.20112 256 THR A O   
1436 C CB  . THR A 256 ? 2.62799 2.36608 2.85902 0.11927  -0.28847 -0.17950 256 THR A CB  
1437 O OG1 . THR A 256 ? 2.67715 2.44981 2.91709 0.10543  -0.30763 -0.16402 256 THR A OG1 
1438 C CG2 . THR A 256 ? 2.59411 2.32004 2.80816 0.13105  -0.29154 -0.17571 256 THR A CG2 
1439 N N   . ILE A 257 ? 2.53480 2.21400 2.78289 0.17864  -0.25891 -0.17527 257 ILE A N   
1440 C CA  . ILE A 257 ? 2.47620 2.13186 2.72025 0.19504  -0.24326 -0.17977 257 ILE A CA  
1441 C C   . ILE A 257 ? 2.43785 2.08748 2.66490 0.20623  -0.24656 -0.17805 257 ILE A C   
1442 O O   . ILE A 257 ? 2.44058 2.10183 2.67014 0.20985  -0.25938 -0.16807 257 ILE A O   
1443 C CB  . ILE A 257 ? 2.44715 2.10338 2.71300 0.21003  -0.23537 -0.17076 257 ILE A CB  
1444 C CG1 . ILE A 257 ? 2.49551 2.15685 2.77756 0.19743  -0.23141 -0.17246 257 ILE A CG1 
1445 C CG2 . ILE A 257 ? 2.40088 2.04021 2.66248 0.22565  -0.22097 -0.17104 257 ILE A CG2 
1446 C CD1 . ILE A 257 ? 2.47551 2.14195 2.77802 0.20848  -0.22370 -0.16340 257 ILE A CD1 
1447 N N   . PHE A 258 ? 2.50407 2.13555 2.71713 0.21161  -0.23495 -0.18738 258 PHE A N   
1448 C CA  . PHE A 258 ? 2.46399 2.08935 2.65875 0.22129  -0.23576 -0.18811 258 PHE A CA  
1449 C C   . PHE A 258 ? 2.40377 2.01673 2.60159 0.24028  -0.22117 -0.18663 258 PHE A C   
1450 O O   . PHE A 258 ? 2.39894 1.99973 2.60146 0.24036  -0.20919 -0.19159 258 PHE A O   
1451 C CB  . PHE A 258 ? 2.48592 2.10846 2.65810 0.20586  -0.23694 -0.20250 258 PHE A CB  
1452 C CG  . PHE A 258 ? 2.45351 2.07286 2.60468 0.21253  -0.23949 -0.20339 258 PHE A CG  
1453 C CD1 . PHE A 258 ? 2.40170 2.00624 2.54634 0.22729  -0.22669 -0.20845 258 PHE A CD1 
1454 C CD2 . PHE A 258 ? 2.48430 2.11752 2.62322 0.20260  -0.25525 -0.19761 258 PHE A CD2 
1455 C CE1 . PHE A 258 ? 2.37508 1.97847 2.49972 0.23230  -0.22860 -0.21039 258 PHE A CE1 
1456 C CE2 . PHE A 258 ? 2.47070 2.10083 2.59049 0.20706  -0.25746 -0.19825 258 PHE A CE2 
1457 C CZ  . PHE A 258 ? 2.40323 2.01827 2.51486 0.22190  -0.24360 -0.20619 258 PHE A CZ  
1458 N N   . LYS A 259 ? 2.59600 2.21421 2.79408 0.25527  -0.22211 -0.17947 259 LYS A N   
1459 C CA  . LYS A 259 ? 2.55435 2.16950 2.75268 0.27136  -0.20923 -0.17722 259 LYS A CA  
1460 C C   . LYS A 259 ? 2.51038 2.11778 2.68535 0.27547  -0.20764 -0.18391 259 LYS A C   
1461 O O   . LYS A 259 ? 2.48636 2.09854 2.65257 0.27736  -0.21551 -0.18382 259 LYS A O   
1462 C CB  . LYS A 259 ? 2.19598 1.82821 2.41122 0.28304  -0.20866 -0.16950 259 LYS A CB  
1463 C CG  . LYS A 259 ? 2.19397 1.83279 2.40913 0.29626  -0.19513 -0.16659 259 LYS A CG  
1464 C CD  . LYS A 259 ? 2.18032 1.84160 2.41833 0.30134  -0.19065 -0.16060 259 LYS A CD  
1465 C CE  . LYS A 259 ? 2.19363 1.87238 2.43919 0.30990  -0.19203 -0.16524 259 LYS A CE  
1466 N NZ  . LYS A 259 ? 2.38713 2.07387 2.61934 0.31892  -0.18198 -0.16796 259 LYS A NZ  
1467 N N   . ALA A 260 ? 2.40652 2.00210 2.57483 0.27688  -0.19745 -0.18928 260 ALA A N   
1468 C CA  . ALA A 260 ? 2.40583 1.99530 2.55234 0.27905  -0.19562 -0.19786 260 ALA A CA  
1469 C C   . ALA A 260 ? 2.39122 1.99017 2.53099 0.29383  -0.19264 -0.19271 260 ALA A C   
1470 O O   . ALA A 260 ? 2.38329 1.99161 2.53539 0.30448  -0.18452 -0.18415 260 ALA A O   
1471 C CB  . ALA A 260 ? 2.41635 1.99233 2.56595 0.27942  -0.18426 -0.20468 260 ALA A CB  
1472 N N   . PRO A 261 ? 2.49637 2.09644 2.61721 0.29293  -0.19861 -0.19800 261 PRO A N   
1473 C CA  . PRO A 261 ? 2.44716 2.05665 2.56173 0.30555  -0.19380 -0.19660 261 PRO A CA  
1474 C C   . PRO A 261 ? 2.41429 2.02373 2.52122 0.31436  -0.18117 -0.19782 261 PRO A C   
1475 O O   . PRO A 261 ? 2.41989 2.01814 2.51728 0.31018  -0.17910 -0.20514 261 PRO A O   
1476 C CB  . PRO A 261 ? 2.45213 2.05939 2.54901 0.29884  -0.20439 -0.20185 261 PRO A CB  
1477 C CG  . PRO A 261 ? 2.49319 2.09159 2.57784 0.28333  -0.21035 -0.20858 261 PRO A CG  
1478 C CD  . PRO A 261 ? 2.52796 2.12401 2.63191 0.27809  -0.20964 -0.20561 261 PRO A CD  
1479 N N   . PHE A 262 ? 2.62277 2.24878 2.73644 0.32580  -0.17258 -0.19100 262 PHE A N   
1480 C CA  . PHE A 262 ? 2.59817 2.23002 2.70977 0.33428  -0.16144 -0.18629 262 PHE A CA  
1481 C C   . PHE A 262 ? 2.57392 2.20051 2.66283 0.33540  -0.16050 -0.19620 262 PHE A C   
1482 O O   . PHE A 262 ? 2.57114 2.19411 2.66096 0.33965  -0.15386 -0.19493 262 PHE A O   
1483 C CB  . PHE A 262 ? 2.57868 2.23898 2.69846 0.34289  -0.15345 -0.17718 262 PHE A CB  
1484 C CG  . PHE A 262 ? 2.57667 2.24868 2.70228 0.34975  -0.14364 -0.16412 262 PHE A CG  
1485 C CD1 . PHE A 262 ? 2.61067 2.27093 2.75519 0.34841  -0.14174 -0.15276 262 PHE A CD1 
1486 C CD2 . PHE A 262 ? 2.54693 2.24342 2.66199 0.35674  -0.13660 -0.16176 262 PHE A CD2 
1487 C CE1 . PHE A 262 ? 2.61774 2.28857 2.77361 0.35485  -0.13412 -0.13617 262 PHE A CE1 
1488 C CE2 . PHE A 262 ? 2.55170 2.26326 2.67495 0.36258  -0.12922 -0.14519 262 PHE A CE2 
1489 C CZ  . PHE A 262 ? 2.58947 2.28731 2.73471 0.36212  -0.12853 -0.13079 262 PHE A CZ  
1490 N N   . TYR A 263 ? 2.62145 2.24791 2.69306 0.33143  -0.16721 -0.20542 263 TYR A N   
1491 C CA  . TYR A 263 ? 2.60754 2.22964 2.65564 0.32942  -0.16752 -0.21607 263 TYR A CA  
1492 C C   . TYR A 263 ? 2.63272 2.24751 2.66758 0.31755  -0.18008 -0.22306 263 TYR A C   
1493 O O   . TYR A 263 ? 2.63257 2.25359 2.66968 0.31853  -0.18433 -0.22098 263 TYR A O   
1494 C CB  . TYR A 263 ? 2.56786 2.20887 2.60588 0.33980  -0.15877 -0.21567 263 TYR A CB  
1495 C CG  . TYR A 263 ? 2.55756 2.19617 2.57262 0.33849  -0.15762 -0.22647 263 TYR A CG  
1496 C CD1 . TYR A 263 ? 2.55170 2.18692 2.56940 0.34249  -0.15127 -0.22765 263 TYR A CD1 
1497 C CD2 . TYR A 263 ? 2.56224 2.20237 2.55655 0.33299  -0.16279 -0.23553 263 TYR A CD2 
1498 C CE1 . TYR A 263 ? 2.54537 2.18132 2.54439 0.34129  -0.14967 -0.23961 263 TYR A CE1 
1499 C CE2 . TYR A 263 ? 2.56192 2.20265 2.53413 0.33037  -0.16161 -0.24602 263 TYR A CE2 
1500 C CZ  . TYR A 263 ? 2.55055 2.19044 2.52453 0.33465  -0.15483 -0.24907 263 TYR A CZ  
1501 O OH  . TYR A 263 ? 2.55098 2.19427 2.50519 0.33209  -0.15308 -0.26157 263 TYR A OH  
1502 N N   . VAL A 264 ? 2.57516 2.17929 2.59941 0.30523  -0.18584 -0.23125 264 VAL A N   
1503 C CA  . VAL A 264 ? 2.61660 2.21921 2.62459 0.29077  -0.19865 -0.23546 264 VAL A CA  
1504 C C   . VAL A 264 ? 2.61089 2.21675 2.59296 0.28824  -0.19598 -0.24686 264 VAL A C   
1505 O O   . VAL A 264 ? 2.59236 2.19780 2.57124 0.29206  -0.18655 -0.25563 264 VAL A O   
1506 C CB  . VAL A 264 ? 2.67313 2.27113 2.68531 0.27408  -0.20761 -0.23737 264 VAL A CB  
1507 C CG1 . VAL A 264 ? 2.67956 2.27312 2.69013 0.26934  -0.19935 -0.25137 264 VAL A CG1 
1508 C CG2 . VAL A 264 ? 2.72909 2.33233 2.72619 0.25713  -0.22314 -0.23578 264 VAL A CG2 
1509 N N   . THR A 265 ? 2.64719 2.25662 2.61405 0.28200  -0.20418 -0.24627 265 THR A N   
1510 C CA  . THR A 265 ? 2.64516 2.26039 2.58717 0.28097  -0.20066 -0.25612 265 THR A CA  
1511 C C   . THR A 265 ? 2.68897 2.30652 2.61136 0.26335  -0.20529 -0.26853 265 THR A C   
1512 O O   . THR A 265 ? 2.66502 2.28683 2.57643 0.26552  -0.19636 -0.28185 265 THR A O   
1513 C CB  . THR A 265 ? 2.66284 2.28072 2.59906 0.28018  -0.20668 -0.25093 265 THR A CB  
1514 O OG1 . THR A 265 ? 2.72527 2.33878 2.66804 0.26654  -0.22271 -0.24093 265 THR A OG1 
1515 C CG2 . THR A 265 ? 2.61430 2.23677 2.56921 0.29709  -0.19763 -0.24627 265 THR A CG2 
1516 N N   . SER A 266 ? 2.71997 2.33903 2.63957 0.24481  -0.21908 -0.26471 266 SER A N   
1517 C CA  . SER A 266 ? 2.75942 2.38956 2.65693 0.22304  -0.22488 -0.27688 266 SER A CA  
1518 C C   . SER A 266 ? 2.73880 2.37012 2.64079 0.22135  -0.21360 -0.29641 266 SER A C   
1519 O O   . SER A 266 ? 2.71261 2.33359 2.63830 0.23333  -0.20517 -0.29582 266 SER A O   
1520 C CB  . SER A 266 ? 2.83182 2.46965 2.72913 0.20192  -0.24267 -0.26518 266 SER A CB  
1521 O OG  . SER A 266 ? 2.87414 2.53041 2.74995 0.17714  -0.24771 -0.27800 266 SER A OG  
1522 N N   . LYS A 267 ? 2.74636 2.39162 2.62799 0.20524  -0.21318 -0.31466 267 LYS A N   
1523 C CA  . LYS A 267 ? 2.75159 2.39982 2.64224 0.20144  -0.20170 -0.33831 267 LYS A CA  
1524 C C   . LYS A 267 ? 2.79042 2.44337 2.69345 0.18334  -0.20620 -0.34354 267 LYS A C   
1525 O O   . LYS A 267 ? 2.77193 2.41529 2.70029 0.18908  -0.19561 -0.35387 267 LYS A O   
1526 C CB  . LYS A 267 ? 2.79167 2.45825 2.65842 0.18844  -0.19882 -0.36008 267 LYS A CB  
1527 C CG  . LYS A 267 ? 2.76547 2.43066 2.62009 0.20536  -0.19246 -0.35874 267 LYS A CG  
1528 C CD  . LYS A 267 ? 2.77478 2.46137 2.60524 0.18987  -0.19033 -0.38149 267 LYS A CD  
1529 C CE  . LYS A 267 ? 2.75781 2.44598 2.57434 0.20510  -0.18460 -0.37998 267 LYS A CE  
1530 N NZ  . LYS A 267 ? 2.95988 2.67148 2.75086 0.18830  -0.18352 -0.40172 267 LYS A NZ  
1531 N N   . ASP A 268 ? 2.61229 2.28173 2.49977 0.16045  -0.22200 -0.33547 268 ASP A N   
1532 C CA  . ASP A 268 ? 2.65972 2.34215 2.55512 0.13889  -0.22784 -0.34007 268 ASP A CA  
1533 C C   . ASP A 268 ? 2.67402 2.35375 2.57654 0.13857  -0.24341 -0.31046 268 ASP A C   
1534 O O   . ASP A 268 ? 2.69697 2.38530 2.58470 0.13137  -0.25799 -0.29215 268 ASP A O   
1535 C CB  . ASP A 268 ? 2.77397 2.49058 2.64509 0.10580  -0.23337 -0.35875 268 ASP A CB  
1536 C CG  . ASP A 268 ? 2.94192 2.66474 2.80707 0.10564  -0.21819 -0.39029 268 ASP A CG  
1537 O OD1 . ASP A 268 ? 2.84364 2.54509 2.73259 0.12752  -0.20212 -0.40174 268 ASP A OD1 
1538 O OD2 . ASP A 268 ? 3.18583 2.93715 3.02454 0.08298  -0.22280 -0.40254 268 ASP A OD2 
1539 N N   . VAL A 269 ? 2.61544 2.28337 2.54395 0.14632  -0.24032 -0.30549 269 VAL A N   
1540 C CA  . VAL A 269 ? 2.63515 2.30357 2.57608 0.14516  -0.25416 -0.28054 269 VAL A CA  
1541 C C   . VAL A 269 ? 2.66705 2.34095 2.62593 0.13383  -0.25167 -0.28876 269 VAL A C   
1542 O O   . VAL A 269 ? 2.63997 2.30256 2.61310 0.13991  -0.23591 -0.30782 269 VAL A O   
1543 C CB  . VAL A 269 ? 2.56297 2.20820 2.52114 0.17414  -0.25182 -0.26138 269 VAL A CB  
1544 C CG1 . VAL A 269 ? 2.52643 2.17055 2.46941 0.18039  -0.25773 -0.25079 269 VAL A CG1 
1545 C CG2 . VAL A 269 ? 2.54779 2.17397 2.52160 0.19571  -0.23288 -0.27195 269 VAL A CG2 
1546 N N   . ASN A 270 ? 2.56967 2.26166 2.53095 0.11701  -0.26749 -0.27326 270 ASN A N   
1547 C CA  . ASN A 270 ? 2.59245 2.29627 2.56781 0.10139  -0.26634 -0.28200 270 ASN A CA  
1548 C C   . ASN A 270 ? 2.63819 2.35051 2.62739 0.09880  -0.28285 -0.25429 270 ASN A C   
1549 O O   . ASN A 270 ? 2.65795 2.37198 2.64541 0.10359  -0.29726 -0.22963 270 ASN A O   
1550 C CB  . ASN A 270 ? 2.62072 2.35859 2.57782 0.06749  -0.26712 -0.30556 270 ASN A CB  
1551 C CG  . ASN A 270 ? 2.65856 2.43259 2.59541 0.04152  -0.28927 -0.28667 270 ASN A CG  
1552 O OD1 . ASN A 270 ? 2.67694 2.45313 2.59622 0.04292  -0.29820 -0.27330 270 ASN A OD1 
1553 N ND2 . ASN A 270 ? 2.67014 2.47489 2.61072 0.01643  -0.29867 -0.28392 270 ASN A ND2 
1554 N N   . THR A 271 ? 2.54672 2.26455 2.55337 0.09100  -0.28027 -0.25923 271 THR A N   
1555 C CA  . THR A 271 ? 2.59568 2.32737 2.61750 0.08555  -0.29575 -0.23545 271 THR A CA  
1556 C C   . THR A 271 ? 2.63408 2.39065 2.66043 0.05961  -0.29443 -0.25041 271 THR A C   
1557 O O   . THR A 271 ? 2.61167 2.35709 2.64581 0.05927  -0.27668 -0.27650 271 THR A O   
1558 C CB  . THR A 271 ? 2.56402 2.26793 2.61249 0.11561  -0.29209 -0.21951 271 THR A CB  
1559 O OG1 . THR A 271 ? 2.61381 2.33400 2.68015 0.10994  -0.30751 -0.19769 271 THR A OG1 
1560 C CG2 . THR A 271 ? 2.52611 2.20735 2.58967 0.12842  -0.27168 -0.23750 271 THR A CG2 
1561 N N   . GLU A 272 ? 2.59505 2.38708 2.61911 0.03698  -0.31329 -0.23343 272 GLU A N   
1562 C CA  . GLU A 272 ? 2.62831 2.45438 2.65357 0.00702  -0.31416 -0.24689 272 GLU A CA  
1563 C C   . GLU A 272 ? 2.66296 2.49362 2.71360 0.01133  -0.32332 -0.22544 272 GLU A C   
1564 O O   . GLU A 272 ? 2.68997 2.52518 2.74995 0.01966  -0.34106 -0.19302 272 GLU A O   
1565 C CB  . GLU A 272 ? 2.65590 2.53260 2.65542 -0.02945 -0.32934 -0.24520 272 GLU A CB  
1566 C CG  . GLU A 272 ? 2.62754 2.50825 2.60057 -0.03864 -0.32090 -0.26880 272 GLU A CG  
1567 C CD  . GLU A 272 ? 2.65196 2.59070 2.59889 -0.07896 -0.33642 -0.26638 272 GLU A CD  
1568 O OE1 . GLU A 272 ? 2.68797 2.66308 2.63843 -0.09827 -0.35522 -0.24205 272 GLU A OE1 
1569 O OE2 . GLU A 272 ? 2.63170 2.58350 2.55542 -0.09242 -0.33028 -0.28785 272 GLU A OE2 
1570 N N   . CYS A 273 ? 2.69861 2.52863 2.76366 0.00523  -0.31105 -0.24414 273 CYS A N   
1571 C CA  . CYS A 273 ? 2.73467 2.57670 2.82206 0.00350  -0.31895 -0.22812 273 CYS A CA  
1572 C C   . CYS A 273 ? 2.76731 2.65404 2.84862 -0.03477 -0.31986 -0.24605 273 CYS A C   
1573 O O   . CYS A 273 ? 2.76075 2.64092 2.84622 -0.04374 -0.30077 -0.27904 273 CYS A O   
1574 C CB  . CYS A 273 ? 2.71012 2.51185 2.82240 0.03096  -0.30297 -0.23246 273 CYS A CB  
1575 S SG  . CYS A 273 ? 2.74715 2.55847 2.88914 0.03663  -0.31275 -0.20925 273 CYS A SG  
1576 N N   . THR A 274 ? 2.70687 2.64115 2.78119 -0.05838 -0.34185 -0.22427 274 THR A N   
1577 C CA  . THR A 274 ? 2.73273 2.72060 2.79934 -0.09886 -0.34462 -0.23932 274 THR A CA  
1578 C C   . THR A 274 ? 2.75939 2.75544 2.85169 -0.09806 -0.34812 -0.22816 274 THR A C   
1579 O O   . THR A 274 ? 2.77767 2.79528 2.88121 -0.09679 -0.36933 -0.19265 274 THR A O   
1580 C CB  . THR A 274 ? 2.74288 2.78622 2.78620 -0.12915 -0.36695 -0.22060 274 THR A CB  
1581 O OG1 . THR A 274 ? 2.76227 2.86671 2.79936 -0.17069 -0.37109 -0.23230 274 THR A OG1 
1582 C CG2 . THR A 274 ? 2.75158 2.79626 2.80608 -0.11333 -0.39284 -0.17003 274 THR A CG2 
1583 N N   . CYS A 275 ? 2.84146 2.81918 2.94668 -0.09802 -0.32704 -0.25808 275 CYS A N   
1584 C CA  . CYS A 275 ? 2.86561 2.84871 2.99473 -0.09809 -0.32692 -0.25244 275 CYS A CA  
1585 C C   . CYS A 275 ? 2.88279 2.91496 3.00710 -0.13986 -0.32229 -0.27908 275 CYS A C   
1586 O O   . CYS A 275 ? 2.87175 2.91346 2.98306 -0.16102 -0.30786 -0.31520 275 CYS A O   
1587 C CB  . CYS A 275 ? 2.85190 2.77762 3.00315 -0.06727 -0.30654 -0.26335 275 CYS A CB  
1588 S SG  . CYS A 275 ? 2.87243 2.79497 3.05479 -0.05237 -0.31227 -0.23984 275 CYS A SG  
1589 N N   . LYS A 276 ? 2.78151 2.84764 2.91863 -0.15242 -0.33385 -0.26312 276 LYS A N   
1590 C CA  . LYS A 276 ? 2.79135 2.91056 2.92537 -0.19388 -0.33034 -0.28681 276 LYS A CA  
1591 C C   . LYS A 276 ? 2.80769 2.90551 2.96777 -0.18858 -0.31425 -0.30269 276 LYS A C   
1592 O O   . LYS A 276 ? 2.80458 2.87300 2.98483 -0.15981 -0.31801 -0.27880 276 LYS A O   
1593 C CB  . LYS A 276 ? 2.79790 2.98745 2.92397 -0.22035 -0.35854 -0.25467 276 LYS A CB  
1594 C CG  . LYS A 276 ? 2.79707 3.05574 2.91178 -0.27059 -0.35609 -0.28103 276 LYS A CG  
1595 C CD  . LYS A 276 ? 2.79517 3.12989 2.89809 -0.29892 -0.38636 -0.24463 276 LYS A CD  
1596 C CE  . LYS A 276 ? 2.79432 3.20708 2.88309 -0.35312 -0.38323 -0.27295 276 LYS A CE  
1597 N NZ  . LYS A 276 ? 2.78795 3.28267 2.86657 -0.38321 -0.41451 -0.23267 276 LYS A NZ  
1598 N N   . PHE A 277 ? 2.87101 2.98550 3.03238 -0.21795 -0.29551 -0.34489 277 PHE A N   
1599 C CA  . PHE A 277 ? 2.88574 2.98524 3.07237 -0.22025 -0.27906 -0.36388 277 PHE A CA  
1600 C C   . PHE A 277 ? 2.88075 3.02522 3.06556 -0.26585 -0.26487 -0.40856 277 PHE A C   
1601 O O   . PHE A 277 ? 2.85749 3.00648 3.03220 -0.28192 -0.25194 -0.44258 277 PHE A O   
1602 C CB  . PHE A 277 ? 2.87693 2.89954 3.08330 -0.18441 -0.25823 -0.37395 277 PHE A CB  
1603 C CG  . PHE A 277 ? 2.88627 2.88893 3.12065 -0.18775 -0.23959 -0.39419 277 PHE A CG  
1604 C CD1 . PHE A 277 ? 2.89704 2.90765 3.14584 -0.18223 -0.24802 -0.37111 277 PHE A CD1 
1605 C CD2 . PHE A 277 ? 2.86604 2.84097 3.11611 -0.19588 -0.21340 -0.43602 277 PHE A CD2 
1606 C CE1 . PHE A 277 ? 2.90154 2.89399 3.17559 -0.18660 -0.23093 -0.38874 277 PHE A CE1 
1607 C CE2 . PHE A 277 ? 2.87624 2.83025 3.15571 -0.19948 -0.19635 -0.45281 277 PHE A CE2 
1608 C CZ  . PHE A 277 ? 2.89551 2.85853 3.18496 -0.19556 -0.20522 -0.42870 277 PHE A CZ  
1609 N N   . LYS A 278 ? 2.89831 3.07935 3.09425 -0.28809 -0.26640 -0.41115 278 LYS A N   
1610 C CA  . LYS A 278 ? 2.89946 3.12849 3.09647 -0.33430 -0.25181 -0.45601 278 LYS A CA  
1611 C C   . LYS A 278 ? 2.88264 3.18245 3.04919 -0.37211 -0.26257 -0.46514 278 LYS A C   
1612 O O   . LYS A 278 ? 2.86576 3.18891 3.02922 -0.40330 -0.24437 -0.51302 278 LYS A O   
1613 C CB  . LYS A 278 ? 2.89129 3.06748 3.11247 -0.33060 -0.21875 -0.50395 278 LYS A CB  
1614 C CG  . LYS A 278 ? 2.89767 3.10636 3.13606 -0.37044 -0.19949 -0.54968 278 LYS A CG  
1615 C CD  . LYS A 278 ? 2.88198 3.03160 3.15182 -0.36291 -0.16739 -0.59432 278 LYS A CD  
1616 C CE  . LYS A 278 ? 2.88497 3.06956 3.17507 -0.40641 -0.14606 -0.64682 278 LYS A CE  
1617 N NZ  . LYS A 278 ? 2.86769 2.99512 3.19586 -0.40003 -0.11453 -0.69188 278 LYS A NZ  
1618 N N   . ASN A 279 ? 2.90131 3.23652 3.04812 -0.36968 -0.29225 -0.41869 279 ASN A N   
1619 C CA  . ASN A 279 ? 2.88440 3.29088 3.00081 -0.40404 -0.30850 -0.41377 279 ASN A CA  
1620 C C   . ASN A 279 ? 2.85903 3.24533 2.95915 -0.40306 -0.29639 -0.44060 279 ASN A C   
1621 O O   . ASN A 279 ? 2.84347 3.29290 2.91800 -0.43876 -0.30370 -0.44949 279 ASN A O   
1622 C CB  . ASN A 279 ? 2.88305 3.37777 2.99267 -0.46017 -0.30724 -0.43968 279 ASN A CB  
1623 C CG  . ASN A 279 ? 2.89242 3.43999 3.00529 -0.46991 -0.33324 -0.39586 279 ASN A CG  
1624 O OD1 . ASN A 279 ? 2.89054 3.42720 3.00507 -0.44244 -0.35820 -0.34205 279 ASN A OD1 
1625 N ND2 . ASN A 279 ? 2.89327 3.50026 3.01029 -0.50961 -0.32715 -0.41974 279 ASN A ND2 
1626 N N   . ASN A 280 ? 2.88113 3.18574 2.99562 -0.36459 -0.27850 -0.45292 280 ASN A N   
1627 C CA  . ASN A 280 ? 2.85481 3.13438 2.95667 -0.35690 -0.26835 -0.47331 280 ASN A CA  
1628 C C   . ASN A 280 ? 2.85445 3.08816 2.94812 -0.31417 -0.28500 -0.42734 280 ASN A C   
1629 O O   . ASN A 280 ? 2.87276 3.07021 2.98127 -0.28161 -0.29428 -0.39188 280 ASN A O   
1630 C CB  . ASN A 280 ? 2.84041 3.06392 2.96854 -0.34602 -0.23476 -0.52295 280 ASN A CB  
1631 C CG  . ASN A 280 ? 2.84567 3.11091 2.98770 -0.38898 -0.21469 -0.57548 280 ASN A CG  
1632 O OD1 . ASN A 280 ? 2.83925 3.18490 2.96171 -0.43402 -0.22219 -0.58760 280 ASN A OD1 
1633 N ND2 . ASN A 280 ? 2.85649 3.06956 3.03444 -0.37681 -0.18881 -0.60687 280 ASN A ND2 
1634 N N   . ASN A 281 ? 2.83550 3.07336 2.90662 -0.31576 -0.28776 -0.43050 281 ASN A N   
1635 C CA  . ASN A 281 ? 2.83280 3.02983 2.89510 -0.27876 -0.30164 -0.39212 281 ASN A CA  
1636 C C   . ASN A 281 ? 2.80798 2.93870 2.87823 -0.24980 -0.27859 -0.41901 281 ASN A C   
1637 O O   . ASN A 281 ? 2.78263 2.92452 2.84650 -0.26878 -0.26215 -0.46075 281 ASN A O   
1638 C CB  . ASN A 281 ? 2.82629 3.07906 2.85696 -0.30172 -0.32504 -0.36845 281 ASN A CB  
1639 C CG  . ASN A 281 ? 2.82633 3.03892 2.85168 -0.26490 -0.34110 -0.32570 281 ASN A CG  
1640 O OD1 . ASN A 281 ? 2.82252 2.97821 2.86830 -0.22462 -0.34037 -0.30523 281 ASN A OD1 
1641 N ND2 . ASN A 281 ? 2.83044 3.07558 2.82905 -0.28057 -0.35521 -0.31309 281 ASN A ND2 
1642 N N   . TYR A 282 ? 2.76802 2.83423 2.85409 -0.20501 -0.27739 -0.39549 282 TYR A N   
1643 C CA  . TYR A 282 ? 2.73777 2.74099 2.83477 -0.17431 -0.25726 -0.41371 282 TYR A CA  
1644 C C   . TYR A 282 ? 2.72610 2.70173 2.80843 -0.14352 -0.27038 -0.38007 282 TYR A C   
1645 O O   . TYR A 282 ? 2.74405 2.71267 2.82905 -0.12470 -0.28790 -0.33956 282 TYR A O   
1646 C CB  . TYR A 282 ? 2.73970 2.69248 2.87067 -0.15010 -0.24130 -0.41795 282 TYR A CB  
1647 C CG  . TYR A 282 ? 2.75860 2.73620 2.90783 -0.17893 -0.23010 -0.44557 282 TYR A CG  
1648 C CD1 . TYR A 282 ? 2.73890 2.71173 2.90466 -0.19624 -0.20527 -0.49518 282 TYR A CD1 
1649 C CD2 . TYR A 282 ? 2.79501 2.80130 2.94864 -0.18890 -0.24367 -0.42338 282 TYR A CD2 
1650 C CE1 . TYR A 282 ? 2.75580 2.75110 2.94104 -0.22400 -0.19356 -0.52318 282 TYR A CE1 
1651 C CE2 . TYR A 282 ? 2.80988 2.84090 2.97954 -0.21661 -0.23295 -0.44951 282 TYR A CE2 
1652 C CZ  . TYR A 282 ? 2.79076 2.81569 2.97574 -0.23467 -0.20751 -0.50000 282 TYR A CZ  
1653 O OH  . TYR A 282 ? 2.80644 2.85587 3.01003 -0.26371 -0.19542 -0.52872 282 TYR A OH  
1654 N N   . LYS A 283 ? 2.60935 2.57055 2.67919 -0.13880 -0.26110 -0.39878 283 LYS A N   
1655 C CA  . LYS A 283 ? 2.58972 2.52338 2.64562 -0.11070 -0.27019 -0.37271 283 LYS A CA  
1656 C C   . LYS A 283 ? 2.54612 2.41784 2.61971 -0.07571 -0.24982 -0.38540 283 LYS A C   
1657 O O   . LYS A 283 ? 2.51945 2.38195 2.60013 -0.08152 -0.23022 -0.42276 283 LYS A O   
1658 C CB  . LYS A 283 ? 2.58164 2.55442 2.60555 -0.13445 -0.27865 -0.37905 283 LYS A CB  
1659 C CG  . LYS A 283 ? 2.55397 2.49590 2.56410 -0.10659 -0.28479 -0.35783 283 LYS A CG  
1660 C CD  . LYS A 283 ? 2.57070 2.55878 2.54973 -0.13013 -0.30567 -0.33964 283 LYS A CD  
1661 C CE  . LYS A 283 ? 2.53986 2.54142 2.49739 -0.14524 -0.29467 -0.37252 283 LYS A CE  
1662 N NZ  . LYS A 283 ? 2.55297 2.59727 2.47933 -0.16680 -0.31599 -0.35003 283 LYS A NZ  
1663 N N   . ILE A 284 ? 2.47604 2.30915 2.55947 -0.04051 -0.25445 -0.35455 284 ILE A N   
1664 C CA  . ILE A 284 ? 2.46468 2.24447 2.56441 -0.00688 -0.23789 -0.35873 284 ILE A CA  
1665 C C   . ILE A 284 ? 2.45103 2.21803 2.53050 0.01215  -0.24457 -0.34324 284 ILE A C   
1666 O O   . ILE A 284 ? 2.43734 2.20369 2.51040 0.02553  -0.26054 -0.31066 284 ILE A O   
1667 C CB  . ILE A 284 ? 2.45286 2.20411 2.57828 0.01646  -0.23613 -0.33808 284 ILE A CB  
1668 C CG1 . ILE A 284 ? 2.46575 2.24034 2.60592 -0.00659 -0.23617 -0.34565 284 ILE A CG1 
1669 C CG2 . ILE A 284 ? 2.44831 2.15299 2.59483 0.04253  -0.21628 -0.34733 284 ILE A CG2 
1670 C CD1 . ILE A 284 ? 2.45561 2.20691 2.62076 0.01318  -0.23446 -0.32652 284 ILE A CD1 
1671 N N   . VAL A 285 ? 2.50798 2.26547 2.58057 0.01313  -0.23174 -0.36800 285 VAL A N   
1672 C CA  . VAL A 285 ? 2.47418 2.22095 2.52672 0.02919  -0.23568 -0.35808 285 VAL A CA  
1673 C C   . VAL A 285 ? 2.41985 2.12003 2.49062 0.06423  -0.22080 -0.35626 285 VAL A C   
1674 O O   . VAL A 285 ? 2.39999 2.08194 2.49246 0.06771  -0.20251 -0.37993 285 VAL A O   
1675 C CB  . VAL A 285 ? 2.47127 2.24663 2.50155 0.00455  -0.23283 -0.38607 285 VAL A CB  
1676 C CG1 . VAL A 285 ? 2.42867 2.18741 2.44178 0.02372  -0.23269 -0.38013 285 VAL A CG1 
1677 C CG2 . VAL A 285 ? 2.52041 2.34939 2.52817 -0.03122 -0.25132 -0.37954 285 VAL A CG2 
1678 N N   . LEU A 286 ? 2.53087 2.21422 2.59601 0.08909  -0.22851 -0.32796 286 LEU A N   
1679 C CA  . LEU A 286 ? 2.47561 2.12307 2.55540 0.12100  -0.21662 -0.32114 286 LEU A CA  
1680 C C   . LEU A 286 ? 2.43528 2.07814 2.49398 0.13287  -0.21691 -0.31985 286 LEU A C   
1681 O O   . LEU A 286 ? 2.44848 2.10837 2.48385 0.12564  -0.23124 -0.30832 286 LEU A O   
1682 C CB  . LEU A 286 ? 2.46976 2.10522 2.56406 0.14007  -0.22242 -0.29233 286 LEU A CB  
1683 C CG  . LEU A 286 ? 2.48768 2.11460 2.61034 0.14020  -0.21559 -0.29184 286 LEU A CG  
1684 C CD1 . LEU A 286 ? 2.55054 2.20398 2.67333 0.11022  -0.22172 -0.30315 286 LEU A CD1 
1685 C CD2 . LEU A 286 ? 2.46985 2.08905 2.60440 0.16021  -0.22097 -0.26442 286 LEU A CD2 
1686 N N   . LYS A 287 ? 2.50224 2.12297 2.57154 0.15062  -0.20142 -0.33015 287 LYS A N   
1687 C CA  . LYS A 287 ? 2.45963 2.07610 2.51135 0.16337  -0.19933 -0.33060 287 LYS A CA  
1688 C C   . LYS A 287 ? 2.41682 2.00703 2.48924 0.19166  -0.18589 -0.32383 287 LYS A C   
1689 O O   . LYS A 287 ? 2.40813 1.98375 2.50995 0.19627  -0.17531 -0.32781 287 LYS A O   
1690 C CB  . LYS A 287 ? 2.45967 2.09253 2.49740 0.14428  -0.19447 -0.36075 287 LYS A CB  
1691 C CG  . LYS A 287 ? 2.49285 2.16030 2.50269 0.11446  -0.20976 -0.36343 287 LYS A CG  
1692 C CD  . LYS A 287 ? 2.47725 2.16708 2.47350 0.09293  -0.20342 -0.39642 287 LYS A CD  
1693 C CE  . LYS A 287 ? 2.49385 2.17497 2.47708 0.10872  -0.19773 -0.40061 287 LYS A CE  
1694 N NZ  . LYS A 287 ? 2.53826 2.24550 2.50939 0.08613  -0.19140 -0.43501 287 LYS A NZ  
1695 N N   . PRO A 288 ? 2.57541 2.16156 2.63468 0.20949  -0.18622 -0.31227 288 PRO A N   
1696 C CA  . PRO A 288 ? 2.50986 2.07881 2.58774 0.23450  -0.17440 -0.30301 288 PRO A CA  
1697 C C   . PRO A 288 ? 2.49738 2.05927 2.58778 0.23793  -0.16075 -0.32329 288 PRO A C   
1698 O O   . PRO A 288 ? 2.51164 2.08424 2.58794 0.22428  -0.16013 -0.34590 288 PRO A O   
1699 C CB  . PRO A 288 ? 2.45884 2.03322 2.51571 0.24811  -0.18031 -0.28627 288 PRO A CB  
1700 C CG  . PRO A 288 ? 2.48916 2.07852 2.51626 0.23102  -0.19069 -0.29571 288 PRO A CG  
1701 C CD  . PRO A 288 ? 2.56419 2.16344 2.59298 0.20678  -0.19820 -0.30403 288 PRO A CD  
1702 N N   . LYS A 289 ? 2.63428 2.18045 2.75426 0.25596  -0.15000 -0.31393 289 LYS A N   
1703 C CA  . LYS A 289 ? 2.62007 2.15783 2.76106 0.26477  -0.13714 -0.32714 289 LYS A CA  
1704 C C   . LYS A 289 ? 2.56104 2.10914 2.67794 0.27601  -0.13760 -0.32514 289 LYS A C   
1705 O O   . LYS A 289 ? 2.53309 2.09155 2.62116 0.27908  -0.14644 -0.31110 289 LYS A O   
1706 C CB  . LYS A 289 ? 2.62460 2.14490 2.80627 0.28139  -0.12803 -0.30938 289 LYS A CB  
1707 C CG  . LYS A 289 ? 2.60266 2.10938 2.82337 0.28754  -0.11445 -0.32366 289 LYS A CG  
1708 C CD  . LYS A 289 ? 2.56663 2.05723 2.82910 0.30298  -0.10813 -0.29811 289 LYS A CD  
1709 C CE  . LYS A 289 ? 2.58423 2.05796 2.89636 0.30956  -0.09506 -0.30992 289 LYS A CE  
1710 N NZ  . LYS A 289 ? 2.62115 2.10358 2.92956 0.32239  -0.09157 -0.31472 289 LYS A NZ  
1711 N N   . TYR A 290 ? 3.22283 2.76863 3.35495 0.28198  -0.12745 -0.34066 290 TYR A N   
1712 C CA  . TYR A 290 ? 3.17837 2.73420 3.29389 0.29619  -0.12614 -0.33507 290 TYR A CA  
1713 C C   . TYR A 290 ? 3.13907 2.69507 3.25863 0.31586  -0.12696 -0.30169 290 TYR A C   
1714 O O   . TYR A 290 ? 3.13581 2.68313 3.29016 0.32949  -0.11967 -0.28701 290 TYR A O   
1715 C CB  . TYR A 290 ? 2.65429 2.20754 2.79619 0.30328  -0.11416 -0.35327 290 TYR A CB  
1716 C CG  . TYR A 290 ? 2.64276 2.20540 2.78035 0.32384  -0.11131 -0.33789 290 TYR A CG  
1717 C CD1 . TYR A 290 ? 2.63071 2.21176 2.72624 0.32193  -0.11678 -0.34062 290 TYR A CD1 
1718 C CD2 . TYR A 290 ? 2.64531 2.20084 2.82229 0.34388  -0.10358 -0.31888 290 TYR A CD2 
1719 C CE1 . TYR A 290 ? 2.62057 2.21400 2.71159 0.33918  -0.11354 -0.32791 290 TYR A CE1 
1720 C CE2 . TYR A 290 ? 2.63539 2.20582 2.80855 0.36112  -0.10158 -0.30309 290 TYR A CE2 
1721 C CZ  . TYR A 290 ? 2.62255 2.21258 2.75173 0.35855  -0.10605 -0.30920 290 TYR A CZ  
1722 O OH  . TYR A 290 ? 2.61310 2.22151 2.73800 0.37418  -0.10343 -0.29494 290 TYR A OH  
1723 N N   . GLU A 291 ? 2.99243 2.56024 3.08008 0.31578  -0.13567 -0.28950 291 GLU A N   
1724 C CA  . GLU A 291 ? 2.97690 2.55120 3.06842 0.33084  -0.13551 -0.26202 291 GLU A CA  
1725 C C   . GLU A 291 ? 2.99041 2.57521 3.08951 0.34787  -0.12753 -0.25315 291 GLU A C   
1726 O O   . GLU A 291 ? 3.06797 2.66267 3.14716 0.34861  -0.12665 -0.26513 291 GLU A O   
1727 C CB  . GLU A 291 ? 2.88925 2.47489 2.95001 0.32636  -0.14512 -0.25612 291 GLU A CB  
1728 C CG  . GLU A 291 ? 2.83815 2.43733 2.86674 0.32622  -0.14747 -0.26379 291 GLU A CG  
1729 C CD  . GLU A 291 ? 2.87166 2.46931 2.88122 0.31008  -0.15158 -0.28707 291 GLU A CD  
1730 O OE1 . GLU A 291 ? 2.86831 2.45713 2.88876 0.29753  -0.15250 -0.29947 291 GLU A OE1 
1731 O OE2 . GLU A 291 ? 3.00195 2.61053 2.98543 0.30810  -0.15343 -0.29393 291 GLU A OE2 
1732 N N   . LYS A 292 ? 2.98729 2.57199 3.11715 0.36030  -0.12200 -0.23133 292 LYS A N   
1733 C CA  . LYS A 292 ? 2.97033 2.57356 3.10592 0.37600  -0.11664 -0.21515 292 LYS A CA  
1734 C C   . LYS A 292 ? 2.92904 2.55694 3.02821 0.37710  -0.12019 -0.21017 292 LYS A C   
1735 O O   . LYS A 292 ? 2.92308 2.56200 3.01894 0.37717  -0.12238 -0.19528 292 LYS A O   
1736 C CB  . LYS A 292 ? 3.09522 2.70009 3.26883 0.38630  -0.11244 -0.18611 292 LYS A CB  
1737 C CG  . LYS A 292 ? 3.10732 2.68630 3.32606 0.38713  -0.10724 -0.18960 292 LYS A CG  
1738 C CD  . LYS A 292 ? 3.11545 2.69883 3.37357 0.39776  -0.10410 -0.15474 292 LYS A CD  
1739 C CE  . LYS A 292 ? 3.13871 2.69260 3.44913 0.39853  -0.09846 -0.15744 292 LYS A CE  
1740 N NZ  . LYS A 292 ? 3.13751 2.66627 3.45050 0.38274  -0.09931 -0.17887 292 LYS A NZ  
1741 N N   . LYS A 293 ? 2.99429 2.63171 3.06780 0.37650  -0.12014 -0.22518 293 LYS A N   
1742 C CA  . LYS A 293 ? 2.97193 2.63247 3.01440 0.37723  -0.12178 -0.22303 293 LYS A CA  
1743 C C   . LYS A 293 ? 2.94577 2.63477 2.99759 0.39102  -0.11494 -0.20334 293 LYS A C   
1744 O O   . LYS A 293 ? 2.92722 2.63233 2.96853 0.39626  -0.11145 -0.20780 293 LYS A O   
1745 C CB  . LYS A 293 ? 2.97391 2.63317 2.98497 0.36831  -0.12509 -0.24646 293 LYS A CB  
1746 C CG  . LYS A 293 ? 2.97123 2.60848 2.97579 0.35223  -0.13271 -0.26262 293 LYS A CG  
1747 C CD  . LYS A 293 ? 2.98427 2.62355 2.96014 0.34063  -0.13627 -0.28440 293 LYS A CD  
1748 C CE  . LYS A 293 ? 2.96583 2.61216 2.94865 0.34746  -0.12806 -0.29546 293 LYS A CE  
1749 N NZ  . LYS A 293 ? 2.95413 2.58534 2.95718 0.33927  -0.12595 -0.31399 293 LYS A NZ  
1750 N N   . VAL A 294 ? 2.79613 2.49562 2.86806 0.39547  -0.11340 -0.18001 294 VAL A N   
1751 C CA  . VAL A 294 ? 2.77603 2.51176 2.85612 0.40512  -0.10815 -0.15654 294 VAL A CA  
1752 C C   . VAL A 294 ? 2.74665 2.50935 2.80996 0.40021  -0.10804 -0.15163 294 VAL A C   
1753 O O   . VAL A 294 ? 2.76577 2.53939 2.84584 0.39938  -0.10749 -0.13384 294 VAL A O   
1754 C CB  . VAL A 294 ? 2.80930 2.54212 2.93174 0.41285  -0.10590 -0.13055 294 VAL A CB  
1755 C CG1 . VAL A 294 ? 2.81456 2.59148 2.94549 0.42133  -0.10197 -0.10256 294 VAL A CG1 
1756 C CG2 . VAL A 294 ? 2.80187 2.50307 2.94792 0.41653  -0.10481 -0.14226 294 VAL A CG2 
1757 N N   . ILE A 295 ? 2.62445 2.39890 2.65712 0.39593  -0.10793 -0.16903 295 ILE A N   
1758 C CA  . ILE A 295 ? 2.63385 2.43329 2.65477 0.39058  -0.10624 -0.17100 295 ILE A CA  
1759 C C   . ILE A 295 ? 2.62233 2.47281 2.64403 0.39467  -0.09848 -0.15482 295 ILE A C   
1760 O O   . ILE A 295 ? 2.59924 2.46980 2.60569 0.39745  -0.09494 -0.15909 295 ILE A O   
1761 C CB  . ILE A 295 ? 2.63165 2.42129 2.62541 0.38337  -0.10906 -0.19597 295 ILE A CB  
1762 C CG1 . ILE A 295 ? 2.63502 2.38091 2.62680 0.37711  -0.11816 -0.20859 295 ILE A CG1 
1763 C CG2 . ILE A 295 ? 2.56215 2.37430 2.55385 0.37824  -0.10626 -0.20075 295 ILE A CG2 
1764 C CD1 . ILE A 295 ? 2.49465 2.23048 2.46280 0.36846  -0.12317 -0.22789 295 ILE A CD1 
1765 N N   . HIS A 296 ? 2.43825 2.31427 2.47738 0.39340  -0.09597 -0.13570 296 HIS A N   
1766 C CA  . HIS A 296 ? 2.43042 2.36487 2.46999 0.39316  -0.08895 -0.11879 296 HIS A CA  
1767 C C   . HIS A 296 ? 2.42407 2.38728 2.43923 0.38567  -0.08322 -0.14194 296 HIS A C   
1768 O O   . HIS A 296 ? 2.43725 2.42574 2.45507 0.37792  -0.07908 -0.14750 296 HIS A O   
1769 C CB  . HIS A 296 ? 2.46884 2.42580 2.53223 0.38999  -0.08819 -0.09389 296 HIS A CB  
1770 C CG  . HIS A 296 ? 2.51791 2.43558 2.60865 0.39492  -0.09398 -0.07664 296 HIS A CG  
1771 N ND1 . HIS A 296 ? 2.52807 2.39652 2.62338 0.39284  -0.09927 -0.09117 296 HIS A ND1 
1772 C CD2 . HIS A 296 ? 2.55137 2.47281 2.66954 0.40095  -0.09507 -0.04603 296 HIS A CD2 
1773 C CE1 . HIS A 296 ? 2.56409 2.40773 2.68686 0.39660  -0.10211 -0.07356 296 HIS A CE1 
1774 N NE2 . HIS A 296 ? 2.58578 2.45836 2.72495 0.40217  -0.09966 -0.04572 296 HIS A NE2 
1775 N N   . GLY A 297 ? 2.26931 2.22888 2.26307 0.38735  -0.08224 -0.15766 297 GLY A N   
1776 C CA  . GLY A 297 ? 2.26074 2.23987 2.23333 0.37989  -0.07676 -0.18218 297 GLY A CA  
1777 C C   . GLY A 297 ? 2.25939 2.25634 2.21061 0.38182  -0.07328 -0.18908 297 GLY A C   
1778 O O   . GLY A 297 ? 2.26377 2.26988 2.21899 0.38960  -0.07403 -0.17179 297 GLY A O   
1779 N N   . CYS A 298 ? 2.28897 2.29039 2.22067 0.37462  -0.06941 -0.21478 298 CYS A N   
1780 C CA  . CYS A 298 ? 2.27743 2.30210 2.18631 0.37356  -0.06452 -0.22510 298 CYS A CA  
1781 C C   . CYS A 298 ? 2.25816 2.23891 2.14892 0.37025  -0.06966 -0.24859 298 CYS A C   
1782 O O   . CYS A 298 ? 2.25675 2.21313 2.14973 0.36383  -0.07204 -0.26367 298 CYS A O   
1783 C CB  . CYS A 298 ? 2.27391 2.35923 2.17652 0.36424  -0.05242 -0.23424 298 CYS A CB  
1784 S SG  . CYS A 298 ? 2.31598 2.46267 2.23928 0.36216  -0.04672 -0.20699 298 CYS A SG  
1785 N N   . ASN A 299 ? 2.38824 2.36175 2.26348 0.37393  -0.07171 -0.25055 299 ASN A N   
1786 C CA  . ASN A 299 ? 2.37515 2.31354 2.23028 0.36856  -0.07699 -0.27073 299 ASN A CA  
1787 C C   . ASN A 299 ? 2.41132 2.38296 2.24263 0.36338  -0.06929 -0.28501 299 ASN A C   
1788 O O   . ASN A 299 ? 2.41484 2.40671 2.23723 0.36854  -0.06713 -0.28031 299 ASN A O   
1789 C CB  . ASN A 299 ? 2.41458 2.31869 2.27135 0.37426  -0.08505 -0.26616 299 ASN A CB  
1790 C CG  . ASN A 299 ? 2.44996 2.32481 2.28394 0.36544  -0.09100 -0.28615 299 ASN A CG  
1791 O OD1 . ASN A 299 ? 2.45527 2.34624 2.26832 0.36280  -0.08770 -0.29685 299 ASN A OD1 
1792 N ND2 . ASN A 299 ? 2.49088 2.32621 2.32872 0.35941  -0.10029 -0.28992 299 ASN A ND2 
1793 N N   . PHE A 300 ? 2.36477 2.34236 2.18926 0.35310  -0.06477 -0.30322 300 PHE A N   
1794 C CA  . PHE A 300 ? 2.40562 2.41059 2.20799 0.34539  -0.05695 -0.32078 300 PHE A CA  
1795 C C   . PHE A 300 ? 2.48102 2.44930 2.26274 0.33906  -0.06416 -0.33496 300 PHE A C   
1796 O O   . PHE A 300 ? 2.50790 2.48995 2.27206 0.33000  -0.05873 -0.35198 300 PHE A O   
1797 C CB  . PHE A 300 ? 2.42716 2.45777 2.23740 0.33578  -0.04677 -0.33675 300 PHE A CB  
1798 C CG  . PHE A 300 ? 2.34849 2.41395 2.18085 0.33820  -0.04057 -0.32527 300 PHE A CG  
1799 C CD1 . PHE A 300 ? 2.32657 2.45532 2.15575 0.33777  -0.03066 -0.31690 300 PHE A CD1 
1800 C CD2 . PHE A 300 ? 2.29641 2.33581 2.15283 0.33934  -0.04508 -0.32181 300 PHE A CD2 
1801 C CE1 . PHE A 300 ? 2.24700 2.41372 2.09538 0.33695  -0.02543 -0.30484 300 PHE A CE1 
1802 C CE2 . PHE A 300 ? 2.25340 2.32811 2.12938 0.33969  -0.03919 -0.31197 300 PHE A CE2 
1803 C CZ  . PHE A 300 ? 2.22373 2.36288 2.09506 0.33771  -0.02936 -0.30331 300 PHE A CZ  
1804 N N   . SER A 301 ? 2.51514 2.44068 2.29868 0.34159  -0.07587 -0.32878 301 SER A N   
1805 C CA  . SER A 301 ? 2.56348 2.45697 2.32812 0.33198  -0.08418 -0.34074 301 SER A CA  
1806 C C   . SER A 301 ? 2.57380 2.48463 2.31487 0.33209  -0.08190 -0.34687 301 SER A C   
1807 O O   . SER A 301 ? 2.53570 2.46595 2.28202 0.34318  -0.07889 -0.33717 301 SER A O   
1808 C CB  . SER A 301 ? 2.57126 2.42129 2.34602 0.33159  -0.09702 -0.33326 301 SER A CB  
1809 O OG  . SER A 301 ? 2.58789 2.42111 2.38388 0.33007  -0.10021 -0.32914 301 SER A OG  
1810 N N   . SER A 302 ? 2.63464 2.53860 2.35274 0.31940  -0.08371 -0.36224 302 SER A N   
1811 C CA  . SER A 302 ? 2.67029 2.59026 2.36359 0.31655  -0.08202 -0.37162 302 SER A CA  
1812 C C   . SER A 302 ? 2.68672 2.57837 2.37332 0.31294  -0.09250 -0.37336 302 SER A C   
1813 O O   . SER A 302 ? 2.70335 2.59469 2.36595 0.30149  -0.09518 -0.38603 302 SER A O   
1814 C CB  . SER A 302 ? 2.70812 2.63884 2.37977 0.30230  -0.07775 -0.38812 302 SER A CB  
1815 O OG  . SER A 302 ? 2.74975 2.64640 2.42692 0.29075  -0.08503 -0.39087 302 SER A OG  
1816 N N   . ASN A 303 ? 2.82070 2.69136 2.52847 0.32058  -0.09794 -0.36237 303 ASN A N   
1817 C CA  . ASN A 303 ? 2.83155 2.67874 2.53677 0.31507  -0.10661 -0.36700 303 ASN A CA  
1818 C C   . ASN A 303 ? 2.75780 2.60534 2.48937 0.33058  -0.10417 -0.35820 303 ASN A C   
1819 O O   . ASN A 303 ? 2.71810 2.56947 2.47307 0.34285  -0.10077 -0.34254 303 ASN A O   
1820 C CB  . ASN A 303 ? 2.86223 2.67479 2.56881 0.30193  -0.11858 -0.36454 303 ASN A CB  
1821 C CG  . ASN A 303 ? 2.83662 2.62941 2.55068 0.29824  -0.12626 -0.36555 303 ASN A CG  
1822 O OD1 . ASN A 303 ? 2.86069 2.63798 2.59873 0.30530  -0.12842 -0.35519 303 ASN A OD1 
1823 N ND2 . ASN A 303 ? 2.80520 2.60176 2.49916 0.28551  -0.12956 -0.37997 303 ASN A ND2 
1824 N N   . VAL A 304 ? 2.85802 2.70298 2.58826 0.32881  -0.10551 -0.36918 304 VAL A N   
1825 C CA  . VAL A 304 ? 2.80978 2.65218 2.57106 0.34276  -0.10257 -0.36415 304 VAL A CA  
1826 C C   . VAL A 304 ? 2.81122 2.62077 2.58688 0.33604  -0.11001 -0.36582 304 VAL A C   
1827 O O   . VAL A 304 ? 2.77917 2.57736 2.58587 0.34713  -0.10884 -0.35342 304 VAL A O   
1828 C CB  . VAL A 304 ? 2.80140 2.66544 2.56143 0.34665  -0.09695 -0.37854 304 VAL A CB  
1829 C CG1 . VAL A 304 ? 2.84358 2.70648 2.57133 0.32617  -0.10138 -0.40210 304 VAL A CG1 
1830 C CG2 . VAL A 304 ? 2.76359 2.61966 2.56357 0.35983  -0.09407 -0.37664 304 VAL A CG2 
1831 N N   . SER A 305 ? 2.86652 2.66343 2.61999 0.31618  -0.11804 -0.37968 305 SER A N   
1832 C CA  . SER A 305 ? 2.87612 2.64924 2.64002 0.30584  -0.12540 -0.38345 305 SER A CA  
1833 C C   . SER A 305 ? 2.89007 2.64350 2.66023 0.30444  -0.13240 -0.36575 305 SER A C   
1834 O O   . SER A 305 ? 2.93292 2.67762 2.68537 0.28907  -0.14172 -0.36445 305 SER A O   
1835 C CB  . SER A 305 ? 2.91443 2.69073 2.65181 0.28236  -0.13192 -0.40324 305 SER A CB  
1836 O OG  . SER A 305 ? 2.96425 2.73999 2.67272 0.26771  -0.13999 -0.39844 305 SER A OG  
1837 N N   . SER A 306 ? 2.78981 2.53768 2.58883 0.32064  -0.12812 -0.35067 306 SER A N   
1838 C CA  . SER A 306 ? 2.79600 2.52846 2.60640 0.32138  -0.13312 -0.33492 306 SER A CA  
1839 C C   . SER A 306 ? 2.79106 2.50334 2.62657 0.32121  -0.13618 -0.33194 306 SER A C   
1840 O O   . SER A 306 ? 2.76551 2.47787 2.62308 0.33054  -0.12983 -0.33402 306 SER A O   
1841 C CB  . SER A 306 ? 2.76011 2.50828 2.58229 0.33712  -0.12541 -0.31962 306 SER A CB  
1842 O OG  . SER A 306 ? 2.75182 2.48684 2.59101 0.33853  -0.12899 -0.30652 306 SER A OG  
1843 N N   . LYS A 307 ? 2.68717 2.38271 2.52248 0.31022  -0.14589 -0.32704 307 LYS A N   
1844 C CA  . LYS A 307 ? 2.68964 2.36802 2.54893 0.30924  -0.14869 -0.32291 307 LYS A CA  
1845 C C   . LYS A 307 ? 2.65286 2.32870 2.53995 0.32610  -0.14325 -0.30468 307 LYS A C   
1846 O O   . LYS A 307 ? 2.66449 2.32576 2.57261 0.32548  -0.14547 -0.29910 307 LYS A O   
1847 C CB  . LYS A 307 ? 2.73780 2.40421 2.58834 0.29130  -0.16197 -0.32100 307 LYS A CB  
1848 C CG  . LYS A 307 ? 2.77697 2.44971 2.60000 0.26999  -0.16984 -0.33485 307 LYS A CG  
1849 C CD  . LYS A 307 ? 2.83252 2.49705 2.65172 0.25292  -0.18471 -0.32550 307 LYS A CD  
1850 C CE  . LYS A 307 ? 2.88092 2.55719 2.67077 0.22937  -0.19433 -0.33362 307 LYS A CE  
1851 N NZ  . LYS A 307 ? 2.94367 2.61554 2.73264 0.21202  -0.21092 -0.31893 307 LYS A NZ  
1852 N N   . HIS A 308 ? 2.66398 2.35724 2.55074 0.33867  -0.13642 -0.29526 308 HIS A N   
1853 C CA  . HIS A 308 ? 2.63621 2.33536 2.54658 0.35147  -0.13155 -0.27687 308 HIS A CA  
1854 C C   . HIS A 308 ? 2.57397 2.29835 2.49069 0.36555  -0.12142 -0.26951 308 HIS A C   
1855 O O   . HIS A 308 ? 2.56659 2.31110 2.46293 0.36589  -0.11798 -0.27575 308 HIS A O   
1856 C CB  . HIS A 308 ? 2.64216 2.34555 2.54824 0.34878  -0.13448 -0.27090 308 HIS A CB  
1857 C CG  . HIS A 308 ? 2.68376 2.36630 2.58358 0.33478  -0.14610 -0.27584 308 HIS A CG  
1858 N ND1 . HIS A 308 ? 2.72304 2.39225 2.64187 0.33287  -0.15170 -0.26713 308 HIS A ND1 
1859 C CD2 . HIS A 308 ? 2.69814 2.37402 2.57616 0.32108  -0.15409 -0.28609 308 HIS A CD2 
1860 C CE1 . HIS A 308 ? 2.76112 2.41698 2.67160 0.31939  -0.16307 -0.27078 308 HIS A CE1 
1861 N NE2 . HIS A 308 ? 2.74686 2.40657 2.63260 0.31146  -0.16507 -0.28115 308 HIS A NE2 
1862 N N   . THR A 309 ? 2.72802 2.45313 2.67449 0.37630  -0.11715 -0.25456 309 THR A N   
1863 C CA  . THR A 309 ? 2.70776 2.45884 2.66707 0.38978  -0.10924 -0.24173 309 THR A CA  
1864 C C   . THR A 309 ? 2.68868 2.46490 2.65785 0.39539  -0.10588 -0.21961 309 THR A C   
1865 O O   . THR A 309 ? 2.69057 2.45786 2.68291 0.39705  -0.10705 -0.20514 309 THR A O   
1866 C CB  . THR A 309 ? 2.71930 2.45615 2.71157 0.39750  -0.10689 -0.23837 309 THR A CB  
1867 O OG1 . THR A 309 ? 2.75627 2.47963 2.73893 0.39094  -0.10777 -0.26353 309 THR A OG1 
1868 C CG2 . THR A 309 ? 2.69936 2.46462 2.71327 0.41261  -0.10048 -0.21720 309 THR A CG2 
1869 N N   . PHE A 310 ? 2.59758 2.40870 2.54900 0.39633  -0.10115 -0.21851 310 PHE A N   
1870 C CA  . PHE A 310 ? 2.59040 2.43695 2.54970 0.39896  -0.09628 -0.20029 310 PHE A CA  
1871 C C   . PHE A 310 ? 2.58296 2.46023 2.56218 0.41002  -0.09168 -0.17667 310 PHE A C   
1872 O O   . PHE A 310 ? 2.58426 2.46529 2.56363 0.41622  -0.09038 -0.17899 310 PHE A O   
1873 C CB  . PHE A 310 ? 2.57416 2.44800 2.50714 0.39166  -0.09221 -0.21362 310 PHE A CB  
1874 C CG  . PHE A 310 ? 2.61697 2.46362 2.53885 0.38149  -0.09724 -0.23164 310 PHE A CG  
1875 C CD1 . PHE A 310 ? 2.60348 2.45364 2.53763 0.37792  -0.09699 -0.22866 310 PHE A CD1 
1876 C CD2 . PHE A 310 ? 2.63782 2.45808 2.53977 0.37481  -0.10273 -0.25026 310 PHE A CD2 
1877 C CE1 . PHE A 310 ? 2.49263 2.31803 2.42332 0.36989  -0.10249 -0.24295 310 PHE A CE1 
1878 C CE2 . PHE A 310 ? 2.66094 2.45788 2.55695 0.36513  -0.10911 -0.26171 310 PHE A CE2 
1879 C CZ  . PHE A 310 ? 2.58841 2.38673 2.50080 0.36367  -0.10917 -0.25755 310 PHE A CZ  
1880 N N   . THR A 311 ? 2.42129 2.32320 2.41981 0.41183  -0.08970 -0.15245 311 THR A N   
1881 C CA  . THR A 311 ? 2.41873 2.35527 2.43972 0.42087  -0.08696 -0.12309 311 THR A CA  
1882 C C   . THR A 311 ? 2.40419 2.39390 2.40540 0.42049  -0.08131 -0.12199 311 THR A C   
1883 O O   . THR A 311 ? 2.40663 2.42935 2.42546 0.42813  -0.08009 -0.09686 311 THR A O   
1884 C CB  . THR A 311 ? 2.44239 2.39669 2.48740 0.41941  -0.08712 -0.09528 311 THR A CB  
1885 O OG1 . THR A 311 ? 2.43510 2.42163 2.46075 0.40857  -0.08322 -0.10289 311 THR A OG1 
1886 C CG2 . THR A 311 ? 2.46918 2.37251 2.53659 0.41980  -0.09228 -0.09491 311 THR A CG2 
1887 N N   . ASP A 312 ? 2.29309 2.29348 2.26136 0.41123  -0.07794 -0.14721 312 ASP A N   
1888 C CA  . ASP A 312 ? 2.27540 2.32761 2.22283 0.40828  -0.07131 -0.15078 312 ASP A CA  
1889 C C   . ASP A 312 ? 2.27382 2.30583 2.18932 0.40166  -0.07047 -0.18509 312 ASP A C   
1890 O O   . ASP A 312 ? 2.28610 2.28672 2.19284 0.39413  -0.07274 -0.20360 312 ASP A O   
1891 C CB  . ASP A 312 ? 2.26841 2.37543 2.21357 0.39886  -0.06480 -0.14235 312 ASP A CB  
1892 C CG  . ASP A 312 ? 2.28976 2.40601 2.26483 0.40047  -0.06727 -0.11192 312 ASP A CG  
1893 O OD1 . ASP A 312 ? 2.28710 2.40962 2.28674 0.40993  -0.07082 -0.08202 312 ASP A OD1 
1894 O OD2 . ASP A 312 ? 2.30657 2.42399 2.28356 0.39205  -0.06572 -0.11758 312 ASP A OD2 
1895 N N   . SER A 313 ? 2.27980 2.33105 2.18000 0.40394  -0.06783 -0.19182 313 SER A N   
1896 C CA  . SER A 313 ? 2.29303 2.32764 2.16266 0.39643  -0.06730 -0.22226 313 SER A CA  
1897 C C   . SER A 313 ? 2.30155 2.39067 2.15001 0.39167  -0.05890 -0.22841 313 SER A C   
1898 O O   . SER A 313 ? 2.31141 2.45234 2.16901 0.39517  -0.05447 -0.20785 313 SER A O   
1899 C CB  . SER A 313 ? 2.30224 2.29625 2.17196 0.40164  -0.07323 -0.23173 313 SER A CB  
1900 O OG  . SER A 313 ? 2.31395 2.26105 2.20251 0.40331  -0.08005 -0.22923 313 SER A OG  
1901 N N   . LEU A 314 ? 2.27489 2.35383 2.09550 0.38213  -0.05714 -0.25592 314 LEU A N   
1902 C CA  . LEU A 314 ? 2.28336 2.40855 2.08058 0.37434  -0.04837 -0.26887 314 LEU A CA  
1903 C C   . LEU A 314 ? 2.31623 2.40926 2.08858 0.36296  -0.04931 -0.29874 314 LEU A C   
1904 O O   . LEU A 314 ? 2.33142 2.37471 2.10685 0.35988  -0.05651 -0.30608 314 LEU A O   
1905 C CB  . LEU A 314 ? 2.28080 2.45951 2.08222 0.36698  -0.03907 -0.26419 314 LEU A CB  
1906 C CG  . LEU A 314 ? 2.28537 2.51481 2.06489 0.35394  -0.02741 -0.28392 314 LEU A CG  
1907 C CD1 . LEU A 314 ? 2.30121 2.57281 2.06794 0.35777  -0.02486 -0.27687 314 LEU A CD1 
1908 C CD2 . LEU A 314 ? 2.28893 2.56928 2.07871 0.34482  -0.01804 -0.28170 314 LEU A CD2 
1909 N N   . ASP A 315 ? 2.39321 2.51709 2.14203 0.35576  -0.04258 -0.31397 315 ASP A N   
1910 C CA  . ASP A 315 ? 2.47120 2.57480 2.19785 0.34203  -0.04154 -0.34093 315 ASP A CA  
1911 C C   . ASP A 315 ? 2.47976 2.62401 2.20284 0.33051  -0.02928 -0.35481 315 ASP A C   
1912 O O   . ASP A 315 ? 2.46558 2.66925 2.18731 0.33035  -0.02011 -0.34906 315 ASP A O   
1913 C CB  . ASP A 315 ? 2.51069 2.61561 2.21269 0.33990  -0.04263 -0.35216 315 ASP A CB  
1914 C CG  . ASP A 315 ? 2.59470 2.68213 2.27401 0.32366  -0.04166 -0.37730 315 ASP A CG  
1915 O OD1 . ASP A 315 ? 2.63718 2.67644 2.31967 0.31792  -0.04980 -0.38227 315 ASP A OD1 
1916 O OD2 . ASP A 315 ? 2.63369 2.75682 2.29369 0.31587  -0.03316 -0.39059 315 ASP A OD2 
1917 N N   . ILE A 316 ? 2.51153 2.62612 2.23639 0.31996  -0.02905 -0.37324 316 ILE A N   
1918 C CA  . ILE A 316 ? 2.51094 2.65782 2.23938 0.30763  -0.01611 -0.39288 316 ILE A CA  
1919 C C   . ILE A 316 ? 2.57886 2.72765 2.28529 0.29439  -0.01076 -0.41766 316 ILE A C   
1920 O O   . ILE A 316 ? 2.59336 2.77191 2.30304 0.28243  0.00209  -0.43854 316 ILE A O   
1921 C CB  . ILE A 316 ? 2.50515 2.62053 2.26108 0.30547  -0.01793 -0.39741 316 ILE A CB  
1922 C CG1 . ILE A 316 ? 2.46288 2.62159 2.23260 0.29408  -0.00194 -0.41830 316 ILE A CG1 
1923 C CG2 . ILE A 316 ? 2.55887 2.60948 2.31453 0.30161  -0.02938 -0.40474 316 ILE A CG2 
1924 C CD1 . ILE A 316 ? 2.50003 2.62688 2.30150 0.29161  -0.00283 -0.42775 316 ILE A CD1 
1925 N N   . SER A 317 ? 2.63300 2.75384 2.31828 0.29472  -0.01937 -0.41754 317 SER A N   
1926 C CA  . SER A 317 ? 2.68981 2.80778 2.35315 0.28082  -0.01610 -0.43900 317 SER A CA  
1927 C C   . SER A 317 ? 2.69265 2.87340 2.33588 0.27609  -0.00330 -0.44828 317 SER A C   
1928 O O   . SER A 317 ? 2.73410 2.91804 2.35774 0.26349  0.00087  -0.46711 317 SER A O   
1929 C CB  . SER A 317 ? 2.71954 2.79193 2.36589 0.28055  -0.03019 -0.43507 317 SER A CB  
1930 O OG  . SER A 317 ? 2.70979 2.73570 2.37329 0.28758  -0.04298 -0.42037 317 SER A OG  
1931 N N   . LEU A 318 ? 2.71145 2.94445 2.35980 0.28454  0.00252  -0.43402 318 LEU A N   
1932 C CA  . LEU A 318 ? 2.71232 3.00864 2.34170 0.28201  0.01163  -0.43607 318 LEU A CA  
1933 C C   . LEU A 318 ? 2.65953 3.02533 2.29521 0.27296  0.02732  -0.44322 318 LEU A C   
1934 O O   . LEU A 318 ? 2.65531 3.07605 2.27280 0.26448  0.03711  -0.45302 318 LEU A O   
1935 C CB  . LEU A 318 ? 2.69203 3.00021 2.32246 0.29946  0.00348  -0.40860 318 LEU A CB  
1936 C CG  . LEU A 318 ? 2.64450 2.93648 2.30348 0.31408  -0.00398 -0.38171 318 LEU A CG  
1937 C CD1 . LEU A 318 ? 2.57172 2.92993 2.24451 0.31464  0.00446  -0.36622 318 LEU A CD1 
1938 C CD2 . LEU A 318 ? 2.64419 2.90861 2.30894 0.33020  -0.01568 -0.36278 318 LEU A CD2 
1939 N N   . VAL A 319 ? 2.63996 3.00955 2.30048 0.27284  0.03042  -0.43994 319 VAL A N   
1940 C CA  . VAL A 319 ? 2.59302 3.03781 2.26184 0.26397  0.04459  -0.44278 319 VAL A CA  
1941 C C   . VAL A 319 ? 2.62001 3.09904 2.28032 0.24279  0.06160  -0.48022 319 VAL A C   
1942 O O   . VAL A 319 ? 2.68876 3.12396 2.34191 0.23574  0.06159  -0.50256 319 VAL A O   
1943 C CB  . VAL A 319 ? 2.53887 2.97475 2.23769 0.26735  0.04360  -0.43363 319 VAL A CB  
1944 C CG1 . VAL A 319 ? 2.52040 2.91746 2.22955 0.28703  0.02727  -0.39856 319 VAL A CG1 
1945 C CG2 . VAL A 319 ? 2.55559 2.94134 2.27126 0.25939  0.04625  -0.46104 319 VAL A CG2 
1946 N N   . ASP A 320 ? 2.71576 3.27626 2.37794 0.23079  0.07635  -0.48705 320 ASP A N   
1947 C CA  . ASP A 320 ? 2.73017 3.32626 2.39217 0.20844  0.09533  -0.52756 320 ASP A CA  
1948 C C   . ASP A 320 ? 2.74125 3.28540 2.43359 0.20357  0.09873  -0.55172 320 ASP A C   
1949 O O   . ASP A 320 ? 2.70867 3.21493 2.42293 0.21493  0.08950  -0.53592 320 ASP A O   
1950 C CB  . ASP A 320 ? 2.66386 3.36438 2.32558 0.19413  0.11095  -0.53074 320 ASP A CB  
1951 C CG  . ASP A 320 ? 2.63201 3.39276 2.26925 0.19871  0.10708  -0.50287 320 ASP A CG  
1952 O OD1 . ASP A 320 ? 2.66900 3.40109 2.28553 0.20684  0.09889  -0.49707 320 ASP A OD1 
1953 O OD2 . ASP A 320 ? 2.57258 3.41265 2.21339 0.19352  0.11185  -0.48564 320 ASP A OD2 
1954 N N   . ASP A 321 ? 2.76837 3.31166 2.46529 0.18628  0.11240  -0.59063 321 ASP A N   
1955 C CA  . ASP A 321 ? 2.78711 3.29129 2.52175 0.18025  0.11839  -0.61664 321 ASP A CA  
1956 C C   . ASP A 321 ? 2.69834 3.25766 2.46004 0.17434  0.13043  -0.62406 321 ASP A C   
1957 O O   . ASP A 321 ? 2.68636 3.20815 2.48275 0.17822  0.12881  -0.62987 321 ASP A O   
1958 C CB  . ASP A 321 ? 2.84660 3.34550 2.58594 0.16152  0.13260  -0.65773 321 ASP A CB  
1959 C CG  . ASP A 321 ? 2.91584 3.34686 2.63564 0.16578  0.11887  -0.65086 321 ASP A CG  
1960 O OD1 . ASP A 321 ? 2.92437 3.30538 2.63274 0.18309  0.09848  -0.61819 321 ASP A OD1 
1961 O OD2 . ASP A 321 ? 2.95981 3.38983 2.67672 0.15008  0.12900  -0.67918 321 ASP A OD2 
1962 N N   . SER A 322 ? 2.84707 3.49905 2.59393 0.16412  0.14185  -0.62248 322 SER A N   
1963 C CA  . SER A 322 ? 2.77915 3.49932 2.54674 0.15461  0.15367  -0.62766 322 SER A CA  
1964 C C   . SER A 322 ? 2.73225 3.49315 2.48480 0.16590  0.14200  -0.58033 322 SER A C   
1965 O O   . SER A 322 ? 2.67636 3.52997 2.42480 0.15249  0.15239  -0.57713 322 SER A O   
1966 C CB  . SER A 322 ? 2.74899 3.55753 2.51765 0.12671  0.17953  -0.66944 322 SER A CB  
1967 O OG  . SER A 322 ? 2.73894 3.60256 2.46951 0.12061  0.18137  -0.66013 322 SER A OG  
1968 N N   . ALA A 323 ? 2.61823 3.31251 2.36491 0.18929  0.12034  -0.54273 323 ALA A N   
1969 C CA  . ALA A 323 ? 2.57732 3.29505 2.31840 0.20265  0.10762  -0.49577 323 ALA A CA  
1970 C C   . ALA A 323 ? 2.57735 3.23751 2.34499 0.21610  0.09642  -0.47990 323 ALA A C   
1971 O O   . ALA A 323 ? 2.60570 3.17926 2.37672 0.23118  0.08259  -0.47332 323 ALA A O   
1972 C CB  . ALA A 323 ? 2.59881 3.29338 2.31356 0.21844  0.09294  -0.46600 323 ALA A CB  
1973 N N   . HIS A 324 ? 2.45292 3.16546 2.23840 0.20906  0.10217  -0.47318 324 HIS A N   
1974 C CA  . HIS A 324 ? 2.43717 3.10495 2.24786 0.22027  0.09239  -0.45709 324 HIS A CA  
1975 C C   . HIS A 324 ? 2.43321 3.08287 2.23659 0.23939  0.07372  -0.40558 324 HIS A C   
1976 O O   . HIS A 324 ? 2.42016 3.13492 2.21250 0.23737  0.07321  -0.37805 324 HIS A O   
1977 C CB  . HIS A 324 ? 2.41011 3.14648 2.24349 0.20266  0.10722  -0.47316 324 HIS A CB  
1978 C CG  . HIS A 324 ? 2.40426 3.17815 2.24786 0.18074  0.12936  -0.52670 324 HIS A CG  
1979 N ND1 . HIS A 324 ? 2.38847 3.23770 2.21214 0.16253  0.14399  -0.54471 324 HIS A ND1 
1980 C CD2 . HIS A 324 ? 2.41401 3.16079 2.28995 0.17386  0.13992  -0.56732 324 HIS A CD2 
1981 C CE1 . HIS A 324 ? 2.38545 3.25174 2.22838 0.14441  0.16367  -0.59633 324 HIS A CE1 
1982 N NE2 . HIS A 324 ? 2.40250 3.20628 2.27959 0.15160  0.16155  -0.61074 324 HIS A NE2 
1983 N N   . ILE A 325 ? 2.23450 2.79756 2.04740 0.25717  0.05843  -0.39220 325 ILE A N   
1984 C CA  . ILE A 325 ? 2.24381 2.77347 2.05312 0.27644  0.04097  -0.34968 325 ILE A CA  
1985 C C   . ILE A 325 ? 2.24461 2.75480 2.07937 0.28262  0.03398  -0.32958 325 ILE A C   
1986 O O   . ILE A 325 ? 2.25901 2.72427 2.11102 0.28234  0.03382  -0.34840 325 ILE A O   
1987 C CB  . ILE A 325 ? 2.28598 2.73508 2.08237 0.28951  0.02948  -0.35300 325 ILE A CB  
1988 C CG1 . ILE A 325 ? 2.29942 2.76774 2.07065 0.28069  0.03759  -0.37718 325 ILE A CG1 
1989 C CG2 . ILE A 325 ? 2.29031 2.71183 2.08627 0.30779  0.01428  -0.31499 325 ILE A CG2 
1990 C CD1 . ILE A 325 ? 2.28070 2.83407 2.03596 0.27484  0.04443  -0.36387 325 ILE A CD1 
1991 N N   . SER A 326 ? 2.03566 2.57965 1.87537 0.28809  0.02768  -0.28993 326 SER A N   
1992 C CA  . SER A 326 ? 2.03583 2.58828 1.89905 0.28772  0.02476  -0.27053 326 SER A CA  
1993 C C   . SER A 326 ? 2.03964 2.54021 1.91294 0.30721  0.00771  -0.23101 326 SER A C   
1994 O O   . SER A 326 ? 2.04216 2.57189 1.91446 0.31337  0.00228  -0.19702 326 SER A O   
1995 C CB  . SER A 326 ? 2.03457 2.69214 1.89900 0.27001  0.03531  -0.25954 326 SER A CB  
1996 O OG  . SER A 326 ? 2.03221 2.73905 1.89253 0.24962  0.05332  -0.30221 326 SER A OG  
1997 N N   . CYS A 327 ? 2.14587 2.57183 2.03240 0.31636  -0.00049 -0.23543 327 CYS A N   
1998 C CA  . CYS A 327 ? 2.16586 2.53944 2.06595 0.33280  -0.01513 -0.20340 327 CYS A CA  
1999 C C   . CYS A 327 ? 2.17164 2.54631 2.09547 0.32960  -0.01657 -0.19174 327 CYS A C   
2000 O O   . CYS A 327 ? 2.16190 2.49824 2.09430 0.32767  -0.01627 -0.21409 327 CYS A O   
2001 C CB  . CYS A 327 ? 2.16881 2.45816 2.06191 0.34405  -0.02397 -0.21827 327 CYS A CB  
2002 S SG  . CYS A 327 ? 2.20096 2.42445 2.11022 0.36243  -0.03979 -0.18836 327 CYS A SG  
2003 N N   . ASN A 328 ? 2.00995 2.42991 1.94643 0.32857  -0.01874 -0.15509 328 ASN A N   
2004 C CA  . ASN A 328 ? 2.03816 2.48469 1.99404 0.31952  -0.01694 -0.14474 328 ASN A CA  
2005 C C   . ASN A 328 ? 2.05340 2.46433 2.03130 0.33088  -0.02949 -0.10593 328 ASN A C   
2006 O O   . ASN A 328 ? 2.05657 2.51202 2.04493 0.32976  -0.03251 -0.06731 328 ASN A O   
2007 C CB  . ASN A 328 ? 2.01434 2.56444 1.96675 0.30066  -0.00609 -0.13733 328 ASN A CB  
2008 C CG  . ASN A 328 ? 2.00703 2.59799 1.94026 0.28730  0.00836  -0.17818 328 ASN A CG  
2009 O OD1 . ASN A 328 ? 2.01479 2.55614 1.94297 0.28996  0.01141  -0.21510 328 ASN A OD1 
2010 N ND2 . ASN A 328 ? 1.99752 2.68170 1.92185 0.27146  0.01726  -0.17083 328 ASN A ND2 
2011 N N   . VAL A 329 ? 2.08852 2.42420 2.07626 0.33969  -0.03648 -0.11549 329 VAL A N   
2012 C CA  . VAL A 329 ? 2.10868 2.40588 2.11913 0.34924  -0.04717 -0.08372 329 VAL A CA  
2013 C C   . VAL A 329 ? 2.14060 2.48425 2.16854 0.33746  -0.04497 -0.06406 329 VAL A C   
2014 O O   . VAL A 329 ? 2.17075 2.53993 2.19779 0.32493  -0.03712 -0.08791 329 VAL A O   
2015 C CB  . VAL A 329 ? 2.11133 2.32180 2.12527 0.35882  -0.05452 -0.10247 329 VAL A CB  
2016 C CG1 . VAL A 329 ? 2.14727 2.31826 2.18608 0.36733  -0.06412 -0.07306 329 VAL A CG1 
2017 C CG2 . VAL A 329 ? 2.07806 2.24966 2.07272 0.36700  -0.05658 -0.12247 329 VAL A CG2 
2018 N N   . HIS A 330 ? 2.09615 2.45180 2.14346 0.34088  -0.05179 -0.02037 330 HIS A N   
2019 C CA  . HIS A 330 ? 2.13063 2.52852 2.19616 0.32913  -0.05179 0.00554  330 HIS A CA  
2020 C C   . HIS A 330 ? 2.18317 2.52138 2.27546 0.33989  -0.06263 0.03253  330 HIS A C   
2021 O O   . HIS A 330 ? 2.18958 2.49908 2.29531 0.35311  -0.06989 0.05752  330 HIS A O   
2022 C CB  . HIS A 330 ? 2.12279 2.61203 2.18901 0.31766  -0.04930 0.03993  330 HIS A CB  
2023 C CG  . HIS A 330 ? 2.12423 2.69149 2.16853 0.29913  -0.03608 0.01315  330 HIS A CG  
2024 N ND1 . HIS A 330 ? 2.11056 2.66926 2.13195 0.30053  -0.02847 -0.02800 330 HIS A ND1 
2025 C CD2 . HIS A 330 ? 2.11631 2.77455 2.15973 0.27679  -0.02825 0.01985  330 HIS A CD2 
2026 C CE1 . HIS A 330 ? 2.09420 2.73271 2.10365 0.28058  -0.01570 -0.04735 330 HIS A CE1 
2027 N NE2 . HIS A 330 ? 2.08833 2.79075 2.11008 0.26535  -0.01503 -0.02005 330 HIS A NE2 
2028 N N   . LEU A 331 ? 2.16357 2.48507 2.26665 0.33376  -0.06296 0.02598  331 LEU A N   
2029 C CA  . LEU A 331 ? 2.22462 2.48850 2.35271 0.34139  -0.07185 0.04565  331 LEU A CA  
2030 C C   . LEU A 331 ? 2.28272 2.59226 2.42875 0.32708  -0.07182 0.07376  331 LEU A C   
2031 O O   . LEU A 331 ? 2.29582 2.64985 2.43388 0.31220  -0.06451 0.05544  331 LEU A O   
2032 C CB  . LEU A 331 ? 2.21461 2.40617 2.33835 0.34760  -0.07376 0.00915  331 LEU A CB  
2033 C CG  . LEU A 331 ? 2.16614 2.31575 2.26923 0.35773  -0.07384 -0.02235 331 LEU A CG  
2034 C CD1 . LEU A 331 ? 2.16084 2.25888 2.25951 0.35816  -0.07553 -0.05643 331 LEU A CD1 
2035 C CD2 . LEU A 331 ? 2.16619 2.27469 2.27830 0.37206  -0.08044 -0.00514 331 LEU A CD2 
2036 N N   . SER A 332 ? 2.29043 2.58839 2.46390 0.33090  -0.07965 0.11702  332 SER A N   
2037 C CA  . SER A 332 ? 2.35573 2.70037 2.54804 0.31591  -0.08103 0.15169  332 SER A CA  
2038 C C   . SER A 332 ? 2.42079 2.70551 2.64718 0.32454  -0.09016 0.18110  332 SER A C   
2039 O O   . SER A 332 ? 2.43378 2.71538 2.68444 0.33190  -0.09626 0.22027  332 SER A O   
2040 C CB  . SER A 332 ? 2.34410 2.77858 2.53578 0.30431  -0.07990 0.18777  332 SER A CB  
2041 O OG  . SER A 332 ? 2.40003 2.88383 2.60983 0.28752  -0.08229 0.22499  332 SER A OG  
2042 N N   . GLU A 333 ? 2.38924 2.62922 2.62080 0.32293  -0.09072 0.16200  333 GLU A N   
2043 C CA  . GLU A 333 ? 2.44546 2.62725 2.70870 0.32842  -0.09758 0.18224  333 GLU A CA  
2044 C C   . GLU A 333 ? 2.49583 2.68086 2.76192 0.31498  -0.09627 0.17340  333 GLU A C   
2045 O O   . GLU A 333 ? 2.48719 2.70202 2.73140 0.30614  -0.09014 0.14200  333 GLU A O   
2046 C CB  . GLU A 333 ? 2.42090 2.51764 2.68717 0.34641  -0.10038 0.15726  333 GLU A CB  
2047 C CG  . GLU A 333 ? 2.39067 2.47599 2.66051 0.36117  -0.10192 0.16517  333 GLU A CG  
2048 C CD  . GLU A 333 ? 2.31569 2.42515 2.54806 0.36331  -0.09683 0.13371  333 GLU A CD  
2049 O OE1 . GLU A 333 ? 2.28397 2.40979 2.49099 0.35467  -0.09203 0.10283  333 GLU A OE1 
2050 O OE2 . GLU A 333 ? 2.29173 2.40386 2.52300 0.37349  -0.09733 0.13931  333 GLU A OE2 
2051 N N   . PRO A 334 ? 2.58451 2.74006 2.88088 0.31288  -0.10144 0.19984  334 PRO A N   
2052 C CA  . PRO A 334 ? 2.62807 2.78134 2.92823 0.30066  -0.10056 0.19003  334 PRO A CA  
2053 C C   . PRO A 334 ? 2.61531 2.71062 2.90214 0.30777  -0.09966 0.14218  334 PRO A C   
2054 O O   . PRO A 334 ? 2.61705 2.73447 2.88842 0.29999  -0.09544 0.11358  334 PRO A O   
2055 C CB  . PRO A 334 ? 2.67155 2.79945 3.01024 0.29869  -0.10673 0.23220  334 PRO A CB  
2056 C CG  . PRO A 334 ? 2.65318 2.80526 3.00886 0.30402  -0.11020 0.27441  334 PRO A CG  
2057 C CD  . PRO A 334 ? 2.59732 2.73518 2.93002 0.31893  -0.10776 0.24570  334 PRO A CD  
2058 N N   . LYS A 335 ? 2.66758 2.69150 2.96341 0.32167  -0.10366 0.13335  335 LYS A N   
2059 C CA  . LYS A 335 ? 2.64214 2.61302 2.92478 0.32769  -0.10443 0.09158  335 LYS A CA  
2060 C C   . LYS A 335 ? 2.58023 2.53695 2.83958 0.33945  -0.10342 0.06684  335 LYS A C   
2061 O O   . LYS A 335 ? 2.56454 2.53713 2.82335 0.34586  -0.10272 0.08272  335 LYS A O   
2062 C CB  . LYS A 335 ? 2.65974 2.56552 2.96670 0.33087  -0.10883 0.09376  335 LYS A CB  
2063 C CG  . LYS A 335 ? 2.68980 2.59537 3.00985 0.31847  -0.10972 0.09674  335 LYS A CG  
2064 C CD  . LYS A 335 ? 2.68121 2.52318 3.02486 0.32046  -0.11289 0.09509  335 LYS A CD  
2065 C CE  . LYS A 335 ? 2.69652 2.53325 3.04706 0.30853  -0.11391 0.08790  335 LYS A CE  
2066 N NZ  . LYS A 335 ? 2.69166 2.46866 3.06408 0.30844  -0.11597 0.08193  335 LYS A NZ  
2067 N N   . TYR A 336 ? 2.55510 2.48383 2.79639 0.34159  -0.10395 0.02915  336 TYR A N   
2068 C CA  . TYR A 336 ? 2.48563 2.40394 2.70241 0.34991  -0.10312 0.00329  336 TYR A CA  
2069 C C   . TYR A 336 ? 2.45762 2.31338 2.67049 0.35487  -0.10833 -0.02234 336 TYR A C   
2070 O O   . TYR A 336 ? 2.46677 2.30656 2.68093 0.34962  -0.11104 -0.03780 336 TYR A O   
2071 C CB  . TYR A 336 ? 2.44911 2.41421 2.64573 0.34418  -0.09763 -0.01752 336 TYR A CB  
2072 C CG  . TYR A 336 ? 2.45060 2.47972 2.64025 0.34064  -0.09147 -0.00094 336 TYR A CG  
2073 C CD1 . TYR A 336 ? 2.50880 2.59014 2.71199 0.32989  -0.08906 0.02845  336 TYR A CD1 
2074 C CD2 . TYR A 336 ? 2.39140 2.43312 2.56038 0.34605  -0.08830 -0.01383 336 TYR A CD2 
2075 C CE1 . TYR A 336 ? 2.50416 2.65184 2.70040 0.32395  -0.08406 0.04550  336 TYR A CE1 
2076 C CE2 . TYR A 336 ? 2.38681 2.49261 2.54886 0.34111  -0.08259 0.00122  336 TYR A CE2 
2077 C CZ  . TYR A 336 ? 2.43975 2.60007 2.61544 0.32970  -0.08068 0.03130  336 TYR A CZ  
2078 O OH  . TYR A 336 ? 2.43510 2.66689 2.60346 0.32209  -0.07562 0.04822  336 TYR A OH  
2079 N N   . ASN A 337 ? 2.51263 2.33776 2.72192 0.36374  -0.10982 -0.02645 337 ASN A N   
2080 C CA  . ASN A 337 ? 2.48057 2.25649 2.68024 0.36632  -0.11422 -0.05329 337 ASN A CA  
2081 C C   . ASN A 337 ? 2.41996 2.19826 2.59537 0.37283  -0.11316 -0.06894 337 ASN A C   
2082 O O   . ASN A 337 ? 2.40459 2.15237 2.57875 0.37779  -0.11468 -0.07747 337 ASN A O   
2083 C CB  . ASN A 337 ? 2.51036 2.24332 2.73486 0.36764  -0.11624 -0.04665 337 ASN A CB  
2084 C CG  . ASN A 337 ? 2.56304 2.28038 2.80479 0.35876  -0.11867 -0.04437 337 ASN A CG  
2085 O OD1 . ASN A 337 ? 2.56522 2.28244 2.79504 0.35270  -0.12182 -0.06104 337 ASN A OD1 
2086 N ND2 . ASN A 337 ? 2.61040 2.31469 2.88354 0.35786  -0.11735 -0.02300 337 ASN A ND2 
2087 N N   . HIS A 338 ? 2.48943 2.30720 2.64652 0.37158  -0.10956 -0.07485 338 HIS A N   
2088 C CA  . HIS A 338 ? 2.42063 2.25103 2.55557 0.37659  -0.10698 -0.08569 338 HIS A CA  
2089 C C   . HIS A 338 ? 2.29218 2.10698 2.40517 0.37390  -0.10963 -0.11644 338 HIS A C   
2090 O O   . HIS A 338 ? 2.27665 2.08963 2.39245 0.36826  -0.11168 -0.12700 338 HIS A O   
2091 C CB  . HIS A 338 ? 2.41512 2.30621 2.54600 0.37518  -0.09994 -0.07120 338 HIS A CB  
2092 C CG  . HIS A 338 ? 2.47285 2.38766 2.62715 0.37584  -0.09878 -0.03491 338 HIS A CG  
2093 N ND1 . HIS A 338 ? 2.54797 2.45901 2.72557 0.37060  -0.10066 -0.01709 338 HIS A ND1 
2094 C CD2 . HIS A 338 ? 2.47944 2.42397 2.63978 0.38047  -0.09671 -0.01048 338 HIS A CD2 
2095 C CE1 . HIS A 338 ? 2.59084 2.52648 2.78856 0.37154  -0.10007 0.01797  338 HIS A CE1 
2096 N NE2 . HIS A 338 ? 2.54812 2.50513 2.73697 0.37791  -0.09808 0.02362  338 HIS A NE2 
2097 N N   . LEU A 339 ? 2.48496 2.28953 2.57883 0.37779  -0.10997 -0.12941 339 LEU A N   
2098 C CA  . LEU A 339 ? 2.36970 2.16353 2.44253 0.37462  -0.11260 -0.15490 339 LEU A CA  
2099 C C   . LEU A 339 ? 2.29043 2.12231 2.34600 0.37591  -0.10536 -0.16042 339 LEU A C   
2100 O O   . LEU A 339 ? 2.28227 2.12493 2.33075 0.38115  -0.10243 -0.15319 339 LEU A O   
2101 C CB  . LEU A 339 ? 2.37562 2.12659 2.43856 0.37438  -0.11956 -0.16754 339 LEU A CB  
2102 C CG  . LEU A 339 ? 2.37789 2.11197 2.42317 0.36826  -0.12574 -0.18899 339 LEU A CG  
2103 C CD1 . LEU A 339 ? 2.33702 2.06276 2.39609 0.36271  -0.13110 -0.19114 339 LEU A CD1 
2104 C CD2 . LEU A 339 ? 2.48541 2.18804 2.51825 0.36535  -0.13179 -0.19954 339 LEU A CD2 
2105 N N   . VAL A 340 ? 2.17998 2.03383 2.23210 0.37083  -0.10187 -0.17439 340 VAL A N   
2106 C CA  . VAL A 340 ? 2.18062 2.07752 2.21962 0.36920  -0.09282 -0.18265 340 VAL A CA  
2107 C C   . VAL A 340 ? 2.14047 2.02066 2.16625 0.36597  -0.09434 -0.20890 340 VAL A C   
2108 O O   . VAL A 340 ? 2.15037 2.01264 2.18764 0.36250  -0.09836 -0.22019 340 VAL A O   
2109 C CB  . VAL A 340 ? 2.18847 2.13774 2.24100 0.36346  -0.08409 -0.17770 340 VAL A CB  
2110 C CG1 . VAL A 340 ? 2.24273 2.24175 2.28168 0.35904  -0.07338 -0.19003 340 VAL A CG1 
2111 C CG2 . VAL A 340 ? 2.21508 2.18170 2.28213 0.36488  -0.08412 -0.14686 340 VAL A CG2 
2112 N N   . GLY A 341 ? 2.04426 1.93148 2.04880 0.36687  -0.09149 -0.21703 341 GLY A N   
2113 C CA  . GLY A 341 ? 2.04313 1.91628 2.03577 0.36255  -0.09264 -0.23982 341 GLY A CA  
2114 C C   . GLY A 341 ? 2.04141 1.93486 2.01027 0.36249  -0.08678 -0.24714 341 GLY A C   
2115 O O   . GLY A 341 ? 2.03909 1.96807 2.00295 0.36552  -0.08023 -0.23540 341 GLY A O   
2116 N N   . LEU A 342 ? 2.14342 2.01578 2.09894 0.35822  -0.08987 -0.26485 342 LEU A N   
2117 C CA  . LEU A 342 ? 2.18445 2.07386 2.11588 0.35660  -0.08460 -0.27450 342 LEU A CA  
2118 C C   . LEU A 342 ? 2.25130 2.10153 2.16830 0.35155  -0.09343 -0.28702 342 LEU A C   
2119 O O   . LEU A 342 ? 2.19246 2.01245 2.12145 0.34752  -0.10149 -0.29107 342 LEU A O   
2120 C CB  . LEU A 342 ? 2.18994 2.12802 2.12284 0.35117  -0.07089 -0.28835 342 LEU A CB  
2121 C CG  . LEU A 342 ? 2.19048 2.12539 2.14264 0.34426  -0.06769 -0.30868 342 LEU A CG  
2122 C CD1 . LEU A 342 ? 2.29798 2.21369 2.23863 0.33816  -0.06863 -0.32808 342 LEU A CD1 
2123 C CD2 . LEU A 342 ? 2.18678 2.17905 2.15327 0.33950  -0.05279 -0.31699 342 LEU A CD2 
2124 N N   . ASN A 343 ? 2.32692 2.18136 2.21920 0.35094  -0.09240 -0.29144 343 ASN A N   
2125 C CA  . ASN A 343 ? 2.33557 2.16266 2.20983 0.34322  -0.09950 -0.30357 343 ASN A CA  
2126 C C   . ASN A 343 ? 2.32803 2.18370 2.18799 0.33789  -0.08948 -0.31962 343 ASN A C   
2127 O O   . ASN A 343 ? 2.39668 2.27864 2.23799 0.34001  -0.08325 -0.32039 343 ASN A O   
2128 C CB  . ASN A 343 ? 2.42790 2.23580 2.28549 0.34454  -0.10674 -0.29860 343 ASN A CB  
2129 C CG  . ASN A 343 ? 2.54169 2.32152 2.38191 0.33318  -0.11660 -0.30846 343 ASN A CG  
2130 O OD1 . ASN A 343 ? 2.58158 2.35985 2.41805 0.32522  -0.11666 -0.31830 343 ASN A OD1 
2131 N ND2 . ASN A 343 ? 2.56290 2.32271 2.39468 0.33084  -0.12468 -0.30615 343 ASN A ND2 
2132 N N   . CYS A 344 ? 2.25157 2.10285 2.12383 0.33084  -0.08760 -0.33299 344 CYS A N   
2133 C CA  . CYS A 344 ? 2.36305 2.24021 2.22726 0.32381  -0.07664 -0.35185 344 CYS A CA  
2134 C C   . CYS A 344 ? 2.47353 2.31978 2.32303 0.31433  -0.08475 -0.36009 344 CYS A C   
2135 O O   . CYS A 344 ? 2.47316 2.28312 2.33812 0.31009  -0.09572 -0.35749 344 CYS A O   
2136 C CB  . CYS A 344 ? 2.23686 2.13272 2.13117 0.32102  -0.06681 -0.36494 344 CYS A CB  
2137 S SG  . CYS A 344 ? 2.40615 2.32567 2.30106 0.30921  -0.05280 -0.39457 344 CYS A SG  
2138 N N   . PRO A 345 ? 2.44563 2.30693 2.26661 0.30982  -0.08066 -0.36808 345 PRO A N   
2139 C CA  . PRO A 345 ? 2.52040 2.35526 2.32710 0.29813  -0.08836 -0.37531 345 PRO A CA  
2140 C C   . PRO A 345 ? 2.54573 2.37482 2.37395 0.28934  -0.08386 -0.39031 345 PRO A C   
2141 O O   . PRO A 345 ? 2.61020 2.40598 2.44204 0.28009  -0.09468 -0.38890 345 PRO A O   
2142 C CB  . PRO A 345 ? 2.52210 2.38321 2.29439 0.29632  -0.08245 -0.38154 345 PRO A CB  
2143 C CG  . PRO A 345 ? 2.46809 2.37712 2.24358 0.30456  -0.06781 -0.38298 345 PRO A CG  
2144 C CD  . PRO A 345 ? 2.41366 2.31868 2.21521 0.31445  -0.06991 -0.36857 345 PRO A CD  
2145 N N   . GLY A 346 ? 2.44347 2.30623 2.28908 0.29070  -0.06810 -0.40465 346 GLY A N   
2146 C CA  . GLY A 346 ? 2.47220 2.33157 2.34748 0.28289  -0.06102 -0.42345 346 GLY A CA  
2147 C C   . GLY A 346 ? 2.44910 2.28879 2.36760 0.28778  -0.06517 -0.41957 346 GLY A C   
2148 O O   . GLY A 346 ? 2.44639 2.26210 2.36883 0.29448  -0.07830 -0.39963 346 GLY A O   
2149 N N   . ASP A 347 ? 2.33741 2.18973 2.29121 0.28370  -0.05283 -0.44123 347 ASP A N   
2150 C CA  . ASP A 347 ? 2.31832 2.15711 2.31935 0.28837  -0.05457 -0.44190 347 ASP A CA  
2151 C C   . ASP A 347 ? 2.24420 2.12439 2.25065 0.29559  -0.04419 -0.44251 347 ASP A C   
2152 O O   . ASP A 347 ? 2.22059 2.14818 2.20389 0.29440  -0.03135 -0.44877 347 ASP A O   
2153 C CB  . ASP A 347 ? 2.36080 2.19498 2.40583 0.28078  -0.04497 -0.46762 347 ASP A CB  
2154 C CG  . ASP A 347 ? 2.42663 2.21768 2.47251 0.27248  -0.05691 -0.46259 347 ASP A CG  
2155 O OD1 . ASP A 347 ? 2.45609 2.21561 2.47753 0.27284  -0.07611 -0.43647 347 ASP A OD1 
2156 O OD2 . ASP A 347 ? 2.44551 2.23630 2.51808 0.26400  -0.04680 -0.48511 347 ASP A OD2 
2157 N N   . ILE A 348 ? 2.25420 2.11877 2.29253 0.30207  -0.05064 -0.43396 348 ILE A N   
2158 C CA  . ILE A 348 ? 2.16171 2.06077 2.20733 0.30796  -0.04379 -0.43013 348 ILE A CA  
2159 C C   . ILE A 348 ? 2.17994 2.09985 2.27546 0.30512  -0.03075 -0.45513 348 ILE A C   
2160 O O   . ILE A 348 ? 2.24407 2.12916 2.37938 0.30617  -0.03740 -0.45936 348 ILE A O   
2161 C CB  . ILE A 348 ? 2.12104 1.98922 2.16173 0.31689  -0.06105 -0.40076 348 ILE A CB  
2162 C CG1 . ILE A 348 ? 2.10306 1.96366 2.09724 0.31930  -0.06916 -0.38138 348 ILE A CG1 
2163 C CG2 . ILE A 348 ? 2.08008 1.97811 2.14018 0.32152  -0.05476 -0.39782 348 ILE A CG2 
2164 C CD1 . ILE A 348 ? 2.14495 1.96759 2.13442 0.32482  -0.08684 -0.35692 348 ILE A CD1 
2165 N N   . ILE A 349 ? 2.15195 2.13215 2.24796 0.30061  -0.01225 -0.47163 349 ILE A N   
2166 C CA  . ILE A 349 ? 2.13170 2.14430 2.27466 0.29525  0.00381  -0.50141 349 ILE A CA  
2167 C C   . ILE A 349 ? 2.07836 2.14184 2.21945 0.29567  0.01094  -0.49508 349 ILE A C   
2168 O O   . ILE A 349 ? 2.07176 2.17652 2.17598 0.29315  0.01562  -0.48385 349 ILE A O   
2169 C CB  . ILE A 349 ? 2.12469 2.17251 2.27506 0.28244  0.02378  -0.53786 349 ILE A CB  
2170 C CG1 . ILE A 349 ? 2.17821 2.17337 2.33597 0.28070  0.01643  -0.54316 349 ILE A CG1 
2171 C CG2 . ILE A 349 ? 2.09452 2.18524 2.29522 0.27503  0.04325  -0.57349 349 ILE A CG2 
2172 C CD1 . ILE A 349 ? 2.20983 2.19792 2.31310 0.27838  0.01069  -0.52931 349 ILE A CD1 
2173 N N   . PRO A 350 ? 2.04403 2.10822 2.22534 0.29834  0.01122  -0.49972 350 PRO A N   
2174 C CA  . PRO A 350 ? 2.07230 2.08851 2.30240 0.30333  0.00342  -0.50763 350 PRO A CA  
2175 C C   . PRO A 350 ? 2.07301 2.02588 2.29086 0.31426  -0.02169 -0.47182 350 PRO A C   
2176 O O   . PRO A 350 ? 2.04346 1.98092 2.21506 0.31662  -0.03165 -0.44831 350 PRO A O   
2177 C CB  . PRO A 350 ? 2.06386 2.11975 2.33537 0.30123  0.01482  -0.52487 350 PRO A CB  
2178 C CG  . PRO A 350 ? 2.04329 2.14347 2.27764 0.29971  0.01669  -0.50467 350 PRO A CG  
2179 C CD  . PRO A 350 ? 2.01043 2.13068 2.19472 0.29516  0.02019  -0.49764 350 PRO A CD  
2180 N N   . ASP A 351 ? 2.09360 2.01374 2.35414 0.31999  -0.03148 -0.46872 351 ASP A N   
2181 C CA  . ASP A 351 ? 2.12041 1.98714 2.37120 0.32770  -0.05521 -0.43563 351 ASP A CA  
2182 C C   . ASP A 351 ? 2.02210 1.90313 2.24541 0.33186  -0.05967 -0.41257 351 ASP A C   
2183 O O   . ASP A 351 ? 1.97660 1.85755 2.22462 0.33581  -0.06370 -0.40610 351 ASP A O   
2184 C CB  . ASP A 351 ? 2.10721 1.93994 2.41484 0.33185  -0.06481 -0.43737 351 ASP A CB  
2185 C CG  . ASP A 351 ? 2.19586 1.99353 2.52356 0.32882  -0.06993 -0.44375 351 ASP A CG  
2186 O OD1 . ASP A 351 ? 2.22274 2.03340 2.53012 0.32200  -0.05907 -0.45933 351 ASP A OD1 
2187 O OD2 . ASP A 351 ? 2.24137 2.00002 2.60551 0.33244  -0.08544 -0.43116 351 ASP A OD2 
2188 N N   . CYS A 352 ? 2.17096 2.06473 2.34502 0.33082  -0.05874 -0.39989 352 CYS A N   
2189 C CA  . CYS A 352 ? 2.07458 1.97860 2.22366 0.33471  -0.06307 -0.37583 352 CYS A CA  
2190 C C   . CYS A 352 ? 2.07893 1.93048 2.22111 0.34017  -0.08387 -0.35045 352 CYS A C   
2191 O O   . CYS A 352 ? 2.09614 1.90861 2.23527 0.33937  -0.09556 -0.34705 352 CYS A O   
2192 C CB  . CYS A 352 ? 2.06539 1.99963 2.17144 0.33256  -0.05565 -0.37023 352 CYS A CB  
2193 S SG  . CYS A 352 ? 2.16435 2.17786 2.27647 0.32288  -0.03074 -0.39588 352 CYS A SG  
2194 N N   . PHE A 353 ? 2.10476 1.95860 2.24553 0.34374  -0.08838 -0.33257 353 PHE A N   
2195 C CA  . PHE A 353 ? 2.08918 1.99135 2.23151 0.34273  -0.07595 -0.33183 353 PHE A CA  
2196 C C   . PHE A 353 ? 2.11199 2.03193 2.29611 0.34181  -0.07159 -0.34199 353 PHE A C   
2197 O O   . PHE A 353 ? 2.11482 2.07411 2.30215 0.33931  -0.06358 -0.33818 353 PHE A O   
2198 C CB  . PHE A 353 ? 2.07576 1.97184 2.19138 0.34633  -0.08258 -0.30413 353 PHE A CB  
2199 C CG  . PHE A 353 ? 2.04764 1.97361 2.13206 0.34561  -0.07457 -0.29826 353 PHE A CG  
2200 C CD1 . PHE A 353 ? 2.03545 1.94141 2.09217 0.34674  -0.07834 -0.29818 353 PHE A CD1 
2201 C CD2 . PHE A 353 ? 2.09474 2.07290 2.17886 0.34277  -0.06375 -0.29156 353 PHE A CD2 
2202 C CE1 . PHE A 353 ? 2.02599 1.96177 2.05720 0.34688  -0.07132 -0.29234 353 PHE A CE1 
2203 C CE2 . PHE A 353 ? 2.09218 2.10162 2.15099 0.34213  -0.05770 -0.28252 353 PHE A CE2 
2204 C CZ  . PHE A 353 ? 2.03993 2.02739 2.07326 0.34510  -0.06138 -0.28340 353 PHE A CZ  
2205 N N   . PHE A 354 ? 1.99986 1.89323 2.21847 0.34323  -0.07710 -0.35400 354 PHE A N   
2206 C CA  . PHE A 354 ? 2.03745 1.95018 2.30227 0.34288  -0.07166 -0.36816 354 PHE A CA  
2207 C C   . PHE A 354 ? 2.00344 1.97509 2.28463 0.33551  -0.04958 -0.39827 354 PHE A C   
2208 O O   . PHE A 354 ? 2.10974 2.12411 2.40749 0.33146  -0.04002 -0.40490 354 PHE A O   
2209 C CB  . PHE A 354 ? 2.21125 2.08232 2.51520 0.34694  -0.08334 -0.37261 354 PHE A CB  
2210 C CG  . PHE A 354 ? 2.26135 2.12814 2.60135 0.35042  -0.09017 -0.36697 354 PHE A CG  
2211 C CD1 . PHE A 354 ? 2.26991 2.18112 2.62293 0.34779  -0.07854 -0.37460 354 PHE A CD1 
2212 C CD2 . PHE A 354 ? 2.28728 2.10972 2.64770 0.35481  -0.10878 -0.35263 354 PHE A CD2 
2213 C CE1 . PHE A 354 ? 2.29044 2.19939 2.67642 0.35045  -0.08464 -0.37024 354 PHE A CE1 
2214 C CE2 . PHE A 354 ? 2.30686 2.12810 2.70091 0.35783  -0.11543 -0.34698 354 PHE A CE2 
2215 C CZ  . PHE A 354 ? 2.30673 2.17005 2.71359 0.35615  -0.10298 -0.35685 354 PHE A CZ  
2216 N N   . GLN A 355 ? 2.01983 1.99844 2.29603 0.33164  -0.04071 -0.41775 355 GLN A N   
2217 C CA  . GLN A 355 ? 2.01426 2.05211 2.30505 0.32191  -0.01833 -0.45058 355 GLN A CA  
2218 C C   . GLN A 355 ? 2.01081 2.08546 2.25313 0.31573  -0.01016 -0.44429 355 GLN A C   
2219 O O   . GLN A 355 ? 2.01815 2.06154 2.22442 0.31967  -0.01972 -0.42669 355 GLN A O   
2220 C CB  . GLN A 355 ? 2.14816 2.17077 2.47764 0.32044  -0.01203 -0.48189 355 GLN A CB  
2221 C CG  . GLN A 355 ? 2.19407 2.19169 2.58443 0.32608  -0.01701 -0.49239 355 GLN A CG  
2222 C CD  . GLN A 355 ? 2.21045 2.18420 2.64340 0.32586  -0.01322 -0.51791 355 GLN A CD  
2223 O OE1 . GLN A 355 ? 2.22612 2.16899 2.63685 0.32550  -0.01918 -0.51144 355 GLN A OE1 
2224 N NE2 . GLN A 355 ? 2.23273 2.22126 2.73056 0.32562  -0.00294 -0.54759 355 GLN A NE2 
2225 N N   . VAL A 356 ? 1.97027 2.11581 2.21345 0.30490  0.00753  -0.45895 356 VAL A N   
2226 C CA  . VAL A 356 ? 2.05519 2.24744 2.25651 0.29766  0.01542  -0.45030 356 VAL A CA  
2227 C C   . VAL A 356 ? 2.09195 2.36375 2.30922 0.28120  0.03900  -0.48515 356 VAL A C   
2228 O O   . VAL A 356 ? 2.09387 2.39368 2.35120 0.27523  0.04892  -0.50926 356 VAL A O   
2229 C CB  . VAL A 356 ? 1.98294 2.18458 2.15631 0.30085  0.00620  -0.41050 356 VAL A CB  
2230 C CG1 . VAL A 356 ? 1.93098 2.06499 2.07764 0.31395  -0.01334 -0.37983 356 VAL A CG1 
2231 C CG2 . VAL A 356 ? 2.11735 2.33321 2.31993 0.29946  0.00582  -0.40747 356 VAL A CG2 
2232 N N   . TYR A 357 ? 2.09048 2.40287 2.27718 0.27266  0.04855  -0.48935 357 TYR A N   
2233 C CA  . TYR A 357 ? 2.07621 2.47683 2.27062 0.25348  0.07129  -0.51941 357 TYR A CA  
2234 C C   . TYR A 357 ? 2.09016 2.55462 2.27458 0.24483  0.07365  -0.49760 357 TYR A C   
2235 O O   . TYR A 357 ? 2.11151 2.55622 2.27120 0.25354  0.05856  -0.45468 357 TYR A O   
2236 C CB  . TYR A 357 ? 2.06514 2.49370 2.22793 0.24577  0.07986  -0.52800 357 TYR A CB  
2237 C CG  . TYR A 357 ? 2.04344 2.45532 2.23061 0.24147  0.09116  -0.57099 357 TYR A CG  
2238 C CD1 . TYR A 357 ? 2.02002 2.35038 2.20707 0.25448  0.07788  -0.56627 357 TYR A CD1 
2239 C CD2 . TYR A 357 ? 2.05031 2.53084 2.26246 0.22250  0.11556  -0.61664 357 TYR A CD2 
2240 C CE1 . TYR A 357 ? 2.00009 2.31363 2.21290 0.24977  0.08756  -0.60256 357 TYR A CE1 
2241 C CE2 . TYR A 357 ? 2.03513 2.49849 2.27510 0.21807  0.12698  -0.65725 357 TYR A CE2 
2242 C CZ  . TYR A 357 ? 2.00751 2.38519 2.24842 0.23230  0.11237  -0.64832 357 TYR A CZ  
2243 O OH  . TYR A 357 ? 1.98953 2.34801 2.26141 0.22728  0.12293  -0.68560 357 TYR A OH  
2244 N N   . GLN A 358 ? 2.09347 2.63775 2.29997 0.22592  0.09340  -0.52851 358 GLN A N   
2245 C CA  . GLN A 358 ? 2.10835 2.71700 2.31170 0.21482  0.09568  -0.50946 358 GLN A CA  
2246 C C   . GLN A 358 ? 2.11082 2.77141 2.26952 0.20750  0.09315  -0.47240 358 GLN A C   
2247 O O   . GLN A 358 ? 2.14916 2.80650 2.29457 0.21216  0.08024  -0.42923 358 GLN A O   
2248 C CB  . GLN A 358 ? 2.09555 2.77938 2.33749 0.19442  0.11807  -0.55616 358 GLN A CB  
2249 C CG  . GLN A 358 ? 2.11130 2.74712 2.40581 0.20344  0.11808  -0.58447 358 GLN A CG  
2250 C CD  . GLN A 358 ? 2.11242 2.82314 2.45149 0.18334  0.14262  -0.63794 358 GLN A CD  
2251 O OE1 . GLN A 358 ? 2.08158 2.86942 2.41535 0.16262  0.16231  -0.66655 358 GLN A OE1 
2252 N NE2 . GLN A 358 ? 2.14140 2.83345 2.52650 0.18837  0.14220  -0.65351 358 GLN A NE2 
2253 N N   . PRO A 359 ? 2.16598 2.87682 2.30313 0.19580  0.10450  -0.48488 359 PRO A N   
2254 C CA  . PRO A 359 ? 2.13629 2.86514 2.28357 0.18618  0.12193  -0.53386 359 PRO A CA  
2255 C C   . PRO A 359 ? 2.11599 2.93963 2.29127 0.15993  0.14682  -0.57951 359 PRO A C   
2256 O O   . PRO A 359 ? 2.07753 2.94377 2.25557 0.14540  0.16471  -0.61813 359 PRO A O   
2257 C CB  . PRO A 359 ? 2.11936 2.87019 2.22255 0.18442  0.11992  -0.51307 359 PRO A CB  
2258 C CG  . PRO A 359 ? 2.12696 2.93175 2.20746 0.17902  0.11263  -0.46632 359 PRO A CG  
2259 C CD  . PRO A 359 ? 2.16870 2.92303 2.26658 0.19202  0.09821  -0.44126 359 PRO A CD  
2260 N N   . SER A 367 ? 2.02342 2.56457 2.40108 0.18412  0.18512  -0.80082 367 SER A N   
2261 C CA  . SER A 367 ? 2.05712 2.53519 2.48374 0.20082  0.17283  -0.79582 367 SER A CA  
2262 C C   . SER A 367 ? 2.05325 2.57500 2.48508 0.19903  0.17219  -0.78453 367 SER A C   
2263 O O   . SER A 367 ? 2.05008 2.61237 2.53455 0.18991  0.18872  -0.82327 367 SER A O   
2264 C CB  . SER A 367 ? 2.07283 2.53485 2.57585 0.19744  0.18891  -0.84914 367 SER A CB  
2265 O OG  . SER A 367 ? 2.09589 2.49556 2.64962 0.21489  0.17511  -0.84074 367 SER A OG  
2266 N N   . ASN A 368 ? 2.09788 2.61207 2.47732 0.20707  0.15360  -0.73233 368 ASN A N   
2267 C CA  . ASN A 368 ? 2.08703 2.63513 2.46671 0.20600  0.14979  -0.71352 368 ASN A CA  
2268 C C   . ASN A 368 ? 2.11008 2.57463 2.48011 0.22901  0.12186  -0.66637 368 ASN A C   
2269 O O   . ASN A 368 ? 2.10910 2.57999 2.44069 0.23237  0.10944  -0.62474 368 ASN A O   
2270 C CB  . ASN A 368 ? 2.07397 2.70697 2.40323 0.18974  0.15580  -0.69428 368 ASN A CB  
2271 C CG  . ASN A 368 ? 2.03920 2.76164 2.37081 0.16426  0.18281  -0.73871 368 ASN A CG  
2272 O OD1 . ASN A 368 ? 2.01985 2.77563 2.30652 0.15629  0.18484  -0.72627 368 ASN A OD1 
2273 N ND2 . ASN A 368 ? 2.02088 2.78567 2.40743 0.15061  0.20434  -0.79253 368 ASN A ND2 
2274 N N   . ILE A 369 ? 1.93092 2.31939 2.33863 0.24366  0.11201  -0.67239 369 ILE A N   
2275 C CA  . ILE A 369 ? 1.95672 2.26326 2.35245 0.26372  0.08491  -0.62913 369 ILE A CA  
2276 C C   . ILE A 369 ? 1.98559 2.29812 2.40468 0.26784  0.07903  -0.61784 369 ILE A C   
2277 O O   . ILE A 369 ? 2.01744 2.32720 2.49522 0.26928  0.08463  -0.64492 369 ILE A O   
2278 C CB  . ILE A 369 ? 1.97119 2.20135 2.39892 0.27512  0.07544  -0.63637 369 ILE A CB  
2279 C CG1 . ILE A 369 ? 1.95522 2.18212 2.35730 0.26910  0.08182  -0.64748 369 ILE A CG1 
2280 C CG2 . ILE A 369 ? 2.00349 2.15841 2.41744 0.29240  0.04752  -0.59201 369 ILE A CG2 
2281 C CD1 . ILE A 369 ? 1.97686 2.13244 2.40928 0.27739  0.07266  -0.65253 369 ILE A CD1 
2282 N N   . VAL A 370 ? 1.98134 2.30145 2.35765 0.26986  0.06775  -0.57777 370 VAL A N   
2283 C CA  . VAL A 370 ? 2.01351 2.33839 2.40442 0.27280  0.06081  -0.56173 370 VAL A CA  
2284 C C   . VAL A 370 ? 2.03317 2.27576 2.40957 0.29087  0.03470  -0.52110 370 VAL A C   
2285 O O   . VAL A 370 ? 2.01228 2.20582 2.35879 0.29876  0.02277  -0.50221 370 VAL A O   
2286 C CB  . VAL A 370 ? 2.01727 2.41733 2.37659 0.25883  0.06824  -0.54625 370 VAL A CB  
2287 C CG1 . VAL A 370 ? 2.02604 2.39959 2.32910 0.26604  0.05159  -0.49606 370 VAL A CG1 
2288 C CG2 . VAL A 370 ? 2.06728 2.49824 2.45796 0.25428  0.07077  -0.55007 370 VAL A CG2 
2289 N N   . TYR A 371 ? 2.05852 2.29038 2.45668 0.29567  0.02646  -0.50948 371 TYR A N   
2290 C CA  . TYR A 371 ? 2.04470 2.20793 2.43197 0.30979  0.00297  -0.47327 371 TYR A CA  
2291 C C   . TYR A 371 ? 2.05330 2.22794 2.39669 0.30836  -0.00441 -0.43543 371 TYR A C   
2292 O O   . TYR A 371 ? 2.11837 2.35215 2.46063 0.29780  0.00554  -0.43540 371 TYR A O   
2293 C CB  . TYR A 371 ? 2.09371 2.23525 2.53474 0.31623  -0.00281 -0.48247 371 TYR A CB  
2294 C CG  . TYR A 371 ? 2.08672 2.17946 2.56798 0.32481  -0.00813 -0.49888 371 TYR A CG  
2295 C CD1 . TYR A 371 ? 2.08813 2.20654 2.61513 0.31985  0.00944  -0.54180 371 TYR A CD1 
2296 C CD2 . TYR A 371 ? 2.07524 2.09870 2.55126 0.33630  -0.03066 -0.47101 371 TYR A CD2 
2297 C CE1 . TYR A 371 ? 2.08479 2.15618 2.65455 0.32777  0.00384  -0.55365 371 TYR A CE1 
2298 C CE2 . TYR A 371 ? 2.07826 2.05938 2.59285 0.34277  -0.03743 -0.48044 371 TYR A CE2 
2299 C CZ  . TYR A 371 ? 2.09220 2.09509 2.65517 0.33928  -0.02053 -0.52037 371 TYR A CZ  
2300 O OH  . TYR A 371 ? 2.10746 2.06623 2.71477 0.34575  -0.02780 -0.52703 371 TYR A OH  
2301 N N   . LEU A 372 ? 2.13978 2.25888 2.44995 0.31791  -0.02175 -0.40340 372 LEU A N   
2302 C CA  . LEU A 372 ? 2.16594 2.29151 2.43637 0.31730  -0.02772 -0.36836 372 LEU A CA  
2303 C C   . LEU A 372 ? 2.23528 2.36440 2.51926 0.31683  -0.03349 -0.35132 372 LEU A C   
2304 O O   . LEU A 372 ? 2.28033 2.45526 2.55262 0.30859  -0.02785 -0.33704 372 LEU A O   
2305 C CB  . LEU A 372 ? 2.07039 2.13632 2.30751 0.32692  -0.04300 -0.34479 372 LEU A CB  
2306 C CG  . LEU A 372 ? 2.07042 2.14181 2.27152 0.32731  -0.04748 -0.31140 372 LEU A CG  
2307 C CD1 . LEU A 372 ? 2.06696 2.19951 2.24813 0.31875  -0.03345 -0.31371 372 LEU A CD1 
2308 C CD2 . LEU A 372 ? 2.07542 2.08492 2.25171 0.33665  -0.06281 -0.29218 372 LEU A CD2 
2309 N N   . ASP A 373 ? 2.20764 2.29090 2.51689 0.32453  -0.04537 -0.35058 373 ASP A N   
2310 C CA  . ASP A 373 ? 2.27897 2.36072 2.59959 0.32411  -0.05211 -0.33366 373 ASP A CA  
2311 C C   . ASP A 373 ? 2.32675 2.47880 2.66796 0.31209  -0.03689 -0.34795 373 ASP A C   
2312 O O   . ASP A 373 ? 2.38039 2.55328 2.71331 0.30647  -0.03817 -0.32680 373 ASP A O   
2313 C CB  . ASP A 373 ? 2.29866 2.33053 2.64966 0.33266  -0.06562 -0.33618 373 ASP A CB  
2314 C CG  . ASP A 373 ? 2.29276 2.26092 2.62111 0.34093  -0.08222 -0.31849 373 ASP A CG  
2315 O OD1 . ASP A 373 ? 2.26363 2.21820 2.58245 0.34300  -0.08103 -0.32838 373 ASP A OD1 
2316 O OD2 . ASP A 373 ? 2.32096 2.25570 2.64119 0.34362  -0.09590 -0.29603 373 ASP A OD2 
2317 N N   . SER A 374 ? 2.23032 2.42193 2.60027 0.30643  -0.02174 -0.38486 374 SER A N   
2318 C CA  . SER A 374 ? 2.26228 2.53037 2.65210 0.29178  -0.00507 -0.40396 374 SER A CA  
2319 C C   . SER A 374 ? 2.27374 2.60205 2.62715 0.27831  0.00509  -0.39178 374 SER A C   
2320 O O   . SER A 374 ? 2.31828 2.70318 2.67085 0.26516  0.01133  -0.38359 374 SER A O   
2321 C CB  . SER A 374 ? 2.24046 2.53322 2.67806 0.28905  0.00951  -0.45203 374 SER A CB  
2322 O OG  . SER A 374 ? 2.20632 2.48689 2.63554 0.29120  0.01463  -0.46807 374 SER A OG  
2323 N N   . GLN A 375 ? 2.19213 2.51220 2.51608 0.28040  0.00617  -0.38856 375 GLN A N   
2324 C CA  . GLN A 375 ? 2.17872 2.55847 2.46975 0.26800  0.01463  -0.37445 375 GLN A CA  
2325 C C   . GLN A 375 ? 2.22685 2.59751 2.49122 0.26923  0.00240  -0.32623 375 GLN A C   
2326 O O   . GLN A 375 ? 2.25856 2.69342 2.51305 0.25498  0.00863  -0.31023 375 GLN A O   
2327 C CB  . GLN A 375 ? 2.12497 2.49296 2.39230 0.27149  0.01733  -0.38182 375 GLN A CB  
2328 C CG  . GLN A 375 ? 2.11943 2.55189 2.35409 0.25905  0.02556  -0.36713 375 GLN A CG  
2329 C CD  . GLN A 375 ? 2.10063 2.62804 2.35007 0.23741  0.04693  -0.39907 375 GLN A CD  
2330 O OE1 . GLN A 375 ? 2.08893 2.62855 2.37438 0.23328  0.05843  -0.44165 375 GLN A OE1 
2331 N NE2 . GLN A 375 ? 2.09961 2.69812 2.32440 0.22246  0.05252  -0.37878 375 GLN A NE2 
2332 N N   . ILE A 376 ? 2.27097 2.56489 2.52595 0.28468  -0.01483 -0.30256 376 ILE A N   
2333 C CA  . ILE A 376 ? 2.31477 2.59334 2.55310 0.28634  -0.02580 -0.26017 376 ILE A CA  
2334 C C   . ILE A 376 ? 2.36924 2.65979 2.63146 0.28046  -0.02744 -0.25525 376 ILE A C   
2335 O O   . ILE A 376 ? 2.40303 2.71830 2.65819 0.27292  -0.02941 -0.22512 376 ILE A O   
2336 C CB  . ILE A 376 ? 2.29496 2.49170 2.51659 0.30259  -0.04170 -0.24169 376 ILE A CB  
2337 C CG1 . ILE A 376 ? 2.23036 2.40986 2.43352 0.30865  -0.04009 -0.25546 376 ILE A CG1 
2338 C CG2 . ILE A 376 ? 2.33195 2.51884 2.53697 0.30368  -0.04976 -0.19999 376 ILE A CG2 
2339 C CD1 . ILE A 376 ? 2.19757 2.41227 2.37277 0.30512  -0.03569 -0.23682 376 ILE A CD1 
2340 N N   . ASN A 377 ? 2.34842 2.62228 2.64167 0.28362  -0.02707 -0.28318 377 ASN A N   
2341 C CA  . ASN A 377 ? 2.38644 2.66719 2.70544 0.27945  -0.02932 -0.28217 377 ASN A CA  
2342 C C   . ASN A 377 ? 2.41997 2.64488 2.72759 0.28678  -0.04561 -0.24648 377 ASN A C   
2343 O O   . ASN A 377 ? 2.46578 2.71184 2.77330 0.27839  -0.04681 -0.22379 377 ASN A O   
2344 C CB  . ASN A 377 ? 2.41147 2.77984 2.73774 0.25966  -0.01547 -0.28551 377 ASN A CB  
2345 C CG  . ASN A 377 ? 2.43634 2.82301 2.79843 0.25417  -0.01304 -0.30219 377 ASN A CG  
2346 O OD1 . ASN A 377 ? 2.43325 2.77083 2.81931 0.26596  -0.02049 -0.31546 377 ASN A OD1 
2347 N ND2 . ASN A 377 ? 2.45722 2.91886 2.82407 0.23516  -0.00294 -0.30075 377 ASN A ND2 
2348 N N   . ILE A 378 ? 2.50310 2.65821 2.80229 0.30085  -0.05776 -0.24262 378 ILE A N   
2349 C CA  . ILE A 378 ? 2.52308 2.62154 2.81572 0.30727  -0.07253 -0.21717 378 ILE A CA  
2350 C C   . ILE A 378 ? 2.49462 2.53974 2.80212 0.31737  -0.08281 -0.23263 378 ILE A C   
2351 O O   . ILE A 378 ? 2.45092 2.47740 2.75515 0.32374  -0.08330 -0.24825 378 ILE A O   
2352 C CB  . ILE A 378 ? 2.51632 2.58802 2.77744 0.31161  -0.07785 -0.18938 378 ILE A CB  
2353 C CG1 . ILE A 378 ? 2.55249 2.67759 2.80407 0.30143  -0.07025 -0.16628 378 ILE A CG1 
2354 C CG2 . ILE A 378 ? 2.52308 2.53362 2.78173 0.31754  -0.09165 -0.17136 378 ILE A CG2 
2355 C CD1 . ILE A 378 ? 2.54227 2.64875 2.76971 0.30688  -0.07387 -0.14114 378 ILE A CD1 
2356 N N   . GLY A 379 ? 2.55330 2.57653 2.87788 0.31762  -0.09149 -0.22661 379 GLY A N   
2357 C CA  . GLY A 379 ? 2.53232 2.51298 2.87498 0.32527  -0.10268 -0.23735 379 GLY A CA  
2358 C C   . GLY A 379 ? 2.50617 2.43028 2.82493 0.33233  -0.11501 -0.22635 379 GLY A C   
2359 O O   . GLY A 379 ? 2.47239 2.37654 2.79419 0.33796  -0.11867 -0.23942 379 GLY A O   
2360 N N   . ASP A 380 ? 2.54155 2.44110 2.83892 0.33087  -0.12101 -0.20321 380 ASP A N   
2361 C CA  . ASP A 380 ? 2.51928 2.36827 2.79617 0.33495  -0.13247 -0.19502 380 ASP A CA  
2362 C C   . ASP A 380 ? 2.48540 2.33330 2.73380 0.33810  -0.12736 -0.19234 380 ASP A C   
2363 O O   . ASP A 380 ? 2.49070 2.33587 2.72258 0.33727  -0.12530 -0.17531 380 ASP A O   
2364 C CB  . ASP A 380 ? 2.55275 2.37672 2.82648 0.33076  -0.13990 -0.17688 380 ASP A CB  
2365 C CG  . ASP A 380 ? 2.55029 2.36393 2.84771 0.32817  -0.14929 -0.18050 380 ASP A CG  
2366 O OD1 . ASP A 380 ? 2.51483 2.33377 2.83205 0.33154  -0.15221 -0.19515 380 ASP A OD1 
2367 O OD2 . ASP A 380 ? 2.58792 2.38888 2.88718 0.32260  -0.15367 -0.16854 380 ASP A OD2 
2368 N N   . ILE A 381 ? 2.51581 2.36576 2.76198 0.34182  -0.12537 -0.20919 381 ILE A N   
2369 C CA  . ILE A 381 ? 2.38803 2.23335 2.60686 0.34486  -0.12215 -0.20970 381 ILE A CA  
2370 C C   . ILE A 381 ? 2.38856 2.19284 2.60012 0.34768  -0.13342 -0.21650 381 ILE A C   
2371 O O   . ILE A 381 ? 2.43229 2.23485 2.66271 0.34876  -0.13580 -0.23114 381 ILE A O   
2372 C CB  . ILE A 381 ? 2.32217 2.21400 2.54260 0.34369  -0.10794 -0.22449 381 ILE A CB  
2373 C CG1 . ILE A 381 ? 2.35949 2.30117 2.58754 0.33732  -0.09746 -0.21635 381 ILE A CG1 
2374 C CG2 . ILE A 381 ? 2.27773 2.16594 2.46878 0.34644  -0.10509 -0.22411 381 ILE A CG2 
2375 C CD1 . ILE A 381 ? 2.42579 2.42408 2.65905 0.33220  -0.08243 -0.23463 381 ILE A CD1 
2376 N N   . GLU A 382 ? 2.48312 2.25643 2.67082 0.34789  -0.14032 -0.20586 382 GLU A N   
2377 C CA  . GLU A 382 ? 2.44525 2.18483 2.62226 0.34727  -0.15160 -0.21037 382 GLU A CA  
2378 C C   . GLU A 382 ? 2.35649 2.10152 2.51617 0.34969  -0.14654 -0.22119 382 GLU A C   
2379 O O   . GLU A 382 ? 2.31860 2.08705 2.46490 0.35192  -0.13556 -0.22129 382 GLU A O   
2380 C CB  . GLU A 382 ? 2.53957 2.24920 2.69921 0.34377  -0.15967 -0.19921 382 GLU A CB  
2381 C CG  . GLU A 382 ? 2.61582 2.31347 2.79222 0.33863  -0.16771 -0.19166 382 GLU A CG  
2382 C CD  . GLU A 382 ? 2.64672 2.35900 2.83288 0.33860  -0.15992 -0.18102 382 GLU A CD  
2383 O OE1 . GLU A 382 ? 2.63947 2.37753 2.82350 0.34240  -0.14876 -0.17801 382 GLU A OE1 
2384 O OE2 . GLU A 382 ? 2.68340 2.38379 2.87974 0.33329  -0.16527 -0.17451 382 GLU A OE2 
2385 N N   . TYR A 383 ? 2.40998 2.13527 2.57121 0.34820  -0.15524 -0.22862 383 TYR A N   
2386 C CA  . TYR A 383 ? 2.37736 2.10464 2.52467 0.34889  -0.15154 -0.23991 383 TYR A CA  
2387 C C   . TYR A 383 ? 2.43477 2.12974 2.56060 0.34408  -0.16444 -0.23557 383 TYR A C   
2388 O O   . TYR A 383 ? 2.50900 2.18351 2.64485 0.33932  -0.17811 -0.22888 383 TYR A O   
2389 C CB  . TYR A 383 ? 2.33982 2.08002 2.51773 0.35007  -0.14774 -0.25563 383 TYR A CB  
2390 C CG  . TYR A 383 ? 2.32135 2.10394 2.51702 0.35198  -0.13153 -0.26692 383 TYR A CG  
2391 C CD1 . TYR A 383 ? 2.32937 2.12720 2.55218 0.35215  -0.13013 -0.26506 383 TYR A CD1 
2392 C CD2 . TYR A 383 ? 2.28951 2.10199 2.47435 0.35154  -0.11738 -0.28032 383 TYR A CD2 
2393 C CE1 . TYR A 383 ? 2.35861 2.20185 2.59693 0.35094  -0.11498 -0.27651 383 TYR A CE1 
2394 C CE2 . TYR A 383 ? 2.31019 2.16974 2.51025 0.34983  -0.10216 -0.29171 383 TYR A CE2 
2395 C CZ  . TYR A 383 ? 2.31766 2.19316 2.54432 0.34909  -0.10101 -0.28990 383 TYR A CZ  
2396 O OH  . TYR A 383 ? 2.35105 2.27963 2.59216 0.34459  -0.08558 -0.30223 383 TYR A OH  
2397 N N   . TYR A 384 ? 2.39445 2.08954 2.49105 0.34388  -0.16030 -0.23912 384 TYR A N   
2398 C CA  . TYR A 384 ? 2.42177 2.09268 2.49501 0.33723  -0.17100 -0.23732 384 TYR A CA  
2399 C C   . TYR A 384 ? 2.37736 2.05483 2.43281 0.33695  -0.16552 -0.24824 384 TYR A C   
2400 O O   . TYR A 384 ? 2.36559 2.06777 2.41695 0.34223  -0.15185 -0.25566 384 TYR A O   
2401 C CB  . TYR A 384 ? 2.42087 2.08216 2.47367 0.33526  -0.17237 -0.23034 384 TYR A CB  
2402 C CG  . TYR A 384 ? 2.40536 2.06289 2.47565 0.33527  -0.17456 -0.22087 384 TYR A CG  
2403 C CD1 . TYR A 384 ? 2.45403 2.09670 2.53704 0.32785  -0.18753 -0.21573 384 TYR A CD1 
2404 C CD2 . TYR A 384 ? 2.40538 2.07649 2.48057 0.34153  -0.16417 -0.21522 384 TYR A CD2 
2405 C CE1 . TYR A 384 ? 2.50782 2.14859 2.60644 0.32667  -0.18897 -0.20836 384 TYR A CE1 
2406 C CE2 . TYR A 384 ? 2.48686 2.15378 2.57896 0.34028  -0.16588 -0.20631 384 TYR A CE2 
2407 C CZ  . TYR A 384 ? 2.55144 2.20279 2.65439 0.33285  -0.17773 -0.20450 384 TYR A CZ  
2408 O OH  . TYR A 384 ? 2.60374 2.25234 2.72305 0.33045  -0.17894 -0.19691 384 TYR A OH  
2409 N N   . GLU A 385 ? 2.35622 2.01481 2.40072 0.32892  -0.17661 -0.24824 385 GLU A N   
2410 C CA  . GLU A 385 ? 2.34656 2.00833 2.37457 0.32636  -0.17309 -0.25816 385 GLU A CA  
2411 C C   . GLU A 385 ? 2.35615 2.00140 2.35470 0.31581  -0.18408 -0.25436 385 GLU A C   
2412 O O   . GLU A 385 ? 2.37049 2.00138 2.36855 0.30809  -0.19688 -0.24465 385 GLU A O   
2413 C CB  . GLU A 385 ? 2.40351 2.06343 2.46090 0.32559  -0.17435 -0.26441 385 GLU A CB  
2414 C CG  . GLU A 385 ? 2.58330 2.22219 2.66702 0.32051  -0.19136 -0.25187 385 GLU A CG  
2415 C CD  . GLU A 385 ? 2.63419 2.27002 2.75725 0.32171  -0.19198 -0.25769 385 GLU A CD  
2416 O OE1 . GLU A 385 ? 2.65119 2.29684 2.77452 0.32297  -0.18049 -0.27326 385 GLU A OE1 
2417 O OE2 . GLU A 385 ? 2.63874 2.26339 2.79573 0.32118  -0.20363 -0.24732 385 GLU A OE2 
2418 N N   . ASP A 386 ? 2.43611 2.08806 2.40970 0.31378  -0.17854 -0.26338 386 ASP A N   
2419 C CA  . ASP A 386 ? 2.47236 2.11514 2.41563 0.30252  -0.18688 -0.26303 386 ASP A CA  
2420 C C   . ASP A 386 ? 2.58035 2.23008 2.50656 0.29907  -0.18208 -0.27324 386 ASP A C   
2421 O O   . ASP A 386 ? 2.65413 2.31966 2.58714 0.30674  -0.16922 -0.28274 386 ASP A O   
2422 C CB  . ASP A 386 ? 2.65964 2.30676 2.58430 0.30490  -0.18233 -0.26444 386 ASP A CB  
2423 C CG  . ASP A 386 ? 2.71346 2.35483 2.61041 0.29117  -0.19045 -0.26786 386 ASP A CG  
2424 O OD1 . ASP A 386 ? 2.72373 2.37221 2.59858 0.28720  -0.18768 -0.27618 386 ASP A OD1 
2425 O OD2 . ASP A 386 ? 2.74438 2.37747 2.64177 0.28269  -0.19911 -0.26374 386 ASP A OD2 
2426 N N   . ALA A 387 ? 2.62324 2.26465 2.52689 0.28529  -0.19230 -0.27194 387 ALA A N   
2427 C CA  . ALA A 387 ? 2.68206 2.32856 2.56715 0.27891  -0.18951 -0.28064 387 ALA A CA  
2428 C C   . ALA A 387 ? 2.70716 2.35692 2.55571 0.26733  -0.19407 -0.28390 387 ALA A C   
2429 O O   . ALA A 387 ? 2.76395 2.40487 2.60504 0.25191  -0.20888 -0.27537 387 ALA A O   
2430 C CB  . ALA A 387 ? 2.73863 2.37063 2.64502 0.27042  -0.19974 -0.27369 387 ALA A CB  
2431 N N   . GLU A 388 ? 2.75408 2.42081 2.58156 0.27363  -0.18142 -0.29629 388 GLU A N   
2432 C CA  . GLU A 388 ? 2.76820 2.44224 2.56357 0.26351  -0.18315 -0.30412 388 GLU A CA  
2433 C C   . GLU A 388 ? 2.82296 2.50063 2.59937 0.25126  -0.18539 -0.30909 388 GLU A C   
2434 O O   . GLU A 388 ? 2.79884 2.49257 2.56041 0.25543  -0.17408 -0.32084 388 GLU A O   
2435 C CB  . GLU A 388 ? 2.69970 2.39074 2.48737 0.27683  -0.16926 -0.31364 388 GLU A CB  
2436 C CG  . GLU A 388 ? 2.65203 2.33758 2.45776 0.28578  -0.16807 -0.30835 388 GLU A CG  
2437 C CD  . GLU A 388 ? 2.60201 2.30218 2.40327 0.29635  -0.15690 -0.31594 388 GLU A CD  
2438 O OE1 . GLU A 388 ? 2.59720 2.31485 2.38094 0.29808  -0.14982 -0.32481 388 GLU A OE1 
2439 O OE2 . GLU A 388 ? 2.57339 2.26780 2.39161 0.30282  -0.15530 -0.31257 388 GLU A OE2 
2440 N N   . GLY A 389 ? 2.69967 2.36398 2.47777 0.23469  -0.20091 -0.29817 389 GLY A N   
2441 C CA  . GLY A 389 ? 2.75226 2.41651 2.51760 0.22096  -0.20515 -0.29868 389 GLY A CA  
2442 C C   . GLY A 389 ? 2.74800 2.40825 2.53664 0.23015  -0.19634 -0.30206 389 GLY A C   
2443 O O   . GLY A 389 ? 2.77236 2.41589 2.59370 0.23009  -0.20343 -0.29089 389 GLY A O   
2444 N N   . ASP A 390 ? 2.64514 2.32362 2.42011 0.23751  -0.18029 -0.31877 390 ASP A N   
2445 C CA  . ASP A 390 ? 2.63361 2.31643 2.43043 0.24539  -0.16812 -0.32783 390 ASP A CA  
2446 C C   . ASP A 390 ? 2.55639 2.25819 2.36544 0.26412  -0.15257 -0.33553 390 ASP A C   
2447 O O   . ASP A 390 ? 2.53874 2.24684 2.37340 0.27000  -0.14285 -0.34307 390 ASP A O   
2448 C CB  . ASP A 390 ? 2.66594 2.36170 2.44022 0.23632  -0.16071 -0.34159 390 ASP A CB  
2449 C CG  . ASP A 390 ? 2.75824 2.43597 2.52678 0.21593  -0.17572 -0.33199 390 ASP A CG  
2450 O OD1 . ASP A 390 ? 2.79689 2.45989 2.56617 0.20677  -0.19277 -0.31450 390 ASP A OD1 
2451 O OD2 . ASP A 390 ? 2.79815 2.47888 2.56220 0.20752  -0.17066 -0.34098 390 ASP A OD2 
2452 N N   . ASP A 391 ? 2.65214 2.36527 2.44656 0.27230  -0.14977 -0.33398 391 ASP A N   
2453 C CA  . ASP A 391 ? 2.59489 2.32505 2.40488 0.28860  -0.13827 -0.33424 391 ASP A CA  
2454 C C   . ASP A 391 ? 2.56455 2.27868 2.41042 0.29315  -0.14317 -0.32487 391 ASP A C   
2455 O O   . ASP A 391 ? 2.61996 2.30874 2.47580 0.28590  -0.15777 -0.31415 391 ASP A O   
2456 C CB  . ASP A 391 ? 2.56408 2.30263 2.35909 0.29567  -0.13716 -0.33045 391 ASP A CB  
2457 C CG  . ASP A 391 ? 2.56659 2.32967 2.33363 0.29596  -0.12862 -0.34095 391 ASP A CG  
2458 O OD1 . ASP A 391 ? 2.59392 2.37218 2.35151 0.29161  -0.12156 -0.35139 391 ASP A OD1 
2459 O OD2 . ASP A 391 ? 2.53733 2.30526 2.29484 0.30036  -0.12848 -0.33992 391 ASP A OD2 
2460 N N   . LYS A 392 ? 2.50760 2.24130 2.37338 0.30401  -0.13102 -0.32856 392 LYS A N   
2461 C CA  . LYS A 392 ? 2.41202 2.13703 2.31406 0.30884  -0.13301 -0.32307 392 LYS A CA  
2462 C C   . LYS A 392 ? 2.25980 2.00078 2.16737 0.32016  -0.12719 -0.31554 392 LYS A C   
2463 O O   . LYS A 392 ? 2.23543 2.00919 2.13768 0.32614  -0.11380 -0.32032 392 LYS A O   
2464 C CB  . LYS A 392 ? 2.45734 2.19422 2.38569 0.30806  -0.12288 -0.33779 392 LYS A CB  
2465 C CG  . LYS A 392 ? 2.54721 2.26688 2.47597 0.29665  -0.12770 -0.34455 392 LYS A CG  
2466 C CD  . LYS A 392 ? 2.56406 2.29083 2.53066 0.29613  -0.11741 -0.36109 392 LYS A CD  
2467 C CE  . LYS A 392 ? 2.64235 2.35382 2.61045 0.28441  -0.11980 -0.36876 392 LYS A CE  
2468 N NZ  . LYS A 392 ? 2.65552 2.38603 2.58023 0.27869  -0.11273 -0.37753 392 LYS A NZ  
2469 N N   . ILE A 393 ? 2.44746 2.16775 2.36665 0.32168  -0.13762 -0.30236 393 ILE A N   
2470 C CA  . ILE A 393 ? 2.37634 2.10613 2.30422 0.33092  -0.13391 -0.29277 393 ILE A CA  
2471 C C   . ILE A 393 ? 2.32542 2.05369 2.28801 0.33377  -0.13446 -0.28973 393 ILE A C   
2472 O O   . ILE A 393 ? 2.34803 2.05224 2.32697 0.32895  -0.14585 -0.28630 393 ILE A O   
2473 C CB  . ILE A 393 ? 2.41661 2.12624 2.33199 0.32935  -0.14355 -0.28312 393 ILE A CB  
2474 C CG1 . ILE A 393 ? 2.59622 2.30961 2.48043 0.32574  -0.14249 -0.28977 393 ILE A CG1 
2475 C CG2 . ILE A 393 ? 2.36167 2.07888 2.29057 0.33869  -0.13900 -0.27258 393 ILE A CG2 
2476 C CD1 . ILE A 393 ? 2.64621 2.34277 2.52065 0.32157  -0.15045 -0.28659 393 ILE A CD1 
2477 N N   . LYS A 394 ? 2.17005 1.92777 2.14515 0.34063  -0.12256 -0.29001 394 LYS A N   
2478 C CA  . LYS A 394 ? 2.16622 1.93020 2.17447 0.34309  -0.12086 -0.28908 394 LYS A CA  
2479 C C   . LYS A 394 ? 2.15964 1.94604 2.17025 0.34919  -0.11450 -0.27718 394 LYS A C   
2480 O O   . LYS A 394 ? 2.15423 1.97318 2.15245 0.35159  -0.10386 -0.27680 394 LYS A O   
2481 C CB  . LYS A 394 ? 2.16271 1.95019 2.19102 0.34099  -0.10980 -0.30798 394 LYS A CB  
2482 C CG  . LYS A 394 ? 2.21059 1.97319 2.24814 0.33501  -0.11627 -0.31807 394 LYS A CG  
2483 C CD  . LYS A 394 ? 2.27842 2.01318 2.34955 0.33483  -0.12880 -0.31130 394 LYS A CD  
2484 C CE  . LYS A 394 ? 2.41849 2.13416 2.51086 0.32942  -0.13367 -0.32001 394 LYS A CE  
2485 N NZ  . LYS A 394 ? 2.50556 2.20129 2.64095 0.33070  -0.14450 -0.31332 394 LYS A NZ  
2486 N N   . LEU A 395 ? 2.22272 1.99391 2.25037 0.35077  -0.12146 -0.26570 395 LEU A N   
2487 C CA  . LEU A 395 ? 2.21357 2.00088 2.24529 0.35535  -0.11712 -0.25107 395 LEU A CA  
2488 C C   . LEU A 395 ? 2.24193 2.02305 2.30143 0.35505  -0.12126 -0.24521 395 LEU A C   
2489 O O   . LEU A 395 ? 2.29366 2.05344 2.36821 0.35224  -0.12968 -0.25031 395 LEU A O   
2490 C CB  . LEU A 395 ? 2.22078 1.98877 2.23390 0.35768  -0.12210 -0.23951 395 LEU A CB  
2491 C CG  . LEU A 395 ? 2.27210 1.99922 2.27816 0.35278  -0.13556 -0.24005 395 LEU A CG  
2492 C CD1 . LEU A 395 ? 2.34151 2.05180 2.36567 0.35211  -0.14183 -0.22914 395 LEU A CD1 
2493 C CD2 . LEU A 395 ? 2.27463 1.99385 2.25616 0.35275  -0.13606 -0.24173 395 LEU A CD2 
2494 N N   . PHE A 396 ? 2.14608 1.94820 2.21398 0.35749  -0.11579 -0.23243 396 PHE A N   
2495 C CA  . PHE A 396 ? 2.14647 1.94652 2.23898 0.35655  -0.11879 -0.22527 396 PHE A CA  
2496 C C   . PHE A 396 ? 2.18448 1.98360 2.27629 0.35864  -0.11878 -0.20468 396 PHE A C   
2497 O O   . PHE A 396 ? 2.17737 1.98457 2.25509 0.36191  -0.11484 -0.19574 396 PHE A O   
2498 C CB  . PHE A 396 ? 2.13873 1.97866 2.25327 0.35439  -0.10876 -0.23553 396 PHE A CB  
2499 C CG  . PHE A 396 ? 2.15313 2.04201 2.26384 0.35332  -0.09634 -0.22784 396 PHE A CG  
2500 C CD1 . PHE A 396 ? 2.13094 2.05123 2.22561 0.35224  -0.08678 -0.23586 396 PHE A CD1 
2501 C CD2 . PHE A 396 ? 2.16025 2.06742 2.28386 0.35167  -0.09468 -0.21102 396 PHE A CD2 
2502 C CE1 . PHE A 396 ? 2.13499 2.10729 2.22630 0.34923  -0.07648 -0.22584 396 PHE A CE1 
2503 C CE2 . PHE A 396 ? 2.18196 2.13905 2.30289 0.34851  -0.08479 -0.19947 396 PHE A CE2 
2504 C CZ  . PHE A 396 ? 2.16973 2.16121 2.27445 0.34710  -0.07600 -0.20620 396 PHE A CZ  
2505 N N   . GLY A 397 ? 2.19090 1.98045 2.30176 0.35675  -0.12320 -0.19668 397 GLY A N   
2506 C CA  . GLY A 397 ? 2.17866 1.96255 2.29472 0.35756  -0.12353 -0.17727 397 GLY A CA  
2507 C C   . GLY A 397 ? 2.23526 2.04769 2.37267 0.35467  -0.11874 -0.16669 397 GLY A C   
2508 O O   . GLY A 397 ? 2.29722 2.10377 2.45129 0.35123  -0.12277 -0.17131 397 GLY A O   
2509 N N   . ILE A 398 ? 2.19593 2.04277 2.33404 0.35505  -0.11068 -0.15099 398 ILE A N   
2510 C CA  . ILE A 398 ? 2.28872 2.17014 2.44517 0.34968  -0.10585 -0.13779 398 ILE A CA  
2511 C C   . ILE A 398 ? 2.40384 2.26196 2.57212 0.34957  -0.11025 -0.11480 398 ILE A C   
2512 O O   . ILE A 398 ? 2.40545 2.25125 2.57024 0.35416  -0.11053 -0.10004 398 ILE A O   
2513 C CB  . ILE A 398 ? 2.30436 2.24513 2.45614 0.34668  -0.09507 -0.13110 398 ILE A CB  
2514 C CG1 . ILE A 398 ? 2.47931 2.45739 2.64797 0.33916  -0.09146 -0.10882 398 ILE A CG1 
2515 C CG2 . ILE A 398 ? 2.30223 2.24323 2.43636 0.35270  -0.09383 -0.12117 398 ILE A CG2 
2516 C CD1 . ILE A 398 ? 2.49713 2.54316 2.66111 0.33257  -0.08161 -0.09893 398 ILE A CD1 
2517 N N   . VAL A 399 ? 2.46785 2.31963 2.65361 0.34428  -0.11329 -0.11283 399 VAL A N   
2518 C CA  . VAL A 399 ? 2.53488 2.36505 2.73560 0.34212  -0.11651 -0.09273 399 VAL A CA  
2519 C C   . VAL A 399 ? 2.59707 2.46211 2.81614 0.33365  -0.11298 -0.07953 399 VAL A C   
2520 O O   . VAL A 399 ? 2.61269 2.48045 2.84108 0.32898  -0.11484 -0.09206 399 VAL A O   
2521 C CB  . VAL A 399 ? 2.52199 2.30090 2.72431 0.34171  -0.12541 -0.10451 399 VAL A CB  
2522 C CG1 . VAL A 399 ? 2.56991 2.32806 2.79124 0.33750  -0.12700 -0.08776 399 VAL A CG1 
2523 C CG2 . VAL A 399 ? 2.47332 2.22283 2.65677 0.34733  -0.12866 -0.11647 399 VAL A CG2 
2524 N N   . GLY A 400 ? 2.50666 2.40126 2.73284 0.33089  -0.10843 -0.05295 400 GLY A N   
2525 C CA  . GLY A 400 ? 2.56248 2.49251 2.80551 0.32036  -0.10560 -0.03646 400 GLY A CA  
2526 C C   . GLY A 400 ? 2.57697 2.57330 2.81678 0.31428  -0.09792 -0.02122 400 GLY A C   
2527 O O   . GLY A 400 ? 2.54301 2.55612 2.76873 0.31906  -0.09491 -0.01989 400 GLY A O   
2528 N N   . SER A 401 ? 2.57215 2.61137 2.82481 0.30173  -0.09467 -0.00943 401 SER A N   
2529 C CA  . SER A 401 ? 2.58878 2.70287 2.83887 0.29091  -0.08714 0.00456  401 SER A CA  
2530 C C   . SER A 401 ? 2.55716 2.71018 2.79425 0.28909  -0.07911 -0.03008 401 SER A C   
2531 O O   . SER A 401 ? 2.54269 2.66346 2.77741 0.29617  -0.08020 -0.06215 401 SER A O   
2532 C CB  . SER A 401 ? 2.64627 2.79797 2.91372 0.27523  -0.08589 0.02402  401 SER A CB  
2533 O OG  . SER A 401 ? 2.67140 2.90576 2.93481 0.26092  -0.07794 0.03208  401 SER A OG  
2534 N N   . ILE A 402 ? 2.51581 2.74155 2.74712 0.27813  -0.07087 -0.02293 402 ILE A N   
2535 C CA  . ILE A 402 ? 2.47707 2.74698 2.69887 0.27415  -0.06074 -0.05726 402 ILE A CA  
2536 C C   . ILE A 402 ? 2.49500 2.85637 2.72212 0.25323  -0.05058 -0.05428 402 ILE A C   
2537 O O   . ILE A 402 ? 2.51434 2.91938 2.73997 0.24299  -0.05110 -0.01740 402 ILE A O   
2538 C CB  . ILE A 402 ? 2.41952 2.68246 2.62081 0.28355  -0.05968 -0.06062 402 ILE A CB  
2539 C CG1 . ILE A 402 ? 2.39064 2.69960 2.58481 0.27773  -0.04784 -0.09844 402 ILE A CG1 
2540 C CG2 . ILE A 402 ? 2.41510 2.70666 2.61083 0.28120  -0.06169 -0.01846 402 ILE A CG2 
2541 C CD1 . ILE A 402 ? 2.33497 2.62270 2.50946 0.28831  -0.04735 -0.11062 402 ILE A CD1 
2542 N N   . PRO A 403 ? 2.45293 2.84861 2.68954 0.24516  -0.04124 -0.09180 403 PRO A N   
2543 C CA  . PRO A 403 ? 2.46243 2.94525 2.70827 0.22256  -0.03152 -0.09163 403 PRO A CA  
2544 C C   . PRO A 403 ? 2.41812 2.98586 2.65084 0.20783  -0.01962 -0.09679 403 PRO A C   
2545 O O   . PRO A 403 ? 2.42763 3.07276 2.66062 0.18701  -0.01502 -0.07647 403 PRO A O   
2546 C CB  . PRO A 403 ? 2.45913 2.93647 2.72700 0.22206  -0.02637 -0.13414 403 PRO A CB  
2547 C CG  . PRO A 403 ? 2.42374 2.84164 2.68921 0.24049  -0.02812 -0.16394 403 PRO A CG  
2548 C CD  . PRO A 403 ? 2.43074 2.78124 2.67748 0.25596  -0.04102 -0.13293 403 PRO A CD  
2549 N N   . LYS A 404 ? 2.30316 2.86195 2.52383 0.21621  -0.01473 -0.12214 404 LYS A N   
2550 C CA  . LYS A 404 ? 2.25769 2.90031 2.46616 0.20069  -0.00197 -0.13258 404 LYS A CA  
2551 C C   . LYS A 404 ? 2.22303 2.83940 2.40891 0.21344  -0.00553 -0.12268 404 LYS A C   
2552 O O   . LYS A 404 ? 2.22117 2.75663 2.40343 0.23393  -0.01272 -0.13237 404 LYS A O   
2553 C CB  . LYS A 404 ? 2.22793 2.90990 2.45171 0.19152  0.01414  -0.18990 404 LYS A CB  
2554 C CG  . LYS A 404 ? 2.26106 2.86834 2.49204 0.21156  0.01325  -0.22702 404 LYS A CG  
2555 C CD  . LYS A 404 ? 2.22610 2.87493 2.48064 0.20220  0.03032  -0.28342 404 LYS A CD  
2556 C CE  . LYS A 404 ? 2.24589 2.91914 2.53183 0.19283  0.03458  -0.29976 404 LYS A CE  
2557 N NZ  . LYS A 404 ? 2.20635 2.91670 2.52395 0.18534  0.05198  -0.35809 404 LYS A NZ  
2558 N N   . THR A 405 ? 2.17567 2.86557 2.34654 0.19976  -0.00070 -0.10285 405 THR A N   
2559 C CA  . THR A 405 ? 2.13352 2.81269 2.28343 0.20952  -0.00261 -0.09441 405 THR A CA  
2560 C C   . THR A 405 ? 2.08714 2.75789 2.23291 0.21304  0.00853  -0.14841 405 THR A C   
2561 O O   . THR A 405 ? 2.06013 2.80716 2.20487 0.19504  0.02383  -0.17724 405 THR A O   
2562 C CB  . THR A 405 ? 2.11791 2.88885 2.25578 0.19151  0.00002  -0.05985 405 THR A CB  
2563 O OG1 . THR A 405 ? 2.16028 2.92989 2.30716 0.18996  -0.01224 -0.00479 405 THR A OG1 
2564 C CG2 . THR A 405 ? 2.06346 2.82899 2.18087 0.20132  -0.00112 -0.05411 405 THR A CG2 
2565 N N   . THR A 406 ? 2.20205 2.78153 2.34747 0.23470  0.00110  -0.16264 406 THR A N   
2566 C CA  . THR A 406 ? 2.16504 2.72157 2.31202 0.23990  0.00906  -0.21076 406 THR A CA  
2567 C C   . THR A 406 ? 2.11793 2.66267 2.24000 0.24773  0.00840  -0.20874 406 THR A C   
2568 O O   . THR A 406 ? 2.11289 2.62240 2.22109 0.25955  -0.00332 -0.17357 406 THR A O   
2569 C CB  . THR A 406 ? 2.18385 2.65209 2.34780 0.25634  0.00019  -0.22630 406 THR A CB  
2570 O OG1 . THR A 406 ? 2.21777 2.71053 2.40958 0.24683  0.00669  -0.24843 406 THR A OG1 
2571 C CG2 . THR A 406 ? 2.14776 2.56685 2.30785 0.26785  0.00098  -0.25783 406 THR A CG2 
2572 N N   . SER A 407 ? 2.11370 2.69052 2.23303 0.24033  0.02196  -0.24817 407 SER A N   
2573 C CA  . SER A 407 ? 2.06836 2.63491 2.16457 0.24641  0.02283  -0.25292 407 SER A CA  
2574 C C   . SER A 407 ? 2.03387 2.56547 2.13968 0.25027  0.03013  -0.30160 407 SER A C   
2575 O O   . SER A 407 ? 2.02864 2.59942 2.15616 0.23768  0.04420  -0.33912 407 SER A O   
2576 C CB  . SER A 407 ? 2.03161 2.69610 2.11131 0.22790  0.03362  -0.24501 407 SER A CB  
2577 O OG  . SER A 407 ? 2.05670 2.76529 2.13519 0.22042  0.02747  -0.19908 407 SER A OG  
2578 N N   . PHE A 408 ? 2.05829 2.51808 2.15127 0.26668  0.02080  -0.30121 408 PHE A N   
2579 C CA  . PHE A 408 ? 2.02942 2.45197 2.13166 0.27032  0.02555  -0.34142 408 PHE A CA  
2580 C C   . PHE A 408 ? 2.00388 2.39958 2.07745 0.27779  0.02187  -0.33810 408 PHE A C   
2581 O O   . PHE A 408 ? 1.98859 2.37742 2.03902 0.28463  0.01284  -0.30415 408 PHE A O   
2582 C CB  . PHE A 408 ? 2.04591 2.39259 2.17248 0.28270  0.01487  -0.34812 408 PHE A CB  
2583 C CG  . PHE A 408 ? 2.05673 2.34045 2.17216 0.29740  -0.00407 -0.31057 408 PHE A CG  
2584 C CD1 . PHE A 408 ? 2.09402 2.38726 2.21687 0.29655  -0.00953 -0.28323 408 PHE A CD1 
2585 C CD2 . PHE A 408 ? 1.98024 2.19725 2.07967 0.31022  -0.01566 -0.30476 408 PHE A CD2 
2586 C CE1 . PHE A 408 ? 2.02629 2.26206 2.14288 0.30872  -0.02523 -0.25245 408 PHE A CE1 
2587 C CE2 . PHE A 408 ? 2.00071 2.16422 2.09263 0.32152  -0.03121 -0.27529 408 PHE A CE2 
2588 C CZ  . PHE A 408 ? 2.01314 2.18494 2.11487 0.32105  -0.03553 -0.25011 408 PHE A CZ  
2589 N N   . THR A 409 ? 1.89102 2.27180 1.96991 0.27618  0.02926  -0.37442 409 THR A N   
2590 C CA  . THR A 409 ? 1.89182 2.26252 1.94386 0.27844  0.02975  -0.37869 409 THR A CA  
2591 C C   . THR A 409 ? 1.89545 2.19717 1.95812 0.28580  0.02553  -0.40297 409 THR A C   
2592 O O   . THR A 409 ? 1.89712 2.20049 1.99089 0.28003  0.03467  -0.43653 409 THR A O   
2593 C CB  . THR A 409 ? 1.88993 2.34777 1.93335 0.26023  0.04869  -0.39953 409 THR A CB  
2594 O OG1 . THR A 409 ? 1.88828 2.41460 1.92114 0.25196  0.05030  -0.37040 409 THR A OG1 
2595 C CG2 . THR A 409 ? 1.89097 2.34008 1.90679 0.26177  0.04977  -0.40575 409 THR A CG2 
2596 N N   . CYS A 410 ? 1.93485 2.17868 1.97498 0.29757  0.01178  -0.38589 410 CYS A N   
2597 C CA  . CYS A 410 ? 1.91634 2.09941 1.96038 0.30226  0.00603  -0.40305 410 CYS A CA  
2598 C C   . CYS A 410 ? 1.96517 2.16074 1.98016 0.29823  0.01129  -0.41212 410 CYS A C   
2599 O O   . CYS A 410 ? 1.96473 2.20583 1.95426 0.29551  0.01556  -0.39879 410 CYS A O   
2600 C CB  . CYS A 410 ? 1.93623 2.04512 1.97740 0.31572  -0.01440 -0.37858 410 CYS A CB  
2601 S SG  . CYS A 410 ? 2.10063 2.13904 2.16177 0.31858  -0.02393 -0.39605 410 CYS A SG  
2602 N N   . ILE A 411 ? 2.09410 2.25013 2.11495 0.29735  0.01040  -0.43330 411 ILE A N   
2603 C CA  . ILE A 411 ? 2.10036 2.27117 2.09910 0.29040  0.01815  -0.44958 411 ILE A CA  
2604 C C   . ILE A 411 ? 2.13135 2.23409 2.11410 0.29718  0.00299  -0.44130 411 ILE A C   
2605 O O   . ILE A 411 ? 2.13313 2.18079 2.13658 0.30170  -0.00816 -0.44015 411 ILE A O   
2606 C CB  . ILE A 411 ? 2.10960 2.31501 2.13598 0.27646  0.03740  -0.49184 411 ILE A CB  
2607 C CG1 . ILE A 411 ? 2.06173 2.35679 2.08715 0.26392  0.05558  -0.50227 411 ILE A CG1 
2608 C CG2 . ILE A 411 ? 2.09525 2.28324 2.10941 0.27075  0.04093  -0.51123 411 ILE A CG2 
2609 C CD1 . ILE A 411 ? 2.04677 2.38433 2.10175 0.24770  0.07729  -0.54894 411 ILE A CD1 
2610 N N   . CYS A 412 ? 2.27577 2.38707 2.22225 0.29667  0.00231  -0.43481 412 CYS A N   
2611 C CA  . CYS A 412 ? 2.27920 2.33881 2.20576 0.29902  -0.00949 -0.43095 412 CYS A CA  
2612 C C   . CYS A 412 ? 2.36081 2.44372 2.27577 0.28739  0.00285  -0.45704 412 CYS A C   
2613 O O   . CYS A 412 ? 2.34492 2.48395 2.23979 0.28239  0.01437  -0.46118 412 CYS A O   
2614 C CB  . CYS A 412 ? 2.31475 2.36260 2.21019 0.30864  -0.02131 -0.40169 412 CYS A CB  
2615 S SG  . CYS A 412 ? 2.38427 2.38068 2.25084 0.30866  -0.03465 -0.39863 412 CYS A SG  
2616 N N   . LYS A 413 ? 2.20931 2.25119 2.13860 0.28220  0.00011  -0.47304 413 LYS A N   
2617 C CA  . LYS A 413 ? 2.21616 2.27525 2.14214 0.26943  0.01283  -0.50111 413 LYS A CA  
2618 C C   . LYS A 413 ? 2.27686 2.28718 2.18091 0.26770  -0.00011 -0.49432 413 LYS A C   
2619 O O   . LYS A 413 ? 2.32485 2.28065 2.24817 0.26853  -0.01294 -0.48867 413 LYS A O   
2620 C CB  . LYS A 413 ? 2.22306 2.28536 2.19739 0.26140  0.02537  -0.53208 413 LYS A CB  
2621 C CG  . LYS A 413 ? 2.23324 2.30744 2.21059 0.24708  0.03912  -0.56348 413 LYS A CG  
2622 C CD  . LYS A 413 ? 2.27034 2.32776 2.30546 0.24103  0.04792  -0.59245 413 LYS A CD  
2623 C CE  . LYS A 413 ? 2.31409 2.36770 2.35468 0.22708  0.05835  -0.61997 413 LYS A CE  
2624 N NZ  . LYS A 413 ? 2.37244 2.37211 2.38510 0.22811  0.03991  -0.59788 413 LYS A NZ  
2625 N N   . LYS A 414 ? 2.40089 2.43511 2.26578 0.26400  0.00304  -0.49417 414 LYS A N   
2626 C CA  . LYS A 414 ? 2.47833 2.47920 2.31889 0.25843  -0.00583 -0.49289 414 LYS A CA  
2627 C C   . LYS A 414 ? 2.50054 2.53381 2.33643 0.24380  0.01106  -0.52252 414 LYS A C   
2628 O O   . LYS A 414 ? 2.47351 2.56121 2.28436 0.24085  0.02267  -0.52894 414 LYS A O   
2629 C CB  . LYS A 414 ? 2.47705 2.47810 2.27728 0.26611  -0.01639 -0.46980 414 LYS A CB  
2630 C CG  . LYS A 414 ? 2.53437 2.51503 2.30448 0.25797  -0.02302 -0.47176 414 LYS A CG  
2631 C CD  . LYS A 414 ? 2.58844 2.50725 2.36954 0.25407  -0.04003 -0.46280 414 LYS A CD  
2632 C CE  . LYS A 414 ? 2.57116 2.46142 2.35136 0.26509  -0.05625 -0.43718 414 LYS A CE  
2633 N NZ  . LYS A 414 ? 2.54407 2.44855 2.28871 0.27045  -0.05993 -0.42651 414 LYS A NZ  
2634 N N   . ASP A 415 ? 2.54944 2.55061 2.41221 0.23421  0.01223  -0.53947 415 ASP A N   
2635 C CA  . ASP A 415 ? 2.57433 2.59979 2.44194 0.21839  0.02947  -0.57167 415 ASP A CA  
2636 C C   . ASP A 415 ? 2.51925 2.61232 2.40171 0.21454  0.05191  -0.59584 415 ASP A C   
2637 O O   . ASP A 415 ? 2.47781 2.57719 2.39171 0.22077  0.05421  -0.59586 415 ASP A O   
2638 C CB  . ASP A 415 ? 2.61900 2.65034 2.43943 0.21166  0.02664  -0.56848 415 ASP A CB  
2639 C CG  . ASP A 415 ? 2.67511 2.64401 2.48565 0.21050  0.00572  -0.54881 415 ASP A CG  
2640 O OD1 . ASP A 415 ? 2.66522 2.60849 2.46429 0.22146  -0.01126 -0.52147 415 ASP A OD1 
2641 O OD2 . ASP A 415 ? 2.73208 2.67972 2.54786 0.19693  0.00641  -0.56073 415 ASP A OD2 
2642 N N   . LYS A 416 ? 2.60205 2.75083 2.46245 0.20273  0.06861  -0.61664 416 LYS A N   
2643 C CA  . LYS A 416 ? 2.54980 2.77339 2.42109 0.19504  0.09029  -0.63993 416 LYS A CA  
2644 C C   . LYS A 416 ? 2.49226 2.76046 2.34190 0.20569  0.08697  -0.61379 416 LYS A C   
2645 O O   . LYS A 416 ? 2.43416 2.76241 2.29814 0.20007  0.10149  -0.62627 416 LYS A O   
2646 C CB  . LYS A 416 ? 2.56586 2.83955 2.41868 0.17686  0.10872  -0.66949 416 LYS A CB  
2647 C CG  . LYS A 416 ? 2.60002 2.84657 2.48777 0.16204  0.11972  -0.70511 416 LYS A CG  
2648 C CD  . LYS A 416 ? 2.61804 2.92429 2.48785 0.14217  0.14077  -0.73752 416 LYS A CD  
2649 C CE  . LYS A 416 ? 2.64736 2.93542 2.56257 0.12558  0.15653  -0.77924 416 LYS A CE  
2650 N NZ  . LYS A 416 ? 2.71872 2.95284 2.62184 0.11978  0.14752  -0.77611 416 LYS A NZ  
2651 N N   . LYS A 417 ? 2.50068 2.74316 2.31936 0.21955  0.06866  -0.57846 417 LYS A N   
2652 C CA  . LYS A 417 ? 2.41775 2.69816 2.22032 0.23029  0.06456  -0.55066 417 LYS A CA  
2653 C C   . LYS A 417 ? 2.37447 2.63570 2.20819 0.24010  0.05838  -0.53733 417 LYS A C   
2654 O O   . LYS A 417 ? 2.40555 2.61212 2.26830 0.24261  0.05201  -0.54254 417 LYS A O   
2655 C CB  . LYS A 417 ? 2.43562 2.69199 2.20222 0.24180  0.04836  -0.52141 417 LYS A CB  
2656 C CG  . LYS A 417 ? 2.50612 2.77403 2.24244 0.23207  0.05273  -0.53510 417 LYS A CG  
2657 C CD  . LYS A 417 ? 2.53552 2.78211 2.23989 0.24287  0.03770  -0.51011 417 LYS A CD  
2658 C CE  . LYS A 417 ? 2.58916 2.84554 2.26473 0.23151  0.04213  -0.52643 417 LYS A CE  
2659 N NZ  . LYS A 417 ? 2.58146 2.85428 2.22612 0.24054  0.03469  -0.50679 417 LYS A NZ  
2660 N N   . SER A 418 ? 2.36881 2.67798 2.19780 0.24510  0.05975  -0.51799 418 SER A N   
2661 C CA  . SER A 418 ? 2.33805 2.64269 2.19514 0.25176  0.05643  -0.50646 418 SER A CA  
2662 C C   . SER A 418 ? 2.31249 2.62982 2.15344 0.26474  0.04529  -0.46665 418 SER A C   
2663 O O   . SER A 418 ? 2.31008 2.66050 2.12356 0.26645  0.04468  -0.45155 418 SER A O   
2664 C CB  . SER A 418 ? 2.30184 2.67077 2.18512 0.23700  0.07672  -0.53466 418 SER A CB  
2665 O OG  . SER A 418 ? 2.27321 2.65208 2.17775 0.24239  0.07383  -0.51963 418 SER A OG  
2666 N N   . ALA A 419 ? 2.19521 2.48602 2.05738 0.27390  0.03654  -0.44957 419 ALA A N   
2667 C CA  . ALA A 419 ? 2.17943 2.47581 2.03452 0.28609  0.02592  -0.41155 419 ALA A CA  
2668 C C   . ALA A 419 ? 2.16150 2.46234 2.04627 0.28721  0.02587  -0.40503 419 ALA A C   
2669 O O   . ALA A 419 ? 2.17403 2.41973 2.07956 0.29194  0.01860  -0.40982 419 ALA A O   
2670 C CB  . ALA A 419 ? 2.20540 2.43433 2.04645 0.30026  0.00793  -0.39105 419 ALA A CB  
2671 N N   . TYR A 420 ? 2.17962 2.54912 2.06672 0.28179  0.03334  -0.39263 420 TYR A N   
2672 C CA  . TYR A 420 ? 2.15997 2.54466 2.07307 0.28049  0.03419  -0.38514 420 TYR A CA  
2673 C C   . TYR A 420 ? 2.10834 2.46527 2.02100 0.29515  0.01838  -0.34301 420 TYR A C   
2674 O O   . TYR A 420 ? 2.12081 2.47840 2.01509 0.30328  0.01118  -0.31745 420 TYR A O   
2675 C CB  . TYR A 420 ? 2.13592 2.61749 2.05282 0.26276  0.05120  -0.39444 420 TYR A CB  
2676 C CG  . TYR A 420 ? 2.12957 2.64606 2.05245 0.24563  0.06995  -0.44111 420 TYR A CG  
2677 C CD1 . TYR A 420 ? 2.14234 2.61078 2.09147 0.24482  0.07347  -0.47452 420 TYR A CD1 
2678 C CD2 . TYR A 420 ? 2.11006 2.70897 2.01582 0.22964  0.08424  -0.45154 420 TYR A CD2 
2679 C CE1 . TYR A 420 ? 2.13868 2.63634 2.10027 0.22909  0.09170  -0.51897 420 TYR A CE1 
2680 C CE2 . TYR A 420 ? 2.10204 2.73413 2.01570 0.21229  0.10311  -0.49774 420 TYR A CE2 
2681 C CZ  . TYR A 420 ? 2.12056 2.69974 2.06376 0.21238  0.10724  -0.53229 420 TYR A CZ  
2682 O OH  . TYR A 420 ? 2.12202 2.73170 2.07973 0.19505  0.12706  -0.57995 420 TYR A OH  
2683 N N   . MET A 421 ? 1.99990 2.33277 1.93667 0.29833  0.01361  -0.33727 421 MET A N   
2684 C CA  . MET A 421 ? 2.02402 2.33070 1.96595 0.31017  0.00015  -0.30016 421 MET A CA  
2685 C C   . MET A 421 ? 2.03939 2.37936 2.00541 0.30341  0.00413  -0.29467 421 MET A C   
2686 O O   . MET A 421 ? 2.05850 2.39014 2.04504 0.29797  0.00944  -0.32080 421 MET A O   
2687 C CB  . MET A 421 ? 2.00497 2.22316 1.94868 0.32340  -0.01479 -0.29699 421 MET A CB  
2688 C CG  . MET A 421 ? 2.02048 2.20951 1.97968 0.33211  -0.02587 -0.26890 421 MET A CG  
2689 S SD  . MET A 421 ? 2.06997 2.17266 2.02296 0.34634  -0.04331 -0.25702 421 MET A SD  
2690 C CE  . MET A 421 ? 2.07926 2.17313 2.05370 0.35260  -0.05093 -0.22378 421 MET A CE  
2691 N N   . THR A 422 ? 1.91536 2.29268 1.88206 0.30367  0.00112  -0.25983 422 THR A N   
2692 C CA  . THR A 422 ? 1.95008 2.37190 1.93655 0.29407  0.00534  -0.25090 422 THR A CA  
2693 C C   . THR A 422 ? 1.98385 2.36653 1.98155 0.30552  -0.00889 -0.21320 422 THR A C   
2694 O O   . THR A 422 ? 1.98801 2.37899 1.98006 0.31170  -0.01572 -0.17785 422 THR A O   
2695 C CB  . THR A 422 ? 1.94296 2.46527 1.92191 0.27737  0.01685  -0.24297 422 THR A CB  
2696 O OG1 . THR A 422 ? 1.93443 2.49426 1.90456 0.26489  0.03185  -0.28272 422 THR A OG1 
2697 C CG2 . THR A 422 ? 1.97793 2.55197 1.97633 0.26442  0.02123  -0.23392 422 THR A CG2 
2698 N N   . VAL A 423 ? 1.95684 2.29829 1.97398 0.30806  -0.01303 -0.22083 423 VAL A N   
2699 C CA  . VAL A 423 ? 1.99534 2.30698 2.02654 0.31522  -0.02421 -0.18896 423 VAL A CA  
2700 C C   . VAL A 423 ? 2.01860 2.39956 2.06382 0.30088  -0.01770 -0.17561 423 VAL A C   
2701 O O   . VAL A 423 ? 2.02270 2.44536 2.07694 0.28761  -0.00621 -0.20368 423 VAL A O   
2702 C CB  . VAL A 423 ? 1.96136 2.19655 2.00536 0.32389  -0.03275 -0.20272 423 VAL A CB  
2703 C CG1 . VAL A 423 ? 1.94147 2.14891 2.00048 0.32933  -0.04296 -0.17211 423 VAL A CG1 
2704 C CG2 . VAL A 423 ? 1.93601 2.11046 1.96443 0.33449  -0.03957 -0.21470 423 VAL A CG2 
2705 N N   . THR A 424 ? 1.97816 2.37359 2.02817 0.30247  -0.02471 -0.13311 424 THR A N   
2706 C CA  . THR A 424 ? 1.98133 2.44734 2.04316 0.28697  -0.02049 -0.11211 424 THR A CA  
2707 C C   . THR A 424 ? 1.99039 2.41513 2.07071 0.29421  -0.03248 -0.07801 424 THR A C   
2708 O O   . THR A 424 ? 1.99957 2.41900 2.08369 0.30082  -0.04075 -0.03832 424 THR A O   
2709 C CB  . THR A 424 ? 1.98384 2.53079 2.03372 0.27677  -0.01612 -0.08791 424 THR A CB  
2710 O OG1 . THR A 424 ? 1.97631 2.55009 2.00715 0.27212  -0.00565 -0.12112 424 THR A OG1 
2711 C CG2 . THR A 424 ? 1.98696 2.62119 2.04649 0.25496  -0.00983 -0.07259 424 THR A CG2 
2712 N N   . ILE A 425 ? 2.08614 2.48231 2.18149 0.29282  -0.03312 -0.09390 425 ILE A N   
2713 C CA  . ILE A 425 ? 2.14709 2.50332 2.26063 0.29775  -0.04329 -0.06681 425 ILE A CA  
2714 C C   . ILE A 425 ? 2.18762 2.61589 2.31331 0.27990  -0.03950 -0.04349 425 ILE A C   
2715 O O   . ILE A 425 ? 2.19337 2.66664 2.32422 0.26558  -0.03005 -0.06798 425 ILE A O   
2716 C CB  . ILE A 425 ? 2.15728 2.44675 2.28060 0.30491  -0.04714 -0.09416 425 ILE A CB  
2717 C CG1 . ILE A 425 ? 2.09322 2.34120 2.20285 0.31406  -0.04633 -0.12870 425 ILE A CG1 
2718 C CG2 . ILE A 425 ? 2.19916 2.42564 2.33491 0.31518  -0.05953 -0.06814 425 ILE A CG2 
2719 C CD1 . ILE A 425 ? 2.02071 2.20606 2.14125 0.32055  -0.05199 -0.15165 425 ILE A CD1 
2720 N N   . ASP A 426 ? 2.16473 2.60564 2.29809 0.27994  -0.04680 0.00395  426 ASP A N   
2721 C CA  . ASP A 426 ? 2.21320 2.72669 2.35753 0.26131  -0.04523 0.03502  426 ASP A CA  
2722 C C   . ASP A 426 ? 2.28881 2.77044 2.45371 0.25918  -0.05019 0.04284  426 ASP A C   
2723 O O   . ASP A 426 ? 2.31097 2.71064 2.48416 0.27421  -0.05769 0.03787  426 ASP A O   
2724 C CB  . ASP A 426 ? 2.21692 2.75864 2.36548 0.26224  -0.05229 0.08752  426 ASP A CB  
2725 C CG  . ASP A 426 ? 2.14750 2.72782 2.27585 0.26334  -0.04764 0.08197  426 ASP A CG  
2726 O OD1 . ASP A 426 ? 2.10593 2.75994 2.21941 0.24634  -0.03601 0.05879  426 ASP A OD1 
2727 O OD2 . ASP A 426 ? 2.12922 2.66807 2.25790 0.28040  -0.05470 0.09796  426 ASP A OD2 
2728 N N   . SER A 427 ? 2.36978 2.92263 2.54232 0.23814  -0.04558 0.05466  427 SER A N   
2729 C CA  . SER A 427 ? 2.42626 2.96397 2.61772 0.23199  -0.04887 0.06205  427 SER A CA  
2730 C C   . SER A 427 ? 2.47277 3.05723 2.67725 0.21861  -0.05476 0.11838  427 SER A C   
2731 O O   . SER A 427 ? 2.45178 3.12918 2.65045 0.19826  -0.04934 0.13360  427 SER A O   
2732 C CB  . SER A 427 ? 2.42921 3.01012 2.62201 0.21721  -0.03716 0.01903  427 SER A CB  
2733 O OG  . SER A 427 ? 2.37219 3.05266 2.55460 0.19678  -0.02549 0.01131  427 SER A OG  
2734 N N   . ALA A 428 ? 2.39868 2.92152 2.62252 0.22838  -0.06571 0.14940  428 ALA A N   
2735 C CA  . ALA A 428 ? 2.44928 3.00508 2.69235 0.21710  -0.07290 0.20704  428 ALA A CA  
2736 C C   . ALA A 428 ? 2.45882 2.95653 2.72517 0.21920  -0.07958 0.21941  428 ALA A C   
2737 O O   . ALA A 428 ? 2.47142 2.93118 2.76065 0.22598  -0.08886 0.26033  428 ALA A O   
2738 C CB  . ALA A 428 ? 2.49692 3.04210 2.74690 0.22915  -0.08058 0.24699  428 ALA A CB  
2739 N N   . VAL B 2   ? 2.56383 1.85299 2.53303 0.26497  0.29541  -0.37394 2   VAL B N   
2740 C CA  . VAL B 2   ? 2.47569 1.88846 2.53495 0.23055  0.23364  -0.38480 2   VAL B CA  
2741 C C   . VAL B 2   ? 2.46660 1.90355 2.55907 0.21540  0.21479  -0.38010 2   VAL B C   
2742 O O   . VAL B 2   ? 2.55918 1.92351 2.55911 0.21776  0.21807  -0.38207 2   VAL B O   
2743 C CB  . VAL B 2   ? 2.43795 1.87795 2.42658 0.20920  0.17581  -0.40934 2   VAL B CB  
2744 C CG1 . VAL B 2   ? 2.31515 1.87614 2.39674 0.17945  0.12265  -0.41755 2   VAL B CG1 
2745 C CG2 . VAL B 2   ? 2.51406 1.91381 2.45121 0.22821  0.19724  -0.41310 2   VAL B CG2 
2746 N N   . GLN B 3   ? 2.40841 1.94119 2.62769 0.20009  0.19349  -0.37389 3   GLN B N   
2747 C CA  . GLN B 3   ? 2.39331 1.95555 2.65259 0.18647  0.17361  -0.36832 3   GLN B CA  
2748 C C   . GLN B 3   ? 2.15914 1.83255 2.53203 0.16363  0.12847  -0.37052 3   GLN B C   
2749 O O   . GLN B 3   ? 2.08349 1.79888 2.54165 0.16705  0.13505  -0.36408 3   GLN B O   
2750 C CB  . GLN B 3   ? 2.41054 1.91786 2.70548 0.21261  0.23288  -0.34124 3   GLN B CB  
2751 C CG  . GLN B 3   ? 2.40780 1.93995 2.74229 0.20178  0.21584  -0.33322 3   GLN B CG  
2752 C CD  . GLN B 3   ? 2.46310 1.91533 2.79175 0.23105  0.27868  -0.30766 3   GLN B CD  
2753 O OE1 . GLN B 3   ? 2.51426 1.93400 2.79819 0.22803  0.27489  -0.30642 3   GLN B OE1 
2754 N NE2 . GLN B 3   ? 2.44596 1.86281 2.82017 0.26100  0.34063  -0.28526 3   GLN B NE2 
2755 N N   . LEU B 4   ? 2.32445 2.03738 2.69193 0.14070  0.08275  -0.37935 4   LEU B N   
2756 C CA  . LEU B 4   ? 2.21095 2.01490 2.66201 0.11968  0.03626  -0.38293 4   LEU B CA  
2757 C C   . LEU B 4   ? 2.21118 2.02903 2.70985 0.11525  0.02822  -0.37044 4   LEU B C   
2758 O O   . LEU B 4   ? 2.27172 2.07031 2.70765 0.10559  0.01296  -0.37681 4   LEU B O   
2759 C CB  . LEU B 4   ? 2.13778 1.97855 2.53180 0.09731  -0.01279 -0.40529 4   LEU B CB  
2760 C CG  . LEU B 4   ? 2.13684 1.97254 2.48993 0.10150  -0.00995 -0.41663 4   LEU B CG  
2761 C CD1 . LEU B 4   ? 2.09461 1.96293 2.39229 0.08147  -0.05459 -0.43382 4   LEU B CD1 
2762 C CD2 . LEU B 4   ? 2.08206 1.95772 2.52318 0.10707  -0.00261 -0.41120 4   LEU B CD2 
2763 N N   . VAL B 5   ? 2.13843 1.98922 2.75106 0.12174  0.03660  -0.35143 5   VAL B N   
2764 C CA  . VAL B 5   ? 2.15618 2.02140 2.82876 0.12125  0.03079  -0.33500 5   VAL B CA  
2765 C C   . VAL B 5   ? 2.07153 2.00869 2.78638 0.09774  -0.03095 -0.34397 5   VAL B C   
2766 O O   . VAL B 5   ? 2.03393 2.01670 2.82092 0.09187  -0.05291 -0.34318 5   VAL B O   
2767 C CB  . VAL B 5   ? 2.16728 2.02540 2.94891 0.14326  0.07447  -0.30420 5   VAL B CB  
2768 C CG1 . VAL B 5   ? 2.24988 2.13240 3.10561 0.14234  0.06157  -0.28514 5   VAL B CG1 
2769 C CG2 . VAL B 5   ? 2.29903 2.07095 3.02499 0.17143  0.14376  -0.29300 5   VAL B CG2 
2770 N N   . GLU B 6   ? 2.22454 2.16434 2.88942 0.08487  -0.05829 -0.35196 6   GLU B N   
2771 C CA  . GLU B 6   ? 2.18138 2.17525 2.86595 0.06554  -0.11294 -0.36015 6   GLU B CA  
2772 C C   . GLU B 6   ? 2.19590 2.20656 2.96030 0.06856  -0.12398 -0.34042 6   GLU B C   
2773 O O   . GLU B 6   ? 2.23070 2.20796 3.00391 0.08187  -0.09221 -0.32402 6   GLU B O   
2774 C CB  . GLU B 6   ? 2.18391 2.17223 2.77044 0.04986  -0.13568 -0.37849 6   GLU B CB  
2775 C CG  . GLU B 6   ? 2.18507 2.15439 2.69363 0.04707  -0.12707 -0.39478 6   GLU B CG  
2776 C CD  . GLU B 6   ? 2.12451 2.12771 2.58676 0.02805  -0.16598 -0.41111 6   GLU B CD  
2777 O OE1 . GLU B 6   ? 2.07796 2.12066 2.57202 0.01953  -0.19786 -0.41153 6   GLU B OE1 
2778 O OE2 . GLU B 6   ? 2.12098 2.10752 2.51445 0.02274  -0.16453 -0.42171 6   GLU B OE2 
2779 N N   . SER B 7   ? 2.06462 2.12186 2.88244 0.05722  -0.17046 -0.34133 7   SER B N   
2780 C CA  . SER B 7   ? 2.12200 2.19878 3.02388 0.05921  -0.19128 -0.32171 7   SER B CA  
2781 C C   . SER B 7   ? 2.07870 2.18275 2.95794 0.04251  -0.25062 -0.33364 7   SER B C   
2782 O O   . SER B 7   ? 2.01702 2.12984 2.83490 0.03101  -0.27242 -0.35429 7   SER B O   
2783 C CB  . SER B 7   ? 2.19405 2.29111 3.21949 0.06750  -0.18480 -0.30090 7   SER B CB  
2784 O OG  . SER B 7   ? 2.19348 2.31526 3.30684 0.06653  -0.21719 -0.28139 7   SER B OG  
2785 N N   . GLY B 8   ? 2.19400 2.30676 3.12121 0.04373  -0.27441 -0.31847 8   GLY B N   
2786 C CA  . GLY B 8   ? 2.16281 2.28953 3.06395 0.03162  -0.32988 -0.32692 8   GLY B CA  
2787 C C   . GLY B 8   ? 2.14246 2.24988 2.95668 0.02858  -0.32860 -0.33427 8   GLY B C   
2788 O O   . GLY B 8   ? 2.15413 2.23735 2.94604 0.03576  -0.29107 -0.32802 8   GLY B O   
2789 N N   . GLY B 9   ? 2.25015 2.36206 3.01109 0.01838  -0.36928 -0.34686 9   GLY B N   
2790 C CA  . GLY B 9   ? 2.28664 2.38182 2.96472 0.01390  -0.36854 -0.35401 9   GLY B CA  
2791 C C   . GLY B 9   ? 2.36436 2.44924 3.05892 0.01934  -0.38326 -0.33892 9   GLY B C   
2792 O O   . GLY B 9   ? 2.38463 2.47028 3.15377 0.02991  -0.37266 -0.31915 9   GLY B O   
2793 N N   . GLY B 10  ? 2.39270 2.46632 3.01947 0.01409  -0.40458 -0.34583 10  GLY B N   
2794 C CA  . GLY B 10  ? 2.47514 2.53430 3.10540 0.02012  -0.41876 -0.33233 10  GLY B CA  
2795 C C   . GLY B 10  ? 2.48081 2.52470 3.03053 0.01519  -0.44641 -0.34170 10  GLY B C   
2796 O O   . GLY B 10  ? 2.41721 2.46031 2.90306 0.00716  -0.44016 -0.35688 10  GLY B O   
2797 N N   . LEU B 11  ? 2.42591 2.45534 2.98075 0.02212  -0.47495 -0.33007 11  LEU B N   
2798 C CA  . LEU B 11  ? 2.45694 2.46110 2.93226 0.02187  -0.50142 -0.33584 11  LEU B CA  
2799 C C   . LEU B 11  ? 2.44454 2.44224 2.91657 0.02253  -0.55203 -0.34087 11  LEU B C   
2800 O O   . LEU B 11  ? 2.44785 2.45389 2.99273 0.02572  -0.58509 -0.33051 11  LEU B O   
2801 C CB  . LEU B 11  ? 2.52529 2.50695 2.99408 0.03078  -0.50715 -0.32093 11  LEU B CB  
2802 C CG  . LEU B 11  ? 2.56638 2.51188 2.94705 0.03420  -0.52871 -0.32364 11  LEU B CG  
2803 C CD1 . LEU B 11  ? 2.62160 2.54733 2.97866 0.03863  -0.50431 -0.31327 11  LEU B CD1 
2804 C CD2 . LEU B 11  ? 2.59244 2.51786 2.97581 0.04238  -0.58865 -0.31865 11  LEU B CD2 
2805 N N   . LEU B 12  ? 2.55641 2.53535 2.94457 0.01975  -0.55795 -0.35501 12  LEU B N   
2806 C CA  . LEU B 12  ? 2.56350 2.51886 2.92163 0.02154  -0.60432 -0.36174 12  LEU B CA  
2807 C C   . LEU B 12  ? 2.61027 2.52012 2.85450 0.02756  -0.60851 -0.36763 12  LEU B C   
2808 O O   . LEU B 12  ? 2.60510 2.51715 2.80265 0.02599  -0.56787 -0.37044 12  LEU B O   
2809 C CB  . LEU B 12  ? 2.50861 2.48561 2.88829 0.01431  -0.59928 -0.37367 12  LEU B CB  
2810 C CG  . LEU B 12  ? 2.47113 2.48543 2.96319 0.01035  -0.59794 -0.36673 12  LEU B CG  
2811 C CD1 . LEU B 12  ? 2.44661 2.47749 2.94326 0.00415  -0.58485 -0.37977 12  LEU B CD1 
2812 C CD2 . LEU B 12  ? 2.49815 2.50422 3.05336 0.01251  -0.65295 -0.35387 12  LEU B CD2 
2813 N N   . GLN B 13  ? 2.59013 2.45428 2.79021 0.03477  -0.65825 -0.36783 13  GLN B N   
2814 C CA  . GLN B 13  ? 2.65402 2.45859 2.73578 0.04534  -0.66484 -0.37148 13  GLN B CA  
2815 C C   . GLN B 13  ? 2.65621 2.43389 2.67769 0.04642  -0.67389 -0.38491 13  GLN B C   
2816 O O   . GLN B 13  ? 2.61644 2.41338 2.68888 0.03862  -0.69339 -0.39118 13  GLN B O   
2817 C CB  . GLN B 13  ? 2.72700 2.48104 2.78059 0.05611  -0.71617 -0.36187 13  GLN B CB  
2818 C CG  . GLN B 13  ? 2.73879 2.51204 2.83758 0.05864  -0.70099 -0.34691 13  GLN B CG  
2819 C CD  . GLN B 13  ? 2.81270 2.54317 2.90082 0.06969  -0.75609 -0.33492 13  GLN B CD  
2820 O OE1 . GLN B 13  ? 2.82087 2.54044 2.94349 0.06844  -0.81395 -0.33296 13  GLN B OE1 
2821 N NE2 . GLN B 13  ? 2.87170 2.57631 2.91395 0.07995  -0.74072 -0.32576 13  GLN B NE2 
2822 N N   . PRO B 14  ? 2.71048 2.44149 2.62415 0.05723  -0.65504 -0.38792 14  PRO B N   
2823 C CA  . PRO B 14  ? 2.72226 2.42685 2.57496 0.06096  -0.65110 -0.39881 14  PRO B CA  
2824 C C   . PRO B 14  ? 2.75076 2.41428 2.59364 0.06052  -0.71283 -0.40636 14  PRO B C   
2825 O O   . PRO B 14  ? 2.80454 2.42261 2.62906 0.06474  -0.76614 -0.40236 14  PRO B O   
2826 C CB  . PRO B 14  ? 2.80308 2.44615 2.53618 0.07849  -0.62628 -0.39435 14  PRO B CB  
2827 C CG  . PRO B 14  ? 2.79235 2.46507 2.55285 0.07637  -0.59304 -0.38298 14  PRO B CG  
2828 C CD  . PRO B 14  ? 2.76136 2.46423 2.60931 0.06742  -0.62649 -0.37915 14  PRO B CD  
2829 N N   . GLY B 15  ? 2.72530 2.40336 2.58165 0.05454  -0.70786 -0.41672 15  GLY B N   
2830 C CA  . GLY B 15  ? 2.75269 2.39294 2.60401 0.05064  -0.76391 -0.42489 15  GLY B CA  
2831 C C   . GLY B 15  ? 2.68271 2.38261 2.67026 0.03327  -0.78993 -0.42283 15  GLY B C   
2832 O O   . GLY B 15  ? 2.68635 2.37253 2.69096 0.02570  -0.82382 -0.43020 15  GLY B O   
2833 N N   . ARG B 16  ? 2.57341 2.33451 2.65760 0.02766  -0.77220 -0.41155 16  ARG B N   
2834 C CA  . ARG B 16  ? 2.51890 2.33399 2.73714 0.01491  -0.78845 -0.40502 16  ARG B CA  
2835 C C   . ARG B 16  ? 2.45066 2.31387 2.71725 0.00708  -0.74772 -0.41309 16  ARG B C   
2836 O O   . ARG B 16  ? 2.43622 2.30225 2.64392 0.01084  -0.70429 -0.42203 16  ARG B O   
2837 C CB  . ARG B 16  ? 2.49801 2.35564 2.79585 0.01540  -0.77267 -0.38870 16  ARG B CB  
2838 C CG  . ARG B 16  ? 2.56853 2.38216 2.82420 0.02464  -0.81008 -0.37872 16  ARG B CG  
2839 C CD  . ARG B 16  ? 2.63231 2.38741 2.86103 0.02420  -0.88936 -0.37926 16  ARG B CD  
2840 N NE  . ARG B 16  ? 2.59846 2.38862 2.95110 0.01094  -0.92626 -0.37221 16  ARG B NE  
2841 C CZ  . ARG B 16  ? 2.60397 2.37274 2.95505 0.00144  -0.96177 -0.38203 16  ARG B CZ  
2842 N NH1 . ARG B 16  ? 2.64778 2.35505 2.87242 0.00550  -0.96589 -0.39996 16  ARG B NH1 
2843 N NH2 . ARG B 16  ? 2.57217 2.37884 3.05271 -0.01164 -0.99171 -0.37182 16  ARG B NH2 
2844 N N   . SER B 17  ? 2.56224 2.46326 2.94187 -0.00291 -0.76159 -0.40746 17  SER B N   
2845 C CA  . SER B 17  ? 2.50588 2.44521 2.93476 -0.00933 -0.72860 -0.41399 17  SER B CA  
2846 C C   . SER B 17  ? 2.43690 2.43530 2.99378 -0.01315 -0.70218 -0.39981 17  SER B C   
2847 O O   . SER B 17  ? 2.44436 2.45203 3.08452 -0.01522 -0.73308 -0.38397 17  SER B O   
2848 C CB  . SER B 17  ? 2.53454 2.44254 2.95993 -0.01663 -0.77268 -0.42255 17  SER B CB  
2849 O OG  . SER B 17  ? 2.49563 2.43501 2.95370 -0.02067 -0.73621 -0.42980 17  SER B OG  
2850 N N   . LEU B 18  ? 2.32394 2.35754 2.89418 -0.01244 -0.64466 -0.40379 18  LEU B N   
2851 C CA  . LEU B 18  ? 2.28243 2.35902 2.95333 -0.01222 -0.60847 -0.39117 18  LEU B CA  
2852 C C   . LEU B 18  ? 2.23184 2.32838 2.92432 -0.01448 -0.57473 -0.39921 18  LEU B C   
2853 O O   . LEU B 18  ? 2.22263 2.30908 2.84025 -0.01460 -0.56279 -0.41475 18  LEU B O   
2854 C CB  . LEU B 18  ? 2.22443 2.31125 2.87316 -0.00627 -0.56675 -0.38606 18  LEU B CB  
2855 C CG  . LEU B 18  ? 2.12667 2.24096 2.85605 -0.00219 -0.52358 -0.37231 18  LEU B CG  
2856 C CD1 . LEU B 18  ? 2.09349 2.21866 2.93361 0.00021  -0.54795 -0.35062 18  LEU B CD1 
2857 C CD2 . LEU B 18  ? 2.12496 2.23424 2.80521 0.00166  -0.48830 -0.37115 18  LEU B CD2 
2858 N N   . LYS B 19  ? 2.12972 2.25250 2.92632 -0.01419 -0.55680 -0.38627 19  LYS B N   
2859 C CA  . LYS B 19  ? 2.06818 2.20631 2.89270 -0.01402 -0.52129 -0.39097 19  LYS B CA  
2860 C C   . LYS B 19  ? 1.96070 2.11493 2.81289 -0.00518 -0.46261 -0.38211 19  LYS B C   
2861 O O   . LYS B 19  ? 1.95667 2.12029 2.89050 0.00017  -0.45217 -0.36233 19  LYS B O   
2862 C CB  . LYS B 19  ? 2.11007 2.25457 3.03196 -0.02033 -0.54905 -0.38199 19  LYS B CB  
2863 C CG  . LYS B 19  ? 2.09050 2.23748 3.01170 -0.02200 -0.52686 -0.39257 19  LYS B CG  
2864 C CD  . LYS B 19  ? 2.10292 2.25854 3.13841 -0.02928 -0.54899 -0.37954 19  LYS B CD  
2865 C CE  . LYS B 19  ? 2.10526 2.25586 3.12854 -0.03172 -0.53228 -0.39188 19  LYS B CE  
2866 N NZ  . LYS B 19  ? 2.10902 2.27152 3.25816 -0.03859 -0.54193 -0.37585 19  LYS B NZ  
2867 N N   . LEU B 20  ? 2.03438 2.18681 2.81662 -0.00268 -0.42524 -0.39522 20  LEU B N   
2868 C CA  . LEU B 20  ? 2.01069 2.16340 2.79498 0.00534  -0.37289 -0.38990 20  LEU B CA  
2869 C C   . LEU B 20  ? 1.99361 2.14966 2.82489 0.01116  -0.33983 -0.38736 20  LEU B C   
2870 O O   . LEU B 20  ? 1.97508 2.13362 2.78429 0.00802  -0.34395 -0.39964 20  LEU B O   
2871 C CB  . LEU B 20  ? 1.99768 2.14270 2.68180 0.00331  -0.35610 -0.40368 20  LEU B CB  
2872 C CG  . LEU B 20  ? 1.99484 2.13286 2.62869 -0.00090 -0.37730 -0.40422 20  LEU B CG  
2873 C CD1 . LEU B 20  ? 1.98349 2.11783 2.53608 -0.00455 -0.35680 -0.41424 20  LEU B CD1 
2874 C CD2 . LEU B 20  ? 2.03732 2.16939 2.71935 0.00391  -0.37442 -0.38723 20  LEU B CD2 
2875 N N   . SER B 21  ? 1.92966 2.08059 2.82163 0.02186  -0.30316 -0.37006 21  SER B N   
2876 C CA  . SER B 21  ? 1.95863 2.10537 2.90013 0.03121  -0.26441 -0.36305 21  SER B CA  
2877 C C   . SER B 21  ? 1.92846 2.04644 2.80255 0.04217  -0.21248 -0.36763 21  SER B C   
2878 O O   . SER B 21  ? 1.95073 2.05098 2.77260 0.04386  -0.20185 -0.36801 21  SER B O   
2879 C CB  . SER B 21  ? 2.01203 2.16701 3.07937 0.03882  -0.25562 -0.33523 21  SER B CB  
2880 O OG  . SER B 21  ? 2.11706 2.29511 3.24970 0.02646  -0.31200 -0.33038 21  SER B OG  
2881 N N   . CYS B 22  ? 1.92432 2.03178 2.79560 0.04940  -0.18220 -0.37108 22  CYS B N   
2882 C CA  . CYS B 22  ? 1.95293 2.02361 2.74863 0.06027  -0.13826 -0.37699 22  CYS B CA  
2883 C C   . CYS B 22  ? 2.02360 2.07423 2.86774 0.07666  -0.09300 -0.36521 22  CYS B C   
2884 O O   . CYS B 22  ? 2.00510 2.06367 2.84805 0.07552  -0.09378 -0.37397 22  CYS B O   
2885 C CB  . CYS B 22  ? 1.95148 2.02721 2.65195 0.05048  -0.15636 -0.40014 22  CYS B CB  
2886 S SG  . CYS B 22  ? 2.04083 2.07012 2.64547 0.06105  -0.11593 -0.40865 22  CYS B SG  
2887 N N   . VAL B 23  ? 1.91419 1.93486 2.79872 0.09374  -0.04989 -0.34383 23  VAL B N   
2888 C CA  . VAL B 23  ? 1.92366 1.91916 2.86107 0.11319  0.00195  -0.32713 23  VAL B CA  
2889 C C   . VAL B 23  ? 1.94549 1.88648 2.77411 0.12625  0.04039  -0.33948 23  VAL B C   
2890 O O   . VAL B 23  ? 1.99923 1.90250 2.73041 0.12792  0.04611  -0.34858 23  VAL B O   
2891 C CB  . VAL B 23  ? 1.97387 1.95300 2.99619 0.13039  0.03948  -0.29532 23  VAL B CB  
2892 C CG1 . VAL B 23  ? 2.02567 1.98352 3.12261 0.15131  0.09563  -0.27299 23  VAL B CG1 
2893 C CG2 . VAL B 23  ? 1.96592 1.99784 3.08598 0.11624  -0.00817 -0.28345 23  VAL B CG2 
2894 N N   . ALA B 24  ? 1.92821 1.86094 2.77127 0.13495  0.06409  -0.33951 24  ALA B N   
2895 C CA  . ALA B 24  ? 1.92247 1.79975 2.66437 0.14953  0.09892  -0.34991 24  ALA B CA  
2896 C C   . ALA B 24  ? 2.04177 1.85088 2.79169 0.17983  0.17060  -0.32700 24  ALA B C   
2897 O O   . ALA B 24  ? 2.12575 1.94180 2.98261 0.18994  0.19735  -0.30038 24  ALA B O   
2898 C CB  . ALA B 24  ? 1.87136 1.77202 2.61205 0.14430  0.08636  -0.36332 24  ALA B CB  
2899 N N   . SER B 25  ? 2.11317 1.85147 2.74683 0.19571  0.20196  -0.33572 25  SER B N   
2900 C CA  . SER B 25  ? 2.21863 1.87141 2.82868 0.22865  0.27472  -0.31534 25  SER B CA  
2901 C C   . SER B 25  ? 2.28430 1.86795 2.77162 0.24373  0.29780  -0.32922 25  SER B C   
2902 O O   . SER B 25  ? 2.34323 1.92100 2.72709 0.23006  0.25849  -0.35360 25  SER B O   
2903 C CB  . SER B 25  ? 2.27981 1.88261 2.84502 0.23684  0.29125  -0.30607 25  SER B CB  
2904 O OG  . SER B 25  ? 2.24164 1.91055 2.90215 0.22010  0.25828  -0.29732 25  SER B OG  
2905 N N   . GLY B 26  ? 2.34270 1.87299 2.84514 0.27260  0.36157  -0.31144 26  GLY B N   
2906 C CA  . GLY B 26  ? 2.41106 1.85184 2.78473 0.29468  0.39447  -0.31985 26  GLY B CA  
2907 C C   . GLY B 26  ? 2.39033 1.86090 2.75444 0.28882  0.37606  -0.33556 26  GLY B C   
2908 O O   . GLY B 26  ? 2.36485 1.79963 2.74501 0.31166  0.42612  -0.32356 26  GLY B O   
2909 N N   . PHE B 27  ? 2.52538 2.05833 2.86299 0.26016  0.30826  -0.36052 27  PHE B N   
2910 C CA  . PHE B 27  ? 2.51213 2.06662 2.82090 0.25606  0.28913  -0.37643 27  PHE B CA  
2911 C C   . PHE B 27  ? 2.39705 2.01954 2.83745 0.24948  0.29122  -0.36820 27  PHE B C   
2912 O O   . PHE B 27  ? 2.28963 1.95737 2.84887 0.24107  0.29065  -0.35292 27  PHE B O   
2913 C CB  . PHE B 27  ? 2.42623 2.02720 2.67455 0.22916  0.21991  -0.40111 27  PHE B CB  
2914 C CG  . PHE B 27  ? 2.21497 1.90975 2.55221 0.19988  0.17024  -0.40477 27  PHE B CG  
2915 C CD1 . PHE B 27  ? 2.21107 1.91330 2.56797 0.19019  0.15800  -0.39921 27  PHE B CD1 
2916 C CD2 . PHE B 27  ? 2.13672 1.90346 2.52862 0.18387  0.13689  -0.41352 27  PHE B CD2 
2917 C CE1 . PHE B 27  ? 2.13957 1.91969 2.56887 0.16559  0.11248  -0.40219 27  PHE B CE1 
2918 C CE2 . PHE B 27  ? 2.06983 1.90837 2.52771 0.15956  0.09162  -0.41694 27  PHE B CE2 
2919 C CZ  . PHE B 27  ? 2.06130 1.90674 2.53775 0.15065  0.07885  -0.41123 27  PHE B CZ  
2920 N N   . THR B 28  ? 2.26216 1.88833 2.67901 0.25292  0.29076  -0.37800 28  THR B N   
2921 C CA  . THR B 28  ? 2.13927 1.82674 2.66370 0.24243  0.28269  -0.37509 28  THR B CA  
2922 C C   . THR B 28  ? 2.04795 1.82050 2.60622 0.20930  0.21172  -0.39087 28  THR B C   
2923 O O   . THR B 28  ? 2.09302 1.88245 2.57441 0.19929  0.17403  -0.41056 28  THR B O   
2924 C CB  . THR B 28  ? 2.25146 1.90925 2.72584 0.25772  0.30506  -0.38157 28  THR B CB  
2925 O OG1 . THR B 28  ? 2.34591 1.90780 2.75282 0.29153  0.36929  -0.36938 28  THR B OG1 
2926 C CG2 . THR B 28  ? 2.18000 1.88286 2.77049 0.25047  0.30982  -0.37401 28  THR B CG2 
2927 N N   . PHE B 29  ? 2.03430 1.85704 2.70767 0.19366  0.19384  -0.38020 29  PHE B N   
2928 C CA  . PHE B 29  ? 1.97056 1.85802 2.66165 0.16532  0.12887  -0.39317 29  PHE B CA  
2929 C C   . PHE B 29  ? 1.96188 1.88593 2.63666 0.15234  0.09344  -0.41079 29  PHE B C   
2930 O O   . PHE B 29  ? 1.92707 1.87812 2.54361 0.13889  0.05165  -0.42711 29  PHE B O   
2931 C CB  . PHE B 29  ? 1.93680 1.86079 2.75187 0.15353  0.11572  -0.37620 29  PHE B CB  
2932 C CG  . PHE B 29  ? 1.93421 1.91026 2.75519 0.12805  0.05208  -0.38771 29  PHE B CG  
2933 C CD1 . PHE B 29  ? 1.95977 1.93547 2.68753 0.12209  0.02838  -0.40231 29  PHE B CD1 
2934 C CD2 . PHE B 29  ? 1.90233 1.92192 2.82001 0.11019  0.01507  -0.38278 29  PHE B CD2 
2935 C CE1 . PHE B 29  ? 1.92805 1.94599 2.65806 0.10133  -0.02422 -0.41098 29  PHE B CE1 
2936 C CE2 . PHE B 29  ? 1.87757 1.93309 2.78714 0.08984  -0.04179 -0.39307 29  PHE B CE2 
2937 C CZ  . PHE B 29  ? 1.90452 1.95922 2.71983 0.08673  -0.05794 -0.40672 29  PHE B CZ  
2938 N N   . ASN B 30  ? 2.06341 1.98586 2.78913 0.15709  0.11230  -0.40610 30  ASN B N   
2939 C CA  . ASN B 30  ? 2.01769 1.96785 2.72963 0.14603  0.08188  -0.42136 30  ASN B CA  
2940 C C   . ASN B 30  ? 2.02880 1.95669 2.62911 0.15890  0.09088  -0.43549 30  ASN B C   
2941 O O   . ASN B 30  ? 2.01367 1.95264 2.60081 0.15720  0.08150  -0.44451 30  ASN B O   
2942 C CB  . ASN B 30  ? 1.98569 1.93758 2.79312 0.14485  0.09737  -0.41083 30  ASN B CB  
2943 C CG  . ASN B 30  ? 1.93550 1.92348 2.85777 0.12398  0.06406  -0.40010 30  ASN B CG  
2944 O OD1 . ASN B 30  ? 1.93949 1.94102 2.88553 0.11832  0.04966  -0.39318 30  ASN B OD1 
2945 N ND2 . ASN B 30  ? 1.92350 1.92391 2.91558 0.11183  0.04836  -0.39840 30  ASN B ND2 
2946 N N   . ASN B 31  ? 1.96055 1.85409 2.47921 0.17154  0.10617  -0.43686 31  ASN B N   
2947 C CA  . ASN B 31  ? 2.03603 1.90564 2.45143 0.18382  0.10977  -0.44769 31  ASN B CA  
2948 C C   . ASN B 31  ? 2.07529 1.96248 2.41944 0.17300  0.07057  -0.45808 31  ASN B C   
2949 O O   . ASN B 31  ? 2.12597 1.99156 2.38636 0.18225  0.06883  -0.46422 31  ASN B O   
2950 C CB  . ASN B 31  ? 2.13361 1.92801 2.50160 0.21196  0.16485  -0.43881 31  ASN B CB  
2951 C CG  . ASN B 31  ? 2.10045 1.87496 2.52488 0.22599  0.20813  -0.42873 31  ASN B CG  
2952 O OD1 . ASN B 31  ? 1.99019 1.80673 2.50385 0.21188  0.19567  -0.42665 31  ASN B OD1 
2953 N ND2 . ASN B 31  ? 2.19320 1.89699 2.56203 0.25390  0.25852  -0.42188 31  ASN B ND2 
2954 N N   . TYR B 32  ? 1.89954 1.82428 2.27714 0.15358  0.03789  -0.45871 32  TYR B N   
2955 C CA  . TYR B 32  ? 1.89329 1.83388 2.21309 0.14219  0.00384  -0.46580 32  TYR B CA  
2956 C C   . TYR B 32  ? 1.87554 1.87501 2.23724 0.12048  -0.03779 -0.46971 32  TYR B C   
2957 O O   . TYR B 32  ? 1.82812 1.84277 2.26102 0.11237  -0.04273 -0.46454 32  TYR B O   
2958 C CB  . TYR B 32  ? 1.94314 1.83944 2.23147 0.14606  0.01724  -0.46006 32  TYR B CB  
2959 C CG  . TYR B 32  ? 2.06349 1.88391 2.28503 0.16991  0.05753  -0.45653 32  TYR B CG  
2960 C CD1 . TYR B 32  ? 2.12745 1.91674 2.25086 0.17428  0.04468  -0.46378 32  TYR B CD1 
2961 C CD2 . TYR B 32  ? 2.12416 1.89946 2.38035 0.18895  0.10812  -0.44399 32  TYR B CD2 
2962 C CE1 . TYR B 32  ? 2.28823 1.99527 2.33544 0.19761  0.07825  -0.46119 32  TYR B CE1 
2963 C CE2 . TYR B 32  ? 2.23403 1.92766 2.41720 0.21447  0.14981  -0.43972 32  TYR B CE2 
2964 C CZ  . TYR B 32  ? 2.34572 2.00128 2.41715 0.21904  0.13326  -0.44964 32  TYR B CZ  
2965 O OH  . TYR B 32  ? 2.60064 2.16251 2.58468 0.24589  0.17151  -0.44605 32  TYR B OH  
2966 N N   . TRP B 33  ? 1.83260 1.86176 2.15010 0.11243  -0.06740 -0.47682 33  TRP B N   
2967 C CA  . TRP B 33  ? 1.79988 1.87411 2.13949 0.09507  -0.10297 -0.47931 33  TRP B CA  
2968 C C   . TRP B 33  ? 1.80991 1.88392 2.16226 0.08391  -0.11474 -0.47534 33  TRP B C   
2969 O O   . TRP B 33  ? 1.88518 1.92720 2.20657 0.08770  -0.10192 -0.47250 33  TRP B O   
2970 C CB  . TRP B 33  ? 1.81103 1.91371 2.10259 0.09253  -0.12346 -0.48302 33  TRP B CB  
2971 C CG  . TRP B 33  ? 1.76895 1.88519 2.05881 0.09979  -0.12124 -0.48624 33  TRP B CG  
2972 C CD1 . TRP B 33  ? 1.82565 1.91982 2.12172 0.11305  -0.09648 -0.48763 33  TRP B CD1 
2973 C CD2 . TRP B 33  ? 1.72240 1.87085 1.99960 0.09593  -0.14089 -0.48713 33  TRP B CD2 
2974 N NE1 . TRP B 33  ? 1.77951 1.89007 2.06550 0.11651  -0.10191 -0.49065 33  TRP B NE1 
2975 C CE2 . TRP B 33  ? 1.75904 1.90091 2.03117 0.10734  -0.12772 -0.48992 33  TRP B CE2 
2976 C CE3 . TRP B 33  ? 1.72764 1.90480 1.99498 0.08575  -0.16423 -0.48426 33  TRP B CE3 
2977 C CZ2 . TRP B 33  ? 1.80171 1.96093 2.05410 0.11003  -0.13659 -0.49004 33  TRP B CZ2 
2978 C CZ3 . TRP B 33  ? 1.72543 1.92050 1.97600 0.08954  -0.17050 -0.48296 33  TRP B CZ3 
2979 C CH2 . TRP B 33  ? 1.77080 1.95509 2.01152 0.10213  -0.15653 -0.48592 33  TRP B CH2 
2980 N N   . MET B 34  ? 1.77422 1.87692 2.16452 0.07100  -0.13998 -0.47518 34  MET B N   
2981 C CA  . MET B 34  ? 1.78249 1.88821 2.18687 0.06052  -0.15359 -0.47092 34  MET B CA  
2982 C C   . MET B 34  ? 1.72078 1.85925 2.10336 0.04792  -0.18617 -0.47404 34  MET B C   
2983 O O   . MET B 34  ? 1.70172 1.85941 2.07313 0.04791  -0.19796 -0.47799 34  MET B O   
2984 C CB  . MET B 34  ? 1.80118 1.90355 2.28115 0.05903  -0.15167 -0.46358 34  MET B CB  
2985 C CG  . MET B 34  ? 1.85624 1.92756 2.37348 0.07332  -0.11311 -0.45571 34  MET B CG  
2986 S SD  . MET B 34  ? 1.92561 1.94523 2.39257 0.08666  -0.07614 -0.44999 34  MET B SD  
2987 C CE  . MET B 34  ? 1.88615 1.91198 2.37749 0.07564  -0.09259 -0.44261 34  MET B CE  
2988 N N   . SER B 35  ? 1.74412 1.88334 2.11772 0.03887  -0.19688 -0.47082 35  SER B N   
2989 C CA  . SER B 35  ? 1.73087 1.89653 2.08384 0.02814  -0.22222 -0.47099 35  SER B CA  
2990 C C   . SER B 35  ? 1.73252 1.89355 2.10058 0.01906  -0.23290 -0.46632 35  SER B C   
2991 O O   . SER B 35  ? 1.73516 1.87190 2.12040 0.02137  -0.21871 -0.46239 35  SER B O   
2992 C CB  . SER B 35  ? 1.72772 1.90440 2.03309 0.02621  -0.22356 -0.47060 35  SER B CB  
2993 O OG  . SER B 35  ? 1.73558 1.92221 2.02768 0.03574  -0.21664 -0.47297 35  SER B OG  
2994 N N   . TRP B 36  ? 1.83052 2.01049 2.18846 0.01108  -0.25464 -0.46525 36  TRP B N   
2995 C CA  . TRP B 36  ? 1.79485 1.97122 2.15866 0.00271  -0.26644 -0.46045 36  TRP B CA  
2996 C C   . TRP B 36  ? 1.83460 2.02591 2.15975 -0.00590 -0.27431 -0.45772 36  TRP B C   
2997 O O   . TRP B 36  ? 1.83871 2.04888 2.14702 -0.00485 -0.28149 -0.45696 36  TRP B O   
2998 C CB  . TRP B 36  ? 1.77660 1.95408 2.16940 0.00224  -0.28742 -0.45945 36  TRP B CB  
2999 C CG  . TRP B 36  ? 1.84024 2.00650 2.29065 0.00704  -0.28454 -0.45740 36  TRP B CG  
3000 C CD1 . TRP B 36  ? 1.87554 2.04134 2.35205 0.01183  -0.28514 -0.46069 36  TRP B CD1 
3001 C CD2 . TRP B 36  ? 1.85132 2.00549 2.34799 0.00771  -0.27915 -0.44859 36  TRP B CD2 
3002 N NE1 . TRP B 36  ? 1.86578 2.02342 2.40977 0.01392  -0.28162 -0.45338 36  TRP B NE1 
3003 C CE2 . TRP B 36  ? 1.86111 2.01261 2.42018 0.01283  -0.27638 -0.44480 36  TRP B CE2 
3004 C CE3 . TRP B 36  ? 1.85703 2.00087 2.35072 0.00507  -0.27460 -0.44183 36  TRP B CE3 
3005 C CZ2 . TRP B 36  ? 1.88555 2.02902 2.51202 0.01661  -0.26763 -0.43180 36  TRP B CZ2 
3006 C CZ3 . TRP B 36  ? 1.90247 2.03398 2.45329 0.01030  -0.26487 -0.43057 36  TRP B CZ3 
3007 C CH2 . TRP B 36  ? 1.90218 2.03584 2.52260 0.01660  -0.26070 -0.42435 36  TRP B CH2 
3008 N N   . ILE B 37  ? 1.93938 2.11842 2.25123 -0.01385 -0.27112 -0.45451 37  ILE B N   
3009 C CA  . ILE B 37  ? 1.93241 2.12463 2.21802 -0.02528 -0.27941 -0.44955 37  ILE B CA  
3010 C C   . ILE B 37  ? 1.93264 2.11144 2.21990 -0.03356 -0.28577 -0.44512 37  ILE B C   
3011 O O   . ILE B 37  ? 1.96341 2.11447 2.25974 -0.03201 -0.27830 -0.44548 37  ILE B O   
3012 C CB  . ILE B 37  ? 1.93221 2.11626 2.19227 -0.03034 -0.27505 -0.44980 37  ILE B CB  
3013 C CG1 . ILE B 37  ? 1.91177 2.09679 2.16922 -0.01822 -0.26471 -0.45480 37  ILE B CG1 
3014 C CG2 . ILE B 37  ? 1.92934 2.13960 2.17898 -0.04288 -0.28749 -0.44151 37  ILE B CG2 
3015 C CD1 . ILE B 37  ? 1.90538 2.12648 2.16901 -0.01233 -0.26774 -0.45274 37  ILE B CD1 
3016 N N   . ARG B 38  ? 2.10098 2.29635 2.37897 -0.04023 -0.29566 -0.43899 38  ARG B N   
3017 C CA  . ARG B 38  ? 2.13311 2.31526 2.40891 -0.04709 -0.30131 -0.43397 38  ARG B CA  
3018 C C   . ARG B 38  ? 2.14227 2.33310 2.40077 -0.06169 -0.30349 -0.42624 38  ARG B C   
3019 O O   . ARG B 38  ? 2.10706 2.32205 2.36321 -0.06538 -0.30358 -0.42213 38  ARG B O   
3020 C CB  . ARG B 38  ? 2.10642 2.29021 2.38661 -0.03957 -0.31216 -0.43208 38  ARG B CB  
3021 C CG  . ARG B 38  ? 2.11980 2.32081 2.37789 -0.03794 -0.31378 -0.42609 38  ARG B CG  
3022 C CD  . ARG B 38  ? 2.15635 2.34025 2.39998 -0.02901 -0.32621 -0.42484 38  ARG B CD  
3023 N NE  . ARG B 38  ? 2.21634 2.40391 2.42789 -0.02262 -0.32099 -0.41754 38  ARG B NE  
3024 C CZ  . ARG B 38  ? 2.24110 2.40256 2.41982 -0.01145 -0.33031 -0.41650 38  ARG B CZ  
3025 N NH1 . ARG B 38  ? 2.23520 2.37020 2.41489 -0.00796 -0.35252 -0.42256 38  ARG B NH1 
3026 N NH2 . ARG B 38  ? 2.29209 2.44952 2.43510 -0.00248 -0.31731 -0.40742 38  ARG B NH2 
3027 N N   . GLN B 39  ? 2.23447 2.40583 2.48644 -0.07017 -0.30546 -0.42227 39  GLN B N   
3028 C CA  . GLN B 39  ? 2.29468 2.47056 2.53618 -0.08661 -0.30869 -0.41342 39  GLN B CA  
3029 C C   . GLN B 39  ? 2.33096 2.49382 2.56778 -0.08778 -0.30942 -0.40725 39  GLN B C   
3030 O O   . GLN B 39  ? 2.37596 2.50974 2.61028 -0.08522 -0.30835 -0.41015 39  GLN B O   
3031 C CB  . GLN B 39  ? 2.30992 2.45927 2.53460 -0.10068 -0.31103 -0.41619 39  GLN B CB  
3032 C CG  . GLN B 39  ? 2.34829 2.50176 2.56883 -0.12190 -0.32015 -0.40620 39  GLN B CG  
3033 C CD  . GLN B 39  ? 2.42376 2.52942 2.61356 -0.13700 -0.32650 -0.41008 39  GLN B CD  
3034 O OE1 . GLN B 39  ? 2.46426 2.53241 2.62983 -0.12959 -0.32108 -0.41975 39  GLN B OE1 
3035 N NE2 . GLN B 39  ? 2.48662 2.58662 2.67365 -0.15764 -0.33627 -0.40152 39  GLN B NE2 
3036 N N   . ALA B 40  ? 2.29964 2.48124 2.53512 -0.08945 -0.30823 -0.39665 40  ALA B N   
3037 C CA  . ALA B 40  ? 2.31652 2.48153 2.54049 -0.09034 -0.30691 -0.38900 40  ALA B CA  
3038 C C   . ALA B 40  ? 2.39804 2.55125 2.61987 -0.11120 -0.30625 -0.38261 40  ALA B C   
3039 O O   . ALA B 40  ? 2.46968 2.63641 2.70106 -0.12622 -0.30979 -0.37993 40  ALA B O   
3040 C CB  . ALA B 40  ? 2.33296 2.51193 2.54808 -0.08039 -0.30024 -0.37842 40  ALA B CB  
3041 N N   . PRO B 41  ? 2.44882 2.57345 2.65723 -0.11307 -0.30460 -0.37967 41  PRO B N   
3042 C CA  . PRO B 41  ? 2.53546 2.63929 2.73654 -0.13404 -0.30463 -0.37475 41  PRO B CA  
3043 C C   . PRO B 41  ? 2.57316 2.70447 2.79216 -0.15059 -0.30374 -0.36057 41  PRO B C   
3044 O O   . PRO B 41  ? 2.63947 2.78709 2.86524 -0.14416 -0.29316 -0.34791 41  PRO B O   
3045 C CB  . PRO B 41  ? 2.57898 2.65169 2.76319 -0.12730 -0.29975 -0.37145 41  PRO B CB  
3046 C CG  . PRO B 41  ? 2.50837 2.57879 2.69502 -0.10482 -0.30320 -0.37861 41  PRO B CG  
3047 C CD  . PRO B 41  ? 2.42417 2.52889 2.62228 -0.09627 -0.30596 -0.38104 41  PRO B CD  
3048 N N   . GLY B 42  ? 2.47252 2.60466 2.69912 -0.17123 -0.31509 -0.36089 42  GLY B N   
3049 C CA  . GLY B 42  ? 2.55558 2.71813 2.81468 -0.19026 -0.31933 -0.34446 42  GLY B CA  
3050 C C   . GLY B 42  ? 2.52333 2.73721 2.81563 -0.18054 -0.31484 -0.33568 42  GLY B C   
3051 O O   . GLY B 42  ? 2.54151 2.78738 2.87122 -0.18810 -0.30821 -0.31530 42  GLY B O   
3052 N N   . LYS B 43  ? 2.44738 2.66882 2.73013 -0.16288 -0.31524 -0.34832 43  LYS B N   
3053 C CA  . LYS B 43  ? 2.39678 2.66125 2.70431 -0.15085 -0.30880 -0.34086 43  LYS B CA  
3054 C C   . LYS B 43  ? 2.36105 2.62778 2.66381 -0.14951 -0.32201 -0.35438 43  LYS B C   
3055 O O   . LYS B 43  ? 2.35452 2.58477 2.62840 -0.15061 -0.32983 -0.37076 43  LYS B O   
3056 C CB  . LYS B 43  ? 2.36621 2.63117 2.65717 -0.12403 -0.29039 -0.34092 43  LYS B CB  
3057 C CG  . LYS B 43  ? 2.46877 2.72163 2.75184 -0.12065 -0.27486 -0.32689 43  LYS B CG  
3058 C CD  . LYS B 43  ? 2.49824 2.73050 2.74422 -0.09383 -0.26473 -0.33137 43  LYS B CD  
3059 C CE  . LYS B 43  ? 2.56137 2.76569 2.78400 -0.08903 -0.25210 -0.32023 43  LYS B CE  
3060 N NZ  . LYS B 43  ? 2.57815 2.74737 2.75200 -0.06441 -0.25262 -0.32784 43  LYS B NZ  
3061 N N   . GLY B 44  ? 2.31075 2.61727 2.64089 -0.14474 -0.32088 -0.34538 44  GLY B N   
3062 C CA  . GLY B 44  ? 2.29955 2.60888 2.62487 -0.14297 -0.33314 -0.35550 44  GLY B CA  
3063 C C   . GLY B 44  ? 2.21294 2.50371 2.50961 -0.12087 -0.32390 -0.37413 44  GLY B C   
3064 O O   . GLY B 44  ? 2.14280 2.42118 2.42674 -0.10736 -0.31244 -0.37908 44  GLY B O   
3065 N N   . LEU B 45  ? 2.25531 2.54159 2.54289 -0.11765 -0.33115 -0.38349 45  LEU B N   
3066 C CA  . LEU B 45  ? 2.12130 2.39184 2.39089 -0.09795 -0.32118 -0.39896 45  LEU B CA  
3067 C C   . LEU B 45  ? 2.08886 2.39072 2.37160 -0.07934 -0.30783 -0.39450 45  LEU B C   
3068 O O   . LEU B 45  ? 2.15179 2.48892 2.45500 -0.07795 -0.30526 -0.38094 45  LEU B O   
3069 C CB  . LEU B 45  ? 2.09104 2.34069 2.34135 -0.09805 -0.32865 -0.40865 45  LEU B CB  
3070 C CG  . LEU B 45  ? 2.14715 2.33899 2.36227 -0.10109 -0.32888 -0.42111 45  LEU B CG  
3071 C CD1 . LEU B 45  ? 2.15788 2.32170 2.34492 -0.09323 -0.32858 -0.43021 45  LEU B CD1 
3072 C CD2 . LEU B 45  ? 2.15767 2.33413 2.37666 -0.08882 -0.31344 -0.42725 45  LEU B CD2 
3073 N N   . GLU B 46  ? 2.02008 2.30523 2.29120 -0.06468 -0.30013 -0.40453 46  GLU B N   
3074 C CA  . GLU B 46  ? 2.03673 2.33446 2.30538 -0.04684 -0.29006 -0.40293 46  GLU B CA  
3075 C C   . GLU B 46  ? 2.03172 2.31305 2.29441 -0.03457 -0.28897 -0.41820 46  GLU B C   
3076 O O   . GLU B 46  ? 2.04328 2.29875 2.30665 -0.03532 -0.29301 -0.42792 46  GLU B O   
3077 C CB  . GLU B 46  ? 2.04752 2.33265 2.30309 -0.04195 -0.28715 -0.39794 46  GLU B CB  
3078 C CG  . GLU B 46  ? 2.10545 2.38310 2.33994 -0.02238 -0.28001 -0.39888 46  GLU B CG  
3079 C CD  . GLU B 46  ? 2.21741 2.46643 2.42395 -0.01614 -0.28199 -0.39611 46  GLU B CD  
3080 O OE1 . GLU B 46  ? 2.31831 2.56137 2.52775 -0.02649 -0.28481 -0.39083 46  GLU B OE1 
3081 O OE2 . GLU B 46  ? 2.30130 2.52731 2.47680 -0.00057 -0.28210 -0.39938 46  GLU B OE2 
3082 N N   . TRP B 47  ? 1.93832 2.23462 2.20001 -0.02270 -0.28141 -0.41801 47  TRP B N   
3083 C CA  . TRP B 47  ? 1.90291 2.18368 2.16175 -0.01101 -0.27862 -0.43092 47  TRP B CA  
3084 C C   . TRP B 47  ? 1.95429 2.21658 2.20144 -0.00175 -0.28235 -0.43476 47  TRP B C   
3085 O O   . TRP B 47  ? 1.99512 2.25816 2.22266 0.00364  -0.27971 -0.42639 47  TRP B O   
3086 C CB  . TRP B 47  ? 1.90899 2.20815 2.16659 -0.00146 -0.26915 -0.42903 47  TRP B CB  
3087 C CG  . TRP B 47  ? 1.90508 2.18793 2.15836 0.01162  -0.26355 -0.44030 47  TRP B CG  
3088 C CD1 . TRP B 47  ? 1.91245 2.17342 2.17643 0.01236  -0.26279 -0.45159 47  TRP B CD1 
3089 C CD2 . TRP B 47  ? 1.92758 2.21004 2.16532 0.02608  -0.25580 -0.43971 47  TRP B CD2 
3090 N NE1 . TRP B 47  ? 1.88677 2.13825 2.15020 0.02391  -0.25761 -0.45806 47  TRP B NE1 
3091 C CE2 . TRP B 47  ? 1.93153 2.19290 2.17374 0.03205  -0.25490 -0.45232 47  TRP B CE2 
3092 C CE3 . TRP B 47  ? 1.98569 2.27848 2.20461 0.03588  -0.24646 -0.42810 47  TRP B CE3 
3093 C CZ2 . TRP B 47  ? 1.98248 2.23109 2.20735 0.04474  -0.24971 -0.45598 47  TRP B CZ2 
3094 C CZ3 . TRP B 47  ? 2.03456 2.31013 2.22887 0.05152  -0.23793 -0.43146 47  TRP B CZ3 
3095 C CH2 . TRP B 47  ? 2.04416 2.29701 2.23974 0.05450  -0.24199 -0.44646 47  TRP B CH2 
3096 N N   . ILE B 48  ? 1.90437 2.14503 2.16286 0.00068  -0.28892 -0.44586 48  ILE B N   
3097 C CA  . ILE B 48  ? 1.93777 2.15451 2.18930 0.00544  -0.30308 -0.44990 48  ILE B CA  
3098 C C   . ILE B 48  ? 1.93119 2.13510 2.18666 0.01421  -0.30526 -0.45865 48  ILE B C   
3099 O O   . ILE B 48  ? 1.96401 2.14644 2.19218 0.02108  -0.31571 -0.46067 48  ILE B O   
3100 C CB  . ILE B 48  ? 1.93871 2.14076 2.21333 -0.00247 -0.31612 -0.45096 48  ILE B CB  
3101 C CG1 . ILE B 48  ? 1.96539 2.17099 2.22497 -0.01011 -0.31644 -0.44217 48  ILE B CG1 
3102 C CG2 . ILE B 48  ? 1.92279 2.09964 2.20230 0.00158  -0.33816 -0.45529 48  ILE B CG2 
3103 C CD1 . ILE B 48  ? 2.03352 2.23204 2.25426 -0.00375 -0.31848 -0.43542 48  ILE B CD1 
3104 N N   . ALA B 49  ? 1.80818 2.01716 2.09148 0.01462  -0.29516 -0.46363 49  ALA B N   
3105 C CA  . ALA B 49  ? 1.79773 1.99380 2.09153 0.02163  -0.29533 -0.47094 49  ALA B CA  
3106 C C   . ALA B 49  ? 1.77072 1.97410 2.08423 0.02486  -0.27440 -0.47320 49  ALA B C   
3107 O O   . ALA B 49  ? 1.75222 1.95830 2.07645 0.02065  -0.26535 -0.47080 49  ALA B O   
3108 C CB  . ALA B 49  ? 1.83723 2.01133 2.16304 0.01755  -0.31757 -0.47423 49  ALA B CB  
3109 N N   . SER B 50  ? 1.68137 1.87951 1.99115 0.03355  -0.26618 -0.47780 50  SER B N   
3110 C CA  . SER B 50  ? 1.67232 1.86904 1.99513 0.03984  -0.24467 -0.48000 50  SER B CA  
3111 C C   . SER B 50  ? 1.68002 1.85912 2.02375 0.04500  -0.24328 -0.48570 50  SER B C   
3112 O O   . SER B 50  ? 1.69719 1.86699 2.02154 0.04668  -0.25618 -0.48890 50  SER B O   
3113 C CB  . SER B 50  ? 1.67067 1.88500 1.95870 0.04672  -0.23113 -0.47668 50  SER B CB  
3114 O OG  . SER B 50  ? 1.66659 1.89597 1.94405 0.03883  -0.23535 -0.47021 50  SER B OG  
3115 N N   . ILE B 51  ? 1.73338 1.90140 2.11352 0.04803  -0.22614 -0.48593 51  ILE B N   
3116 C CA  . ILE B 51  ? 1.72349 1.87521 2.13582 0.05146  -0.22170 -0.48909 51  ILE B CA  
3117 C C   . ILE B 51  ? 1.76109 1.90505 2.16609 0.06411  -0.18844 -0.48926 51  ILE B C   
3118 O O   . ILE B 51  ? 1.75402 1.89713 2.13962 0.06889  -0.17161 -0.48641 51  ILE B O   
3119 C CB  . ILE B 51  ? 1.71667 1.85914 2.19961 0.04328  -0.23265 -0.48463 51  ILE B CB  
3120 C CG1 . ILE B 51  ? 1.70148 1.82850 2.22194 0.04142  -0.24107 -0.48707 51  ILE B CG1 
3121 C CG2 . ILE B 51  ? 1.74214 1.87904 2.25807 0.04823  -0.20392 -0.47685 51  ILE B CG2 
3122 C CD1 . ILE B 51  ? 1.68478 1.80560 2.25478 0.02796  -0.27895 -0.48419 51  ILE B CD1 
3123 N N   . SER B 52  ? 1.79977 1.93104 2.21350 0.06970  -0.18073 -0.49283 52  SER B N   
3124 C CA  . SER B 52  ? 1.79929 1.91794 2.20135 0.08392  -0.14821 -0.49292 52  SER B CA  
3125 C C   . SER B 52  ? 1.82154 1.91948 2.28011 0.08705  -0.12409 -0.48684 52  SER B C   
3126 O O   . SER B 52  ? 1.86120 1.95988 2.36593 0.07926  -0.13044 -0.48078 52  SER B O   
3127 C CB  . SER B 52  ? 1.81563 1.92645 2.19736 0.08984  -0.14723 -0.49843 52  SER B CB  
3128 O OG  . SER B 52  ? 1.82709 1.92302 2.25391 0.08003  -0.16383 -0.50066 52  SER B OG  
3129 N N   . ASN B 53  ? 1.82080 1.89765 2.27693 0.10080  -0.09239 -0.48615 53  ASN B N   
3130 C CA  . ASN B 53  ? 1.81674 1.86761 2.32374 0.10831  -0.05949 -0.47701 53  ASN B CA  
3131 C C   . ASN B 53  ? 1.79568 1.84989 2.39397 0.09638  -0.07100 -0.47104 53  ASN B C   
3132 O O   . ASN B 53  ? 1.79035 1.84197 2.45053 0.09383  -0.06361 -0.45948 53  ASN B O   
3133 C CB  . ASN B 53  ? 1.82517 1.84725 2.30118 0.12773  -0.02130 -0.47704 53  ASN B CB  
3134 C CG  . ASN B 53  ? 1.85724 1.86328 2.25430 0.14104  -0.00758 -0.47826 53  ASN B CG  
3135 O OD1 . ASN B 53  ? 1.87903 1.88218 2.25921 0.13756  -0.01363 -0.47587 53  ASN B OD1 
3136 N ND2 . ASN B 53  ? 1.86829 1.86007 2.21457 0.15592  0.00812  -0.48160 53  ASN B ND2 
3137 N N   . ILE B 54  ? 1.79777 1.85446 2.40636 0.08909  -0.09034 -0.47730 54  ILE B N   
3138 C CA  . ILE B 54  ? 1.79188 1.84827 2.48548 0.07420  -0.11189 -0.47219 54  ILE B CA  
3139 C C   . ILE B 54  ? 1.81770 1.88666 2.49828 0.05648  -0.16635 -0.47965 54  ILE B C   
3140 O O   . ILE B 54  ? 1.88672 1.96137 2.63401 0.04232  -0.19479 -0.47279 54  ILE B O   
3141 C CB  . ILE B 54  ? 1.80827 1.84354 2.52469 0.07734  -0.09557 -0.47307 54  ILE B CB  
3142 C CG1 . ILE B 54  ? 1.76043 1.77512 2.48625 0.09785  -0.03729 -0.46388 54  ILE B CG1 
3143 C CG2 . ILE B 54  ? 1.97771 2.01106 2.78914 0.05799  -0.12542 -0.46663 54  ILE B CG2 
3144 C CD1 . ILE B 54  ? 1.80525 1.79705 2.55913 0.10196  -0.01558 -0.46262 54  ILE B CD1 
3145 N N   . GLY B 55  ? 1.81572 1.88577 2.41029 0.05890  -0.18024 -0.49155 55  GLY B N   
3146 C CA  . GLY B 55  ? 1.76024 1.82813 2.32536 0.04646  -0.22610 -0.49835 55  GLY B CA  
3147 C C   . GLY B 55  ? 1.80311 1.84760 2.30407 0.05003  -0.23363 -0.50887 55  GLY B C   
3148 O O   . GLY B 55  ? 1.93609 1.95481 2.43013 0.03879  -0.27002 -0.51415 55  GLY B O   
3149 N N   . GLY B 56  ? 1.90905 1.95642 2.35871 0.06671  -0.20011 -0.51114 56  GLY B N   
3150 C CA  . GLY B 56  ? 1.92253 1.94786 2.30604 0.07476  -0.19920 -0.51859 56  GLY B CA  
3151 C C   . GLY B 56  ? 2.04584 2.08107 2.35420 0.08157  -0.20685 -0.51951 56  GLY B C   
3152 O O   . GLY B 56  ? 2.14609 2.15407 2.39626 0.08564  -0.21702 -0.52411 56  GLY B O   
3153 N N   . THR B 57  ? 1.84204 1.91140 2.15060 0.08341  -0.20010 -0.51359 57  THR B N   
3154 C CA  . THR B 57  ? 1.88568 1.97124 2.13929 0.08859  -0.20464 -0.51029 57  THR B CA  
3155 C C   . THR B 57  ? 1.87295 1.97748 2.15018 0.07640  -0.22382 -0.50662 57  THR B C   
3156 O O   . THR B 57  ? 1.85091 1.97112 2.17290 0.07188  -0.21624 -0.50348 57  THR B O   
3157 C CB  . THR B 57  ? 1.87330 1.98433 2.09865 0.10453  -0.17480 -0.50415 57  THR B CB  
3158 O OG1 . THR B 57  ? 1.85914 1.97800 2.11976 0.10650  -0.15553 -0.50300 57  THR B OG1 
3159 C CG2 . THR B 57  ? 1.90519 1.99774 2.08458 0.12016  -0.15899 -0.50497 57  THR B CG2 
3160 N N   . ILE B 58  ? 1.82616 1.92211 2.06713 0.07316  -0.24569 -0.50625 58  ILE B N   
3161 C CA  . ILE B 58  ? 1.82005 1.92959 2.07486 0.06277  -0.26437 -0.50240 58  ILE B CA  
3162 C C   . ILE B 58  ? 1.85302 1.96604 2.04841 0.06969  -0.26394 -0.49671 58  ILE B C   
3163 O O   . ILE B 58  ? 1.93753 2.01863 2.07949 0.07785  -0.26759 -0.49823 58  ILE B O   
3164 C CB  . ILE B 58  ? 1.80908 1.89271 2.09606 0.04888  -0.29973 -0.50636 58  ILE B CB  
3165 C CG1 . ILE B 58  ? 1.76929 1.85880 2.13692 0.04174  -0.29558 -0.50561 58  ILE B CG1 
3166 C CG2 . ILE B 58  ? 1.81147 1.90210 2.09378 0.04172  -0.31980 -0.50192 58  ILE B CG2 
3167 C CD1 . ILE B 58  ? 1.77454 1.83606 2.15945 0.04074  -0.29895 -0.51098 58  ILE B CD1 
3168 N N   . TYR B 59  ? 1.90602 2.05216 2.10893 0.06716  -0.25749 -0.48877 59  TYR B N   
3169 C CA  . TYR B 59  ? 1.90278 2.05707 2.06422 0.07265  -0.25385 -0.47927 59  TYR B CA  
3170 C C   . TYR B 59  ? 1.89537 2.05333 2.06787 0.06084  -0.27229 -0.47637 59  TYR B C   
3171 O O   . TYR B 59  ? 1.83217 2.00336 2.04898 0.04967  -0.27901 -0.47823 59  TYR B O   
3172 C CB  . TYR B 59  ? 1.87929 2.07346 2.04175 0.08019  -0.22898 -0.46831 59  TYR B CB  
3173 C CG  . TYR B 59  ? 1.89985 2.09875 2.06566 0.09051  -0.21024 -0.47056 59  TYR B CG  
3174 C CD1 . TYR B 59  ? 1.94542 2.11634 2.07835 0.10344  -0.20148 -0.47389 59  TYR B CD1 
3175 C CD2 . TYR B 59  ? 1.90508 2.12860 2.09799 0.08859  -0.20113 -0.46912 59  TYR B CD2 
3176 C CE1 . TYR B 59  ? 1.98712 2.16068 2.12149 0.11409  -0.18247 -0.47526 59  TYR B CE1 
3177 C CE2 . TYR B 59  ? 1.90987 2.13261 2.09947 0.10011  -0.18368 -0.47053 59  TYR B CE2 
3178 C CZ  . TYR B 59  ? 1.98121 2.18225 2.14508 0.11287  -0.17345 -0.47327 59  TYR B CZ  
3179 O OH  . TYR B 59  ? 2.00578 2.20425 2.16491 0.12545  -0.15435 -0.47410 59  TYR B OH  
3180 N N   . TYR B 60  ? 2.07138 2.21199 2.19868 0.06579  -0.27666 -0.47042 60  TYR B N   
3181 C CA  . TYR B 60  ? 2.02777 2.17217 2.15484 0.05810  -0.28773 -0.46444 60  TYR B CA  
3182 C C   . TYR B 60  ? 2.08014 2.23532 2.17243 0.06833  -0.26660 -0.44909 60  TYR B C   
3183 O O   . TYR B 60  ? 2.12703 2.26640 2.17893 0.08436  -0.24939 -0.44398 60  TYR B O   
3184 C CB  . TYR B 60  ? 2.02367 2.12098 2.12783 0.05453  -0.31916 -0.47112 60  TYR B CB  
3185 C CG  . TYR B 60  ? 2.00986 2.09168 2.15416 0.04527  -0.34372 -0.48255 60  TYR B CG  
3186 C CD1 . TYR B 60  ? 1.96462 2.06668 2.17237 0.03266  -0.35457 -0.48279 60  TYR B CD1 
3187 C CD2 . TYR B 60  ? 2.05162 2.09523 2.17275 0.04946  -0.35508 -0.49092 60  TYR B CD2 
3188 C CE1 . TYR B 60  ? 1.96536 2.05684 2.22378 0.02526  -0.37366 -0.48828 60  TYR B CE1 
3189 C CE2 . TYR B 60  ? 2.06520 2.09708 2.23551 0.03894  -0.37896 -0.49838 60  TYR B CE2 
3190 C CZ  . TYR B 60  ? 2.03484 2.09395 2.27925 0.02723  -0.38717 -0.49564 60  TYR B CZ  
3191 O OH  . TYR B 60  ? 2.05813 2.10932 2.36505 0.01782  -0.40745 -0.49833 60  TYR B OH  
3192 N N   . PRO B 61  ? 2.11231 2.29225 2.22192 0.06020  -0.26480 -0.43941 61  PRO B N   
3193 C CA  . PRO B 61  ? 2.17346 2.35815 2.25589 0.06965  -0.24498 -0.42150 61  PRO B CA  
3194 C C   . PRO B 61  ? 2.38738 2.51363 2.40507 0.08040  -0.25169 -0.42149 61  PRO B C   
3195 O O   . PRO B 61  ? 2.37427 2.46504 2.37899 0.07418  -0.28060 -0.43424 61  PRO B O   
3196 C CB  . PRO B 61  ? 2.08311 2.30482 2.20729 0.05358  -0.24701 -0.41340 61  PRO B CB  
3197 C CG  . PRO B 61  ? 2.00959 2.22115 2.15663 0.03944  -0.27188 -0.42856 61  PRO B CG  
3198 C CD  . PRO B 61  ? 2.01905 2.21990 2.17386 0.04289  -0.27743 -0.44246 61  PRO B CD  
3199 N N   . ASP B 62  ? 2.49502 2.60726 2.47076 0.09824  -0.22432 -0.40496 62  ASP B N   
3200 C CA  . ASP B 62  ? 2.58650 2.62686 2.47982 0.11386  -0.22552 -0.40380 62  ASP B CA  
3201 C C   . ASP B 62  ? 2.56320 2.58302 2.44589 0.10492  -0.24575 -0.40446 62  ASP B C   
3202 O O   . ASP B 62  ? 2.65179 2.60181 2.46278 0.11426  -0.26131 -0.40932 62  ASP B O   
3203 C CB  . ASP B 62  ? 2.70010 2.72888 2.55364 0.13823  -0.18180 -0.38085 62  ASP B CB  
3204 C CG  . ASP B 62  ? 2.71287 2.77041 2.58561 0.14854  -0.15829 -0.37580 62  ASP B CG  
3205 O OD1 . ASP B 62  ? 2.68915 2.73885 2.56363 0.14401  -0.17625 -0.39434 62  ASP B OD1 
3206 O OD2 . ASP B 62  ? 2.74970 2.83865 2.64094 0.16151  -0.12125 -0.35131 62  ASP B OD2 
3207 N N   . SER B 63  ? 2.46793 2.54020 2.41396 0.08749  -0.24775 -0.39980 63  SER B N   
3208 C CA  . SER B 63  ? 2.51602 2.56995 2.45332 0.07991  -0.26360 -0.39884 63  SER B CA  
3209 C C   . SER B 63  ? 2.50825 2.52384 2.43359 0.07264  -0.30615 -0.41778 63  SER B C   
3210 O O   . SER B 63  ? 2.58627 2.55631 2.46884 0.07576  -0.32341 -0.41760 63  SER B O   
3211 C CB  . SER B 63  ? 2.42294 2.53731 2.43056 0.06105  -0.25821 -0.39137 63  SER B CB  
3212 O OG  . SER B 63  ? 2.32200 2.47497 2.38682 0.04614  -0.27102 -0.40345 63  SER B OG  
3213 N N   . VAL B 64  ? 2.51548 2.54785 2.48151 0.06355  -0.32357 -0.43200 64  VAL B N   
3214 C CA  . VAL B 64  ? 2.46589 2.47299 2.44526 0.05436  -0.36413 -0.44582 64  VAL B CA  
3215 C C   . VAL B 64  ? 2.52959 2.49473 2.47642 0.06087  -0.38117 -0.45720 64  VAL B C   
3216 O O   . VAL B 64  ? 2.43509 2.39856 2.42280 0.05036  -0.40992 -0.46778 64  VAL B O   
3217 C CB  . VAL B 64  ? 2.28101 2.33939 2.34706 0.03695  -0.36936 -0.44998 64  VAL B CB  
3218 C CG1 . VAL B 64  ? 2.24229 2.32661 2.32960 0.02893  -0.35944 -0.44037 64  VAL B CG1 
3219 C CG2 . VAL B 64  ? 2.25375 2.35122 2.35588 0.03598  -0.34738 -0.45252 64  VAL B CG2 
3220 N N   . LYS B 65  ? 2.48940 2.41753 2.36452 0.07862  -0.36183 -0.45322 65  LYS B N   
3221 C CA  . LYS B 65  ? 2.55742 2.43725 2.38972 0.08568  -0.37468 -0.46389 65  LYS B CA  
3222 C C   . LYS B 65  ? 2.61495 2.42867 2.41196 0.08027  -0.42692 -0.47482 65  LYS B C   
3223 O O   . LYS B 65  ? 2.68234 2.44032 2.40890 0.08873  -0.43999 -0.47114 65  LYS B O   
3224 C CB  . LYS B 65  ? 2.66725 2.50867 2.41665 0.10972  -0.33908 -0.45436 65  LYS B CB  
3225 C CG  . LYS B 65  ? 2.72093 2.52385 2.43255 0.11810  -0.33932 -0.46372 65  LYS B CG  
3226 C CD  . LYS B 65  ? 2.80311 2.57956 2.44516 0.14486  -0.29225 -0.44951 65  LYS B CD  
3227 C CE  . LYS B 65  ? 2.84314 2.59676 2.46209 0.15318  -0.28362 -0.45711 65  LYS B CE  
3228 N NZ  . LYS B 65  ? 2.91537 2.65649 2.48327 0.18122  -0.23016 -0.43880 65  LYS B NZ  
3229 N N   . GLY B 66  ? 2.60721 2.42609 2.45662 0.06610  -0.45779 -0.48651 66  GLY B N   
3230 C CA  . GLY B 66  ? 2.64138 2.40519 2.47796 0.05701  -0.51498 -0.49496 66  GLY B CA  
3231 C C   . GLY B 66  ? 2.58447 2.37811 2.48629 0.04376  -0.54062 -0.49057 66  GLY B C   
3232 O O   . GLY B 66  ? 2.56130 2.35637 2.52454 0.02919  -0.58149 -0.49436 66  GLY B O   
3233 N N   . ARG B 67  ? 2.60176 2.41934 2.49534 0.04902  -0.51546 -0.48040 67  ARG B N   
3234 C CA  . ARG B 67  ? 2.55474 2.39717 2.50217 0.03890  -0.53413 -0.47488 67  ARG B CA  
3235 C C   . ARG B 67  ? 2.40075 2.30869 2.46637 0.02339  -0.53292 -0.47501 67  ARG B C   
3236 O O   . ARG B 67  ? 2.37692 2.29212 2.49929 0.01408  -0.56252 -0.47175 67  ARG B O   
3237 C CB  . ARG B 67  ? 2.56554 2.42676 2.48767 0.04631  -0.49849 -0.46356 67  ARG B CB  
3238 C CG  . ARG B 67  ? 2.66168 2.46526 2.47285 0.06612  -0.47966 -0.45864 67  ARG B CG  
3239 C CD  . ARG B 67  ? 2.64873 2.48918 2.46146 0.07129  -0.43372 -0.44417 67  ARG B CD  
3240 N NE  . ARG B 67  ? 2.58933 2.46908 2.46366 0.05795  -0.44072 -0.43996 67  ARG B NE  
3241 C CZ  . ARG B 67  ? 2.62426 2.46781 2.47091 0.05939  -0.46504 -0.43685 67  ARG B CZ  
3242 N NH1 . ARG B 67  ? 2.71502 2.47809 2.46884 0.07326  -0.48841 -0.43805 67  ARG B NH1 
3243 N NH2 . ARG B 67  ? 2.52740 2.40931 2.43373 0.04794  -0.46618 -0.43218 67  ARG B NH2 
3244 N N   . PHE B 68  ? 2.43191 2.38378 2.53369 0.02271  -0.49707 -0.47674 68  PHE B N   
3245 C CA  . PHE B 68  ? 2.24111 2.24548 2.44111 0.01235  -0.48610 -0.47577 68  PHE B CA  
3246 C C   . PHE B 68  ? 2.27617 2.27657 2.50368 0.01004  -0.49029 -0.48341 68  PHE B C   
3247 O O   . PHE B 68  ? 2.37957 2.34736 2.54618 0.01731  -0.48945 -0.48987 68  PHE B O   
3248 C CB  . PHE B 68  ? 2.16459 2.21827 2.38087 0.01344  -0.44071 -0.47059 68  PHE B CB  
3249 C CG  . PHE B 68  ? 2.18203 2.24759 2.40146 0.01040  -0.43693 -0.46219 68  PHE B CG  
3250 C CD1 . PHE B 68  ? 2.30712 2.33889 2.46557 0.01567  -0.45051 -0.45832 68  PHE B CD1 
3251 C CD2 . PHE B 68  ? 2.11621 2.21846 2.39150 0.00364  -0.41757 -0.45784 68  PHE B CD2 
3252 C CE1 . PHE B 68  ? 2.26371 2.30432 2.42495 0.01288  -0.44523 -0.45015 68  PHE B CE1 
3253 C CE2 . PHE B 68  ? 2.10175 2.20921 2.37561 0.00024  -0.41372 -0.45045 68  PHE B CE2 
3254 C CZ  . PHE B 68  ? 2.15504 2.23490 2.37573 0.00418  -0.42759 -0.44652 68  PHE B CZ  
3255 N N   . THR B 69  ? 2.07640 2.10628 2.39595 0.00127  -0.49128 -0.48098 69  THR B N   
3256 C CA  . THR B 69  ? 2.08446 2.11161 2.44471 -0.00224 -0.49417 -0.48593 69  THR B CA  
3257 C C   . THR B 69  ? 1.98013 2.05206 2.43091 -0.00487 -0.46388 -0.47936 69  THR B C   
3258 O O   . THR B 69  ? 1.95238 2.03665 2.47688 -0.01091 -0.47570 -0.47001 69  THR B O   
3259 C CB  . THR B 69  ? 2.15821 2.14462 2.53529 -0.01161 -0.54936 -0.48758 69  THR B CB  
3260 O OG1 . THR B 69  ? 2.29947 2.22838 2.57235 -0.00635 -0.57682 -0.49402 69  THR B OG1 
3261 C CG2 . THR B 69  ? 2.14635 2.12787 2.56781 -0.01710 -0.55180 -0.49195 69  THR B CG2 
3262 N N   . ILE B 70  ? 1.95252 2.04358 2.39460 0.00182  -0.42373 -0.48255 70  ILE B N   
3263 C CA  . ILE B 70  ? 1.86721 1.98677 2.37537 0.00305  -0.39037 -0.47669 70  ILE B CA  
3264 C C   . ILE B 70  ? 1.89273 2.00631 2.47591 -0.00118 -0.39728 -0.47427 70  ILE B C   
3265 O O   . ILE B 70  ? 1.94255 2.03177 2.51531 -0.00539 -0.42303 -0.48050 70  ILE B O   
3266 C CB  . ILE B 70  ? 1.85772 1.99311 2.32323 0.01227  -0.34977 -0.48035 70  ILE B CB  
3267 C CG1 . ILE B 70  ? 1.84687 1.99886 2.35385 0.01512  -0.31677 -0.47371 70  ILE B CG1 
3268 C CG2 . ILE B 70  ? 1.89494 2.01896 2.34106 0.01773  -0.34145 -0.48778 70  ILE B CG2 
3269 C CD1 . ILE B 70  ? 1.82857 1.99035 2.29009 0.02289  -0.28511 -0.47672 70  ILE B CD1 
3270 N N   . SER B 71  ? 1.85626 1.98714 2.51544 0.00038  -0.37242 -0.46359 71  SER B N   
3271 C CA  . SER B 71  ? 1.85498 1.98432 2.60307 -0.00280 -0.37174 -0.45600 71  SER B CA  
3272 C C   . SER B 71  ? 1.82837 1.96997 2.62542 0.00767  -0.32025 -0.44508 71  SER B C   
3273 O O   . SER B 71  ? 1.81687 1.96429 2.59113 0.01396  -0.29761 -0.44160 71  SER B O   
3274 C CB  . SER B 71  ? 1.87265 1.99837 2.69214 -0.01508 -0.41922 -0.44594 71  SER B CB  
3275 O OG  . SER B 71  ? 1.87384 2.00027 2.79002 -0.02061 -0.42221 -0.43624 71  SER B OG  
3276 N N   . ARG B 72  ? 1.75606 1.89392 2.61531 0.01009  -0.30090 -0.43920 72  ARG B N   
3277 C CA  . ARG B 72  ? 1.76828 1.90529 2.67092 0.02361  -0.24705 -0.42673 72  ARG B CA  
3278 C C   . ARG B 72  ? 1.80132 1.93674 2.81062 0.02178  -0.23942 -0.41282 72  ARG B C   
3279 O O   . ARG B 72  ? 1.82329 1.95257 2.83936 0.01302  -0.26183 -0.42017 72  ARG B O   
3280 C CB  . ARG B 72  ? 1.77368 1.89949 2.59114 0.03696  -0.20780 -0.43789 72  ARG B CB  
3281 C CG  . ARG B 72  ? 1.78374 1.90289 2.56063 0.03657  -0.21289 -0.45131 72  ARG B CG  
3282 C CD  . ARG B 72  ? 1.75688 1.86587 2.46374 0.05200  -0.17258 -0.45778 72  ARG B CD  
3283 N NE  . ARG B 72  ? 1.70601 1.79649 2.45130 0.06613  -0.12456 -0.44578 72  ARG B NE  
3284 C CZ  . ARG B 72  ? 1.71884 1.78937 2.40506 0.08134  -0.08835 -0.44703 72  ARG B CZ  
3285 N NH1 . ARG B 72  ? 1.74284 1.81777 2.34161 0.08194  -0.09774 -0.45846 72  ARG B NH1 
3286 N NH2 . ARG B 72  ? 1.73862 1.77995 2.45415 0.09689  -0.04202 -0.43479 72  ARG B NH2 
3287 N N   . ASP B 73  ? 1.72180 1.85919 2.81461 0.03067  -0.20551 -0.39105 73  ASP B N   
3288 C CA  . ASP B 73  ? 1.84015 1.98006 3.05611 0.03011  -0.19192 -0.37075 73  ASP B CA  
3289 C C   . ASP B 73  ? 1.83831 1.95655 3.06029 0.05309  -0.11767 -0.35969 73  ASP B C   
3290 O O   . ASP B 73  ? 1.84739 1.95206 3.04375 0.06870  -0.08028 -0.35187 73  ASP B O   
3291 C CB  . ASP B 73  ? 1.85147 2.01218 3.18142 0.02210  -0.21800 -0.34738 73  ASP B CB  
3292 C CG  . ASP B 73  ? 1.85119 2.02057 3.32866 0.01977  -0.20639 -0.32135 73  ASP B CG  
3293 O OD1 . ASP B 73  ? 1.83854 1.99694 3.32684 0.01895  -0.19134 -0.32530 73  ASP B OD1 
3294 O OD2 . ASP B 73  ? 1.84650 2.03448 3.43480 0.01911  -0.21128 -0.29477 73  ASP B OD2 
3295 N N   . SER B 74  ? 1.76837 1.87530 3.01752 0.05603  -0.09589 -0.35880 74  SER B N   
3296 C CA  . SER B 74  ? 1.75477 1.83107 2.99928 0.08048  -0.02315 -0.34833 74  SER B CA  
3297 C C   . SER B 74  ? 1.77426 1.84837 3.14347 0.09198  0.01779  -0.31386 74  SER B C   
3298 O O   . SER B 74  ? 1.79214 1.83283 3.13557 0.11663  0.07843  -0.30216 74  SER B O   
3299 C CB  . SER B 74  ? 1.75409 1.81662 2.98807 0.08123  -0.01068 -0.35706 74  SER B CB  
3300 O OG  . SER B 74  ? 1.77571 1.80267 3.01109 0.10656  0.06128  -0.34412 74  SER B OG  
3301 N N   . ALA B 75  ? 1.78926 1.89405 3.29333 0.07532  -0.01479 -0.29547 75  ALA B N   
3302 C CA  . ALA B 75  ? 1.75209 1.86025 3.39842 0.08683  0.02734  -0.25692 75  ALA B CA  
3303 C C   . ALA B 75  ? 1.77620 1.87936 3.41890 0.10217  0.05106  -0.24166 75  ALA B C   
3304 O O   . ALA B 75  ? 1.76944 1.84861 3.46374 0.12694  0.11880  -0.21361 75  ALA B O   
3305 C CB  . ALA B 75  ? 1.72453 1.87147 3.52202 0.06143  -0.02575 -0.23985 75  ALA B CB  
3306 N N   . GLN B 76  ? 1.78493 1.90446 3.36378 0.08966  0.00011  -0.25837 76  GLN B N   
3307 C CA  . GLN B 76  ? 1.79883 1.91253 3.37023 0.10190  0.01697  -0.24531 76  GLN B CA  
3308 C C   . GLN B 76  ? 1.82646 1.90558 3.23350 0.11226  0.03322  -0.27007 76  GLN B C   
3309 O O   . GLN B 76  ? 1.83596 1.90146 3.21883 0.12205  0.04803  -0.26212 76  GLN B O   
3310 C CB  . GLN B 76  ? 1.80508 1.96158 3.44481 0.08076  -0.05222 -0.23928 76  GLN B CB  
3311 C CG  . GLN B 76  ? 1.77426 1.96148 3.60077 0.07695  -0.05765 -0.20112 76  GLN B CG  
3312 C CD  . GLN B 76  ? 1.76977 1.98751 3.66564 0.04708  -0.13030 -0.20690 76  GLN B CD  
3313 O OE1 . GLN B 76  ? 1.77694 1.98513 3.65979 0.04070  -0.12793 -0.21920 76  GLN B OE1 
3314 N NE2 . GLN B 76  ? 1.76081 2.00889 3.72465 0.02895  -0.19720 -0.19802 76  GLN B NE2 
3315 N N   . ASN B 77  ? 1.81864 1.88259 3.11617 0.10988  0.02924  -0.29821 77  ASN B N   
3316 C CA  . ASN B 77  ? 1.83942 1.86872 2.98924 0.11953  0.04562  -0.31893 77  ASN B CA  
3317 C C   . ASN B 77  ? 1.73924 1.78498 2.83828 0.10701  0.00313  -0.32944 77  ASN B C   
3318 O O   . ASN B 77  ? 1.77955 1.79520 2.82436 0.11841  0.02800  -0.32621 77  ASN B O   
3319 C CB  . ASN B 77  ? 1.88764 1.85696 3.00811 0.14975  0.12187  -0.30330 77  ASN B CB  
3320 C CG  . ASN B 77  ? 1.91667 1.85573 3.03698 0.16522  0.16763  -0.30035 77  ASN B CG  
3321 O OD1 . ASN B 77  ? 1.93057 1.82478 2.93657 0.17843  0.19270  -0.31504 77  ASN B OD1 
3322 N ND2 . ASN B 77  ? 1.88248 1.84405 3.13276 0.16330  0.17689  -0.28014 77  ASN B ND2 
3323 N N   . THR B 78  ? 1.77492 1.86125 2.88524 0.08408  -0.06055 -0.34188 78  THR B N   
3324 C CA  . THR B 78  ? 1.78650 1.88792 2.85356 0.07237  -0.10159 -0.35038 78  THR B CA  
3325 C C   . THR B 78  ? 1.77141 1.88984 2.76051 0.05568  -0.15009 -0.37685 78  THR B C   
3326 O O   . THR B 78  ? 1.75535 1.88225 2.75492 0.04884  -0.16671 -0.38510 78  THR B O   
3327 C CB  . THR B 78  ? 1.79403 1.92204 2.97021 0.06486  -0.13107 -0.32974 78  THR B CB  
3328 O OG1 . THR B 78  ? 1.90822 2.06069 3.17380 0.05188  -0.16473 -0.32484 78  THR B OG1 
3329 C CG2 . THR B 78  ? 1.78365 1.89352 3.02898 0.08482  -0.07802 -0.30027 78  THR B CG2 
3330 N N   . LEU B 79  ? 1.91406 2.03353 2.82488 0.05030  -0.16936 -0.38827 79  LEU B N   
3331 C CA  . LEU B 79  ? 1.86282 1.99568 2.69770 0.03762  -0.20917 -0.40903 79  LEU B CA  
3332 C C   . LEU B 79  ? 1.84392 1.99259 2.69329 0.02528  -0.25672 -0.40726 79  LEU B C   
3333 O O   . LEU B 79  ? 1.86675 2.01508 2.75305 0.02752  -0.25416 -0.39350 79  LEU B O   
3334 C CB  . LEU B 79  ? 1.83314 1.95244 2.56397 0.04186  -0.19070 -0.42169 79  LEU B CB  
3335 C CG  . LEU B 79  ? 1.80607 1.93678 2.46041 0.03532  -0.21178 -0.43968 79  LEU B CG  
3336 C CD1 . LEU B 79  ? 1.78304 1.91291 2.44629 0.03936  -0.20397 -0.44517 79  LEU B CD1 
3337 C CD2 . LEU B 79  ? 1.80466 1.92464 2.37810 0.03806  -0.19564 -0.44595 79  LEU B CD2 
3338 N N   . TYR B 80  ? 1.81096 1.96683 2.62508 0.01444  -0.29843 -0.42031 80  TYR B N   
3339 C CA  . TYR B 80  ? 1.80878 1.96863 2.62563 0.00440  -0.34679 -0.41928 80  TYR B CA  
3340 C C   . TYR B 80  ? 1.77856 1.93298 2.49315 0.00030  -0.36717 -0.43606 80  TYR B C   
3341 O O   . TYR B 80  ? 1.76616 1.91856 2.42659 0.00301  -0.35353 -0.44766 80  TYR B O   
3342 C CB  . TYR B 80  ? 1.83405 1.99505 2.73010 -0.00440 -0.38620 -0.41234 80  TYR B CB  
3343 C CG  . TYR B 80  ? 1.88589 2.05718 2.90247 -0.00021 -0.36484 -0.39043 80  TYR B CG  
3344 C CD1 . TYR B 80  ? 2.00341 2.18408 3.09055 0.00185  -0.36920 -0.37026 80  TYR B CD1 
3345 C CD2 . TYR B 80  ? 1.97716 2.14750 3.03986 0.00363  -0.33630 -0.38728 80  TYR B CD2 
3346 C CE1 . TYR B 80  ? 2.01569 2.20648 3.22177 0.00846  -0.34379 -0.34542 80  TYR B CE1 
3347 C CE2 . TYR B 80  ? 2.00645 2.18468 3.18555 0.00957  -0.31018 -0.36338 80  TYR B CE2 
3348 C CZ  . TYR B 80  ? 2.01857 2.20799 3.27184 0.01237  -0.31304 -0.34144 80  TYR B CZ  
3349 O OH  . TYR B 80  ? 2.02227 2.22026 3.39980 0.02091  -0.28154 -0.31307 80  TYR B OH  
3350 N N   . LEU B 81  ? 1.86574 2.01616 2.55643 -0.00437 -0.39764 -0.43480 81  LEU B N   
3351 C CA  . LEU B 81  ? 1.88408 2.02458 2.48131 -0.00595 -0.41368 -0.44631 81  LEU B CA  
3352 C C   . LEU B 81  ? 1.91799 2.04088 2.51111 -0.01095 -0.46147 -0.44313 81  LEU B C   
3353 O O   . LEU B 81  ? 1.92181 2.04479 2.50780 -0.01068 -0.46571 -0.43656 81  LEU B O   
3354 C CB  . LEU B 81  ? 1.87002 2.01937 2.41615 -0.00302 -0.38337 -0.44733 81  LEU B CB  
3355 C CG  . LEU B 81  ? 1.88360 2.02939 2.34399 -0.00262 -0.38626 -0.45567 81  LEU B CG  
3356 C CD1 . LEU B 81  ? 1.88228 2.02900 2.31700 0.00160  -0.37531 -0.46432 81  LEU B CD1 
3357 C CD2 . LEU B 81  ? 1.87187 2.02837 2.30032 -0.00374 -0.36303 -0.45291 81  LEU B CD2 
3358 N N   . GLN B 82  ? 2.07306 2.17442 2.66506 -0.01533 -0.49897 -0.44794 82  GLN B N   
3359 C CA  . GLN B 82  ? 2.18998 2.26194 2.76640 -0.01980 -0.55226 -0.44605 82  GLN B CA  
3360 C C   . GLN B 82  ? 2.25888 2.30266 2.72014 -0.01404 -0.55582 -0.45478 82  GLN B C   
3361 O O   . GLN B 82  ? 2.30980 2.33200 2.70273 -0.01016 -0.55172 -0.46534 82  GLN B O   
3362 C CB  . GLN B 82  ? 2.29902 2.34724 2.90700 -0.02801 -0.59518 -0.44853 82  GLN B CB  
3363 C CG  . GLN B 82  ? 2.37326 2.38076 2.96009 -0.03352 -0.65961 -0.44669 82  GLN B CG  
3364 C CD  . GLN B 82  ? 2.37324 2.39902 3.01973 -0.03371 -0.67245 -0.43035 82  GLN B CD  
3365 O OE1 . GLN B 82  ? 2.38980 2.40457 2.97455 -0.02729 -0.67038 -0.43018 82  GLN B OE1 
3366 N NE2 . GLN B 82  ? 2.35747 2.41081 3.12830 -0.03990 -0.68277 -0.41426 82  GLN B NE2 
3367 N N   . MET B 83  ? 2.34555 2.38679 2.78610 -0.01179 -0.55976 -0.44835 83  MET B N   
3368 C CA  . MET B 83  ? 2.37118 2.38622 2.71056 -0.00482 -0.55607 -0.45233 83  MET B CA  
3369 C C   . MET B 83  ? 2.46545 2.43208 2.76548 -0.00355 -0.60655 -0.45002 83  MET B C   
3370 O O   . MET B 83  ? 2.46000 2.43208 2.81672 -0.00737 -0.63162 -0.44024 83  MET B O   
3371 C CB  . MET B 83  ? 2.25491 2.30041 2.59144 -0.00311 -0.51572 -0.44656 83  MET B CB  
3372 C CG  . MET B 83  ? 2.19499 2.25728 2.59719 -0.00636 -0.51832 -0.43505 83  MET B CG  
3373 S SD  . MET B 83  ? 2.17388 2.26678 2.57869 -0.00723 -0.46744 -0.43054 83  MET B SD  
3374 C CE  . MET B 83  ? 2.17182 2.29265 2.62875 -0.00841 -0.43497 -0.43436 83  MET B CE  
3375 N N   . ASN B 84  ? 2.38838 2.30248 2.58780 0.00384  -0.62053 -0.45758 84  ASN B N   
3376 C CA  . ASN B 84  ? 2.48604 2.33571 2.62132 0.00782  -0.67010 -0.45715 84  ASN B CA  
3377 C C   . ASN B 84  ? 2.53468 2.35394 2.57063 0.02140  -0.64767 -0.45451 84  ASN B C   
3378 O O   . ASN B 84  ? 2.50063 2.34395 2.51159 0.02702  -0.59749 -0.45398 84  ASN B O   
3379 C CB  . ASN B 84  ? 2.57354 2.36304 2.65633 0.00737  -0.70949 -0.46769 84  ASN B CB  
3380 C CG  . ASN B 84  ? 2.52493 2.34106 2.71000 -0.00749 -0.73303 -0.46882 84  ASN B CG  
3381 O OD1 . ASN B 84  ? 2.47716 2.32738 2.76450 -0.01701 -0.75338 -0.45850 84  ASN B OD1 
3382 N ND2 . ASN B 84  ? 2.54394 2.34312 2.70476 -0.00834 -0.72749 -0.47919 84  ASN B ND2 
3383 N N   . SER B 85  ? 2.59399 2.35833 2.57673 0.02686  -0.68672 -0.45092 85  SER B N   
3384 C CA  . SER B 85  ? 2.67355 2.38718 2.54551 0.04292  -0.67102 -0.44750 85  SER B CA  
3385 C C   . SER B 85  ? 2.59902 2.36741 2.49215 0.04440  -0.61146 -0.43922 85  SER B C   
3386 O O   . SER B 85  ? 2.62166 2.38374 2.45714 0.05428  -0.56976 -0.43728 85  SER B O   
3387 C CB  . SER B 85  ? 2.77234 2.41664 2.53030 0.05649  -0.66743 -0.45534 85  SER B CB  
3388 O OG  . SER B 85  ? 2.87253 2.45563 2.51928 0.07539  -0.65163 -0.44917 85  SER B OG  
3389 N N   . LEU B 86  ? 2.53867 2.35880 2.51825 0.03435  -0.60803 -0.43253 86  LEU B N   
3390 C CA  . LEU B 86  ? 2.46764 2.33885 2.47643 0.03115  -0.55757 -0.42594 86  LEU B CA  
3391 C C   . LEU B 86  ? 2.53850 2.37512 2.46735 0.04240  -0.53813 -0.41768 86  LEU B C   
3392 O O   . LEU B 86  ? 2.63333 2.41237 2.50291 0.05208  -0.56693 -0.41455 86  LEU B O   
3393 C CB  . LEU B 86  ? 2.39902 2.31611 2.50486 0.02029  -0.55988 -0.42020 86  LEU B CB  
3394 C CG  . LEU B 86  ? 2.32640 2.28082 2.52100 0.01099  -0.56698 -0.42437 86  LEU B CG  
3395 C CD1 . LEU B 86  ? 2.30080 2.28647 2.58506 0.00547  -0.56835 -0.41447 86  LEU B CD1 
3396 C CD2 . LEU B 86  ? 2.28301 2.27319 2.48541 0.00783  -0.52530 -0.43071 86  LEU B CD2 
3397 N N   . ARG B 87  ? 2.53227 2.40248 2.46148 0.04110  -0.48952 -0.41267 87  ARG B N   
3398 C CA  . ARG B 87  ? 2.58915 2.43492 2.45670 0.05063  -0.46125 -0.40148 87  ARG B CA  
3399 C C   . ARG B 87  ? 2.54499 2.44379 2.47026 0.03741  -0.43015 -0.39371 87  ARG B C   
3400 O O   . ARG B 87  ? 2.47491 2.42361 2.47424 0.02318  -0.42649 -0.39800 87  ARG B O   
3401 C CB  . ARG B 87  ? 2.63322 2.45780 2.43712 0.06385  -0.43094 -0.39854 87  ARG B CB  
3402 C CG  . ARG B 87  ? 2.69547 2.45207 2.42398 0.07813  -0.46005 -0.40698 87  ARG B CG  
3403 C CD  . ARG B 87  ? 2.74853 2.48231 2.41500 0.09401  -0.42284 -0.40222 87  ARG B CD  
3404 N NE  . ARG B 87  ? 2.67726 2.48295 2.41379 0.08404  -0.39396 -0.40300 87  ARG B NE  
3405 C CZ  . ARG B 87  ? 2.69924 2.49689 2.40826 0.09410  -0.37533 -0.40400 87  ARG B CZ  
3406 N NH1 . ARG B 87  ? 2.78945 2.50602 2.39867 0.11420  -0.38121 -0.40549 87  ARG B NH1 
3407 N NH2 . ARG B 87  ? 2.63784 2.50371 2.41467 0.08494  -0.35098 -0.40329 87  ARG B NH2 
3408 N N   . SER B 88  ? 2.62498 2.50484 2.50979 0.04285  -0.40664 -0.38150 88  SER B N   
3409 C CA  . SER B 88  ? 2.60017 2.51877 2.53116 0.02872  -0.38153 -0.37355 88  SER B CA  
3410 C C   . SER B 88  ? 2.53960 2.51604 2.52226 0.01488  -0.35395 -0.37370 88  SER B C   
3411 O O   . SER B 88  ? 2.50093 2.51097 2.53284 -0.00139 -0.34456 -0.37255 88  SER B O   
3412 C CB  . SER B 88  ? 2.68009 2.56372 2.55696 0.03754  -0.35924 -0.35864 88  SER B CB  
3413 O OG  . SER B 88  ? 2.72703 2.59585 2.55829 0.04990  -0.32988 -0.34980 88  SER B OG  
3414 N N   . GLU B 89  ? 2.62709 2.60981 2.59405 0.02190  -0.34205 -0.37455 89  GLU B N   
3415 C CA  . GLU B 89  ? 2.57578 2.61271 2.59189 0.01019  -0.32051 -0.37365 89  GLU B CA  
3416 C C   . GLU B 89  ? 2.48773 2.55575 2.56054 -0.00229 -0.33717 -0.38742 89  GLU B C   
3417 O O   . GLU B 89  ? 2.44535 2.55165 2.56038 -0.01621 -0.32442 -0.38700 89  GLU B O   
3418 C CB  . GLU B 89  ? 2.60475 2.63769 2.59001 0.02431  -0.30337 -0.36977 89  GLU B CB  
3419 C CG  . GLU B 89  ? 2.69856 2.69561 2.62579 0.04100  -0.27648 -0.35217 89  GLU B CG  
3420 C CD  . GLU B 89  ? 2.74518 2.72419 2.63094 0.06033  -0.25799 -0.34777 89  GLU B CD  
3421 O OE1 . GLU B 89  ? 2.70971 2.69169 2.59810 0.06169  -0.27488 -0.36198 89  GLU B OE1 
3422 O OE2 . GLU B 89  ? 2.82583 2.78475 2.67669 0.07539  -0.22327 -0.32848 89  GLU B OE2 
3423 N N   . ASP B 90  ? 2.57979 2.62762 2.65411 0.00283  -0.36594 -0.39804 90  ASP B N   
3424 C CA  . ASP B 90  ? 2.39192 2.46454 2.52344 -0.00554 -0.37657 -0.40794 90  ASP B CA  
3425 C C   . ASP B 90  ? 2.35039 2.43210 2.52108 -0.01630 -0.37506 -0.40563 90  ASP B C   
3426 O O   . ASP B 90  ? 2.29229 2.38669 2.50879 -0.02016 -0.37862 -0.41093 90  ASP B O   
3427 C CB  . ASP B 90  ? 2.36405 2.41252 2.49538 0.00251  -0.40843 -0.41620 90  ASP B CB  
3428 C CG  . ASP B 90  ? 2.39600 2.41928 2.47295 0.01444  -0.41171 -0.41945 90  ASP B CG  
3429 O OD1 . ASP B 90  ? 2.58361 2.56732 2.59496 0.02546  -0.41163 -0.41357 90  ASP B OD1 
3430 O OD2 . ASP B 90  ? 2.37426 2.41090 2.46840 0.01452  -0.41157 -0.42717 90  ASP B OD2 
3431 N N   . THR B 91  ? 2.45345 2.52392 2.60511 -0.01967 -0.36646 -0.39666 91  THR B N   
3432 C CA  . THR B 91  ? 2.45386 2.52434 2.63254 -0.02904 -0.36202 -0.39375 91  THR B CA  
3433 C C   . THR B 91  ? 2.37140 2.46786 2.57558 -0.04285 -0.34298 -0.39650 91  THR B C   
3434 O O   . THR B 91  ? 2.40697 2.51348 2.60006 -0.05328 -0.32826 -0.39095 91  THR B O   
3435 C CB  . THR B 91  ? 2.53587 2.58382 2.68126 -0.02947 -0.35590 -0.38324 91  THR B CB  
3436 O OG1 . THR B 91  ? 2.65217 2.66702 2.75673 -0.01402 -0.37408 -0.38072 91  THR B OG1 
3437 C CG2 . THR B 91  ? 2.53871 2.57635 2.70573 -0.03596 -0.35390 -0.38025 91  THR B CG2 
3438 N N   . ALA B 92  ? 2.37440 2.47788 2.61291 -0.04277 -0.34415 -0.40363 92  ALA B N   
3439 C CA  . ALA B 92  ? 2.38720 2.50391 2.63695 -0.05278 -0.32881 -0.40759 92  ALA B CA  
3440 C C   . ALA B 92  ? 2.38422 2.49074 2.66644 -0.04809 -0.32513 -0.41176 92  ALA B C   
3441 O O   . ALA B 92  ? 2.41478 2.51492 2.72444 -0.03799 -0.33561 -0.41031 92  ALA B O   
3442 C CB  . ALA B 92  ? 2.38406 2.52708 2.62828 -0.05255 -0.32547 -0.41090 92  ALA B CB  
3443 N N   . THR B 93  ? 2.35991 2.46113 2.63890 -0.05493 -0.31025 -0.41505 93  THR B N   
3444 C CA  . THR B 93  ? 2.35674 2.44157 2.65856 -0.04755 -0.29755 -0.41754 93  THR B CA  
3445 C C   . THR B 93  ? 2.32695 2.43065 2.63799 -0.04311 -0.29509 -0.42489 93  THR B C   
3446 O O   . THR B 93  ? 2.31987 2.43733 2.60714 -0.05047 -0.29509 -0.42844 93  THR B O   
3447 C CB  . THR B 93  ? 2.40184 2.45048 2.67627 -0.05478 -0.28095 -0.41674 93  THR B CB  
3448 O OG1 . THR B 93  ? 2.46711 2.49513 2.73166 -0.05831 -0.28140 -0.40951 93  THR B OG1 
3449 C CG2 . THR B 93  ? 2.43690 2.45806 2.72663 -0.04236 -0.26002 -0.41695 93  THR B CG2 
3450 N N   . TYR B 94  ? 2.23740 2.34247 2.58810 -0.03123 -0.29335 -0.42525 94  TYR B N   
3451 C CA  . TYR B 94  ? 2.16777 2.28985 2.53114 -0.02568 -0.29224 -0.43170 94  TYR B CA  
3452 C C   . TYR B 94  ? 2.19873 2.29943 2.57148 -0.01876 -0.26714 -0.43265 94  TYR B C   
3453 O O   . TYR B 94  ? 2.31274 2.39037 2.71356 -0.01105 -0.25243 -0.42548 94  TYR B O   
3454 C CB  . TYR B 94  ? 2.15226 2.28697 2.55306 -0.01870 -0.31145 -0.43099 94  TYR B CB  
3455 C CG  . TYR B 94  ? 2.14772 2.29134 2.51985 -0.02160 -0.33475 -0.43158 94  TYR B CG  
3456 C CD1 . TYR B 94  ? 2.19788 2.33096 2.55420 -0.02472 -0.34417 -0.42534 94  TYR B CD1 
3457 C CD2 . TYR B 94  ? 2.16831 2.32317 2.52252 -0.01876 -0.34377 -0.43734 94  TYR B CD2 
3458 C CE1 . TYR B 94  ? 2.25584 2.38698 2.57694 -0.02405 -0.36075 -0.42447 94  TYR B CE1 
3459 C CE2 . TYR B 94  ? 2.20119 2.35154 2.51787 -0.01747 -0.35943 -0.43628 94  TYR B CE2 
3460 C CZ  . TYR B 94  ? 2.24391 2.38120 2.54303 -0.01966 -0.36731 -0.42966 94  TYR B CZ  
3461 O OH  . TYR B 94  ? 2.31053 2.43385 2.56374 -0.01524 -0.37846 -0.42727 94  TYR B OH  
3462 N N   . TYR B 95  ? 2.05716 2.16216 2.40527 -0.01917 -0.26007 -0.43950 95  TYR B N   
3463 C CA  . TYR B 95  ? 2.10977 2.18558 2.44951 -0.01072 -0.23523 -0.44113 95  TYR B CA  
3464 C C   . TYR B 95  ? 2.08003 2.17332 2.44292 -0.00169 -0.23108 -0.44549 95  TYR B C   
3465 O O   . TYR B 95  ? 2.04183 2.16661 2.40067 -0.00512 -0.24742 -0.45008 95  TYR B O   
3466 C CB  . TYR B 95  ? 2.12603 2.17970 2.40428 -0.01934 -0.23318 -0.44522 95  TYR B CB  
3467 C CG  . TYR B 95  ? 2.20884 2.23895 2.45671 -0.03142 -0.23869 -0.44183 95  TYR B CG  
3468 C CD1 . TYR B 95  ? 2.18323 2.24263 2.43216 -0.04468 -0.25950 -0.43936 95  TYR B CD1 
3469 C CD2 . TYR B 95  ? 2.29694 2.26790 2.50844 -0.02852 -0.22045 -0.44042 95  TYR B CD2 
3470 C CE1 . TYR B 95  ? 2.21217 2.24843 2.43502 -0.05671 -0.26351 -0.43573 95  TYR B CE1 
3471 C CE2 . TYR B 95  ? 2.34034 2.28311 2.51877 -0.04053 -0.22597 -0.43788 95  TYR B CE2 
3472 C CZ  . TYR B 95  ? 2.30698 2.28552 2.49497 -0.05571 -0.24839 -0.43568 95  TYR B CZ  
3473 O OH  . TYR B 95  ? 2.37984 2.32892 2.53697 -0.06858 -0.25287 -0.43259 95  TYR B OH  
3474 N N   . CYS B 96  ? 1.99943 2.06764 2.38464 0.01135  -0.20546 -0.44256 96  CYS B N   
3475 C CA  . CYS B 96  ? 1.98876 2.06409 2.38965 0.02052  -0.19525 -0.44635 96  CYS B CA  
3476 C C   . CYS B 96  ? 2.05839 2.09764 2.40509 0.02747  -0.17284 -0.45012 96  CYS B C   
3477 O O   . CYS B 96  ? 2.19456 2.18719 2.50915 0.03156  -0.15443 -0.44665 96  CYS B O   
3478 C CB  . CYS B 96  ? 1.98710 2.06053 2.46230 0.03096  -0.18192 -0.43763 96  CYS B CB  
3479 S SG  . CYS B 96  ? 2.14056 2.16799 2.64386 0.04435  -0.14453 -0.42189 96  CYS B SG  
3480 N N   . THR B 97  ? 1.81386 1.86798 2.14293 0.02992  -0.17532 -0.45689 97  THR B N   
3481 C CA  . THR B 97  ? 1.90805 1.92823 2.17923 0.03662  -0.16135 -0.46079 97  THR B CA  
3482 C C   . THR B 97  ? 1.89856 1.91649 2.18508 0.05152  -0.14167 -0.46251 97  THR B C   
3483 O O   . THR B 97  ? 1.85396 1.90834 2.18583 0.05132  -0.14921 -0.46361 97  THR B O   
3484 C CB  . THR B 97  ? 1.96192 2.00360 2.18727 0.02350  -0.18840 -0.46531 97  THR B CB  
3485 O OG1 . THR B 97  ? 1.91020 1.99650 2.15274 0.02483  -0.19833 -0.46792 97  THR B OG1 
3486 C CG2 . THR B 97  ? 1.91548 1.97496 2.14203 0.00632  -0.21085 -0.46248 97  THR B CG2 
3487 N N   . ARG B 98  ? 1.86106 1.82793 2.10184 0.06491  -0.11665 -0.46281 98  ARG B N   
3488 C CA  . ARG B 98  ? 1.88532 1.84406 2.12051 0.07949  -0.09831 -0.46520 98  ARG B CA  
3489 C C   . ARG B 98  ? 1.92970 1.89775 2.10567 0.07536  -0.11973 -0.47184 98  ARG B C   
3490 O O   . ARG B 98  ? 2.00582 1.94560 2.12359 0.06934  -0.13255 -0.47301 98  ARG B O   
3491 C CB  . ARG B 98  ? 1.95927 1.84875 2.17506 0.10067  -0.05400 -0.45928 98  ARG B CB  
3492 C CG  . ARG B 98  ? 2.00025 1.87924 2.21878 0.11751  -0.02956 -0.45995 98  ARG B CG  
3493 C CD  . ARG B 98  ? 2.10337 1.90304 2.29013 0.14185  0.01992  -0.45224 98  ARG B CD  
3494 N NE  . ARG B 98  ? 2.21653 1.95407 2.29386 0.14972  0.01963  -0.45796 98  ARG B NE  
3495 C CZ  . ARG B 98  ? 2.30291 1.96185 2.32174 0.17422  0.05889  -0.45441 98  ARG B CZ  
3496 N NH1 . ARG B 98  ? 2.35219 1.98863 2.41861 0.19418  0.10778  -0.44339 98  ARG B NH1 
3497 N NH2 . ARG B 98  ? 2.40025 1.99793 2.30996 0.17901  0.04798  -0.46074 98  ARG B NH2 
3498 N N   . ASP B 99  ? 2.02007 2.02622 2.21292 0.07803  -0.12564 -0.47474 99  ASP B N   
3499 C CA  . ASP B 99  ? 2.03547 2.05967 2.18686 0.07603  -0.14517 -0.47707 99  ASP B CA  
3500 C C   . ASP B 99  ? 2.09232 2.09447 2.22120 0.09512  -0.12389 -0.47885 99  ASP B C   
3501 O O   . ASP B 99  ? 2.05927 2.05399 2.22219 0.10655  -0.09795 -0.47890 99  ASP B O   
3502 C CB  . ASP B 99  ? 1.95912 2.04919 2.14243 0.06429  -0.17050 -0.47608 99  ASP B CB  
3503 C CG  . ASP B 99  ? 1.92527 2.03792 2.16301 0.05778  -0.17291 -0.47597 99  ASP B CG  
3504 O OD1 . ASP B 99  ? 1.94297 2.03854 2.19511 0.05201  -0.17144 -0.47411 99  ASP B OD1 
3505 O OD2 . ASP B 99  ? 1.86844 2.01084 2.13004 0.05918  -0.17769 -0.47721 99  ASP B OD2 
3506 N N   . LEU B 100 ? 2.07539 2.06638 2.14923 0.09783  -0.13716 -0.47898 100 LEU B N   
3507 C CA  . LEU B 100 ? 2.12135 2.10161 2.16994 0.11536  -0.12450 -0.47971 100 LEU B CA  
3508 C C   . LEU B 100 ? 2.09186 2.13871 2.16459 0.11003  -0.14617 -0.47681 100 LEU B C   
3509 O O   . LEU B 100 ? 2.09324 2.16783 2.15571 0.09835  -0.17608 -0.47168 100 LEU B O   
3510 C CB  . LEU B 100 ? 2.21869 2.13656 2.18566 0.12431  -0.12782 -0.47989 100 LEU B CB  
3511 C CG  . LEU B 100 ? 2.29741 2.13266 2.21844 0.13197  -0.10503 -0.48115 100 LEU B CG  
3512 C CD1 . LEU B 100 ? 2.42239 2.18358 2.24475 0.14355  -0.11151 -0.48234 100 LEU B CD1 
3513 C CD2 . LEU B 100 ? 2.30139 2.11367 2.26097 0.14879  -0.05692 -0.47955 100 LEU B CD2 
3514 N N   . ARG B 101 ? 2.13742 2.20675 2.24401 0.11875  -0.12986 -0.47826 101 ARG B N   
3515 C CA  . ARG B 101 ? 2.08198 2.20444 2.20425 0.11801  -0.14315 -0.47413 101 ARG B CA  
3516 C C   . ARG B 101 ? 2.16293 2.28846 2.24705 0.12835  -0.15123 -0.46799 101 ARG B C   
3517 O O   . ARG B 101 ? 2.18003 2.35265 2.27701 0.12593  -0.16696 -0.45912 101 ARG B O   
3518 C CB  . ARG B 101 ? 2.04475 2.17502 2.19912 0.12573  -0.12417 -0.47818 101 ARG B CB  
3519 C CG  . ARG B 101 ? 2.02503 2.19796 2.18685 0.12776  -0.13230 -0.47372 101 ARG B CG  
3520 C CD  . ARG B 101 ? 2.01239 2.21857 2.19705 0.11223  -0.15251 -0.47059 101 ARG B CD  
3521 N NE  . ARG B 101 ? 2.04443 2.27241 2.22281 0.10108  -0.17322 -0.46223 101 ARG B NE  
3522 C CZ  . ARG B 101 ? 2.01497 2.23957 2.20291 0.08527  -0.18660 -0.46326 101 ARG B CZ  
3523 N NH1 . ARG B 101 ? 1.95163 2.15571 2.15891 0.08001  -0.18168 -0.47082 101 ARG B NH1 
3524 N NH2 . ARG B 101 ? 1.99781 2.24020 2.18006 0.07408  -0.20640 -0.45488 101 ARG B NH2 
3525 N N   . MET B 102 ? 2.06206 2.13519 2.09895 0.14140  -0.14024 -0.47039 102 MET B N   
3526 C CA  . MET B 102 ? 2.12991 2.20107 2.12700 0.15168  -0.15375 -0.46378 102 MET B CA  
3527 C C   . MET B 102 ? 2.23160 2.31483 2.21425 0.13481  -0.19447 -0.45640 102 MET B C   
3528 O O   . MET B 102 ? 2.26087 2.38227 2.25006 0.13441  -0.21769 -0.44470 102 MET B O   
3529 C CB  . MET B 102 ? 2.22152 2.22159 2.16147 0.17295  -0.12967 -0.46860 102 MET B CB  
3530 C CG  . MET B 102 ? 2.25834 2.25157 2.21574 0.19097  -0.09109 -0.47222 102 MET B CG  
3531 S SD  . MET B 102 ? 2.20557 2.26800 2.19872 0.19545  -0.09594 -0.46540 102 MET B SD  
3532 C CE  . MET B 102 ? 2.30399 2.37023 2.25032 0.20547  -0.12303 -0.45358 102 MET B CE  
3533 N N   . SER B 103 ? 2.17511 2.22581 2.14234 0.12060  -0.20375 -0.46117 103 SER B N   
3534 C CA  . SER B 103 ? 2.19864 2.25195 2.15036 0.10129  -0.24453 -0.45509 103 SER B CA  
3535 C C   . SER B 103 ? 2.11720 2.22968 2.12794 0.07918  -0.25979 -0.44957 103 SER B C   
3536 O O   . SER B 103 ? 2.20010 2.32049 2.20968 0.06014  -0.29327 -0.44294 103 SER B O   
3537 C CB  . SER B 103 ? 2.26832 2.23441 2.14982 0.10034  -0.24607 -0.46325 103 SER B CB  
3538 O OG  . SER B 103 ? 2.56367 2.46416 2.37861 0.12331  -0.23070 -0.46691 103 SER B OG  
3539 N N   . ASP B 104 ? 2.11577 2.26378 2.17419 0.08114  -0.23755 -0.45174 104 ASP B N   
3540 C CA  . ASP B 104 ? 2.06122 2.26038 2.16863 0.06473  -0.24785 -0.44579 104 ASP B CA  
3541 C C   . ASP B 104 ? 2.07378 2.25193 2.17256 0.04429  -0.26622 -0.44743 104 ASP B C   
3542 O O   . ASP B 104 ? 2.06410 2.27648 2.18587 0.02709  -0.28994 -0.43735 104 ASP B O   
3543 C CB  . ASP B 104 ? 2.07150 2.33201 2.21066 0.06322  -0.26334 -0.42880 104 ASP B CB  
3544 C CG  . ASP B 104 ? 2.13569 2.41082 2.27516 0.08542  -0.24484 -0.42547 104 ASP B CG  
3545 O OD1 . ASP B 104 ? 2.17363 2.40636 2.27953 0.10024  -0.22749 -0.43596 104 ASP B OD1 
3546 O OD2 . ASP B 104 ? 2.15175 2.47705 2.32397 0.08962  -0.24403 -0.41091 104 ASP B OD2 
3547 N N   . TYR B 105 ? 2.05974 2.17837 2.12668 0.04724  -0.25184 -0.45839 105 TYR B N   
3548 C CA  . TYR B 105 ? 2.06210 2.14864 2.11006 0.03056  -0.26561 -0.46016 105 TYR B CA  
3549 C C   . TYR B 105 ? 2.05879 2.09973 2.10206 0.03832  -0.23575 -0.46878 105 TYR B C   
3550 O O   . TYR B 105 ? 2.10534 2.13105 2.15503 0.05621  -0.20653 -0.47291 105 TYR B O   
3551 C CB  . TYR B 105 ? 2.13351 2.17248 2.12012 0.02452  -0.29238 -0.45896 105 TYR B CB  
3552 C CG  . TYR B 105 ? 2.24927 2.19655 2.16353 0.03939  -0.27312 -0.46845 105 TYR B CG  
3553 C CD1 . TYR B 105 ? 2.31770 2.23695 2.20530 0.06351  -0.24887 -0.47174 105 TYR B CD1 
3554 C CD2 . TYR B 105 ? 2.29989 2.18178 2.16726 0.03128  -0.27559 -0.47268 105 TYR B CD2 
3555 C CE1 . TYR B 105 ? 2.42997 2.25793 2.24715 0.08048  -0.22499 -0.47791 105 TYR B CE1 
3556 C CE2 . TYR B 105 ? 2.39514 2.18270 2.18813 0.04881  -0.25163 -0.47896 105 TYR B CE2 
3557 C CZ  . TYR B 105 ? 2.47199 2.23247 2.24043 0.07403  -0.22517 -0.48099 105 TYR B CZ  
3558 O OH  . TYR B 105 ? 2.72798 2.38734 2.41846 0.09479  -0.19503 -0.48490 105 TYR B OH  
3559 N N   . PHE B 106 ? 2.15006 2.16959 2.18733 0.02468  -0.24253 -0.46923 106 PHE B N   
3560 C CA  . PHE B 106 ? 2.15525 2.13569 2.19770 0.03114  -0.21526 -0.47290 106 PHE B CA  
3561 C C   . PHE B 106 ? 2.25950 2.15184 2.22681 0.03630  -0.20769 -0.47567 106 PHE B C   
3562 O O   . PHE B 106 ? 2.29091 2.15811 2.21865 0.02043  -0.23313 -0.47526 106 PHE B O   
3563 C CB  . PHE B 106 ? 2.08272 2.09635 2.16814 0.01540  -0.22484 -0.46997 106 PHE B CB  
3564 C CG  . PHE B 106 ? 1.99849 2.08499 2.13838 0.01025  -0.23565 -0.46657 106 PHE B CG  
3565 C CD1 . PHE B 106 ? 1.97903 2.09156 2.14170 0.02348  -0.22424 -0.46796 106 PHE B CD1 
3566 C CD2 . PHE B 106 ? 1.95040 2.07073 2.11142 -0.00642 -0.25476 -0.46137 106 PHE B CD2 
3567 C CE1 . PHE B 106 ? 1.92328 2.08822 2.12110 0.02107  -0.23218 -0.46477 106 PHE B CE1 
3568 C CE2 . PHE B 106 ? 1.89248 2.06641 2.09051 -0.00749 -0.26026 -0.45705 106 PHE B CE2 
3569 C CZ  . PHE B 106 ? 1.88351 2.07678 2.09612 0.00671  -0.24919 -0.45901 106 PHE B CZ  
3570 N N   . ASP B 107 ? 2.22694 2.06571 2.17115 0.05895  -0.17147 -0.47753 107 ASP B N   
3571 C CA  . ASP B 107 ? 2.35424 2.09330 2.21376 0.06918  -0.15668 -0.47905 107 ASP B CA  
3572 C C   . ASP B 107 ? 2.33420 2.03822 2.20016 0.06800  -0.13679 -0.47577 107 ASP B C   
3573 O O   . ASP B 107 ? 2.45556 2.10506 2.26045 0.05851  -0.15054 -0.47698 107 ASP B O   
3574 C CB  . ASP B 107 ? 2.41479 2.10129 2.24087 0.09762  -0.11913 -0.47944 107 ASP B CB  
3575 C CG  . ASP B 107 ? 2.36741 2.09794 2.27851 0.11017  -0.08478 -0.47569 107 ASP B CG  
3576 O OD1 . ASP B 107 ? 2.29111 2.07179 2.27634 0.09984  -0.08562 -0.47256 107 ASP B OD1 
3577 O OD2 . ASP B 107 ? 2.40629 2.11792 2.30877 0.12988  -0.05928 -0.47546 107 ASP B OD2 
3578 N N   . TYR B 108 ? 2.23379 1.96709 2.17469 0.07683  -0.10702 -0.47049 108 TYR B N   
3579 C CA  . TYR B 108 ? 2.27764 1.98281 2.23761 0.07925  -0.08472 -0.46371 108 TYR B CA  
3580 C C   . TYR B 108 ? 2.16597 1.95207 2.20968 0.06150  -0.10595 -0.46126 108 TYR B C   
3581 O O   . TYR B 108 ? 2.10098 1.95797 2.20293 0.05618  -0.12050 -0.46286 108 TYR B O   
3582 C CB  . TYR B 108 ? 2.26755 1.92961 2.25059 0.10697  -0.02977 -0.45454 108 TYR B CB  
3583 C CG  . TYR B 108 ? 2.43095 2.00000 2.32182 0.12949  -0.00120 -0.45549 108 TYR B CG  
3584 C CD1 . TYR B 108 ? 2.60507 2.07050 2.40168 0.13954  0.01684  -0.45361 108 TYR B CD1 
3585 C CD2 . TYR B 108 ? 2.44579 2.02171 2.33428 0.14220  0.00830  -0.45821 108 TYR B CD2 
3586 C CE1 . TYR B 108 ? 2.83338 2.19967 2.53005 0.16259  0.04274  -0.45455 108 TYR B CE1 
3587 C CE2 . TYR B 108 ? 2.69918 2.18307 2.49506 0.16501  0.03467  -0.45868 108 TYR B CE2 
3588 C CZ  . TYR B 108 ? 2.85029 2.22718 2.54758 0.17559  0.05136  -0.45693 108 TYR B CZ  
3589 O OH  . TYR B 108 ? 2.96441 2.23627 2.55485 0.20073  0.07758  -0.45743 108 TYR B OH  
3590 N N   . TRP B 109 ? 2.31244 2.07886 2.35278 0.05392  -0.10691 -0.45718 109 TRP B N   
3591 C CA  . TRP B 109 ? 2.23139 2.06015 2.33600 0.03834  -0.12747 -0.45420 109 TRP B CA  
3592 C C   . TRP B 109 ? 2.25576 2.06097 2.40062 0.04963  -0.09799 -0.44289 109 TRP B C   
3593 O O   . TRP B 109 ? 2.31472 2.05057 2.43050 0.06845  -0.05994 -0.43635 109 TRP B O   
3594 C CB  . TRP B 109 ? 2.25144 2.08826 2.31741 0.01450  -0.16415 -0.45826 109 TRP B CB  
3595 C CG  . TRP B 109 ? 2.21098 2.08683 2.26077 0.00163  -0.19628 -0.46405 109 TRP B CG  
3596 C CD1 . TRP B 109 ? 2.26308 2.11334 2.26428 0.00740  -0.19928 -0.46848 109 TRP B CD1 
3597 C CD2 . TRP B 109 ? 2.09910 2.04373 2.18256 -0.01706 -0.22781 -0.46295 109 TRP B CD2 
3598 N NE1 . TRP B 109 ? 2.20869 2.11422 2.22052 -0.00710 -0.23217 -0.46896 109 TRP B NE1 
3599 C CE2 . TRP B 109 ? 2.10951 2.07268 2.17227 -0.02162 -0.24717 -0.46485 109 TRP B CE2 
3600 C CE3 . TRP B 109 ? 2.03700 2.02543 2.16438 -0.02817 -0.23933 -0.45873 109 TRP B CE3 
3601 C CZ2 . TRP B 109 ? 2.04059 2.06723 2.13275 -0.03617 -0.27327 -0.46037 109 TRP B CZ2 
3602 C CZ3 . TRP B 109 ? 2.00355 2.04796 2.14975 -0.04193 -0.26404 -0.45601 109 TRP B CZ3 
3603 C CH2 . TRP B 109 ? 2.00438 2.06895 2.13679 -0.04549 -0.27869 -0.45575 109 TRP B CH2 
3604 N N   . GLY B 110 ? 2.28623 2.14604 2.49705 0.03993  -0.11468 -0.43861 110 GLY B N   
3605 C CA  . GLY B 110 ? 2.24588 2.09564 2.50842 0.04903  -0.09419 -0.42533 110 GLY B CA  
3606 C C   . GLY B 110 ? 2.26633 2.10365 2.50386 0.03648  -0.10836 -0.42348 110 GLY B C   
3607 O O   . GLY B 110 ? 2.28666 2.13251 2.47801 0.01779  -0.13740 -0.43232 110 GLY B O   
3608 N N   . GLN B 111 ? 2.28907 2.10694 2.56498 0.04769  -0.08573 -0.40934 111 GLN B N   
3609 C CA  . GLN B 111 ? 2.31925 2.11725 2.57194 0.03939  -0.09265 -0.40547 111 GLN B CA  
3610 C C   . GLN B 111 ? 2.23280 2.09119 2.49745 0.01667  -0.13732 -0.41261 111 GLN B C   
3611 O O   . GLN B 111 ? 2.28112 2.12439 2.49014 0.00062  -0.15418 -0.41847 111 GLN B O   
3612 C CB  . GLN B 111 ? 2.37373 2.15955 2.68999 0.05707  -0.06384 -0.38567 111 GLN B CB  
3613 C CG  . GLN B 111 ? 2.44845 2.15728 2.74238 0.08283  -0.00914 -0.37332 111 GLN B CG  
3614 C CD  . GLN B 111 ? 2.51831 2.22423 2.89187 0.10138  0.02057  -0.34868 111 GLN B CD  
3615 O OE1 . GLN B 111 ? 2.45499 2.22691 2.92015 0.09634  -0.00291 -0.34075 111 GLN B OE1 
3616 N NE2 . GLN B 111 ? 2.63162 2.25595 2.96788 0.12416  0.07188  -0.33489 111 GLN B NE2 
3617 N N   . GLY B 112 ? 2.36612 2.28705 2.70051 0.01543  -0.15632 -0.41112 112 GLY B N   
3618 C CA  . GLY B 112 ? 2.25050 2.21871 2.59110 -0.00104 -0.19300 -0.41559 112 GLY B CA  
3619 C C   . GLY B 112 ? 2.28584 2.25804 2.66037 -0.00008 -0.19950 -0.40469 112 GLY B C   
3620 O O   . GLY B 112 ? 2.37588 2.31239 2.71555 -0.00291 -0.19100 -0.40081 112 GLY B O   
3621 N N   . VAL B 113 ? 2.46113 2.47157 2.90014 0.00386  -0.21689 -0.39940 113 VAL B N   
3622 C CA  . VAL B 113 ? 2.48984 2.50612 2.96477 0.00594  -0.22968 -0.38789 113 VAL B CA  
3623 C C   . VAL B 113 ? 2.46764 2.50685 2.90986 -0.00784 -0.26265 -0.39472 113 VAL B C   
3624 O O   . VAL B 113 ? 2.43361 2.49785 2.85651 -0.01509 -0.27935 -0.40495 113 VAL B O   
3625 C CB  . VAL B 113 ? 1.95142 1.98970 2.51683 0.01750  -0.23580 -0.37575 113 VAL B CB  
3626 C CG1 . VAL B 113 ? 1.96797 1.97913 2.57294 0.03423  -0.19366 -0.36307 113 VAL B CG1 
3627 C CG2 . VAL B 113 ? 1.92121 1.99523 2.50353 0.01208  -0.26290 -0.38573 113 VAL B CG2 
3628 N N   . MET B 114 ? 2.46373 2.49000 2.89741 -0.00925 -0.26788 -0.38718 114 MET B N   
3629 C CA  . MET B 114 ? 2.45156 2.48886 2.84799 -0.01996 -0.29149 -0.39071 114 MET B CA  
3630 C C   . MET B 114 ? 2.44439 2.50275 2.87342 -0.01468 -0.32324 -0.38695 114 MET B C   
3631 O O   . MET B 114 ? 2.50874 2.56884 2.99618 -0.00453 -0.33030 -0.37679 114 MET B O   
3632 C CB  . MET B 114 ? 2.55376 2.55929 2.91749 -0.02396 -0.28060 -0.38442 114 MET B CB  
3633 C CG  . MET B 114 ? 2.59517 2.60681 2.92413 -0.03304 -0.29948 -0.38455 114 MET B CG  
3634 S SD  . MET B 114 ? 2.60059 2.63719 2.88801 -0.04808 -0.30723 -0.39538 114 MET B SD  
3635 C CE  . MET B 114 ? 2.65107 2.68494 2.90848 -0.05129 -0.32074 -0.38864 114 MET B CE  
3636 N N   . VAL B 115 ? 2.46741 2.53739 2.85740 -0.02101 -0.34291 -0.39354 115 VAL B N   
3637 C CA  . VAL B 115 ? 2.48256 2.55710 2.87743 -0.01585 -0.37613 -0.39218 115 VAL B CA  
3638 C C   . VAL B 115 ? 2.56040 2.62050 2.89959 -0.01874 -0.38351 -0.38998 115 VAL B C   
3639 O O   . VAL B 115 ? 2.55600 2.62008 2.85197 -0.02669 -0.37073 -0.39420 115 VAL B O   
3640 C CB  . VAL B 115 ? 2.42006 2.51071 2.81177 -0.01562 -0.38899 -0.40205 115 VAL B CB  
3641 C CG1 . VAL B 115 ? 2.44283 2.52097 2.80941 -0.01101 -0.42426 -0.40237 115 VAL B CG1 
3642 C CG2 . VAL B 115 ? 2.36388 2.46595 2.81865 -0.01145 -0.38412 -0.40187 115 VAL B CG2 
3643 N N   . THR B 116 ? 2.48442 2.52743 2.82844 -0.01161 -0.40372 -0.38124 116 THR B N   
3644 C CA  . THR B 116 ? 2.52021 2.54156 2.80955 -0.01108 -0.40908 -0.37711 116 THR B CA  
3645 C C   . THR B 116 ? 2.55765 2.56242 2.81780 -0.00215 -0.44414 -0.37821 116 THR B C   
3646 O O   . THR B 116 ? 2.63370 2.63193 2.92834 0.00488  -0.47532 -0.37435 116 THR B O   
3647 C CB  . THR B 116 ? 2.56985 2.57264 2.87243 -0.00765 -0.40352 -0.36536 116 THR B CB  
3648 O OG1 . THR B 116 ? 2.56113 2.56530 2.87732 -0.01492 -0.37053 -0.36508 116 THR B OG1 
3649 C CG2 . THR B 116 ? 2.62069 2.59775 2.86347 -0.00664 -0.40565 -0.36065 116 THR B CG2 
3650 N N   . VAL B 117 ? 2.48108 2.47426 2.67734 -0.00184 -0.43942 -0.38170 117 VAL B N   
3651 C CA  . VAL B 117 ? 2.57058 2.53135 2.71499 0.00913  -0.46789 -0.38327 117 VAL B CA  
3652 C C   . VAL B 117 ? 2.68326 2.60932 2.76203 0.01529  -0.45969 -0.37509 117 VAL B C   
3653 O O   . VAL B 117 ? 2.69340 2.61960 2.73263 0.01355  -0.43128 -0.37337 117 VAL B O   
3654 C CB  . VAL B 117 ? 2.53799 2.50536 2.65715 0.00963  -0.46316 -0.39254 117 VAL B CB  
3655 C CG1 . VAL B 117 ? 2.63604 2.55801 2.70376 0.02183  -0.49995 -0.39577 117 VAL B CG1 
3656 C CG2 . VAL B 117 ? 2.43620 2.44404 2.62001 0.00124  -0.45504 -0.39967 117 VAL B CG2 
3657 N N   . SER B 118 ? 2.60572 2.50180 2.67675 0.02344  -0.48354 -0.36770 118 SER B N   
3658 C CA  . SER B 118 ? 2.67422 2.52959 2.67906 0.03193  -0.47644 -0.35893 118 SER B CA  
3659 C C   . SER B 118 ? 2.73276 2.53944 2.70538 0.04694  -0.52233 -0.35487 118 SER B C   
3660 O O   . SER B 118 ? 2.71957 2.53651 2.75001 0.04680  -0.55552 -0.35348 118 SER B O   
3661 C CB  . SER B 118 ? 2.68155 2.55071 2.71066 0.02329  -0.44653 -0.35087 118 SER B CB  
3662 O OG  . SER B 118 ? 2.75639 2.58438 2.72287 0.03174  -0.43763 -0.34136 118 SER B OG  
3663 N N   . SER B 119 ? 2.76262 2.51300 2.64327 0.06081  -0.52422 -0.35099 119 SER B N   
3664 C CA  . SER B 119 ? 2.86692 2.55655 2.69608 0.07682  -0.56988 -0.34657 119 SER B CA  
3665 C C   . SER B 119 ? 2.91938 2.59408 2.74845 0.08202  -0.56624 -0.33372 119 SER B C   
3666 O O   . SER B 119 ? 3.03058 2.64335 2.79146 0.09845  -0.59378 -0.32766 119 SER B O   
3667 C CB  . SER B 119 ? 2.97956 2.59872 2.69124 0.09361  -0.57253 -0.34851 119 SER B CB  
3668 O OG  . SER B 119 ? 3.03684 2.63974 2.69618 0.09925  -0.52238 -0.33962 119 SER B OG  
3669 N N   . ALA B 120 ? 2.85070 2.57305 2.74676 0.06949  -0.53365 -0.32944 120 ALA B N   
3670 C CA  . ALA B 120 ? 2.90729 2.61303 2.79764 0.07391  -0.52108 -0.31708 120 ALA B CA  
3671 C C   . ALA B 120 ? 2.93183 2.63601 2.87395 0.08112  -0.56239 -0.30869 120 ALA B C   
3672 O O   . ALA B 120 ? 2.86190 2.60608 2.88735 0.07464  -0.58022 -0.31020 120 ALA B O   
3673 C CB  . ALA B 120 ? 2.83916 2.58595 2.77196 0.05698  -0.47094 -0.31589 120 ALA B CB  
3674 N N   . GLU B 121 ? 2.95361 2.61099 2.84970 0.09581  -0.57570 -0.29734 121 GLU B N   
3675 C CA  . GLU B 121 ? 2.99069 2.64547 2.93744 0.10491  -0.61270 -0.28444 121 GLU B CA  
3676 C C   . GLU B 121 ? 3.01780 2.68948 3.00240 0.10265  -0.57296 -0.27316 121 GLU B C   
3677 O O   . GLU B 121 ? 3.04871 2.70378 2.98230 0.09967  -0.53059 -0.27301 121 GLU B O   
3678 C CB  . GLU B 121 ? 3.08412 2.66787 2.94956 0.12512  -0.66058 -0.27813 121 GLU B CB  
3679 C CG  . GLU B 121 ? 3.07823 2.62925 2.89857 0.12882  -0.71036 -0.28857 121 GLU B CG  
3680 C CD  . GLU B 121 ? 3.09404 2.60321 2.80564 0.13249  -0.68152 -0.29954 121 GLU B CD  
3681 O OE1 . GLU B 121 ? 3.12249 2.62120 2.78979 0.13460  -0.62937 -0.29570 121 GLU B OE1 
3682 O OE2 . GLU B 121 ? 3.08501 2.56959 2.75771 0.13371  -0.70957 -0.31020 121 GLU B OE2 
3683 N N   . THR B 122 ? 2.77807 2.47959 2.85396 0.10446  -0.58548 -0.26192 122 THR B N   
3684 C CA  . THR B 122 ? 2.80925 2.52334 2.92479 0.10356  -0.54491 -0.25076 122 THR B CA  
3685 C C   . THR B 122 ? 2.91742 2.58111 2.97295 0.11894  -0.54530 -0.23785 122 THR B C   
3686 O O   . THR B 122 ? 2.97801 2.62275 3.04699 0.13566  -0.58697 -0.22378 122 THR B O   
3687 C CB  . THR B 122 ? 2.78650 2.54054 3.01650 0.10633  -0.55508 -0.23834 122 THR B CB  
3688 O OG1 . THR B 122 ? 2.82931 2.57070 3.08798 0.12222  -0.61178 -0.22319 122 THR B OG1 
3689 C CG2 . THR B 122 ? 2.67112 2.46978 2.95647 0.09270  -0.55402 -0.25057 122 THR B CG2 
3690 N N   . THR B 123 ? 2.91980 2.56111 2.91261 0.11300  -0.50034 -0.24106 123 THR B N   
3691 C CA  . THR B 123 ? 3.02613 2.61454 2.95209 0.12704  -0.49356 -0.22960 123 THR B CA  
3692 C C   . THR B 123 ? 3.05770 2.64484 2.98853 0.11767  -0.43933 -0.22489 123 THR B C   
3693 O O   . THR B 123 ? 2.99633 2.61404 2.95688 0.09789  -0.40578 -0.23394 123 THR B O   
3694 C CB  . THR B 123 ? 3.05681 2.59806 2.87725 0.13234  -0.49498 -0.23595 123 THR B CB  
3695 O OG1 . THR B 123 ? 2.99267 2.55665 2.80156 0.11281  -0.45580 -0.24866 123 THR B OG1 
3696 C CG2 . THR B 123 ? 3.05457 2.57345 2.84730 0.14559  -0.55397 -0.23934 123 THR B CG2 
3697 N N   . ALA B 124 ? 3.07320 2.61742 2.96717 0.13225  -0.43335 -0.21067 124 ALA B N   
3698 C CA  . ALA B 124 ? 3.11627 2.64683 3.00938 0.12601  -0.38637 -0.20386 124 ALA B CA  
3699 C C   . ALA B 124 ? 3.12998 2.63645 2.95412 0.11064  -0.34767 -0.21097 124 ALA B C   
3700 O O   . ALA B 124 ? 3.12658 2.61961 2.89774 0.11179  -0.35464 -0.21647 124 ALA B O   
3701 C CB  . ALA B 124 ? 3.21474 2.70947 3.10286 0.15017  -0.39753 -0.18343 124 ALA B CB  
3702 N N   . PRO B 125 ? 3.18915 2.68587 3.01341 0.09578  -0.30467 -0.20934 125 PRO B N   
3703 C CA  . PRO B 125 ? 3.13579 2.61443 2.91045 0.07719  -0.26966 -0.21342 125 PRO B CA  
3704 C C   . PRO B 125 ? 3.22220 2.64259 2.93167 0.08932  -0.25186 -0.19977 125 PRO B C   
3705 O O   . PRO B 125 ? 3.30745 2.69763 3.00300 0.11358  -0.26743 -0.18743 125 PRO B O   
3706 C CB  . PRO B 125 ? 2.86083 2.35589 2.67186 0.05125  -0.23975 -0.22008 125 PRO B CB  
3707 C CG  . PRO B 125 ? 2.90605 2.39166 2.75135 0.06613  -0.24190 -0.21093 125 PRO B CG  
3708 C CD  . PRO B 125 ? 3.10681 2.61221 2.98315 0.09128  -0.28544 -0.20542 125 PRO B CD  
3709 N N   . SER B 126 ? 3.12575 2.53069 2.79987 0.07246  -0.21857 -0.19996 126 SER B N   
3710 C CA  . SER B 126 ? 3.24986 2.59817 2.86431 0.07994  -0.19204 -0.18634 126 SER B CA  
3711 C C   . SER B 126 ? 3.23258 2.57693 2.85888 0.04860  -0.15199 -0.18682 126 SER B C   
3712 O O   . SER B 126 ? 3.19608 2.57060 2.84387 0.02292  -0.13973 -0.19390 126 SER B O   
3713 C CB  . SER B 126 ? 3.35378 2.67586 2.90680 0.09380  -0.19009 -0.18141 126 SER B CB  
3714 O OG  . SER B 126 ? 3.29331 2.65259 2.86615 0.07314  -0.17736 -0.18929 126 SER B OG  
3715 N N   . VAL B 127 ? 3.19447 2.49881 2.80667 0.05045  -0.13397 -0.17832 127 VAL B N   
3716 C CA  . VAL B 127 ? 3.18504 2.47467 2.80456 0.01959  -0.10217 -0.17981 127 VAL B CA  
3717 C C   . VAL B 127 ? 3.24849 2.50140 2.82740 0.01030  -0.07056 -0.16859 127 VAL B C   
3718 O O   . VAL B 127 ? 3.31915 2.53520 2.84936 0.03572  -0.06517 -0.15604 127 VAL B O   
3719 C CB  . VAL B 127 ? 3.19482 2.45172 2.81551 0.02704  -0.09506 -0.17570 127 VAL B CB  
3720 C CG1 . VAL B 127 ? 3.16676 2.40503 2.79169 -0.00753 -0.07021 -0.18211 127 VAL B CG1 
3721 C CG2 . VAL B 127 ? 3.14861 2.43879 2.81339 0.04664  -0.12411 -0.17917 127 VAL B CG2 
3722 N N   . TYR B 128 ? 3.20556 2.46540 2.80541 -0.02659 -0.05023 -0.17171 128 TYR B N   
3723 C CA  . TYR B 128 ? 3.25438 2.48379 2.83391 -0.04162 -0.01721 -0.15849 128 TYR B CA  
3724 C C   . TYR B 128 ? 3.23743 2.44392 2.83047 -0.07919 -0.00086 -0.16058 128 TYR B C   
3725 O O   . TYR B 128 ? 3.18857 2.42737 2.82220 -0.10947 -0.01253 -0.17248 128 TYR B O   
3726 C CB  . TYR B 128 ? 3.25473 2.52382 2.85693 -0.05053 -0.01198 -0.15528 128 TYR B CB  
3727 C CG  . TYR B 128 ? 3.28092 2.56022 2.85629 -0.01480 -0.02769 -0.15409 128 TYR B CG  
3728 C CD1 . TYR B 128 ? 3.36023 2.58822 2.87141 0.01652  -0.01304 -0.13910 128 TYR B CD1 
3729 C CD2 . TYR B 128 ? 3.23138 2.56329 2.83797 -0.01227 -0.05785 -0.16802 128 TYR B CD2 
3730 C CE1 . TYR B 128 ? 3.39668 2.61961 2.86881 0.04909  -0.03150 -0.13888 128 TYR B CE1 
3731 C CE2 . TYR B 128 ? 3.25509 2.58698 2.82988 0.01856  -0.07549 -0.16780 128 TYR B CE2 
3732 C CZ  . TYR B 128 ? 3.34396 2.61841 2.84828 0.04892  -0.06388 -0.15362 128 TYR B CZ  
3733 O OH  . TYR B 128 ? 3.37280 2.63335 2.83140 0.07965  -0.08546 -0.15425 128 TYR B OH  
3734 N N   . PRO B 129 ? 3.28355 2.42847 2.83797 -0.07855 0.02396  -0.14954 129 PRO B N   
3735 C CA  . PRO B 129 ? 3.29894 2.41033 2.85744 -0.11674 0.03756  -0.15159 129 PRO B CA  
3736 C C   . PRO B 129 ? 3.30327 2.42909 2.89565 -0.15271 0.05230  -0.14313 129 PRO B C   
3737 O O   . PRO B 129 ? 3.33078 2.46090 2.92206 -0.14172 0.07245  -0.12728 129 PRO B O   
3738 C CB  . PRO B 129 ? 3.37167 2.40963 2.87367 -0.09815 0.06066  -0.14038 129 PRO B CB  
3739 C CG  . PRO B 129 ? 3.39349 2.42732 2.86626 -0.06004 0.06837  -0.12633 129 PRO B CG  
3740 C CD  . PRO B 129 ? 3.34501 2.44111 2.84406 -0.04179 0.03759  -0.13513 129 PRO B CD  
3741 N N   . LEU B 130 ? 3.36973 2.49870 2.99232 -0.19525 0.04210  -0.15192 130 LEU B N   
3742 C CA  . LEU B 130 ? 3.37822 2.52873 3.05146 -0.23496 0.04817  -0.14256 130 LEU B CA  
3743 C C   . LEU B 130 ? 3.40504 2.49600 3.06752 -0.27472 0.05292  -0.14187 130 LEU B C   
3744 O O   . LEU B 130 ? 3.39951 2.44391 3.02110 -0.27890 0.04213  -0.15592 130 LEU B O   
3745 C CB  . LEU B 130 ? 3.32286 2.54508 3.05543 -0.25336 0.01920  -0.15335 130 LEU B CB  
3746 C CG  . LEU B 130 ? 3.29287 2.57136 3.03412 -0.21752 0.00930  -0.15757 130 LEU B CG  
3747 C CD1 . LEU B 130 ? 3.22662 2.56094 3.01123 -0.23411 -0.02299 -0.17413 130 LEU B CD1 
3748 C CD2 . LEU B 130 ? 3.33285 2.63255 3.08974 -0.20311 0.03518  -0.13673 130 LEU B CD2 
3749 N N   . ALA B 131 ? 3.42261 2.51079 3.12187 -0.30351 0.07055  -0.12379 131 ALA B N   
3750 C CA  . ALA B 131 ? 3.45660 2.48593 3.15129 -0.34648 0.07208  -0.12098 131 ALA B CA  
3751 C C   . ALA B 131 ? 3.46250 2.53077 3.24296 -0.39269 0.06584  -0.10652 131 ALA B C   
3752 O O   . ALA B 131 ? 3.50560 2.56669 3.31624 -0.40124 0.09668  -0.08219 131 ALA B O   
3753 C CB  . ALA B 131 ? 3.51356 2.47089 3.15298 -0.32977 0.10978  -0.10715 131 ALA B CB  
3754 N N   . THR B 143 ? 3.64291 2.46299 3.26246 -0.55029 -0.09849 -0.19375 143 THR B N   
3755 C CA  . THR B 143 ? 3.59188 2.43882 3.17958 -0.50696 -0.09829 -0.21036 143 THR B CA  
3756 C C   . THR B 143 ? 3.55396 2.46328 3.16426 -0.45503 -0.06130 -0.19915 143 THR B C   
3757 O O   . THR B 143 ? 3.54071 2.51425 3.21901 -0.45410 -0.04818 -0.18095 143 THR B O   
3758 C CB  . THR B 143 ? 3.54084 2.45068 3.17644 -0.52370 -0.14023 -0.22121 143 THR B CB  
3759 O OG1 . THR B 143 ? 3.58456 2.42706 3.19005 -0.57217 -0.18128 -0.23188 143 THR B OG1 
3760 C CG2 . THR B 143 ? 3.49253 2.42468 3.09584 -0.47985 -0.13780 -0.23769 143 THR B CG2 
3761 N N   . LEU B 144 ? 3.58638 2.47091 3.13788 -0.41112 -0.04473 -0.20830 144 LEU B N   
3762 C CA  . LEU B 144 ? 3.55774 2.49079 3.12039 -0.36072 -0.01886 -0.19962 144 LEU B CA  
3763 C C   . LEU B 144 ? 3.49639 2.48909 3.07603 -0.33347 -0.03603 -0.21283 144 LEU B C   
3764 O O   . LEU B 144 ? 3.48677 2.44972 3.03394 -0.33592 -0.05164 -0.22899 144 LEU B O   
3765 C CB  . LEU B 144 ? 3.59699 2.45716 3.08994 -0.32953 0.01323  -0.19451 144 LEU B CB  
3766 C CG  . LEU B 144 ? 3.66230 2.44721 3.12418 -0.35424 0.03365  -0.18276 144 LEU B CG  
3767 C CD1 . LEU B 144 ? 3.69576 2.40918 3.08534 -0.31791 0.06554  -0.17810 144 LEU B CD1 
3768 C CD2 . LEU B 144 ? 3.67045 2.50267 3.19334 -0.36576 0.04715  -0.16249 144 LEU B CD2 
3769 N N   . GLY B 145 ? 3.40255 2.47178 3.02770 -0.30687 -0.03162 -0.20536 145 GLY B N   
3770 C CA  . GLY B 145 ? 3.34530 2.47341 2.99162 -0.28136 -0.04818 -0.21649 145 GLY B CA  
3771 C C   . GLY B 145 ? 3.33809 2.50152 2.98900 -0.23553 -0.03442 -0.20749 145 GLY B C   
3772 O O   . GLY B 145 ? 3.37068 2.53643 3.02433 -0.22727 -0.01541 -0.19167 145 GLY B O   
3773 N N   . CYS B 146 ? 3.22805 2.41359 2.87768 -0.20528 -0.04505 -0.21671 146 CYS B N   
3774 C CA  . CYS B 146 ? 3.22233 2.44358 2.87960 -0.16413 -0.04372 -0.20979 146 CYS B CA  
3775 C C   . CYS B 146 ? 3.18375 2.48139 2.88905 -0.16467 -0.06106 -0.21285 146 CYS B C   
3776 O O   . CYS B 146 ? 3.15228 2.48102 2.89112 -0.19453 -0.07348 -0.21971 146 CYS B O   
3777 C CB  . CYS B 146 ? 3.20911 2.41838 2.85267 -0.13068 -0.04805 -0.21412 146 CYS B CB  
3778 S SG  . CYS B 146 ? 3.23883 2.35922 2.83073 -0.13296 -0.02857 -0.21521 146 CYS B SG  
3779 N N   . LEU B 147 ? 3.11464 2.43749 2.81904 -0.13023 -0.06366 -0.20707 147 LEU B N   
3780 C CA  . LEU B 147 ? 3.02426 2.40895 2.76159 -0.12439 -0.07759 -0.20921 147 LEU B CA  
3781 C C   . LEU B 147 ? 2.97445 2.37633 2.70673 -0.08652 -0.09676 -0.21311 147 LEU B C   
3782 O O   . LEU B 147 ? 3.11920 2.49247 2.81773 -0.05762 -0.09344 -0.20321 147 LEU B O   
3783 C CB  . LEU B 147 ? 3.07615 2.46257 2.81039 -0.12545 -0.05691 -0.19280 147 LEU B CB  
3784 C CG  . LEU B 147 ? 3.08783 2.52086 2.83730 -0.10924 -0.06310 -0.19058 147 LEU B CG  
3785 C CD1 . LEU B 147 ? 2.98654 2.47862 2.78786 -0.12920 -0.08351 -0.20364 147 LEU B CD1 
3786 C CD2 . LEU B 147 ? 3.18929 2.61111 2.93293 -0.11034 -0.03165 -0.17011 147 LEU B CD2 
3787 N N   . VAL B 148 ? 2.91348 2.35940 2.68003 -0.08728 -0.11893 -0.22650 148 VAL B N   
3788 C CA  . VAL B 148 ? 2.94868 2.41741 2.72450 -0.05644 -0.14209 -0.23024 148 VAL B CA  
3789 C C   . VAL B 148 ? 3.03988 2.55282 2.82847 -0.05263 -0.15448 -0.23273 148 VAL B C   
3790 O O   . VAL B 148 ? 2.98950 2.54534 2.81329 -0.06854 -0.16365 -0.24317 148 VAL B O   
3791 C CB  . VAL B 148 ? 2.83673 2.31784 2.64265 -0.05733 -0.15356 -0.24131 148 VAL B CB  
3792 C CG1 . VAL B 148 ? 2.92543 2.43076 2.75326 -0.02651 -0.17822 -0.24124 148 VAL B CG1 
3793 C CG2 . VAL B 148 ? 2.85404 2.28029 2.63775 -0.06205 -0.13387 -0.23776 148 VAL B CG2 
3794 N N   . LYS B 149 ? 2.99860 2.49413 2.75136 -0.02957 -0.15366 -0.22258 149 LYS B N   
3795 C CA  . LYS B 149 ? 3.01249 2.53238 2.76004 -0.02246 -0.15802 -0.22203 149 LYS B CA  
3796 C C   . LYS B 149 ? 2.98970 2.51616 2.72712 0.00645  -0.19222 -0.22768 149 LYS B C   
3797 O O   . LYS B 149 ? 3.04765 2.53882 2.75414 0.03086  -0.20603 -0.22172 149 LYS B O   
3798 C CB  . LYS B 149 ? 3.09669 2.57940 2.79954 -0.01559 -0.12898 -0.20504 149 LYS B CB  
3799 C CG  . LYS B 149 ? 3.08513 2.58633 2.78159 -0.01000 -0.12063 -0.20061 149 LYS B CG  
3800 C CD  . LYS B 149 ? 3.18136 2.63723 2.83232 0.00027  -0.08346 -0.17993 149 LYS B CD  
3801 C CE  . LYS B 149 ? 3.18213 2.64888 2.82328 0.01032  -0.06739 -0.17190 149 LYS B CE  
3802 N NZ  . LYS B 149 ? 3.28545 2.69858 2.87590 0.02664  -0.02519 -0.14869 149 LYS B NZ  
3803 N N   . GLY B 150 ? 3.05782 2.62783 2.82294 0.00282  -0.20831 -0.23825 150 GLY B N   
3804 C CA  . GLY B 150 ? 3.06168 2.63679 2.81799 0.02619  -0.24333 -0.24401 150 GLY B CA  
3805 C C   . GLY B 150 ? 3.04621 2.62651 2.83452 0.03636  -0.27227 -0.24781 150 GLY B C   
3806 O O   . GLY B 150 ? 3.11039 2.65599 2.87182 0.05917  -0.29044 -0.23963 150 GLY B O   
3807 N N   . TYR B 151 ? 3.07427 2.69564 2.92160 0.02127  -0.27615 -0.25793 151 TYR B N   
3808 C CA  . TYR B 151 ? 3.06672 2.69793 2.95782 0.03198  -0.29767 -0.25832 151 TYR B CA  
3809 C C   . TYR B 151 ? 3.00086 2.67957 2.94137 0.02683  -0.31650 -0.27060 151 TYR B C   
3810 O O   . TYR B 151 ? 2.94452 2.65051 2.89291 0.00874  -0.30468 -0.28037 151 TYR B O   
3811 C CB  . TYR B 151 ? 3.03866 2.65514 2.94851 0.02303  -0.27267 -0.25406 151 TYR B CB  
3812 C CG  . TYR B 151 ? 2.81549 2.45479 2.75431 -0.00211 -0.25425 -0.26510 151 TYR B CG  
3813 C CD1 . TYR B 151 ? 2.83999 2.47508 2.75742 -0.02742 -0.23216 -0.26884 151 TYR B CD1 
3814 C CD2 . TYR B 151 ? 2.75709 2.41753 2.74491 0.00001  -0.25953 -0.26979 151 TYR B CD2 
3815 C CE1 . TYR B 151 ? 2.77410 2.42253 2.71121 -0.05070 -0.22241 -0.27882 151 TYR B CE1 
3816 C CE2 . TYR B 151 ? 2.71349 2.38281 2.71405 -0.02042 -0.24345 -0.27997 151 TYR B CE2 
3817 C CZ  . TYR B 151 ? 2.73807 2.39966 2.70957 -0.04613 -0.22810 -0.28536 151 TYR B CZ  
3818 O OH  . TYR B 151 ? 2.75911 2.42283 2.73698 -0.06692 -0.21907 -0.29550 151 TYR B OH  
3819 N N   . PHE B 152 ? 2.96399 2.65257 2.94253 0.04304  -0.34674 -0.26809 152 PHE B N   
3820 C CA  . PHE B 152 ? 2.89903 2.62891 2.93027 0.04124  -0.36748 -0.27721 152 PHE B CA  
3821 C C   . PHE B 152 ? 2.92799 2.66262 3.01525 0.05884  -0.39482 -0.26668 152 PHE B C   
3822 O O   . PHE B 152 ? 2.99439 2.70183 3.06385 0.07645  -0.41923 -0.25525 152 PHE B O   
3823 C CB  . PHE B 152 ? 2.86608 2.60195 2.86423 0.04306  -0.38872 -0.28585 152 PHE B CB  
3824 C CG  . PHE B 152 ? 2.78948 2.56033 2.83702 0.04370  -0.41627 -0.29424 152 PHE B CG  
3825 C CD1 . PHE B 152 ? 2.80447 2.56839 2.87023 0.05966  -0.46073 -0.28946 152 PHE B CD1 
3826 C CD2 . PHE B 152 ? 2.70628 2.51433 2.78239 0.02768  -0.40035 -0.30604 152 PHE B CD2 
3827 C CE1 . PHE B 152 ? 2.73764 2.53196 2.85344 0.05811  -0.48680 -0.29618 152 PHE B CE1 
3828 C CE2 . PHE B 152 ? 2.64168 2.47902 2.76232 0.02865  -0.42294 -0.31319 152 PHE B CE2 
3829 C CZ  . PHE B 152 ? 2.65743 2.48828 2.79981 0.04311  -0.46526 -0.30823 152 PHE B CZ  
3830 N N   . PRO B 153 ? 2.81254 2.57976 2.97077 0.05591  -0.39188 -0.26783 153 PRO B N   
3831 C CA  . PRO B 153 ? 2.70265 2.49627 2.87836 0.03789  -0.36697 -0.28103 153 PRO B CA  
3832 C C   . PRO B 153 ? 2.66338 2.43727 2.83051 0.02800  -0.32479 -0.27951 153 PRO B C   
3833 O O   . PRO B 153 ? 2.78298 2.52616 2.94384 0.03740  -0.31233 -0.26664 153 PRO B O   
3834 C CB  . PRO B 153 ? 2.68437 2.51115 2.93796 0.04506  -0.38590 -0.27924 153 PRO B CB  
3835 C CG  . PRO B 153 ? 2.78927 2.60482 3.08578 0.06464  -0.40049 -0.25892 153 PRO B CG  
3836 C CD  . PRO B 153 ? 2.87002 2.64970 3.10174 0.07248  -0.41615 -0.25357 153 PRO B CD  
3837 N N   . GLU B 154 ? 2.55758 2.34355 2.71932 0.00960  -0.30528 -0.29238 154 GLU B N   
3838 C CA  . GLU B 154 ? 2.54168 2.29907 2.68591 -0.00176 -0.27076 -0.29327 154 GLU B CA  
3839 C C   . GLU B 154 ? 2.58812 2.33068 2.77606 0.01520  -0.25539 -0.28131 154 GLU B C   
3840 O O   . GLU B 154 ? 2.62627 2.39748 2.87532 0.02863  -0.26866 -0.27644 154 GLU B O   
3841 C CB  . GLU B 154 ? 2.48782 2.26144 2.62226 -0.02295 -0.26231 -0.30899 154 GLU B CB  
3842 C CG  . GLU B 154 ? 2.56614 2.30278 2.65469 -0.04372 -0.23818 -0.31322 154 GLU B CG  
3843 C CD  . GLU B 154 ? 2.52042 2.27404 2.60275 -0.06424 -0.23800 -0.32722 154 GLU B CD  
3844 O OE1 . GLU B 154 ? 2.43984 2.23798 2.54735 -0.06321 -0.25418 -0.33362 154 GLU B OE1 
3845 O OE2 . GLU B 154 ? 2.55505 2.27289 2.60383 -0.08129 -0.22375 -0.33148 154 GLU B OE2 
3846 N N   . PRO B 155 ? 2.57254 2.26702 2.73212 0.01567  -0.22505 -0.27438 155 PRO B N   
3847 C CA  . PRO B 155 ? 2.59849 2.25171 2.69103 -0.00038 -0.20963 -0.27716 155 PRO B CA  
3848 C C   . PRO B 155 ? 2.68359 2.30175 2.75957 0.01457  -0.20296 -0.26083 155 PRO B C   
3849 O O   . PRO B 155 ? 2.75838 2.38802 2.87641 0.03833  -0.21559 -0.24635 155 PRO B O   
3850 C CB  . PRO B 155 ? 2.60775 2.22100 2.67367 -0.01186 -0.18019 -0.28356 155 PRO B CB  
3851 C CG  . PRO B 155 ? 2.63679 2.24715 2.75349 0.01326  -0.16537 -0.27179 155 PRO B CG  
3852 C CD  . PRO B 155 ? 2.59969 2.27187 2.78772 0.02799  -0.19659 -0.26646 155 PRO B CD  
3853 N N   . VAL B 156 ? 2.74408 2.31854 2.76121 -0.00041 -0.18485 -0.26226 156 VAL B N   
3854 C CA  . VAL B 156 ? 2.79417 2.32765 2.78326 0.01107  -0.17407 -0.24792 156 VAL B CA  
3855 C C   . VAL B 156 ? 2.81056 2.27868 2.75488 0.00201  -0.13891 -0.24710 156 VAL B C   
3856 O O   . VAL B 156 ? 2.75724 2.20812 2.67147 -0.02257 -0.13063 -0.26079 156 VAL B O   
3857 C CB  . VAL B 156 ? 2.81986 2.35687 2.77212 0.00205  -0.18707 -0.24899 156 VAL B CB  
3858 C CG1 . VAL B 156 ? 2.88749 2.36761 2.78291 -0.01097 -0.16148 -0.24506 156 VAL B CG1 
3859 C CG2 . VAL B 156 ? 2.89504 2.44911 2.86520 0.02816  -0.21328 -0.23744 156 VAL B CG2 
3860 N N   . THR B 157 ? 2.94315 2.36954 2.87978 0.02267  -0.12001 -0.23027 157 THR B N   
3861 C CA  . THR B 157 ? 2.98387 2.33436 2.86684 0.01784  -0.08429 -0.22766 157 THR B CA  
3862 C C   . THR B 157 ? 3.05447 2.36550 2.87954 0.00343  -0.07857 -0.22639 157 THR B C   
3863 O O   . THR B 157 ? 3.04072 2.36920 2.87223 0.01484  -0.09142 -0.21712 157 THR B O   
3864 C CB  . THR B 157 ? 2.97591 2.29748 2.88536 0.05189  -0.05886 -0.20678 157 THR B CB  
3865 O OG1 . THR B 157 ? 3.01516 2.32489 2.92320 0.07052  -0.05946 -0.18921 157 THR B OG1 
3866 C CG2 . THR B 157 ? 2.88106 2.26136 2.87536 0.07203  -0.07197 -0.20035 157 THR B CG2 
3867 N N   . VAL B 158 ? 3.05298 2.30485 2.81812 -0.02184 -0.06037 -0.23523 158 VAL B N   
3868 C CA  . VAL B 158 ? 3.11189 2.31805 2.82327 -0.03962 -0.05139 -0.23338 158 VAL B CA  
3869 C C   . VAL B 158 ? 3.15407 2.26633 2.80217 -0.04455 -0.02006 -0.23237 158 VAL B C   
3870 O O   . VAL B 158 ? 3.15558 2.23547 2.77574 -0.06143 -0.01652 -0.24487 158 VAL B O   
3871 C CB  . VAL B 158 ? 3.11125 2.34529 2.81604 -0.07675 -0.07067 -0.24656 158 VAL B CB  
3872 C CG1 . VAL B 158 ? 3.17848 2.35464 2.83086 -0.09940 -0.05674 -0.24334 158 VAL B CG1 
3873 C CG2 . VAL B 158 ? 3.08920 2.39985 2.84011 -0.06781 -0.09483 -0.24478 158 VAL B CG2 
3874 N N   . THR B 159 ? 3.36596 2.42691 2.98359 -0.02859 0.00242  -0.21742 159 THR B N   
3875 C CA  . THR B 159 ? 3.38701 2.34694 2.93374 -0.03087 0.03533  -0.21495 159 THR B CA  
3876 C C   . THR B 159 ? 3.49034 2.40330 2.98976 -0.04300 0.04525  -0.20889 159 THR B C   
3877 O O   . THR B 159 ? 3.48565 2.44081 3.01093 -0.03612 0.03449  -0.20068 159 THR B O   
3878 C CB  . THR B 159 ? 3.38192 2.31213 2.94084 0.01166  0.06599  -0.19705 159 THR B CB  
3879 O OG1 . THR B 159 ? 3.40254 2.37738 3.01395 0.04344  0.06170  -0.17713 159 THR B OG1 
3880 C CG2 . THR B 159 ? 3.22999 2.19176 2.82993 0.02188  0.06401  -0.20192 159 THR B CG2 
3881 N N   . TRP B 160 ? 3.53771 2.35445 2.96063 -0.06062 0.06647  -0.21281 160 TRP B N   
3882 C CA  . TRP B 160 ? 3.58834 2.34623 2.95969 -0.07552 0.07942  -0.20741 160 TRP B CA  
3883 C C   . TRP B 160 ? 3.63375 2.30420 2.95413 -0.04508 0.12002  -0.19188 160 TRP B C   
3884 O O   . TRP B 160 ? 3.66296 2.26110 2.93439 -0.04069 0.14090  -0.19507 160 TRP B O   
3885 C CB  . TRP B 160 ? 3.62453 2.33635 2.94779 -0.12701 0.06585  -0.22424 160 TRP B CB  
3886 C CG  . TRP B 160 ? 3.58066 2.37762 2.95934 -0.15705 0.02942  -0.23508 160 TRP B CG  
3887 C CD1 . TRP B 160 ? 3.54091 2.38247 2.94828 -0.16985 0.00488  -0.24926 160 TRP B CD1 
3888 C CD2 . TRP B 160 ? 3.57402 2.41806 2.98548 -0.17531 0.01796  -0.23006 160 TRP B CD2 
3889 N NE1 . TRP B 160 ? 3.50645 2.42268 2.96538 -0.19496 -0.02192 -0.25293 160 TRP B NE1 
3890 C CE2 . TRP B 160 ? 3.52839 2.44666 2.99139 -0.19810 -0.01253 -0.24051 160 TRP B CE2 
3891 C CE3 . TRP B 160 ? 3.60557 2.43237 3.00608 -0.17237 0.03418  -0.21601 160 TRP B CE3 
3892 C CZ2 . TRP B 160 ? 3.51484 2.48981 3.02114 -0.21678 -0.02417 -0.23557 160 TRP B CZ2 
3893 C CZ3 . TRP B 160 ? 3.59541 2.47586 3.03551 -0.19103 0.02293  -0.21190 160 TRP B CZ3 
3894 C CH2 . TRP B 160 ? 3.55136 2.50493 3.04511 -0.21251 -0.00456 -0.22080 160 TRP B CH2 
3895 N N   . ASN B 161 ? 3.63344 2.30474 2.96013 -0.02199 0.13299  -0.17390 161 ASN B N   
3896 C CA  . ASN B 161 ? 3.67060 2.26775 2.95914 0.01247  0.17274  -0.15448 161 ASN B CA  
3897 C C   . ASN B 161 ? 3.64576 2.25325 2.97164 0.05194  0.18936  -0.14297 161 ASN B C   
3898 O O   . ASN B 161 ? 3.72231 2.24599 3.00114 0.07266  0.22893  -0.13223 161 ASN B O   
3899 C CB  . ASN B 161 ? 3.77451 2.24887 2.96107 -0.01164 0.19868  -0.16043 161 ASN B CB  
3900 C CG  . ASN B 161 ? 3.80212 2.25890 2.96056 -0.04265 0.19171  -0.16270 161 ASN B CG  
3901 O OD1 . ASN B 161 ? 3.73809 2.27199 2.94538 -0.06089 0.16304  -0.16758 161 ASN B OD1 
3902 N ND2 . ASN B 161 ? 3.90608 2.25658 2.98458 -0.04733 0.22151  -0.15745 161 ASN B ND2 
3903 N N   . SER B 162 ? 3.72822 2.43599 3.14014 0.06305  0.16126  -0.14353 162 SER B N   
3904 C CA  . SER B 162 ? 3.69989 2.43459 3.17015 0.09933  0.17321  -0.12999 162 SER B CA  
3905 C C   . SER B 162 ? 3.72282 2.38226 3.13964 0.09449  0.20204  -0.13841 162 SER B C   
3906 O O   . SER B 162 ? 3.73122 2.34993 3.15203 0.12981  0.24025  -0.11974 162 SER B O   
3907 C CB  . SER B 162 ? 3.70755 2.43526 3.21039 0.14618  0.19657  -0.09812 162 SER B CB  
3908 O OG  . SER B 162 ? 3.67550 2.44900 3.26105 0.18014  0.20209  -0.08108 162 SER B OG  
3909 N N   . GLY B 163 ? 3.74730 2.38388 3.11254 0.05189  0.18412  -0.16481 163 GLY B N   
3910 C CA  . GLY B 163 ? 3.78038 2.33804 3.08087 0.04430  0.20351  -0.17605 163 GLY B CA  
3911 C C   . GLY B 163 ? 3.86855 2.28643 3.04764 0.03280  0.23402  -0.17894 163 GLY B C   
3912 O O   . GLY B 163 ? 3.91247 2.23995 3.02331 0.04062  0.26192  -0.18160 163 GLY B O   
3913 N N   . ALA B 164 ? 3.88324 2.27229 3.02682 0.01525  0.23098  -0.17812 164 ALA B N   
3914 C CA  . ALA B 164 ? 3.97361 2.22394 2.99824 0.00101  0.25710  -0.18143 164 ALA B CA  
3915 C C   . ALA B 164 ? 4.01633 2.22642 2.97938 -0.05739 0.22148  -0.20857 164 ALA B C   
3916 O O   . ALA B 164 ? 4.10639 2.18806 2.95893 -0.07382 0.23498  -0.21714 164 ALA B O   
3917 C CB  . ALA B 164 ? 3.99089 2.21924 3.00648 0.01525  0.27770  -0.16313 164 ALA B CB  
3918 N N   . LEU B 165 ? 3.98489 2.29724 3.01626 -0.08868 0.17554  -0.22065 165 LEU B N   
3919 C CA  . LEU B 165 ? 4.01692 2.30895 3.01372 -0.14462 0.13667  -0.24275 165 LEU B CA  
3920 C C   . LEU B 165 ? 4.00614 2.30766 3.00077 -0.15092 0.11755  -0.25843 165 LEU B C   
3921 O O   . LEU B 165 ? 3.92458 2.33726 3.00702 -0.14241 0.09841  -0.25988 165 LEU B O   
3922 C CB  . LEU B 165 ? 3.96496 2.35953 3.03980 -0.17205 0.10329  -0.24343 165 LEU B CB  
3923 C CG  . LEU B 165 ? 4.00557 2.36269 3.05617 -0.19080 0.11094  -0.23538 165 LEU B CG  
3924 C CD1 . LEU B 165 ? 4.01343 2.34354 3.05259 -0.14509 0.15356  -0.21408 165 LEU B CD1 
3925 C CD2 . LEU B 165 ? 3.95563 2.41491 3.08643 -0.21703 0.08074  -0.23514 165 LEU B CD2 
3926 N N   . SER B 166 ? 4.14514 2.32213 3.03160 -0.16492 0.12258  -0.27024 166 SER B N   
3927 C CA  . SER B 166 ? 4.15449 2.31656 3.01750 -0.16621 0.10971  -0.28427 166 SER B CA  
3928 C C   . SER B 166 ? 4.14704 2.34243 3.02052 -0.22056 0.05037  -0.30494 166 SER B C   
3929 O O   . SER B 166 ? 4.07642 2.36854 3.02168 -0.22242 0.02528  -0.31125 166 SER B O   
3930 C CB  . SER B 166 ? 4.26692 2.26439 2.99460 -0.14930 0.14637  -0.28556 166 SER B CB  
3931 O OG  . SER B 166 ? 4.36506 2.24245 2.98755 -0.18566 0.13604  -0.29447 166 SER B OG  
3932 N N   . SER B 167 ? 4.17460 2.29059 2.98142 -0.26523 0.02673  -0.31389 167 SER B N   
3933 C CA  . SER B 167 ? 4.17347 2.31403 2.99415 -0.31893 -0.03224 -0.32994 167 SER B CA  
3934 C C   . SER B 167 ? 4.07916 2.36154 3.02629 -0.33894 -0.05643 -0.32259 167 SER B C   
3935 O O   . SER B 167 ? 4.04593 2.37316 3.03971 -0.32137 -0.03131 -0.30733 167 SER B O   
3936 C CB  . SER B 167 ? 4.29438 2.29099 2.99981 -0.36204 -0.05343 -0.34047 167 SER B CB  
3937 O OG  . SER B 167 ? 4.29329 2.31656 3.02306 -0.41590 -0.11604 -0.35298 167 SER B OG  
3938 N N   . GLY B 168 ? 3.95122 2.29946 2.95015 -0.37389 -0.10434 -0.33216 168 GLY B N   
3939 C CA  . GLY B 168 ? 3.87485 2.34558 2.98672 -0.39580 -0.12661 -0.32405 168 GLY B CA  
3940 C C   . GLY B 168 ? 3.76881 2.37505 2.98210 -0.36165 -0.11669 -0.31707 168 GLY B C   
3941 O O   . GLY B 168 ? 3.71105 2.41668 3.01258 -0.37832 -0.13605 -0.31126 168 GLY B O   
3942 N N   . VAL B 169 ? 3.79381 2.40405 2.99873 -0.31442 -0.08674 -0.31577 169 VAL B N   
3943 C CA  . VAL B 169 ? 3.70176 2.43230 2.99921 -0.28194 -0.08065 -0.30918 169 VAL B CA  
3944 C C   . VAL B 169 ? 3.64306 2.45433 2.99740 -0.30329 -0.11922 -0.31929 169 VAL B C   
3945 O O   . VAL B 169 ? 3.64723 2.43356 2.97125 -0.30300 -0.13050 -0.33147 169 VAL B O   
3946 C CB  . VAL B 169 ? 3.69573 2.40678 2.97721 -0.23137 -0.04511 -0.30457 169 VAL B CB  
3947 C CG1 . VAL B 169 ? 3.59452 2.42722 2.97426 -0.20191 -0.04628 -0.29782 169 VAL B CG1 
3948 C CG2 . VAL B 169 ? 3.75234 2.38331 2.98108 -0.20820 -0.00509 -0.29137 169 VAL B CG2 
3949 N N   . HIS B 170 ? 3.52996 2.43392 2.96395 -0.31964 -0.13653 -0.31271 170 HIS B N   
3950 C CA  . HIS B 170 ? 3.46970 2.45465 2.96546 -0.34109 -0.17131 -0.31849 170 HIS B CA  
3951 C C   . HIS B 170 ? 3.39273 2.49072 2.97325 -0.31392 -0.16363 -0.30958 170 HIS B C   
3952 O O   . HIS B 170 ? 3.37751 2.52945 3.00936 -0.32472 -0.16584 -0.29846 170 HIS B O   
3953 C CB  . HIS B 170 ? 3.49606 2.47308 3.00523 -0.39277 -0.20167 -0.31633 170 HIS B CB  
3954 C CG  . HIS B 170 ? 3.59458 2.45351 3.01466 -0.42383 -0.21948 -0.32677 170 HIS B CG  
3955 N ND1 . HIS B 170 ? 3.65958 2.43020 2.99027 -0.40696 -0.21197 -0.33991 170 HIS B ND1 
3956 C CD2 . HIS B 170 ? 3.64470 2.45166 3.04718 -0.47060 -0.24502 -0.32513 170 HIS B CD2 
3957 C CE1 . HIS B 170 ? 3.74843 2.41022 2.99800 -0.44103 -0.23323 -0.34773 170 HIS B CE1 
3958 N NE2 . HIS B 170 ? 3.73924 2.42271 3.03357 -0.48199 -0.25683 -0.33943 170 HIS B NE2 
3959 N N   . THR B 171 ? 3.36047 2.48789 2.95279 -0.27816 -0.15383 -0.31341 171 THR B N   
3960 C CA  . THR B 171 ? 3.27718 2.50080 2.93989 -0.25193 -0.15189 -0.30702 171 THR B CA  
3961 C C   . THR B 171 ? 3.18062 2.47783 2.89431 -0.26763 -0.17961 -0.31399 171 THR B C   
3962 O O   . THR B 171 ? 3.13874 2.42290 2.83654 -0.27353 -0.19313 -0.32614 171 THR B O   
3963 C CB  . THR B 171 ? 3.14904 2.37203 2.81155 -0.20815 -0.13188 -0.30545 171 THR B CB  
3964 O OG1 . THR B 171 ? 3.15157 2.31259 2.77521 -0.19057 -0.10462 -0.29505 171 THR B OG1 
3965 C CG2 . THR B 171 ? 3.09271 2.40849 2.82339 -0.18452 -0.13860 -0.30052 171 THR B CG2 
3966 N N   . PHE B 172 ? 3.07417 2.44264 2.84403 -0.27172 -0.18505 -0.30494 172 PHE B N   
3967 C CA  . PHE B 172 ? 3.07405 2.51399 2.89704 -0.28634 -0.20734 -0.30725 172 PHE B CA  
3968 C C   . PHE B 172 ? 2.90901 2.40906 2.76382 -0.25351 -0.20703 -0.31155 172 PHE B C   
3969 O O   . PHE B 172 ? 2.99755 2.49310 2.84530 -0.22132 -0.19210 -0.30941 172 PHE B O   
3970 C CB  . PHE B 172 ? 2.91785 2.39602 2.78387 -0.30484 -0.20622 -0.29158 172 PHE B CB  
3971 C CG  . PHE B 172 ? 3.17246 2.61577 3.03611 -0.34933 -0.22130 -0.28801 172 PHE B CG  
3972 C CD1 . PHE B 172 ? 3.29208 2.65242 3.10181 -0.36299 -0.21339 -0.28745 172 PHE B CD1 
3973 C CD2 . PHE B 172 ? 3.17967 2.67134 3.09751 -0.37808 -0.24545 -0.28387 172 PHE B CD2 
3974 C CE1 . PHE B 172 ? 3.33608 2.65904 3.14361 -0.40712 -0.23276 -0.28429 172 PHE B CE1 
3975 C CE2 . PHE B 172 ? 3.22930 2.69027 3.15451 -0.42193 -0.26619 -0.27850 172 PHE B CE2 
3976 C CZ  . PHE B 172 ? 3.30078 2.67547 3.16945 -0.43783 -0.26165 -0.27950 172 PHE B CZ  
3977 N N   . PRO B 173 ? 2.87735 2.43438 2.77090 -0.26140 -0.22567 -0.31667 173 PRO B N   
3978 C CA  . PRO B 173 ? 2.75729 2.36568 2.67816 -0.23216 -0.22681 -0.32192 173 PRO B CA  
3979 C C   . PRO B 173 ? 2.74415 2.39821 2.69310 -0.20935 -0.21820 -0.31136 173 PRO B C   
3980 O O   . PRO B 173 ? 2.80603 2.45293 2.75239 -0.21363 -0.20745 -0.29898 173 PRO B O   
3981 C CB  . PRO B 173 ? 2.73482 2.38329 2.68313 -0.25062 -0.24840 -0.32882 173 PRO B CB  
3982 C CG  . PRO B 173 ? 2.89767 2.54779 2.86131 -0.28549 -0.25801 -0.31939 173 PRO B CG  
3983 C CD  . PRO B 173 ? 2.97864 2.55188 2.89336 -0.29738 -0.24888 -0.31741 173 PRO B CD  
3984 N N   . ALA B 174 ? 2.75569 2.44977 2.72629 -0.18455 -0.22334 -0.31612 174 ALA B N   
3985 C CA  . ALA B 174 ? 2.67098 2.39840 2.65610 -0.16132 -0.22139 -0.30847 174 ALA B CA  
3986 C C   . ALA B 174 ? 2.58114 2.36407 2.59766 -0.16740 -0.22830 -0.30674 174 ALA B C   
3987 O O   . ALA B 174 ? 2.54593 2.35125 2.58281 -0.18690 -0.23760 -0.31202 174 ALA B O   
3988 C CB  . ALA B 174 ? 2.63821 2.36881 2.62821 -0.13057 -0.22659 -0.31296 174 ALA B CB  
3989 N N   . VAL B 175 ? 2.54189 2.34113 2.55710 -0.14829 -0.22326 -0.29803 175 VAL B N   
3990 C CA  . VAL B 175 ? 2.63382 2.47723 2.67149 -0.14797 -0.22250 -0.29291 175 VAL B CA  
3991 C C   . VAL B 175 ? 2.67403 2.51623 2.68930 -0.11605 -0.22301 -0.28997 175 VAL B C   
3992 O O   . VAL B 175 ? 2.66263 2.46840 2.64568 -0.09973 -0.22024 -0.28526 175 VAL B O   
3993 C CB  . VAL B 175 ? 2.75019 2.59856 2.80436 -0.17068 -0.20639 -0.27650 175 VAL B CB  
3994 C CG1 . VAL B 175 ? 2.80780 2.61826 2.83105 -0.16019 -0.18589 -0.26206 175 VAL B CG1 
3995 C CG2 . VAL B 175 ? 2.83619 2.73427 2.92507 -0.17114 -0.20234 -0.26850 175 VAL B CG2 
3996 N N   . LEU B 176 ? 2.66629 2.54264 2.69346 -0.10664 -0.22882 -0.29270 176 LEU B N   
3997 C CA  . LEU B 176 ? 2.75224 2.61904 2.74859 -0.07730 -0.23489 -0.29197 176 LEU B CA  
3998 C C   . LEU B 176 ? 2.81110 2.67114 2.78652 -0.07037 -0.21077 -0.27487 176 LEU B C   
3999 O O   . LEU B 176 ? 2.78642 2.67879 2.78406 -0.07472 -0.20060 -0.26990 176 LEU B O   
4000 C CB  . LEU B 176 ? 2.66787 2.56525 2.68207 -0.06946 -0.25468 -0.30560 176 LEU B CB  
4001 C CG  . LEU B 176 ? 2.60163 2.49750 2.63328 -0.06625 -0.27546 -0.31878 176 LEU B CG  
4002 C CD1 . LEU B 176 ? 2.54470 2.47490 2.60305 -0.06374 -0.28962 -0.33076 176 LEU B CD1 
4003 C CD2 . LEU B 176 ? 2.63556 2.49592 2.64028 -0.04411 -0.28939 -0.31591 176 LEU B CD2 
4004 N N   . GLN B 177 ? 2.74312 2.55787 2.67513 -0.05708 -0.19853 -0.26374 177 GLN B N   
4005 C CA  . GLN B 177 ? 2.81730 2.61340 2.72193 -0.04621 -0.16808 -0.24429 177 GLN B CA  
4006 C C   . GLN B 177 ? 2.81687 2.59681 2.67493 -0.01662 -0.17242 -0.24529 177 GLN B C   
4007 O O   . GLN B 177 ? 2.80949 2.61216 2.67958 -0.01438 -0.15574 -0.23823 177 GLN B O   
4008 C CB  . GLN B 177 ? 2.91556 2.65960 2.78056 -0.03971 -0.15176 -0.23203 177 GLN B CB  
4009 C CG  . GLN B 177 ? 2.93315 2.68169 2.83471 -0.06931 -0.14524 -0.23002 177 GLN B CG  
4010 C CD  . GLN B 177 ? 3.03118 2.72417 2.88932 -0.06059 -0.13003 -0.21918 177 GLN B CD  
4011 O OE1 . GLN B 177 ? 3.07429 2.72503 2.87405 -0.03121 -0.13536 -0.21796 177 GLN B OE1 
4012 N NE2 . GLN B 177 ? 3.07110 2.75939 2.95459 -0.08648 -0.11345 -0.21092 177 GLN B NE2 
4013 N N   . SER B 178 ? 2.91895 2.65515 2.72187 0.00663  -0.19636 -0.25285 178 SER B N   
4014 C CA  . SER B 178 ? 2.93034 2.63515 2.67466 0.03430  -0.20918 -0.25601 178 SER B CA  
4015 C C   . SER B 178 ? 2.88407 2.58168 2.62371 0.04192  -0.25770 -0.27374 178 SER B C   
4016 O O   . SER B 178 ? 2.93805 2.58185 2.61738 0.06397  -0.28025 -0.27384 178 SER B O   
4017 C CB  . SER B 178 ? 3.04806 2.68244 2.70855 0.06051  -0.18509 -0.23897 178 SER B CB  
4018 O OG  . SER B 178 ? 3.09917 2.74380 2.77797 0.05364  -0.13563 -0.21829 178 SER B OG  
4019 N N   . GLY B 179 ? 2.83455 2.58549 2.64174 0.02348  -0.27479 -0.28721 179 GLY B N   
4020 C CA  . GLY B 179 ? 2.78866 2.54327 2.61414 0.02798  -0.31552 -0.30044 179 GLY B CA  
4021 C C   . GLY B 179 ? 2.79494 2.55147 2.65461 0.02009  -0.32294 -0.30021 179 GLY B C   
4022 O O   . GLY B 179 ? 2.75155 2.52420 2.65058 0.02042  -0.34950 -0.30822 179 GLY B O   
4023 N N   . LEU B 180 ? 2.81314 2.55147 2.66105 0.01381  -0.29739 -0.28945 180 LEU B N   
4024 C CA  . LEU B 180 ? 2.81891 2.54770 2.68746 0.00917  -0.29934 -0.28722 180 LEU B CA  
4025 C C   . LEU B 180 ? 2.77613 2.52685 2.67984 -0.01803 -0.27139 -0.28672 180 LEU B C   
4026 O O   . LEU B 180 ? 2.81271 2.57782 2.71845 -0.03219 -0.24892 -0.28243 180 LEU B O   
4027 C CB  . LEU B 180 ? 2.94534 2.61758 2.75684 0.02757  -0.29798 -0.27467 180 LEU B CB  
4028 C CG  . LEU B 180 ? 2.98334 2.61668 2.74434 0.05544  -0.33236 -0.27385 180 LEU B CG  
4029 C CD1 . LEU B 180 ? 3.09537 2.66680 2.79151 0.07356  -0.32686 -0.26019 180 LEU B CD1 
4030 C CD2 . LEU B 180 ? 2.93869 2.59242 2.74816 0.05982  -0.37357 -0.28136 180 LEU B CD2 
4031 N N   . TYR B 181 ? 2.85189 2.60062 2.78302 -0.02470 -0.27365 -0.28940 181 TYR B N   
4032 C CA  . TYR B 181 ? 2.74588 2.49727 2.69486 -0.05007 -0.25188 -0.28979 181 TYR B CA  
4033 C C   . TYR B 181 ? 2.91531 2.62614 2.83014 -0.05379 -0.23003 -0.27688 181 TYR B C   
4034 O O   . TYR B 181 ? 3.02479 2.70203 2.90318 -0.03325 -0.23163 -0.26797 181 TYR B O   
4035 C CB  . TYR B 181 ? 2.65946 2.41080 2.63878 -0.05266 -0.25723 -0.29677 181 TYR B CB  
4036 C CG  . TYR B 181 ? 2.60051 2.38695 2.61812 -0.04663 -0.27592 -0.30735 181 TYR B CG  
4037 C CD1 . TYR B 181 ? 2.53495 2.35340 2.57387 -0.06335 -0.27363 -0.31733 181 TYR B CD1 
4038 C CD2 . TYR B 181 ? 2.59457 2.38124 2.63141 -0.02471 -0.29701 -0.30572 181 TYR B CD2 
4039 C CE1 . TYR B 181 ? 2.46679 2.31382 2.53912 -0.05709 -0.28756 -0.32640 181 TYR B CE1 
4040 C CE2 . TYR B 181 ? 2.54565 2.36369 2.62432 -0.02052 -0.31263 -0.31362 181 TYR B CE2 
4041 C CZ  . TYR B 181 ? 2.49470 2.34138 2.58810 -0.03617 -0.30558 -0.32447 181 TYR B CZ  
4042 O OH  . TYR B 181 ? 2.50784 2.38251 2.64110 -0.03118 -0.31817 -0.33178 181 TYR B OH  
4043 N N   . THR B 182 ? 2.73835 2.44853 2.66366 -0.08098 -0.21172 -0.27554 182 THR B N   
4044 C CA  . THR B 182 ? 2.83387 2.50532 2.73385 -0.09013 -0.18951 -0.26329 182 THR B CA  
4045 C C   . THR B 182 ? 2.70150 2.36702 2.61870 -0.12285 -0.18235 -0.26738 182 THR B C   
4046 O O   . THR B 182 ? 2.71548 2.41455 2.66311 -0.14285 -0.18919 -0.27401 182 THR B O   
4047 C CB  . THR B 182 ? 2.90109 2.57349 2.78640 -0.08814 -0.17151 -0.24934 182 THR B CB  
4048 O OG1 . THR B 182 ? 3.06917 2.72694 2.91736 -0.05533 -0.17958 -0.24604 182 THR B OG1 
4049 C CG2 . THR B 182 ? 3.01397 2.64780 2.88192 -0.10098 -0.14547 -0.23514 182 THR B CG2 
4050 N N   . LEU B 183 ? 2.72030 2.33725 2.61262 -0.12770 -0.17063 -0.26326 183 LEU B N   
4051 C CA  . LEU B 183 ? 2.82469 2.41790 2.71741 -0.15806 -0.16723 -0.26830 183 LEU B CA  
4052 C C   . LEU B 183 ? 2.95014 2.48886 2.81112 -0.16771 -0.14736 -0.25710 183 LEU B C   
4053 O O   . LEU B 183 ? 3.08196 2.60052 2.91964 -0.14708 -0.13478 -0.24586 183 LEU B O   
4054 C CB  . LEU B 183 ? 2.70829 2.28650 2.59753 -0.15161 -0.17584 -0.28105 183 LEU B CB  
4055 C CG  . LEU B 183 ? 2.74215 2.27430 2.60505 -0.12757 -0.16564 -0.27657 183 LEU B CG  
4056 C CD1 . LEU B 183 ? 2.79889 2.26552 2.62487 -0.14544 -0.15051 -0.27711 183 LEU B CD1 
4057 C CD2 . LEU B 183 ? 2.70724 2.26024 2.59453 -0.10275 -0.17636 -0.28214 183 LEU B CD2 
4058 N N   . THR B 184 ? 2.92635 2.43513 2.78146 -0.19972 -0.14663 -0.26047 184 THR B N   
4059 C CA  . THR B 184 ? 3.01333 2.46140 2.83559 -0.21409 -0.12968 -0.25209 184 THR B CA  
4060 C C   . THR B 184 ? 2.98818 2.38046 2.77720 -0.22940 -0.13416 -0.26364 184 THR B C   
4061 O O   . THR B 184 ? 2.97733 2.38120 2.77432 -0.23951 -0.15136 -0.27660 184 THR B O   
4062 C CB  . THR B 184 ? 3.20321 2.66201 3.05180 -0.24535 -0.12355 -0.23953 184 THR B CB  
4063 O OG1 . THR B 184 ? 3.16346 2.66803 3.05649 -0.27083 -0.14452 -0.24521 184 THR B OG1 
4064 C CG2 . THR B 184 ? 3.23706 2.71928 3.09474 -0.22379 -0.10440 -0.22284 184 THR B CG2 
4065 N N   . SER B 185 ? 3.06550 2.38926 2.80938 -0.22919 -0.11650 -0.25834 185 SER B N   
4066 C CA  . SER B 185 ? 3.14784 2.39921 2.84280 -0.23926 -0.11452 -0.26753 185 SER B CA  
4067 C C   . SER B 185 ? 3.32684 2.50939 2.98331 -0.26337 -0.10134 -0.25998 185 SER B C   
4068 O O   . SER B 185 ? 3.36057 2.51446 2.99515 -0.24449 -0.07859 -0.24848 185 SER B O   
4069 C CB  . SER B 185 ? 3.21881 2.44809 2.89238 -0.19953 -0.10097 -0.26828 185 SER B CB  
4070 O OG  . SER B 185 ? 3.29177 2.43854 2.90862 -0.20486 -0.09019 -0.27398 185 SER B OG  
4071 N N   . SER B 186 ? 3.35160 2.50417 2.99872 -0.30529 -0.11812 -0.26597 186 SER B N   
4072 C CA  . SER B 186 ? 3.41327 2.49807 3.02827 -0.33584 -0.11176 -0.25948 186 SER B CA  
4073 C C   . SER B 186 ? 3.46484 2.44585 2.99789 -0.34417 -0.11122 -0.27104 186 SER B C   
4074 O O   . SER B 186 ? 3.45019 2.41448 2.95731 -0.33691 -0.12159 -0.28472 186 SER B O   
4075 C CB  . SER B 186 ? 3.41053 2.52956 3.07838 -0.38139 -0.13530 -0.25440 186 SER B CB  
4076 O OG  . SER B 186 ? 3.38361 2.51583 3.06049 -0.40250 -0.16938 -0.26835 186 SER B OG  
4077 N N   . VAL B 187 ? 3.54143 2.44485 3.02767 -0.35815 -0.09595 -0.26456 187 VAL B N   
4078 C CA  . VAL B 187 ? 3.60856 2.39549 3.00364 -0.36935 -0.09344 -0.27420 187 VAL B CA  
4079 C C   . VAL B 187 ? 3.67237 2.39925 3.04786 -0.41500 -0.10177 -0.26904 187 VAL B C   
4080 O O   . VAL B 187 ? 3.68499 2.41518 3.07695 -0.41305 -0.07947 -0.25376 187 VAL B O   
4081 C CB  . VAL B 187 ? 3.62994 2.36219 2.96937 -0.32329 -0.05451 -0.27013 187 VAL B CB  
4082 C CG1 . VAL B 187 ? 3.62968 2.38338 2.99093 -0.30153 -0.02664 -0.25194 187 VAL B CG1 
4083 C CG2 . VAL B 187 ? 3.71307 2.31125 2.94807 -0.33439 -0.04580 -0.27788 187 VAL B CG2 
4084 N N   . THR B 188 ? 3.68147 2.35100 3.02206 -0.45670 -0.13598 -0.28093 188 THR B N   
4085 C CA  . THR B 188 ? 3.74727 2.35468 3.07280 -0.50631 -0.15267 -0.27641 188 THR B CA  
4086 C C   . THR B 188 ? 3.83429 2.30651 3.04715 -0.50002 -0.12791 -0.27991 188 THR B C   
4087 O O   . THR B 188 ? 3.88315 2.26485 3.00460 -0.49492 -0.13250 -0.29496 188 THR B O   
4088 C CB  . THR B 188 ? 3.76199 2.36200 3.09859 -0.55559 -0.20827 -0.28670 188 THR B CB  
4089 O OG1 . THR B 188 ? 3.67714 2.40559 3.12241 -0.55779 -0.22655 -0.28071 188 THR B OG1 
4090 C CG2 . THR B 188 ? 3.83442 2.37101 3.16578 -0.61083 -0.23153 -0.27996 188 THR B CG2 
4091 N N   . VAL B 189 ? 3.86512 2.31735 3.07890 -0.49782 -0.09816 -0.26492 189 VAL B N   
4092 C CA  . VAL B 189 ? 3.94730 2.27152 3.05667 -0.49033 -0.06990 -0.26538 189 VAL B CA  
4093 C C   . VAL B 189 ? 4.02226 2.27470 3.11389 -0.54783 -0.09175 -0.26260 189 VAL B C   
4094 O O   . VAL B 189 ? 3.99595 2.31972 3.17973 -0.58306 -0.11428 -0.25220 189 VAL B O   
4095 C CB  . VAL B 189 ? 3.92225 2.26657 3.03641 -0.43996 -0.01796 -0.24970 189 VAL B CB  
4096 C CG1 . VAL B 189 ? 3.84633 2.27328 2.99700 -0.38830 -0.00556 -0.25034 189 VAL B CG1 
4097 C CG2 . VAL B 189 ? 3.90185 2.30530 3.08951 -0.45329 -0.00830 -0.23081 189 VAL B CG2 
4098 N N   . PRO B 190 ? 4.10164 2.21150 3.07963 -0.55957 -0.08591 -0.26999 190 PRO B N   
4099 C CA  . PRO B 190 ? 4.17985 2.21451 3.14038 -0.61702 -0.10957 -0.26695 190 PRO B CA  
4100 C C   . PRO B 190 ? 4.15659 2.23932 3.18778 -0.61909 -0.07911 -0.24385 190 PRO B C   
4101 O O   . PRO B 190 ? 4.10473 2.24183 3.16047 -0.57083 -0.03400 -0.23193 190 PRO B O   
4102 C CB  . PRO B 190 ? 4.29367 2.15646 3.09941 -0.61333 -0.09631 -0.27929 190 PRO B CB  
4103 C CG  . PRO B 190 ? 4.27695 2.12817 3.02686 -0.56812 -0.08459 -0.29246 190 PRO B CG  
4104 C CD  . PRO B 190 ? 4.15229 2.15608 3.01039 -0.52333 -0.06048 -0.28140 190 PRO B CD  
4105 N N   . SER B 191 ? 4.14353 2.20106 3.20733 -0.67658 -0.10610 -0.23627 191 SER B N   
4106 C CA  . SER B 191 ? 4.12803 2.22824 3.26515 -0.68317 -0.07644 -0.21180 191 SER B CA  
4107 C C   . SER B 191 ? 4.17044 2.18477 3.22278 -0.64951 -0.02136 -0.20563 191 SER B C   
4108 O O   . SER B 191 ? 4.13705 2.20213 3.23648 -0.62449 0.01969  -0.18604 191 SER B O   
4109 C CB  . SER B 191 ? 4.17479 2.25643 3.36769 -0.75512 -0.11787 -0.20301 191 SER B CB  
4110 O OG  . SER B 191 ? 4.13134 2.29746 3.41212 -0.78553 -0.17006 -0.20520 191 SER B OG  
4111 N N   . SER B 192 ? 4.33353 2.21239 3.25567 -0.64585 -0.01783 -0.22087 192 SER B N   
4112 C CA  . SER B 192 ? 4.38098 2.16749 3.21819 -0.61579 0.03444  -0.21361 192 SER B CA  
4113 C C   . SER B 192 ? 4.31986 2.15110 3.14534 -0.54135 0.08203  -0.20868 192 SER B C   
4114 O O   . SER B 192 ? 4.33405 2.12803 3.12490 -0.50963 0.12876  -0.19542 192 SER B O   
4115 C CB  . SER B 192 ? 4.50081 2.11482 3.19561 -0.63731 0.02410  -0.22992 192 SER B CB  
4116 O OG  . SER B 192 ? 4.50929 2.08794 3.13078 -0.60845 0.01839  -0.24794 192 SER B OG  
4117 N N   . THR B 193 ? 4.31191 2.22132 3.16864 -0.51344 0.06941  -0.21765 193 THR B N   
4118 C CA  . THR B 193 ? 4.26081 2.20678 3.10906 -0.44553 0.10787  -0.21264 193 THR B CA  
4119 C C   . THR B 193 ? 4.18425 2.24883 3.12601 -0.41502 0.12865  -0.19391 193 THR B C   
4120 O O   . THR B 193 ? 4.15931 2.23502 3.08789 -0.36096 0.16350  -0.18420 193 THR B O   
4121 C CB  . THR B 193 ? 4.22586 2.20392 3.07164 -0.42772 0.08728  -0.22844 193 THR B CB  
4122 O OG1 . THR B 193 ? 4.17852 2.24891 3.10908 -0.46367 0.04036  -0.23540 193 THR B OG1 
4123 C CG2 . THR B 193 ? 4.32079 2.15519 3.04112 -0.43522 0.08508  -0.24408 193 THR B CG2 
4124 N N   . TRP B 194 ? 4.12300 2.27060 3.15612 -0.44661 0.10833  -0.18688 194 TRP B N   
4125 C CA  . TRP B 194 ? 4.06716 2.31458 3.17740 -0.41860 0.12871  -0.16879 194 TRP B CA  
4126 C C   . TRP B 194 ? 4.09262 2.35092 3.25784 -0.46167 0.12869  -0.15368 194 TRP B C   
4127 O O   . TRP B 194 ? 4.11657 2.36242 3.30780 -0.51695 0.09437  -0.15901 194 TRP B O   
4128 C CB  . TRP B 194 ? 3.98503 2.35306 3.16927 -0.39922 0.10657  -0.17411 194 TRP B CB  
4129 C CG  . TRP B 194 ? 3.94091 2.39130 3.17476 -0.35683 0.12932  -0.15800 194 TRP B CG  
4130 C CD1 . TRP B 194 ? 3.92875 2.37751 3.13225 -0.30117 0.15582  -0.15101 194 TRP B CD1 
4131 C CD2 . TRP B 194 ? 3.91497 2.45304 3.23223 -0.36552 0.12674  -0.14526 194 TRP B CD2 
4132 N NE1 . TRP B 194 ? 3.90170 2.42559 3.15510 -0.27591 0.16494  -0.13712 194 TRP B NE1 
4133 C CE2 . TRP B 194 ? 3.89501 2.47153 3.21439 -0.31303 0.15127  -0.13331 194 TRP B CE2 
4134 C CE3 . TRP B 194 ? 3.91104 2.49579 3.30213 -0.41131 0.10651  -0.14063 194 TRP B CE3 
4135 C CZ2 . TRP B 194 ? 3.88038 2.52936 3.25818 -0.30337 0.15908  -0.11880 194 TRP B CZ2 
4136 C CZ3 . TRP B 194 ? 3.88953 2.55454 3.35088 -0.40049 0.11917  -0.12346 194 TRP B CZ3 
4137 C CH2 . TRP B 194 ? 3.87888 2.57019 3.32600 -0.34615 0.14666  -0.11363 194 TRP B CH2 
4138 N N   . PRO B 195 ? 4.04343 2.32255 3.22945 -0.43738 0.16627  -0.13271 195 PRO B N   
4139 C CA  . PRO B 195 ? 4.02027 2.31783 3.18354 -0.37404 0.20169  -0.12247 195 PRO B CA  
4140 C C   . PRO B 195 ? 4.06617 2.25877 3.13232 -0.34605 0.23418  -0.12020 195 PRO B C   
4141 O O   . PRO B 195 ? 4.06813 2.25808 3.11790 -0.30479 0.26742  -0.10437 195 PRO B O   
4142 C CB  . PRO B 195 ? 4.02096 2.36591 3.24188 -0.37282 0.22502  -0.09952 195 PRO B CB  
4143 C CG  . PRO B 195 ? 4.06902 2.36824 3.31028 -0.43261 0.22119  -0.09332 195 PRO B CG  
4144 C CD  . PRO B 195 ? 4.06853 2.35963 3.31595 -0.47707 0.17252  -0.11446 195 PRO B CD  
4145 N N   . SER B 196 ? 4.20597 2.30788 3.20320 -0.36573 0.22520  -0.13481 196 SER B N   
4146 C CA  . SER B 196 ? 4.25309 2.24925 3.15416 -0.33664 0.25958  -0.13164 196 SER B CA  
4147 C C   . SER B 196 ? 4.20639 2.23396 3.09562 -0.27410 0.27189  -0.13083 196 SER B C   
4148 O O   . SER B 196 ? 4.19234 2.23202 3.07842 -0.22828 0.30046  -0.11420 196 SER B O   
4149 C CB  . SER B 196 ? 4.32755 2.20407 3.14737 -0.37589 0.24760  -0.14714 196 SER B CB  
4150 O OG  . SER B 196 ? 4.30434 2.18765 3.10983 -0.37382 0.22046  -0.16588 196 SER B OG  
4151 N N   . GLN B 197 ? 4.26985 2.30948 3.15525 -0.27171 0.24934  -0.14699 197 GLN B N   
4152 C CA  . GLN B 197 ? 4.23046 2.29571 3.11278 -0.21528 0.26157  -0.14410 197 GLN B CA  
4153 C C   . GLN B 197 ? 4.15487 2.35075 3.12670 -0.18663 0.24732  -0.13740 197 GLN B C   
4154 O O   . GLN B 197 ? 4.12975 2.39893 3.16344 -0.21213 0.22516  -0.13933 197 GLN B O   
4155 C CB  . GLN B 197 ? 4.23631 2.26724 3.08503 -0.22132 0.24633  -0.16191 197 GLN B CB  
4156 C CG  . GLN B 197 ? 4.33249 2.21728 3.07367 -0.24682 0.25817  -0.17036 197 GLN B CG  
4157 C CD  . GLN B 197 ? 4.35184 2.18784 3.04262 -0.23797 0.25353  -0.18439 197 GLN B CD  
4158 O OE1 . GLN B 197 ? 4.31744 2.17436 3.01612 -0.18761 0.27520  -0.17668 197 GLN B OE1 
4159 N NE2 . GLN B 197 ? 4.41175 2.17952 3.05148 -0.28659 0.22446  -0.20342 197 GLN B NE2 
4160 N N   . THR B 198 ? 4.07402 2.29439 3.05230 -0.13223 0.26027  -0.12772 198 THR B N   
4161 C CA  . THR B 198 ? 4.01439 2.34593 3.06668 -0.10101 0.24280  -0.12172 198 THR B CA  
4162 C C   . THR B 198 ? 3.96463 2.36303 3.06475 -0.10996 0.21054  -0.13844 198 THR B C   
4163 O O   . THR B 198 ? 3.95670 2.33018 3.03979 -0.09346 0.21499  -0.14290 198 THR B O   
4164 C CB  . THR B 198 ? 4.00564 2.33310 3.05098 -0.04170 0.26352  -0.10242 198 THR B CB  
4165 O OG1 . THR B 198 ? 4.05054 2.33071 3.05844 -0.03138 0.28961  -0.08591 198 THR B OG1 
4166 C CG2 . THR B 198 ? 3.94975 2.38426 3.06816 -0.01047 0.23614  -0.09898 198 THR B CG2 
4167 N N   . VAL B 199 ? 3.88540 2.36499 3.04432 -0.13407 0.18203  -0.14586 199 VAL B N   
4168 C CA  . VAL B 199 ? 3.83550 2.38290 3.04233 -0.14469 0.15035  -0.16156 199 VAL B CA  
4169 C C   . VAL B 199 ? 3.78474 2.42291 3.04956 -0.10368 0.13770  -0.15495 199 VAL B C   
4170 O O   . VAL B 199 ? 3.78111 2.46693 3.07377 -0.09587 0.13297  -0.14639 199 VAL B O   
4171 C CB  . VAL B 199 ? 3.83048 2.40973 3.06937 -0.19714 0.12546  -0.17240 199 VAL B CB  
4172 C CG1 . VAL B 199 ? 3.77079 2.42792 3.06242 -0.20264 0.09309  -0.18670 199 VAL B CG1 
4173 C CG2 . VAL B 199 ? 3.88916 2.37303 3.07108 -0.24104 0.12808  -0.18002 199 VAL B CG2 
4174 N N   . THR B 200 ? 3.78150 2.43728 3.06179 -0.07730 0.13260  -0.15788 200 THR B N   
4175 C CA  . THR B 200 ? 3.74176 2.47416 3.07765 -0.03763 0.11749  -0.15039 200 THR B CA  
4176 C C   . THR B 200 ? 3.68928 2.49459 3.07831 -0.04971 0.08747  -0.16620 200 THR B C   
4177 O O   . THR B 200 ? 3.68075 2.46150 3.05703 -0.06651 0.08729  -0.17867 200 THR B O   
4178 C CB  . THR B 200 ? 3.74705 2.44540 3.07366 0.00694  0.13816  -0.13497 200 THR B CB  
4179 O OG1 . THR B 200 ? 3.78794 2.43742 3.07664 0.02685  0.16096  -0.11697 200 THR B OG1 
4180 C CG2 . THR B 200 ? 3.70408 2.48361 3.10168 0.04082  0.11469  -0.12937 200 THR B CG2 
4181 N N   . CYS B 201 ? 3.55691 2.44379 2.99720 -0.03981 0.06276  -0.16558 201 CYS B N   
4182 C CA  . CYS B 201 ? 3.50528 2.46586 2.99900 -0.04578 0.03437  -0.17871 201 CYS B CA  
4183 C C   . CYS B 201 ? 3.48563 2.49060 3.02289 -0.00309 0.02188  -0.16971 201 CYS B C   
4184 O O   . CYS B 201 ? 3.50360 2.53668 3.05406 0.02039  0.00964  -0.15900 201 CYS B O   
4185 C CB  . CYS B 201 ? 3.49025 2.50701 3.00983 -0.06905 0.01534  -0.18466 201 CYS B CB  
4186 S SG  . CYS B 201 ? 3.42741 2.53372 3.01013 -0.07278 -0.01837 -0.19972 201 CYS B SG  
4187 N N   . ASN B 202 ? 3.41911 2.42623 2.97804 0.00682  0.02386  -0.17288 202 ASN B N   
4188 C CA  . ASN B 202 ? 3.39631 2.45099 3.01361 0.04330  0.01035  -0.16276 202 ASN B CA  
4189 C C   . ASN B 202 ? 3.34247 2.47296 3.01182 0.03219  -0.02043 -0.17751 202 ASN B C   
4190 O O   . ASN B 202 ? 3.31273 2.44162 2.97807 0.00804  -0.01855 -0.19290 202 ASN B O   
4191 C CB  . ASN B 202 ? 3.40021 2.40894 3.01739 0.06570  0.03916  -0.15188 202 ASN B CB  
4192 C CG  . ASN B 202 ? 3.44722 2.36325 2.99488 0.06773  0.07633  -0.14224 202 ASN B CG  
4193 O OD1 . ASN B 202 ? 3.46915 2.32564 2.95642 0.03703  0.09184  -0.15484 202 ASN B OD1 
4194 N ND2 . ASN B 202 ? 3.46594 2.36594 3.02123 0.10368  0.08842  -0.11911 202 ASN B ND2 
4195 N N   . VAL B 203 ? 3.17716 2.36710 2.88865 0.05014  -0.05026 -0.17288 203 VAL B N   
4196 C CA  . VAL B 203 ? 3.10576 2.36580 2.86532 0.04321  -0.08036 -0.18543 203 VAL B CA  
4197 C C   . VAL B 203 ? 3.07586 2.37607 2.89691 0.07716  -0.10297 -0.17285 203 VAL B C   
4198 O O   . VAL B 203 ? 3.12704 2.42067 2.94875 0.10224  -0.11404 -0.15680 203 VAL B O   
4199 C CB  . VAL B 203 ? 3.08744 2.37678 2.83144 0.02605  -0.09864 -0.19382 203 VAL B CB  
4200 C CG1 . VAL B 203 ? 3.01863 2.37493 2.80771 0.01988  -0.12683 -0.20667 203 VAL B CG1 
4201 C CG2 . VAL B 203 ? 3.11947 2.37250 2.81807 -0.00853 -0.07727 -0.20108 203 VAL B CG2 
4202 N N   . ALA B 204 ? 3.01182 2.35152 2.88603 0.07762  -0.11170 -0.17886 204 ALA B N   
4203 C CA  . ALA B 204 ? 3.07291 2.45548 3.02051 0.10578  -0.13531 -0.16575 204 ALA B CA  
4204 C C   . ALA B 204 ? 3.08837 2.53193 3.08048 0.09449  -0.16190 -0.18083 204 ALA B C   
4205 O O   . ALA B 204 ? 2.79457 2.24093 2.77416 0.07125  -0.14933 -0.19760 204 ALA B O   
4206 C CB  . ALA B 204 ? 2.93513 2.29178 2.91807 0.12828  -0.10534 -0.14735 204 ALA B CB  
4207 N N   . HIS B 205 ? 2.90791 2.39560 2.94874 0.11093  -0.20141 -0.17446 205 HIS B N   
4208 C CA  . HIS B 205 ? 2.84051 2.38433 2.92643 0.10359  -0.23045 -0.18670 205 HIS B CA  
4209 C C   . HIS B 205 ? 2.87497 2.44907 3.05219 0.12683  -0.24430 -0.16933 205 HIS B C   
4210 O O   . HIS B 205 ? 2.92399 2.51597 3.13645 0.14492  -0.28280 -0.15613 205 HIS B O   
4211 C CB  . HIS B 205 ? 2.87520 2.43613 2.93015 0.09995  -0.26804 -0.19518 205 HIS B CB  
4212 C CG  . HIS B 205 ? 2.81725 2.42677 2.90169 0.08938  -0.29369 -0.21033 205 HIS B CG  
4213 N ND1 . HIS B 205 ? 2.84829 2.46908 2.90463 0.08915  -0.32714 -0.21769 205 HIS B ND1 
4214 C CD2 . HIS B 205 ? 2.74054 2.38343 2.87331 0.08033  -0.28830 -0.21897 205 HIS B CD2 
4215 C CE1 . HIS B 205 ? 2.77022 2.43155 2.85894 0.07955  -0.34200 -0.23045 205 HIS B CE1 
4216 N NE2 . HIS B 205 ? 2.69536 2.37318 2.83300 0.07371  -0.31943 -0.23152 205 HIS B NE2 
4217 N N   . PRO B 206 ? 2.80935 2.38599 3.02767 0.12769  -0.21441 -0.16686 206 PRO B N   
4218 C CA  . PRO B 206 ? 2.80958 2.41402 3.12739 0.15189  -0.21916 -0.14438 206 PRO B CA  
4219 C C   . PRO B 206 ? 2.78237 2.44672 3.16703 0.15257  -0.27050 -0.14621 206 PRO B C   
4220 O O   . PRO B 206 ? 2.78184 2.47237 3.25531 0.17283  -0.29054 -0.12322 206 PRO B O   
4221 C CB  . PRO B 206 ? 2.76837 2.35344 3.09514 0.14958  -0.16974 -0.14593 206 PRO B CB  
4222 C CG  . PRO B 206 ? 2.75302 2.28183 2.97610 0.12899  -0.13916 -0.16332 206 PRO B CG  
4223 C CD  . PRO B 206 ? 2.71919 2.26488 2.89223 0.10833  -0.17355 -0.18167 206 PRO B CD  
4224 N N   . ALA B 207 ? 2.72567 2.41066 3.07355 0.13109  -0.29285 -0.17104 207 ALA B N   
4225 C CA  . ALA B 207 ? 2.69652 2.42833 3.09534 0.13094  -0.34264 -0.17443 207 ALA B CA  
4226 C C   . ALA B 207 ? 2.78750 2.51561 3.18830 0.14612  -0.39264 -0.16142 207 ALA B C   
4227 O O   . ALA B 207 ? 2.78578 2.54303 3.26625 0.15796  -0.43232 -0.14676 207 ALA B O   
4228 C CB  . ALA B 207 ? 2.51640 2.26200 2.86279 0.10694  -0.35035 -0.20276 207 ALA B CB  
4229 N N   . SER B 208 ? 2.69894 2.38742 3.01219 0.14590  -0.39298 -0.16541 208 SER B N   
4230 C CA  . SER B 208 ? 2.77482 2.44467 3.06705 0.16213  -0.43888 -0.15406 208 SER B CA  
4231 C C   . SER B 208 ? 2.84737 2.48927 3.15402 0.18423  -0.42607 -0.12806 208 SER B C   
4232 O O   . SER B 208 ? 2.92022 2.53974 3.20386 0.20006  -0.46342 -0.11650 208 SER B O   
4233 C CB  . SER B 208 ? 2.79834 2.43512 2.97969 0.15259  -0.44594 -0.17205 208 SER B CB  
4234 O OG  . SER B 208 ? 2.80535 2.41180 2.92516 0.14191  -0.39428 -0.17805 208 SER B OG  
4235 N N   . SER B 209 ? 2.77254 2.40792 3.10861 0.18728  -0.37370 -0.11824 209 SER B N   
4236 C CA  . SER B 209 ? 2.81281 2.42193 3.17232 0.21109  -0.35413 -0.09044 209 SER B CA  
4237 C C   . SER B 209 ? 2.87378 2.42948 3.13548 0.21584  -0.35162 -0.09061 209 SER B C   
4238 O O   . SER B 209 ? 2.91680 2.45838 3.18250 0.23710  -0.38303 -0.07174 209 SER B O   
4239 C CB  . SER B 209 ? 2.81094 2.45536 3.28187 0.23404  -0.39674 -0.06173 209 SER B CB  
4240 O OG  . SER B 209 ? 2.75611 2.44998 3.32300 0.22924  -0.39730 -0.05987 209 SER B OG  
4241 N N   . THR B 210 ? 3.00664 2.53105 3.18216 0.19550  -0.31442 -0.11082 210 THR B N   
4242 C CA  . THR B 210 ? 3.07179 2.54213 3.15608 0.19739  -0.30022 -0.11045 210 THR B CA  
4243 C C   . THR B 210 ? 3.03092 2.46189 3.07623 0.18548  -0.23898 -0.11380 210 THR B C   
4244 O O   . THR B 210 ? 2.95868 2.40031 3.02682 0.17140  -0.21136 -0.12277 210 THR B O   
4245 C CB  . THR B 210 ? 3.08684 2.54950 3.09424 0.18263  -0.32170 -0.13043 210 THR B CB  
4246 O OG1 . THR B 210 ? 3.19544 2.60292 3.12205 0.19043  -0.30935 -0.12432 210 THR B OG1 
4247 C CG2 . THR B 210 ? 3.04865 2.52586 3.03438 0.15142  -0.29420 -0.15445 210 THR B CG2 
4248 N N   . LYS B 211 ? 3.17287 2.55044 3.15218 0.19159  -0.21930 -0.10641 211 LYS B N   
4249 C CA  . LYS B 211 ? 3.16628 2.49341 3.10017 0.18071  -0.16470 -0.10783 211 LYS B CA  
4250 C C   . LYS B 211 ? 3.23381 2.50897 3.08316 0.17997  -0.15473 -0.10617 211 LYS B C   
4251 O O   . LYS B 211 ? 3.28728 2.53163 3.12706 0.20581  -0.15431 -0.08559 211 LYS B O   
4252 C CB  . LYS B 211 ? 3.16859 2.47898 3.15126 0.20395  -0.13641 -0.08517 211 LYS B CB  
4253 C CG  . LYS B 211 ? 3.17719 2.41912 3.09990 0.19602  -0.08026 -0.08544 211 LYS B CG  
4254 C CD  . LYS B 211 ? 3.18179 2.40005 3.14926 0.22637  -0.04849 -0.05844 211 LYS B CD  
4255 C CE  . LYS B 211 ? 3.23800 2.37299 3.13044 0.21990  0.00787  -0.05919 211 LYS B CE  
4256 N NZ  . LYS B 211 ? 3.25631 2.35980 3.18615 0.25377  0.04627  -0.03026 211 LYS B NZ  
4257 N N   . VAL B 212 ? 3.25969 2.52591 3.05346 0.15144  -0.14550 -0.12543 212 VAL B N   
4258 C CA  . VAL B 212 ? 3.32670 2.54545 3.04434 0.14804  -0.13193 -0.12355 212 VAL B CA  
4259 C C   . VAL B 212 ? 3.32331 2.49090 2.99950 0.12625  -0.08452 -0.12713 212 VAL B C   
4260 O O   . VAL B 212 ? 3.27563 2.44997 2.96344 0.10144  -0.06974 -0.14085 212 VAL B O   
4261 C CB  . VAL B 212 ? 3.32970 2.56990 3.01815 0.13303  -0.15129 -0.13756 212 VAL B CB  
4262 C CG1 . VAL B 212 ? 3.40406 2.59304 3.01847 0.14031  -0.13935 -0.12913 212 VAL B CG1 
4263 C CG2 . VAL B 212 ? 3.33501 2.62428 3.06440 0.14807  -0.20016 -0.13947 212 VAL B CG2 
4264 N N   . ASP B 213 ? 3.50356 2.61341 3.12611 0.13550  -0.06268 -0.11471 213 ASP B N   
4265 C CA  . ASP B 213 ? 3.50531 2.55468 3.07987 0.11467  -0.01997 -0.11668 213 ASP B CA  
4266 C C   . ASP B 213 ? 3.54483 2.56464 3.06183 0.09932  -0.00880 -0.11792 213 ASP B C   
4267 O O   . ASP B 213 ? 3.59324 2.59480 3.08122 0.12345  -0.01483 -0.10471 213 ASP B O   
4268 C CB  . ASP B 213 ? 3.52658 2.52343 3.09098 0.14115  0.00561  -0.09720 213 ASP B CB  
4269 C CG  . ASP B 213 ? 3.48820 2.47956 3.08388 0.14042  0.02400  -0.09858 213 ASP B CG  
4270 O OD1 . ASP B 213 ? 3.43893 2.48065 3.07979 0.12882  0.00702  -0.11157 213 ASP B OD1 
4271 O OD2 . ASP B 213 ? 3.51077 2.44114 3.08019 0.15312  0.05869  -0.08589 213 ASP B OD2 
4272 N N   . LYS B 214 ? 3.50757 2.51910 3.00911 0.06004  0.00752  -0.13170 214 LYS B N   
4273 C CA  . LYS B 214 ? 3.54076 2.52820 3.00241 0.04137  0.02311  -0.13023 214 LYS B CA  
4274 C C   . LYS B 214 ? 3.54861 2.47622 2.97731 0.01024  0.05569  -0.13245 214 LYS B C   
4275 O O   . LYS B 214 ? 3.51708 2.44265 2.95804 -0.01477 0.05644  -0.14522 214 LYS B O   
4276 C CB  . LYS B 214 ? 3.51577 2.56047 3.00411 0.02046  0.00560  -0.14168 214 LYS B CB  
4277 C CG  . LYS B 214 ? 3.51977 2.61315 3.02820 0.04859  -0.02806 -0.14107 214 LYS B CG  
4278 C CD  . LYS B 214 ? 3.59521 2.65270 3.05478 0.08133  -0.02809 -0.12474 214 LYS B CD  
4279 C CE  . LYS B 214 ? 3.61372 2.70780 3.08054 0.10594  -0.06691 -0.12586 214 LYS B CE  
4280 N NZ  . LYS B 214 ? 3.70208 2.74908 3.10791 0.14039  -0.07226 -0.11024 214 LYS B NZ  
4281 N N   . LYS B 215 ? 3.64422 2.51648 3.02572 0.01202  0.08120  -0.11996 215 LYS B N   
4282 C CA  . LYS B 215 ? 3.66142 2.47180 3.00901 -0.02135 0.10997  -0.12104 215 LYS B CA  
4283 C C   . LYS B 215 ? 3.66315 2.49496 3.02660 -0.05920 0.11171  -0.12469 215 LYS B C   
4284 O O   . LYS B 215 ? 3.66079 2.54289 3.04762 -0.05172 0.10034  -0.12234 215 LYS B O   
4285 C CB  . LYS B 215 ? 3.71427 2.45010 3.00579 0.00116  0.13968  -0.10346 215 LYS B CB  
4286 C CG  . LYS B 215 ? 3.74056 2.39723 2.98909 -0.02928 0.16946  -0.10433 215 LYS B CG  
4287 C CD  . LYS B 215 ? 3.79140 2.37567 2.98350 -0.00411 0.20065  -0.08562 215 LYS B CD  
4288 C CE  . LYS B 215 ? 3.82930 2.33214 2.97631 -0.04013 0.22981  -0.08631 215 LYS B CE  
4289 N NZ  . LYS B 215 ? 3.87498 2.30129 2.96295 -0.01380 0.26321  -0.06811 215 LYS B NZ  
4290 N N   . ILE B 216 ? 3.61885 2.40847 2.97034 -0.10009 0.12585  -0.12884 216 ILE B N   
4291 C CA  . ILE B 216 ? 3.62247 2.43312 3.00430 -0.14095 0.12682  -0.12887 216 ILE B CA  
4292 C C   . ILE B 216 ? 3.68039 2.42204 3.02638 -0.15485 0.16019  -0.11406 216 ILE B C   
4293 O O   . ILE B 216 ? 3.70314 2.37708 3.01475 -0.17646 0.17065  -0.11709 216 ILE B O   
4294 C CB  . ILE B 216 ? 3.59149 2.41922 3.00409 -0.18447 0.10425  -0.14633 216 ILE B CB  
4295 C CG1 . ILE B 216 ? 3.53088 2.42906 2.98141 -0.17017 0.07424  -0.15996 216 ILE B CG1 
4296 C CG2 . ILE B 216 ? 3.60468 2.45258 3.05898 -0.22824 0.10444  -0.14126 216 ILE B CG2 
4297 C CD1 . ILE B 216 ? 3.51398 2.38628 2.93937 -0.14759 0.06987  -0.16853 216 ILE B CD1 
4298 N N   . VAL B 217 ? 3.66663 2.41790 3.01491 -0.14147 0.17876  -0.09752 217 VAL B N   
4299 C CA  . VAL B 217 ? 3.72240 2.41470 3.04626 -0.15493 0.21455  -0.08038 217 VAL B CA  
4300 C C   . VAL B 217 ? 3.73759 2.47361 3.10736 -0.16592 0.22645  -0.06681 217 VAL B C   
4301 O O   . VAL B 217 ? 3.73619 2.51218 3.10809 -0.13234 0.22364  -0.06203 217 VAL B O   
4302 C CB  . VAL B 217 ? 3.76417 2.39525 3.01962 -0.11036 0.23933  -0.06709 217 VAL B CB  
4303 C CG1 . VAL B 217 ? 3.82337 2.40552 3.05766 -0.11631 0.27968  -0.04613 217 VAL B CG1 
4304 C CG2 . VAL B 217 ? 3.76216 2.33426 2.97485 -0.10630 0.24014  -0.07458 217 VAL B CG2 
4305 N N   . PRO B 218 ? 3.70215 2.42875 3.11025 -0.21162 0.24019  -0.05838 218 PRO B N   
4306 C CA  . PRO B 218 ? 3.72033 2.49053 3.18454 -0.22152 0.25763  -0.04047 218 PRO B CA  
4307 C C   . PRO B 218 ? 3.78587 2.50516 3.21419 -0.19826 0.30651  -0.01452 218 PRO B C   
4308 O O   . PRO B 218 ? 3.81471 2.54630 3.29181 -0.21720 0.33344  0.00588  218 PRO B O   
4309 C CB  . PRO B 218 ? 3.71356 2.49684 3.24621 -0.28442 0.24478  -0.04155 218 PRO B CB  
4310 C CG  . PRO B 218 ? 3.72541 2.43181 3.20782 -0.30583 0.23756  -0.05364 218 PRO B CG  
4311 C CD  . PRO B 218 ? 3.72189 2.38932 3.12222 -0.25578 0.24161  -0.06223 218 PRO B CD  
4312 N N   . GLN C 1   ? 2.33526 3.76211 2.22219 0.21526  -0.24100 -0.40139 1   GLN C N   
4313 C CA  . GLN C 1   ? 2.27633 3.70047 2.15341 0.19516  -0.24047 -0.39960 1   GLN C CA  
4314 C C   . GLN C 1   ? 2.27984 3.76741 2.19326 0.17282  -0.23744 -0.37421 1   GLN C C   
4315 O O   . GLN C 1   ? 2.36956 3.91019 2.30394 0.18803  -0.22281 -0.35329 1   GLN C O   
4316 C CB  . GLN C 1   ? 2.31760 3.72203 2.15815 0.22098  -0.22566 -0.40509 1   GLN C CB  
4317 C CG  . GLN C 1   ? 2.25509 3.64700 2.08081 0.20132  -0.22696 -0.40603 1   GLN C CG  
4318 C CD  . GLN C 1   ? 2.22136 3.56595 2.04105 0.17403  -0.24721 -0.42108 1   GLN C CD  
4319 O OE1 . GLN C 1   ? 2.22943 3.52244 2.02827 0.18208  -0.25760 -0.43859 1   GLN C OE1 
4320 N NE2 . GLN C 1   ? 2.19920 3.56032 2.03805 0.14193  -0.25267 -0.41234 1   GLN C NE2 
4321 N N   . PHE C 2   ? 2.29277 3.77315 2.21364 0.13690  -0.25138 -0.37430 2   PHE C N   
4322 C CA  . PHE C 2   ? 2.28703 3.81930 2.24063 0.10978  -0.25476 -0.35108 2   PHE C CA  
4323 C C   . PHE C 2   ? 2.17358 3.67882 2.11768 0.07594  -0.26549 -0.35638 2   PHE C C   
4324 O O   . PHE C 2   ? 2.11478 3.56453 2.03191 0.07374  -0.27022 -0.37646 2   PHE C O   
4325 C CB  . PHE C 2   ? 2.29162 3.84995 2.27277 0.10005  -0.26617 -0.34164 2   PHE C CB  
4326 C CG  . PHE C 2   ? 2.22508 3.73171 2.19056 0.09262  -0.28120 -0.36273 2   PHE C CG  
4327 C CD1 . PHE C 2   ? 2.12323 3.60390 2.08286 0.05916  -0.29653 -0.36764 2   PHE C CD1 
4328 C CD2 . PHE C 2   ? 2.24722 3.72913 2.20262 0.12031  -0.27896 -0.37634 2   PHE C CD2 
4329 C CE1 . PHE C 2   ? 2.01103 3.44481 1.95593 0.05530  -0.30710 -0.38427 2   PHE C CE1 
4330 C CE2 . PHE C 2   ? 2.18867 3.62631 2.13351 0.11433  -0.29184 -0.39234 2   PHE C CE2 
4331 C CZ  . PHE C 2   ? 2.04901 3.46395 1.98904 0.08271  -0.30480 -0.39557 2   PHE C CZ  
4332 N N   . VAL C 3   ? 2.20372 3.74878 2.17209 0.04912  -0.26983 -0.33592 3   VAL C N   
4333 C CA  . VAL C 3   ? 2.11352 3.63695 2.07481 0.01597  -0.27894 -0.33733 3   VAL C CA  
4334 C C   . VAL C 3   ? 2.03504 3.56122 2.00890 -0.01671 -0.29787 -0.33104 3   VAL C C   
4335 O O   . VAL C 3   ? 2.12492 3.69860 2.12649 -0.02127 -0.30294 -0.31191 3   VAL C O   
4336 C CB  . VAL C 3   ? 2.15746 3.71921 2.13088 0.01114  -0.26819 -0.31796 3   VAL C CB  
4337 C CG1 . VAL C 3   ? 2.05472 3.58913 2.01952 -0.02238 -0.27735 -0.32034 3   VAL C CG1 
4338 C CG2 . VAL C 3   ? 2.22397 3.78165 2.17814 0.04623  -0.24860 -0.32351 3   VAL C CG2 
4339 N N   . LEU C 4   ? 2.18811 3.66121 2.13957 -0.03893 -0.30825 -0.34587 4   LEU C N   
4340 C CA  . LEU C 4   ? 2.15253 3.61304 2.10257 -0.07090 -0.32623 -0.34306 4   LEU C CA  
4341 C C   . LEU C 4   ? 2.12389 3.59281 2.07833 -0.10286 -0.33189 -0.32957 4   LEU C C   
4342 O O   . LEU C 4   ? 2.06969 3.50126 2.00555 -0.11049 -0.32776 -0.33895 4   LEU C O   
4343 C CB  . LEU C 4   ? 2.06703 3.45971 1.98630 -0.07246 -0.33137 -0.36618 4   LEU C CB  
4344 C CG  . LEU C 4   ? 2.05521 3.43463 1.97093 -0.04242 -0.32747 -0.37918 4   LEU C CG  
4345 C CD1 . LEU C 4   ? 2.05069 3.36692 1.94062 -0.04663 -0.33256 -0.39659 4   LEU C CD1 
4346 C CD2 . LEU C 4   ? 2.10652 3.53411 2.04607 -0.03544 -0.33235 -0.36617 4   LEU C CD2 
4347 N N   . SER C 5   ? 2.12440 3.64276 2.10564 -0.12231 -0.34243 -0.30551 5   SER C N   
4348 C CA  . SER C 5   ? 2.12802 3.66318 2.12028 -0.15330 -0.34972 -0.28760 5   SER C CA  
4349 C C   . SER C 5   ? 2.11772 3.60952 2.08744 -0.19075 -0.37205 -0.29207 5   SER C C   
4350 O O   . SER C 5   ? 2.12860 3.63611 2.10562 -0.20596 -0.38953 -0.28194 5   SER C O   
4351 C CB  . SER C 5   ? 2.23172 3.84845 2.27001 -0.15338 -0.34906 -0.25384 5   SER C CB  
4352 O OG  . SER C 5   ? 2.27509 3.92592 2.32689 -0.11570 -0.32529 -0.24988 5   SER C OG  
4353 N N   . GLN C 6   ? 2.16878 3.60334 2.10842 -0.20514 -0.37134 -0.30647 6   GLN C N   
4354 C CA  . GLN C 6   ? 2.19014 3.57407 2.10025 -0.24002 -0.38956 -0.31109 6   GLN C CA  
4355 C C   . GLN C 6   ? 2.24608 3.63782 2.16427 -0.27001 -0.39613 -0.29501 6   GLN C C   
4356 O O   . GLN C 6   ? 2.25846 3.66437 2.18918 -0.26042 -0.38084 -0.29165 6   GLN C O   
4357 C CB  . GLN C 6   ? 2.18054 3.48451 2.04681 -0.23278 -0.38219 -0.33872 6   GLN C CB  
4358 C CG  . GLN C 6   ? 2.17616 3.45814 2.02718 -0.21374 -0.38242 -0.35350 6   GLN C CG  
4359 C CD  . GLN C 6   ? 2.19298 3.39547 2.00181 -0.21138 -0.37640 -0.37488 6   GLN C CD  
4360 O OE1 . GLN C 6   ? 2.21761 3.37584 2.00285 -0.23009 -0.37604 -0.37803 6   GLN C OE1 
4361 N NE2 . GLN C 6   ? 2.18126 3.36556 1.98210 -0.18725 -0.37048 -0.38758 6   GLN C NE2 
4362 N N   . PRO C 7   ? 2.13105 3.51159 2.04058 -0.30728 -0.42004 -0.28433 7   PRO C N   
4363 C CA  . PRO C 7   ? 2.15249 3.53197 2.06697 -0.33871 -0.42866 -0.26946 7   PRO C CA  
4364 C C   . PRO C 7   ? 2.16535 3.47497 2.04352 -0.34037 -0.41666 -0.28950 7   PRO C C   
4365 O O   . PRO C 7   ? 2.15988 3.42065 2.00896 -0.31904 -0.40320 -0.31343 7   PRO C O   
4366 C CB  . PRO C 7   ? 2.19543 3.56307 2.09781 -0.37818 -0.46087 -0.25787 7   PRO C CB  
4367 C CG  . PRO C 7   ? 2.20467 3.53469 2.07418 -0.36753 -0.46541 -0.27739 7   PRO C CG  
4368 C CD  . PRO C 7   ? 2.15591 3.52413 2.04987 -0.32348 -0.44234 -0.28388 7   PRO C CD  
4369 N N   . ASN C 8   ? 2.28047 3.58580 2.16288 -0.36568 -0.42141 -0.27745 8   ASN C N   
4370 C CA  . ASN C 8   ? 2.27907 3.53071 2.13740 -0.36358 -0.40615 -0.29151 8   ASN C CA  
4371 C C   . ASN C 8   ? 2.31843 3.48087 2.12275 -0.38773 -0.41644 -0.30689 8   ASN C C   
4372 O O   . ASN C 8   ? 2.32261 3.42532 2.09425 -0.37179 -0.40089 -0.32787 8   ASN C O   
4373 C CB  . ASN C 8   ? 2.29534 3.58971 2.18775 -0.37351 -0.40152 -0.27011 8   ASN C CB  
4374 C CG  . ASN C 8   ? 2.25998 3.62184 2.19082 -0.33994 -0.38130 -0.26149 8   ASN C CG  
4375 O OD1 . ASN C 8   ? 2.24396 3.63137 2.18251 -0.31319 -0.37508 -0.26689 8   ASN C OD1 
4376 N ND2 . ASN C 8   ? 2.26291 3.65043 2.21454 -0.34043 -0.37055 -0.24811 8   ASN C ND2 
4377 N N   . SER C 9   ? 2.28292 3.43243 2.07562 -0.42559 -0.44235 -0.29539 9   SER C N   
4378 C CA  . SER C 9   ? 2.34377 3.40043 2.07691 -0.44877 -0.45170 -0.31010 9   SER C CA  
4379 C C   . SER C 9   ? 2.39364 3.43821 2.10624 -0.48343 -0.48568 -0.30180 9   SER C C   
4380 O O   . SER C 9   ? 2.39103 3.49654 2.14276 -0.50568 -0.50624 -0.27572 9   SER C O   
4381 C CB  . SER C 9   ? 2.36322 3.38988 2.09142 -0.46575 -0.44615 -0.30559 9   SER C CB  
4382 O OG  . SER C 9   ? 2.36688 3.44695 2.13310 -0.49446 -0.46477 -0.27795 9   SER C OG  
4383 N N   . VAL C 10  ? 2.42267 3.38755 2.07307 -0.48782 -0.49166 -0.32213 10  VAL C N   
4384 C CA  . VAL C 10  ? 2.48422 3.41807 2.09866 -0.52225 -0.52567 -0.31817 10  VAL C CA  
4385 C C   . VAL C 10  ? 2.56739 3.38536 2.10145 -0.53782 -0.52744 -0.33842 10  VAL C C   
4386 O O   . VAL C 10  ? 2.57177 3.33422 2.07358 -0.51092 -0.49973 -0.35956 10  VAL C O   
4387 C CB  . VAL C 10  ? 2.47003 3.42949 2.08536 -0.50764 -0.53297 -0.32147 10  VAL C CB  
4388 C CG1 . VAL C 10  ? 2.40578 3.47797 2.09854 -0.49639 -0.53434 -0.29725 10  VAL C CG1 
4389 C CG2 . VAL C 10  ? 2.45442 3.36953 2.03934 -0.46864 -0.50453 -0.34826 10  VAL C CG2 
4390 N N   . SER C 11  ? 2.59563 3.37536 2.09689 -0.58110 -0.56009 -0.33014 11  SER C N   
4391 C CA  . SER C 11  ? 2.70410 3.36587 2.11993 -0.59895 -0.56501 -0.34855 11  SER C CA  
4392 C C   . SER C 11  ? 2.78031 3.40128 2.14371 -0.62993 -0.60263 -0.34889 11  SER C C   
4393 O O   . SER C 11  ? 2.77243 3.45139 2.17073 -0.65952 -0.63628 -0.32517 11  SER C O   
4394 C CB  . SER C 11  ? 2.77898 3.41354 2.19364 -0.62556 -0.56924 -0.33961 11  SER C CB  
4395 O OG  . SER C 11  ? 2.80772 3.49011 2.25537 -0.66692 -0.60671 -0.31229 11  SER C OG  
4396 N N   . THR C 12  ? 2.89011 3.41128 2.16946 -0.62275 -0.59682 -0.37368 12  THR C N   
4397 C CA  . THR C 12  ? 2.94198 3.41521 2.16020 -0.64720 -0.62997 -0.37762 12  THR C CA  
4398 C C   . THR C 12  ? 3.08039 3.41758 2.19359 -0.66691 -0.63633 -0.39653 12  THR C C   
4399 O O   . THR C 12  ? 3.13504 3.41342 2.22241 -0.65321 -0.60813 -0.40891 12  THR C O   
4400 C CB  . THR C 12  ? 2.88148 3.36988 2.09444 -0.61317 -0.61643 -0.38935 12  THR C CB  
4401 O OG1 . THR C 12  ? 2.88604 3.31985 2.06846 -0.57218 -0.57371 -0.41221 12  THR C OG1 
4402 C CG2 . THR C 12  ? 2.76344 3.38085 2.07373 -0.59620 -0.61416 -0.36996 12  THR C CG2 
4403 N N   . ASN C 13  ? 3.13394 3.41915 2.18413 -0.69905 -0.67411 -0.39775 13  ASN C N   
4404 C CA  . ASN C 13  ? 3.27316 3.41884 2.20803 -0.71775 -0.68387 -0.41750 13  ASN C CA  
4405 C C   . ASN C 13  ? 3.29283 3.37699 2.15658 -0.69100 -0.67072 -0.43950 13  ASN C C   
4406 O O   . ASN C 13  ? 3.21913 3.36882 2.11703 -0.67816 -0.67591 -0.43411 13  ASN C O   
4407 C CB  . ASN C 13  ? 3.36444 3.48341 2.26851 -0.77813 -0.74084 -0.40240 13  ASN C CB  
4408 C CG  . ASN C 13  ? 3.33572 3.52220 2.31618 -0.80604 -0.75574 -0.37601 13  ASN C CG  
4409 O OD1 . ASN C 13  ? 3.35270 3.52397 2.34643 -0.79445 -0.72834 -0.37981 13  ASN C OD1 
4410 N ND2 . ASN C 13  ? 3.31011 3.57511 2.34476 -0.84212 -0.79851 -0.34632 13  ASN C ND2 
4411 N N   . LEU C 14  ? 3.38582 3.34295 2.15037 -0.68109 -0.65190 -0.46291 14  LEU C N   
4412 C CA  . LEU C 14  ? 3.41704 3.30915 2.11146 -0.64889 -0.63054 -0.48341 14  LEU C CA  
4413 C C   . LEU C 14  ? 3.44424 3.33432 2.10084 -0.67369 -0.67246 -0.48058 14  LEU C C   
4414 O O   . LEU C 14  ? 3.55492 3.37948 2.14404 -0.71834 -0.71459 -0.47983 14  LEU C O   
4415 C CB  . LEU C 14  ? 3.55663 3.30330 2.14203 -0.63942 -0.60682 -0.50544 14  LEU C CB  
4416 C CG  . LEU C 14  ? 3.59622 3.26530 2.10563 -0.59857 -0.57374 -0.52546 14  LEU C CG  
4417 C CD1 . LEU C 14  ? 3.66467 3.25057 2.13431 -0.56571 -0.52443 -0.53781 14  LEU C CD1 
4418 C CD2 . LEU C 14  ? 3.71026 3.28270 2.10527 -0.62464 -0.60779 -0.53671 14  LEU C CD2 
4419 N N   . GLY C 15  ? 3.33621 3.29626 2.03561 -0.64565 -0.66236 -0.47812 15  GLY C N   
4420 C CA  . GLY C 15  ? 3.35223 3.32191 2.02576 -0.66416 -0.69849 -0.47341 15  GLY C CA  
4421 C C   . GLY C 15  ? 3.26094 3.36064 2.03371 -0.68750 -0.73232 -0.44487 15  GLY C C   
4422 O O   . GLY C 15  ? 3.30758 3.40753 2.05568 -0.72219 -0.77707 -0.43435 15  GLY C O   
4423 N N   . SER C 16  ? 3.18775 3.39597 2.06966 -0.66924 -0.71238 -0.43049 16  SER C N   
4424 C CA  . SER C 16  ? 3.11162 3.44679 2.09236 -0.68575 -0.73800 -0.40087 16  SER C CA  
4425 C C   . SER C 16  ? 3.01748 3.43736 2.06016 -0.64400 -0.71481 -0.39875 16  SER C C   
4426 O O   . SER C 16  ? 2.99578 3.38736 2.02013 -0.60127 -0.67624 -0.41850 16  SER C O   
4427 C CB  . SER C 16  ? 3.05426 3.45332 2.11266 -0.69566 -0.73352 -0.38340 16  SER C CB  
4428 O OG  . SER C 16  ? 3.14469 3.46828 2.15050 -0.73647 -0.75743 -0.38311 16  SER C OG  
4429 N N   . THR C 17  ? 2.98486 3.50982 2.10336 -0.65700 -0.73920 -0.37206 17  THR C N   
4430 C CA  . THR C 17  ? 2.89237 3.50912 2.08069 -0.62035 -0.72043 -0.36555 17  THR C CA  
4431 C C   . THR C 17  ? 2.79367 3.51605 2.08666 -0.60704 -0.70365 -0.34688 17  THR C C   
4432 O O   . THR C 17  ? 2.78070 3.56977 2.12737 -0.63676 -0.73063 -0.31842 17  THR C O   
4433 C CB  . THR C 17  ? 2.91002 3.56516 2.10317 -0.64108 -0.75803 -0.34782 17  THR C CB  
4434 O OG1 . THR C 17  ? 3.00021 3.55430 2.09076 -0.64611 -0.76824 -0.36798 17  THR C OG1 
4435 C CG2 . THR C 17  ? 2.80977 3.57026 2.08703 -0.60454 -0.73915 -0.33671 17  THR C CG2 
4436 N N   . VAL C 18  ? 2.70849 3.44475 2.02919 -0.56263 -0.65966 -0.36107 18  VAL C N   
4437 C CA  . VAL C 18  ? 2.62355 3.44433 2.02973 -0.54588 -0.63918 -0.34800 18  VAL C CA  
4438 C C   . VAL C 18  ? 2.53995 3.43923 2.00656 -0.50496 -0.61772 -0.34523 18  VAL C C   
4439 O O   . VAL C 18  ? 2.53468 3.40063 1.97310 -0.47482 -0.59829 -0.36434 18  VAL C O   
4440 C CB  . VAL C 18  ? 2.62216 3.39058 2.00991 -0.53137 -0.60806 -0.36513 18  VAL C CB  
4441 C CG1 . VAL C 18  ? 2.63817 3.32949 1.96913 -0.49765 -0.57791 -0.39339 18  VAL C CG1 
4442 C CG2 . VAL C 18  ? 2.53451 3.38904 2.00615 -0.50990 -0.58532 -0.35313 18  VAL C CG2 
4443 N N   . LYS C 19  ? 2.50639 3.50781 2.05489 -0.50336 -0.62085 -0.32004 19  LYS C N   
4444 C CA  . LYS C 19  ? 2.42802 3.50587 2.03729 -0.46353 -0.59869 -0.31594 19  LYS C CA  
4445 C C   . LYS C 19  ? 2.36788 3.48611 2.02627 -0.43942 -0.56884 -0.31512 19  LYS C C   
4446 O O   . LYS C 19  ? 2.36802 3.51127 2.05203 -0.45994 -0.57531 -0.29926 19  LYS C O   
4447 C CB  . LYS C 19  ? 2.40906 3.57417 2.07264 -0.47550 -0.62303 -0.28540 19  LYS C CB  
4448 C CG  . LYS C 19  ? 2.46260 3.59814 2.08359 -0.49658 -0.65353 -0.28381 19  LYS C CG  
4449 C CD  . LYS C 19  ? 2.43783 3.66865 2.12292 -0.50678 -0.67600 -0.24902 19  LYS C CD  
4450 C CE  . LYS C 19  ? 2.49222 3.69561 2.13543 -0.52915 -0.70869 -0.24562 19  LYS C CE  
4451 N NZ  . LYS C 19  ? 2.46836 3.76838 2.17933 -0.54036 -0.73149 -0.20736 19  LYS C NZ  
4452 N N   . LEU C 20  ? 2.32844 3.45165 1.99878 -0.39678 -0.53766 -0.33108 20  LEU C N   
4453 C CA  . LEU C 20  ? 2.27617 3.42802 1.98389 -0.37080 -0.50900 -0.33358 20  LEU C CA  
4454 C C   . LEU C 20  ? 2.21427 3.44461 1.97911 -0.33735 -0.49568 -0.32485 20  LEU C C   
4455 O O   . LEU C 20  ? 2.20073 3.42344 1.95807 -0.31298 -0.48816 -0.33632 20  LEU C O   
4456 C CB  . LEU C 20  ? 2.28282 3.35835 1.94780 -0.35080 -0.48415 -0.36052 20  LEU C CB  
4457 C CG  . LEU C 20  ? 2.35328 3.33594 1.94975 -0.37700 -0.49252 -0.37260 20  LEU C CG  
4458 C CD1 . LEU C 20  ? 2.36360 3.27363 1.91591 -0.35037 -0.46851 -0.39643 20  LEU C CD1 
4459 C CD2 . LEU C 20  ? 2.36491 3.34200 1.96779 -0.39887 -0.49327 -0.36504 20  LEU C CD2 
4460 N N   . SER C 21  ? 2.25273 3.55564 2.07255 -0.33497 -0.49167 -0.30391 21  SER C N   
4461 C CA  . SER C 21  ? 2.20324 3.58083 2.07509 -0.30383 -0.47908 -0.29246 21  SER C CA  
4462 C C   . SER C 21  ? 2.16399 3.53575 2.04198 -0.26458 -0.44757 -0.30989 21  SER C C   
4463 O O   . SER C 21  ? 2.16945 3.49143 2.02165 -0.26342 -0.43572 -0.32586 21  SER C O   
4464 C CB  . SER C 21  ? 2.19179 3.65206 2.11940 -0.31766 -0.48837 -0.25761 21  SER C CB  
4465 O OG  . SER C 21  ? 2.14985 3.67939 2.12473 -0.28429 -0.47287 -0.24538 21  SER C OG  
4466 N N   . CYS C 22  ? 2.21402 3.63634 2.12618 -0.23247 -0.43501 -0.30527 22  CYS C N   
4467 C CA  . CYS C 22  ? 2.13056 3.55210 2.04963 -0.19469 -0.40872 -0.31932 22  CYS C CA  
4468 C C   . CYS C 22  ? 2.23814 3.73323 2.20258 -0.16819 -0.39936 -0.30256 22  CYS C C   
4469 O O   . CYS C 22  ? 2.27230 3.77251 2.24055 -0.14363 -0.39469 -0.30914 22  CYS C O   
4470 C CB  . CYS C 22  ? 2.13078 3.48975 2.01456 -0.17676 -0.40175 -0.34598 22  CYS C CB  
4471 S SG  . CYS C 22  ? 2.09658 3.44621 1.98572 -0.13339 -0.37561 -0.36291 22  CYS C SG  
4472 N N   . LYS C 23  ? 2.04003 3.59144 2.03893 -0.17169 -0.39526 -0.27937 23  LYS C N   
4473 C CA  . LYS C 23  ? 2.09792 3.72468 2.14219 -0.15074 -0.38751 -0.25566 23  LYS C CA  
4474 C C   . LYS C 23  ? 2.10311 3.73265 2.14822 -0.10632 -0.36046 -0.26832 23  LYS C C   
4475 O O   . LYS C 23  ? 2.09952 3.71981 2.13740 -0.09741 -0.34582 -0.27383 23  LYS C O   
4476 C CB  . LYS C 23  ? 2.12914 3.81618 2.21149 -0.17121 -0.39254 -0.22171 23  LYS C CB  
4477 C CG  . LYS C 23  ? 2.16503 3.93489 2.29929 -0.15460 -0.38718 -0.18920 23  LYS C CG  
4478 C CD  . LYS C 23  ? 2.19442 4.02361 2.37016 -0.18355 -0.39929 -0.14998 23  LYS C CD  
4479 C CE  . LYS C 23  ? 2.22842 4.14270 2.46060 -0.16818 -0.39484 -0.11239 23  LYS C CE  
4480 N NZ  . LYS C 23  ? 2.25249 4.22854 2.53166 -0.19970 -0.41034 -0.06860 23  LYS C NZ  
4481 N N   . ARG C 24  ? 2.09769 3.73764 2.14944 -0.07924 -0.35512 -0.27241 24  ARG C N   
4482 C CA  . ARG C 24  ? 2.12361 3.76564 2.17441 -0.03666 -0.33185 -0.28255 24  ARG C CA  
4483 C C   . ARG C 24  ? 2.18369 3.89581 2.27131 -0.01878 -0.31589 -0.25440 24  ARG C C   
4484 O O   . ARG C 24  ? 2.20125 3.97205 2.32673 -0.02867 -0.32273 -0.22463 24  ARG C O   
4485 C CB  . ARG C 24  ? 2.11889 3.74538 2.16423 -0.01473 -0.33256 -0.29535 24  ARG C CB  
4486 C CG  . ARG C 24  ? 2.16180 3.78615 2.20359 0.02906  -0.31135 -0.30542 24  ARG C CG  
4487 C CD  . ARG C 24  ? 2.15102 3.75809 2.18936 0.04742  -0.31459 -0.31690 24  ARG C CD  
4488 N NE  . ARG C 24  ? 2.19403 3.78898 2.22338 0.08800  -0.29678 -0.32847 24  ARG C NE  
4489 C CZ  . ARG C 24  ? 2.20014 3.77554 2.22509 0.10949  -0.29684 -0.33986 24  ARG C CZ  
4490 N NH1 . ARG C 24  ? 2.22077 3.78966 2.25088 0.09627  -0.31203 -0.34080 24  ARG C NH1 
4491 N NH2 . ARG C 24  ? 2.19242 3.75136 2.20462 0.14499  -0.28190 -0.35039 24  ARG C NH2 
4492 N N   . SER C 25  ? 2.06424 3.76953 2.13989 0.00809  -0.29443 -0.26192 25  SER C N   
4493 C CA  . SER C 25  ? 2.13480 3.90110 2.23883 0.02848  -0.27477 -0.23516 25  SER C CA  
4494 C C   . SER C 25  ? 2.18701 3.98636 2.30859 0.06560  -0.26044 -0.22574 25  SER C C   
4495 O O   . SER C 25  ? 2.21293 4.07879 2.37771 0.06707  -0.25769 -0.19230 25  SER C O   
4496 C CB  . SER C 25  ? 2.16366 3.90546 2.24098 0.04430  -0.25687 -0.24698 25  SER C CB  
4497 O OG  . SER C 25  ? 2.17278 3.86102 2.21240 0.07357  -0.24825 -0.27686 25  SER C OG  
4498 N N   . THR C 26  ? 2.19733 3.95077 2.28749 0.09575  -0.25154 -0.25280 26  THR C N   
4499 C CA  . THR C 26  ? 2.25372 4.02761 2.35330 0.13472  -0.23581 -0.24743 26  THR C CA  
4500 C C   . THR C 26  ? 2.21572 3.95179 2.30379 0.13685  -0.24950 -0.26817 26  THR C C   
4501 O O   . THR C 26  ? 2.16602 3.84368 2.22471 0.12144  -0.26345 -0.29461 26  THR C O   
4502 C CB  . THR C 26  ? 2.33499 4.08629 2.40325 0.17511  -0.21013 -0.25910 26  THR C CB  
4503 O OG1 . THR C 26  ? 2.32077 3.99505 2.34225 0.17700  -0.21731 -0.29585 26  THR C OG1 
4504 C CG2 . THR C 26  ? 2.37250 4.15519 2.44649 0.17303  -0.19583 -0.24032 26  THR C CG2 
4505 N N   . GLY C 27  ? 2.47212 4.24358 2.58577 0.15751  -0.24395 -0.25356 27  GLY C N   
4506 C CA  . GLY C 27  ? 2.43828 4.18078 2.54558 0.16261  -0.25521 -0.26942 27  GLY C CA  
4507 C C   . GLY C 27  ? 2.26890 4.02447 2.39503 0.12482  -0.28115 -0.26075 27  GLY C C   
4508 O O   . GLY C 27  ? 2.05728 3.81372 2.18322 0.08890  -0.29540 -0.25590 27  GLY C O   
4509 N N   . ASN C 28  ? 2.54001 4.30238 2.67912 0.13242  -0.28801 -0.25874 28  ASN C N   
4510 C CA  . ASN C 28  ? 2.46950 4.24110 2.62072 0.09803  -0.31348 -0.25038 28  ASN C CA  
4511 C C   . ASN C 28  ? 2.17193 3.87158 2.28131 0.07664  -0.32873 -0.28097 28  ASN C C   
4512 O O   . ASN C 28  ? 2.12575 3.77509 2.20979 0.09616  -0.32390 -0.30622 28  ASN C O   
4513 C CB  . ASN C 28  ? 2.55857 4.35969 2.73590 0.11464  -0.31508 -0.23785 28  ASN C CB  
4514 C CG  . ASN C 28  ? 2.57638 4.33176 2.73158 0.14963  -0.30413 -0.26352 28  ASN C CG  
4515 O OD1 . ASN C 28  ? 2.59800 4.31178 2.72440 0.16941  -0.29071 -0.28495 28  ASN C OD1 
4516 N ND2 . ASN C 28  ? 2.56785 4.33013 2.73649 0.15626  -0.31160 -0.26011 28  ASN C ND2 
4517 N N   . ILE C 29  ? 2.30773 4.00106 2.40992 0.03682  -0.34698 -0.27683 29  ILE C N   
4518 C CA  . ILE C 29  ? 2.26121 3.88566 2.32238 0.01697  -0.35857 -0.30268 29  ILE C CA  
4519 C C   . ILE C 29  ? 2.23799 3.83478 2.28774 0.01933  -0.36920 -0.31320 29  ILE C C   
4520 O O   . ILE C 29  ? 2.21110 3.74698 2.22751 0.01645  -0.37190 -0.33608 29  ILE C O   
4521 C CB  . ILE C 29  ? 2.24291 3.86497 2.29602 -0.02564 -0.37515 -0.29403 29  ILE C CB  
4522 C CG1 . ILE C 29  ? 2.20779 3.75400 2.21519 -0.04082 -0.37999 -0.32076 29  ILE C CG1 
4523 C CG2 . ILE C 29  ? 2.24081 3.89827 2.31212 -0.05197 -0.39746 -0.27123 29  ILE C CG2 
4524 C CD1 . ILE C 29  ? 2.19597 3.70677 2.18678 -0.01909 -0.36165 -0.34051 29  ILE C CD1 
4525 N N   . GLY C 30  ? 2.26016 3.90206 2.33898 0.02607  -0.37406 -0.29473 30  GLY C N   
4526 C CA  . GLY C 30  ? 2.24265 3.86401 2.31318 0.02852  -0.38429 -0.30160 30  GLY C CA  
4527 C C   . GLY C 30  ? 2.24750 3.83953 2.31222 0.06564  -0.37001 -0.32031 30  GLY C C   
4528 O O   . GLY C 30  ? 2.23760 3.82574 2.30615 0.07481  -0.37523 -0.32109 30  GLY C O   
4529 N N   . SER C 31  ? 2.20171 3.77129 2.25612 0.08616  -0.35360 -0.33460 31  SER C N   
4530 C CA  . SER C 31  ? 2.21203 3.74549 2.25655 0.11854  -0.34322 -0.35308 31  SER C CA  
4531 C C   . SER C 31  ? 2.18558 3.65435 2.19634 0.11607  -0.34170 -0.37702 31  SER C C   
4532 O O   . SER C 31  ? 2.19055 3.62356 2.19201 0.13903  -0.33685 -0.39175 31  SER C O   
4533 C CB  . SER C 31  ? 2.27341 3.83836 2.33609 0.15262  -0.32470 -0.34598 31  SER C CB  
4534 O OG  . SER C 31  ? 2.29799 3.92256 2.39654 0.16035  -0.32362 -0.32153 31  SER C OG  
4535 N N   . ASN C 32  ? 2.16282 3.61521 2.15663 0.08856  -0.34654 -0.37943 32  ASN C N   
4536 C CA  . ASN C 32  ? 2.13651 3.53054 2.10181 0.08455  -0.34466 -0.39826 32  ASN C CA  
4537 C C   . ASN C 32  ? 2.08746 3.45148 2.03216 0.05347  -0.35604 -0.40053 32  ASN C C   
4538 O O   . ASN C 32  ? 2.04570 3.43093 1.99032 0.02734  -0.36327 -0.38957 32  ASN C O   
4539 C CB  . ASN C 32  ? 2.15285 3.55098 2.11355 0.08674  -0.33431 -0.39955 32  ASN C CB  
4540 C CG  . ASN C 32  ? 2.20758 3.62809 2.17898 0.11962  -0.32106 -0.39797 32  ASN C CG  
4541 O OD1 . ASN C 32  ? 2.22271 3.67806 2.20236 0.12337  -0.31143 -0.38734 32  ASN C OD1 
4542 N ND2 . ASN C 32  ? 2.24681 3.64506 2.21634 0.14459  -0.31987 -0.40760 32  ASN C ND2 
4543 N N   . TYR C 33  ? 2.15587 3.46868 2.08211 0.05687  -0.35747 -0.41322 33  TYR C N   
4544 C CA  . TYR C 33  ? 1.98405 3.25776 1.88316 0.03236  -0.36417 -0.41658 33  TYR C CA  
4545 C C   . TYR C 33  ? 1.97554 3.23347 1.85903 0.01190  -0.36164 -0.41852 33  TYR C C   
4546 O O   . TYR C 33  ? 1.96769 3.21180 1.85137 0.02164  -0.35259 -0.42508 33  TYR C O   
4547 C CB  . TYR C 33  ? 1.96500 3.18653 1.85054 0.04548  -0.36092 -0.42726 33  TYR C CB  
4548 C CG  . TYR C 33  ? 2.15179 3.38063 2.04805 0.06096  -0.36498 -0.42455 33  TYR C CG  
4549 C CD1 . TYR C 33  ? 2.16941 3.43120 2.07023 0.05056  -0.37494 -0.41397 33  TYR C CD1 
4550 C CD2 . TYR C 33  ? 2.14107 3.34384 2.04429 0.08469  -0.36046 -0.43062 33  TYR C CD2 
4551 C CE1 . TYR C 33  ? 2.17632 3.44585 2.08770 0.06485  -0.37853 -0.41035 33  TYR C CE1 
4552 C CE2 . TYR C 33  ? 2.16279 3.37248 2.07766 0.09901  -0.36399 -0.42699 33  TYR C CE2 
4553 C CZ  . TYR C 33  ? 2.17316 3.41656 2.09164 0.08971  -0.37214 -0.41731 33  TYR C CZ  
4554 O OH  . TYR C 33  ? 2.18082 3.43229 2.11171 0.10416  -0.37552 -0.41262 33  TYR C OH  
4555 N N   . VAL C 34  ? 1.97161 3.22913 1.83985 -0.01744 -0.37115 -0.41229 34  VAL C N   
4556 C CA  . VAL C 34  ? 1.98621 3.22082 1.83584 -0.03964 -0.36998 -0.41403 34  VAL C CA  
4557 C C   . VAL C 34  ? 2.01125 3.18082 1.82256 -0.05103 -0.37037 -0.42313 34  VAL C C   
4558 O O   . VAL C 34  ? 2.02734 3.18047 1.82232 -0.05378 -0.37724 -0.42332 34  VAL C O   
4559 C CB  . VAL C 34  ? 1.99797 3.27502 1.85672 -0.06602 -0.38101 -0.39869 34  VAL C CB  
4560 C CG1 . VAL C 34  ? 2.00713 3.26819 1.85508 -0.08383 -0.37725 -0.39949 34  VAL C CG1 
4561 C CG2 . VAL C 34  ? 1.97694 3.32342 1.87621 -0.05097 -0.37951 -0.38452 34  VAL C CG2 
4562 N N   . SER C 35  ? 1.96881 3.09995 1.76440 -0.05608 -0.36150 -0.42947 35  SER C N   
4563 C CA  . SER C 35  ? 1.99477 3.06042 1.75439 -0.06199 -0.35637 -0.43647 35  SER C CA  
4564 C C   . SER C 35  ? 2.01923 3.06058 1.75698 -0.08717 -0.35581 -0.43613 35  SER C C   
4565 O O   . SER C 35  ? 2.00381 3.05578 1.75648 -0.08650 -0.34913 -0.43541 35  SER C O   
4566 C CB  . SER C 35  ? 1.97664 3.01247 1.74362 -0.03617 -0.34281 -0.44226 35  SER C CB  
4567 O OG  . SER C 35  ? 1.94851 3.01056 1.74309 -0.02351 -0.33833 -0.44254 35  SER C OG  
4568 N N   . TRP C 36  ? 2.05605 3.06150 1.75541 -0.10929 -0.36331 -0.43663 36  TRP C N   
4569 C CA  . TRP C 36  ? 2.08801 3.06489 1.76168 -0.13586 -0.36523 -0.43612 36  TRP C CA  
4570 C C   . TRP C 36  ? 2.11133 3.01663 1.75223 -0.12999 -0.34847 -0.44356 36  TRP C C   
4571 O O   . TRP C 36  ? 2.13893 2.99827 1.74755 -0.12334 -0.34411 -0.44781 36  TRP C O   
4572 C CB  . TRP C 36  ? 2.13021 3.10451 1.77643 -0.16619 -0.38598 -0.43137 36  TRP C CB  
4573 C CG  . TRP C 36  ? 2.11207 3.15803 1.79513 -0.18033 -0.40169 -0.41768 36  TRP C CG  
4574 C CD1 . TRP C 36  ? 2.09419 3.19524 1.80511 -0.17553 -0.41307 -0.40831 36  TRP C CD1 
4575 C CD2 . TRP C 36  ? 2.11044 3.18333 1.81016 -0.20012 -0.40608 -0.40842 36  TRP C CD2 
4576 N NE1 . TRP C 36  ? 2.08220 3.24368 1.82717 -0.19021 -0.42321 -0.39227 36  TRP C NE1 
4577 C CE2 . TRP C 36  ? 2.09165 3.23753 1.83047 -0.20567 -0.41939 -0.39200 36  TRP C CE2 
4578 C CE3 . TRP C 36  ? 2.12358 3.16721 1.81101 -0.21303 -0.39922 -0.41035 36  TRP C CE3 
4579 C CZ2 . TRP C 36  ? 2.08576 3.27706 1.85237 -0.22314 -0.42554 -0.37638 36  TRP C CZ2 
4580 C CZ3 . TRP C 36  ? 2.11703 3.20464 1.83068 -0.23146 -0.40661 -0.39669 36  TRP C CZ3 
4581 C CH2 . TRP C 36  ? 2.09832 3.25955 1.85149 -0.23616 -0.41942 -0.37938 36  TRP C CH2 
4582 N N   . TYR C 37  ? 2.10807 3.00501 1.75780 -0.13141 -0.33794 -0.44300 37  TYR C N   
4583 C CA  . TYR C 37  ? 2.12737 2.96227 1.75388 -0.12516 -0.32005 -0.44589 37  TYR C CA  
4584 C C   . TYR C 37  ? 2.16800 2.96850 1.76381 -0.15218 -0.32110 -0.44548 37  TYR C C   
4585 O O   . TYR C 37  ? 2.16300 2.99958 1.77293 -0.17211 -0.33274 -0.44104 37  TYR C O   
4586 C CB  . TYR C 37  ? 2.08482 2.93407 1.74831 -0.10355 -0.30694 -0.44346 37  TYR C CB  
4587 C CG  . TYR C 37  ? 2.04756 2.92756 1.74170 -0.07771 -0.30772 -0.44378 37  TYR C CG  
4588 C CD1 . TYR C 37  ? 2.04957 2.89624 1.73892 -0.05757 -0.29817 -0.44341 37  TYR C CD1 
4589 C CD2 . TYR C 37  ? 2.01383 2.95443 1.74134 -0.07236 -0.31704 -0.44295 37  TYR C CD2 
4590 C CE1 . TYR C 37  ? 2.01785 2.89049 1.73608 -0.03530 -0.30067 -0.44286 37  TYR C CE1 
4591 C CE2 . TYR C 37  ? 1.98585 2.94850 1.73753 -0.04855 -0.31801 -0.44397 37  TYR C CE2 
4592 C CZ  . TYR C 37  ? 1.98738 2.91576 1.73496 -0.03134 -0.31120 -0.44426 37  TYR C CZ  
4593 O OH  . TYR C 37  ? 1.96163 2.91018 1.73422 -0.00897 -0.31395 -0.44447 37  TYR C OH  
4594 N N   . GLN C 38  ? 2.22019 2.94940 1.77412 -0.15152 -0.30766 -0.44856 38  GLN C N   
4595 C CA  . GLN C 38  ? 2.26730 2.94979 1.78532 -0.17456 -0.30587 -0.44904 38  GLN C CA  
4596 C C   . GLN C 38  ? 2.25548 2.91291 1.78599 -0.16134 -0.28325 -0.44484 38  GLN C C   
4597 O O   . GLN C 38  ? 2.26343 2.87968 1.78384 -0.13967 -0.26412 -0.44345 38  GLN C O   
4598 C CB  . GLN C 38  ? 2.33917 2.95045 1.78995 -0.18445 -0.30731 -0.45542 38  GLN C CB  
4599 C CG  . GLN C 38  ? 2.39834 2.94519 1.80336 -0.20469 -0.30232 -0.45712 38  GLN C CG  
4600 C CD  . GLN C 38  ? 2.49976 2.96731 1.82772 -0.21357 -0.30428 -0.46500 38  GLN C CD  
4601 O OE1 . GLN C 38  ? 2.54818 3.01070 1.85726 -0.20457 -0.30924 -0.46855 38  GLN C OE1 
4602 N NE2 . GLN C 38  ? 2.59058 2.99226 1.87006 -0.23095 -0.30041 -0.46778 38  GLN C NE2 
4603 N N   . HIS C 39  ? 2.27516 2.95927 1.82980 -0.17415 -0.28526 -0.44015 39  HIS C N   
4604 C CA  . HIS C 39  ? 2.32739 2.99191 1.89590 -0.16545 -0.26638 -0.43399 39  HIS C CA  
4605 C C   . HIS C 39  ? 2.43281 3.04498 1.96343 -0.18786 -0.26243 -0.43357 39  HIS C C   
4606 O O   . HIS C 39  ? 2.44231 3.07544 1.97248 -0.21387 -0.27803 -0.43290 39  HIS C O   
4607 C CB  . HIS C 39  ? 2.26202 2.99177 1.88357 -0.16117 -0.27008 -0.42828 39  HIS C CB  
4608 C CG  . HIS C 39  ? 2.31701 3.03051 1.95586 -0.15161 -0.25312 -0.42016 39  HIS C CG  
4609 N ND1 . HIS C 39  ? 2.37417 3.03147 1.99836 -0.13713 -0.23346 -0.41556 39  HIS C ND1 
4610 C CD2 . HIS C 39  ? 2.30160 3.04835 1.97163 -0.15421 -0.25269 -0.41350 39  HIS C CD2 
4611 C CE1 . HIS C 39  ? 2.39451 3.05328 2.04362 -0.13246 -0.22302 -0.40535 39  HIS C CE1 
4612 N NE2 . HIS C 39  ? 2.35359 3.06487 2.02856 -0.14320 -0.23515 -0.40501 39  HIS C NE2 
4613 N N   . HIS C 40  ? 2.49476 3.03844 1.99462 -0.17705 -0.24103 -0.43211 40  HIS C N   
4614 C CA  . HIS C 40  ? 2.62032 3.10430 2.08166 -0.19371 -0.23270 -0.43130 40  HIS C CA  
4615 C C   . HIS C 40  ? 2.67070 3.15850 2.16617 -0.18488 -0.21472 -0.41951 40  HIS C C   
4616 O O   . HIS C 40  ? 2.65074 3.15191 2.17927 -0.15992 -0.20105 -0.41159 40  HIS C O   
4617 C CB  . HIS C 40  ? 2.74234 3.13960 2.13897 -0.18584 -0.21788 -0.43637 40  HIS C CB  
4618 C CG  . HIS C 40  ? 2.86851 3.19799 2.20778 -0.20945 -0.21813 -0.44063 40  HIS C CG  
4619 N ND1 . HIS C 40  ? 2.96171 3.26006 2.30137 -0.21225 -0.20153 -0.43316 40  HIS C ND1 
4620 C CD2 . HIS C 40  ? 2.93368 3.21685 2.21114 -0.23223 -0.23448 -0.45111 40  HIS C CD2 
4621 C CE1 . HIS C 40  ? 3.05702 3.29103 2.33701 -0.23498 -0.20671 -0.43977 40  HIS C CE1 
4622 N NE2 . HIS C 40  ? 3.04324 3.26518 2.28283 -0.24831 -0.22783 -0.45096 40  HIS C NE2 
4623 N N   . GLU C 41  ? 2.73230 3.20904 2.22117 -0.20675 -0.21662 -0.41665 41  GLU C N   
4624 C CA  . GLU C 41  ? 2.76665 3.25067 2.28887 -0.20126 -0.20155 -0.40408 41  GLU C CA  
4625 C C   . GLU C 41  ? 2.87617 3.29761 2.38335 -0.17810 -0.17195 -0.39567 41  GLU C C   
4626 O O   . GLU C 41  ? 2.97210 3.32296 2.42536 -0.17546 -0.16032 -0.40029 41  GLU C O   
4627 C CB  . GLU C 41  ? 2.83215 3.31094 2.34621 -0.23021 -0.20896 -0.40187 41  GLU C CB  
4628 C CG  . GLU C 41  ? 2.84289 3.34677 2.39923 -0.22749 -0.19831 -0.38801 41  GLU C CG  
4629 C CD  . GLU C 41  ? 2.70581 3.29215 2.31767 -0.21862 -0.20853 -0.38409 41  GLU C CD  
4630 O OE1 . GLU C 41  ? 2.68843 3.32736 2.31297 -0.23265 -0.22868 -0.38820 41  GLU C OE1 
4631 O OE2 . GLU C 41  ? 2.63405 3.23058 2.27545 -0.19728 -0.19661 -0.37556 41  GLU C OE2 
4632 N N   . GLY C 42  ? 2.73233 3.17887 2.28643 -0.16074 -0.15973 -0.38145 42  GLY C N   
4633 C CA  . GLY C 42  ? 2.85094 3.24861 2.40329 -0.13710 -0.13126 -0.36723 42  GLY C CA  
4634 C C   . GLY C 42  ? 2.84613 3.22449 2.38726 -0.11270 -0.12255 -0.36770 42  GLY C C   
4635 O O   . GLY C 42  ? 2.95033 3.27164 2.47123 -0.09395 -0.09640 -0.35718 42  GLY C O   
4636 N N   . ARG C 43  ? 2.77937 3.20407 2.33384 -0.11106 -0.14228 -0.37790 43  ARG C N   
4637 C CA  . ARG C 43  ? 2.75561 3.16833 2.30291 -0.08867 -0.13643 -0.37808 43  ARG C CA  
4638 C C   . ARG C 43  ? 2.60928 3.09364 2.20399 -0.08251 -0.15641 -0.38050 43  ARG C C   
4639 O O   . ARG C 43  ? 2.51459 3.05234 2.14146 -0.09420 -0.17271 -0.38256 43  ARG C O   
4640 C CB  . ARG C 43  ? 2.79264 3.15770 2.27427 -0.09617 -0.13910 -0.39357 43  ARG C CB  
4641 C CG  . ARG C 43  ? 2.96509 3.24164 2.39262 -0.08556 -0.11060 -0.38847 43  ARG C CG  
4642 C CD  . ARG C 43  ? 3.03196 3.25736 2.39785 -0.11229 -0.11655 -0.40167 43  ARG C CD  
4643 N NE  . ARG C 43  ? 3.00828 3.22218 2.32622 -0.12668 -0.13742 -0.41965 43  ARG C NE  
4644 C CZ  . ARG C 43  ? 3.08969 3.24066 2.33763 -0.14681 -0.14318 -0.43146 43  ARG C CZ  
4645 N NH1 . ARG C 43  ? 3.20362 3.29339 2.41812 -0.15374 -0.12793 -0.42882 43  ARG C NH1 
4646 N NH2 . ARG C 43  ? 3.06421 3.21107 2.27345 -0.16094 -0.16590 -0.44544 43  ARG C NH2 
4647 N N   . SER C 44  ? 2.49651 2.97905 2.09317 -0.06260 -0.15392 -0.37957 44  SER C N   
4648 C CA  . SER C 44  ? 2.35446 2.89797 1.98993 -0.05623 -0.17317 -0.38336 44  SER C CA  
4649 C C   . SER C 44  ? 2.28350 2.84533 1.89315 -0.06790 -0.19214 -0.40148 44  SER C C   
4650 O O   . SER C 44  ? 2.36994 2.88824 1.93058 -0.07238 -0.18807 -0.40846 44  SER C O   
4651 C CB  . SER C 44  ? 2.36547 2.90448 2.02741 -0.02840 -0.16273 -0.36922 44  SER C CB  
4652 O OG  . SER C 44  ? 2.42357 2.92217 2.04804 -0.01703 -0.15188 -0.37162 44  SER C OG  
4653 N N   . PRO C 45  ? 2.18190 2.80587 1.82154 -0.07273 -0.21292 -0.40813 45  PRO C N   
4654 C CA  . PRO C 45  ? 2.18762 2.83571 1.80967 -0.08390 -0.23120 -0.42135 45  PRO C CA  
4655 C C   . PRO C 45  ? 2.20116 2.82968 1.80627 -0.06760 -0.22840 -0.42335 45  PRO C C   
4656 O O   . PRO C 45  ? 2.17959 2.80795 1.80898 -0.04442 -0.21990 -0.41506 45  PRO C O   
4657 C CB  . PRO C 45  ? 2.13556 2.85396 1.80086 -0.08403 -0.24781 -0.42331 45  PRO C CB  
4658 C CG  . PRO C 45  ? 2.11583 2.84039 1.80709 -0.08367 -0.24099 -0.41450 45  PRO C CG  
4659 C CD  . PRO C 45  ? 2.13268 2.80530 1.81961 -0.06955 -0.22054 -0.40297 45  PRO C CD  
4660 N N   . THR C 46  ? 2.26324 2.87473 1.82635 -0.08107 -0.23707 -0.43278 46  THR C N   
4661 C CA  . THR C 46  ? 2.28162 2.87624 1.82230 -0.06883 -0.23712 -0.43566 46  THR C CA  
4662 C C   . THR C 46  ? 2.25240 2.90707 1.81244 -0.07483 -0.26073 -0.44222 46  THR C C   
4663 O O   . THR C 46  ? 2.21876 2.92639 1.81001 -0.08540 -0.27414 -0.44338 46  THR C O   
4664 C CB  . THR C 46  ? 2.37433 2.89814 1.84572 -0.07884 -0.23002 -0.44064 46  THR C CB  
4665 O OG1 . THR C 46  ? 2.39703 2.93014 1.84276 -0.10979 -0.25207 -0.44995 46  THR C OG1 
4666 C CG2 . THR C 46  ? 2.49051 2.95594 1.94274 -0.07422 -0.20531 -0.43338 46  THR C CG2 
4667 N N   . THR C 47  ? 2.23209 2.87839 1.77316 -0.06659 -0.26428 -0.44479 47  THR C N   
4668 C CA  . THR C 47  ? 2.20582 2.90770 1.76702 -0.06893 -0.28464 -0.44830 47  THR C CA  
4669 C C   . THR C 47  ? 2.25760 2.93517 1.76803 -0.08594 -0.29694 -0.45379 47  THR C C   
4670 O O   . THR C 47  ? 2.30036 2.92367 1.76845 -0.07716 -0.28648 -0.45456 47  THR C O   
4671 C CB  . THR C 47  ? 2.16612 2.89126 1.76380 -0.04025 -0.28030 -0.44374 47  THR C CB  
4672 O OG1 . THR C 47  ? 2.12728 2.86551 1.76612 -0.02662 -0.27130 -0.43765 47  THR C OG1 
4673 C CG2 . THR C 47  ? 2.13712 2.92254 1.75987 -0.04124 -0.29981 -0.44643 47  THR C CG2 
4674 N N   . MET C 48  ? 2.33336 3.05073 1.84759 -0.10991 -0.31937 -0.45560 48  MET C N   
4675 C CA  . MET C 48  ? 2.38423 3.08368 1.85280 -0.13188 -0.33753 -0.45860 48  MET C CA  
4676 C C   . MET C 48  ? 2.35956 3.11431 1.85247 -0.12900 -0.35506 -0.45544 48  MET C C   
4677 O O   . MET C 48  ? 2.39772 3.12744 1.85304 -0.13198 -0.36279 -0.45693 48  MET C O   
4678 C CB  . MET C 48  ? 2.41217 3.11150 1.86475 -0.16672 -0.35341 -0.45847 48  MET C CB  
4679 C CG  . MET C 48  ? 2.45051 3.08610 1.86864 -0.17393 -0.33817 -0.46175 48  MET C CG  
4680 S SD  . MET C 48  ? 2.54668 3.07503 1.87629 -0.17139 -0.32553 -0.46934 48  MET C SD  
4681 C CE  . MET C 48  ? 2.55926 3.06231 1.90974 -0.13074 -0.28800 -0.46506 48  MET C CE  
4682 N N   . ILE C 49  ? 2.29945 3.12682 1.85169 -0.12250 -0.36091 -0.45040 49  ILE C N   
4683 C CA  . ILE C 49  ? 2.27453 3.15919 1.85535 -0.11851 -0.37600 -0.44515 49  ILE C CA  
4684 C C   . ILE C 49  ? 2.21375 3.14146 1.84898 -0.08820 -0.36529 -0.44365 49  ILE C C   
4685 O O   . ILE C 49  ? 2.18480 3.12555 1.84654 -0.08145 -0.35603 -0.44409 49  ILE C O   
4686 C CB  . ILE C 49  ? 2.27679 3.21152 1.87180 -0.14692 -0.39879 -0.43684 49  ILE C CB  
4687 C CG1 . ILE C 49  ? 2.34461 3.23138 1.88208 -0.18056 -0.41453 -0.43777 49  ILE C CG1 
4688 C CG2 . ILE C 49  ? 2.24865 3.24715 1.87966 -0.13980 -0.41171 -0.42792 49  ILE C CG2 
4689 C CD1 . ILE C 49  ? 2.40823 3.26005 1.90058 -0.18319 -0.42439 -0.43992 49  ILE C CD1 
4690 N N   . TYR C 50  ? 2.26927 3.21557 1.91817 -0.07048 -0.36765 -0.44173 50  TYR C N   
4691 C CA  . TYR C 50  ? 2.25206 3.23741 1.94940 -0.04287 -0.36139 -0.44023 50  TYR C CA  
4692 C C   . TYR C 50  ? 2.31359 3.34637 2.03116 -0.03805 -0.37447 -0.43422 50  TYR C C   
4693 O O   . TYR C 50  ? 2.38365 3.40910 2.07459 -0.05211 -0.38633 -0.43127 50  TYR C O   
4694 C CB  . TYR C 50  ? 2.26009 3.20412 1.95662 -0.01786 -0.34442 -0.44263 50  TYR C CB  
4695 C CG  . TYR C 50  ? 2.32368 3.24535 2.00061 -0.00755 -0.34408 -0.44074 50  TYR C CG  
4696 C CD1 . TYR C 50  ? 2.39316 3.26056 2.01576 -0.01897 -0.34145 -0.44239 50  TYR C CD1 
4697 C CD2 . TYR C 50  ? 2.37635 3.32807 2.08579 0.01436  -0.34596 -0.43709 50  TYR C CD2 
4698 C CE1 . TYR C 50  ? 2.49118 3.33672 2.09164 -0.00830 -0.34005 -0.43994 50  TYR C CE1 
4699 C CE2 . TYR C 50  ? 2.43992 3.37342 2.13286 0.02412  -0.34532 -0.43378 50  TYR C CE2 
4700 C CZ  . TYR C 50  ? 2.48309 3.36441 2.12121 0.01305  -0.34200 -0.43496 50  TYR C CZ  
4701 O OH  . TYR C 50  ? 2.52671 3.38826 2.14429 0.02411  -0.34020 -0.43100 50  TYR C OH  
4702 N N   . ARG C 51  ? 2.20495 3.28298 1.96727 -0.01743 -0.37230 -0.43198 51  ARG C N   
4703 C CA  . ARG C 51  ? 2.25741 3.38577 2.04671 -0.00869 -0.38189 -0.42451 51  ARG C CA  
4704 C C   . ARG C 51  ? 2.28853 3.44766 2.07018 -0.03614 -0.39956 -0.41475 51  ARG C C   
4705 O O   . ARG C 51  ? 2.31235 3.47661 2.08344 -0.04196 -0.41106 -0.40897 51  ARG C O   
4706 C CB  . ARG C 51  ? 2.27467 3.38293 2.06014 0.01032  -0.37932 -0.42495 51  ARG C CB  
4707 C CG  . ARG C 51  ? 2.26142 3.36262 2.07406 0.04029  -0.36734 -0.42863 51  ARG C CG  
4708 C CD  . ARG C 51  ? 2.27928 3.39353 2.10934 0.06051  -0.36969 -0.42402 51  ARG C CD  
4709 N NE  . ARG C 51  ? 2.28658 3.35335 2.10412 0.07407  -0.36049 -0.42468 51  ARG C NE  
4710 C CZ  . ARG C 51  ? 2.31393 3.35234 2.10068 0.06994  -0.36043 -0.42167 51  ARG C CZ  
4711 N NH1 . ARG C 51  ? 2.32914 3.37814 2.09091 0.05028  -0.37228 -0.41921 51  ARG C NH1 
4712 N NH2 . ARG C 51  ? 2.34179 3.33947 2.12184 0.08591  -0.34867 -0.41927 51  ARG C NH2 
4713 N N   . ASP C 52  ? 2.24492 3.42344 2.03193 -0.05455 -0.40284 -0.41119 52  ASP C N   
4714 C CA  . ASP C 52  ? 2.26460 3.48118 2.05526 -0.08239 -0.42099 -0.39744 52  ASP C CA  
4715 C C   . ASP C 52  ? 2.27099 3.43942 2.00936 -0.11356 -0.43525 -0.39904 52  ASP C C   
4716 O O   . ASP C 52  ? 2.27004 3.43054 1.99391 -0.14008 -0.44299 -0.39633 52  ASP C O   
4717 C CB  . ASP C 52  ? 2.30392 3.58146 2.13067 -0.07331 -0.43003 -0.38290 52  ASP C CB  
4718 C CG  . ASP C 52  ? 2.28860 3.60989 2.16136 -0.04205 -0.41562 -0.38104 52  ASP C CG  
4719 O OD1 . ASP C 52  ? 2.28897 3.64020 2.18239 -0.04289 -0.41016 -0.37604 52  ASP C OD1 
4720 O OD2 . ASP C 52  ? 2.28175 3.60391 2.16699 -0.01608 -0.40951 -0.38452 52  ASP C OD2 
4721 N N   . ASP C 53  ? 2.30067 3.43324 2.00703 -0.11080 -0.43903 -0.40315 53  ASP C N   
4722 C CA  . ASP C 53  ? 2.32452 3.40911 1.97363 -0.14068 -0.45497 -0.40416 53  ASP C CA  
4723 C C   . ASP C 53  ? 2.35218 3.35808 1.94614 -0.13107 -0.44331 -0.41771 53  ASP C C   
4724 O O   . ASP C 53  ? 2.39480 3.34383 1.93032 -0.15405 -0.45113 -0.42241 53  ASP C O   
4725 C CB  . ASP C 53  ? 2.36121 3.48579 2.01579 -0.15863 -0.48078 -0.38844 53  ASP C CB  
4726 C CG  . ASP C 53  ? 2.37118 3.52648 2.05328 -0.13144 -0.47691 -0.38434 53  ASP C CG  
4727 O OD1 . ASP C 53  ? 2.35706 3.49264 2.04586 -0.10058 -0.45585 -0.39496 53  ASP C OD1 
4728 O OD2 . ASP C 53  ? 2.39866 3.59869 2.09809 -0.14159 -0.49586 -0.36851 53  ASP C OD2 
4729 N N   . GLN C 54  ? 2.35310 3.35042 1.96089 -0.09827 -0.42502 -0.42268 54  GLN C N   
4730 C CA  . GLN C 54  ? 2.38387 3.30920 1.94244 -0.08710 -0.41142 -0.43119 54  GLN C CA  
4731 C C   . GLN C 54  ? 2.38817 3.25919 1.92162 -0.08846 -0.39411 -0.43995 54  GLN C C   
4732 O O   . GLN C 54  ? 2.35052 3.24424 1.91985 -0.08400 -0.38593 -0.44071 54  GLN C O   
4733 C CB  . GLN C 54  ? 2.37391 3.31013 1.96211 -0.05207 -0.39748 -0.42988 54  GLN C CB  
4734 C CG  . GLN C 54  ? 2.38507 3.36523 1.99155 -0.04847 -0.41236 -0.42083 54  GLN C CG  
4735 C CD  . GLN C 54  ? 2.39588 3.36945 2.01700 -0.01630 -0.39897 -0.41948 54  GLN C CD  
4736 O OE1 . GLN C 54  ? 2.39466 3.34802 2.03093 0.00573  -0.37980 -0.42299 54  GLN C OE1 
4737 N NE2 . GLN C 54  ? 2.41489 3.40639 2.03339 -0.01452 -0.41037 -0.41213 54  GLN C NE2 
4738 N N   . ARG C 55  ? 2.44429 3.24088 1.91287 -0.09385 -0.38779 -0.44578 55  ARG C N   
4739 C CA  . ARG C 55  ? 2.46365 3.20334 1.90385 -0.09504 -0.37004 -0.45224 55  ARG C CA  
4740 C C   . ARG C 55  ? 2.50382 3.18728 1.92074 -0.06641 -0.34369 -0.45329 55  ARG C C   
4741 O O   . ARG C 55  ? 2.54896 3.21262 1.93965 -0.05559 -0.34275 -0.45158 55  ARG C O   
4742 C CB  . ARG C 55  ? 2.51986 3.21155 1.89745 -0.12935 -0.38393 -0.45687 55  ARG C CB  
4743 C CG  . ARG C 55  ? 2.59743 3.22817 1.90052 -0.13683 -0.39092 -0.46028 55  ARG C CG  
4744 C CD  . ARG C 55  ? 2.66047 3.24343 1.90115 -0.17449 -0.41007 -0.46498 55  ARG C CD  
4745 N NE  . ARG C 55  ? 2.74638 3.25455 1.90176 -0.18034 -0.41482 -0.47041 55  ARG C NE  
4746 C CZ  . ARG C 55  ? 2.77339 3.29385 1.90788 -0.19417 -0.44010 -0.46648 55  ARG C CZ  
4747 N NH1 . ARG C 55  ? 2.71921 3.32651 1.91596 -0.20269 -0.46183 -0.45539 55  ARG C NH1 
4748 N NH2 . ARG C 55  ? 2.86052 3.30279 1.90775 -0.19862 -0.44295 -0.47264 55  ARG C NH2 
4749 N N   . PRO C 56  ? 2.55737 3.21650 1.98566 -0.05322 -0.32167 -0.45338 56  PRO C N   
4750 C CA  . PRO C 56  ? 2.60839 3.22123 2.02548 -0.02395 -0.29495 -0.44878 56  PRO C CA  
4751 C C   . PRO C 56  ? 2.71728 3.24825 2.05183 -0.02694 -0.28520 -0.45209 56  PRO C C   
4752 O O   . PRO C 56  ? 2.75367 3.24960 2.03443 -0.05378 -0.29697 -0.46001 56  PRO C O   
4753 C CB  . PRO C 56  ? 2.57673 3.18659 2.02661 -0.01590 -0.27782 -0.44569 56  PRO C CB  
4754 C CG  . PRO C 56  ? 2.44538 3.11758 1.93909 -0.03313 -0.29603 -0.44880 56  PRO C CG  
4755 C CD  . PRO C 56  ? 2.47753 3.16058 1.94027 -0.06191 -0.32022 -0.45412 56  PRO C CD  
4756 N N   . ASP C 57  ? 2.88005 3.37820 2.20348 0.00189  -0.26333 -0.44471 57  ASP C N   
4757 C CA  . ASP C 57  ? 2.98951 3.40228 2.23183 0.00731  -0.24628 -0.44601 57  ASP C CA  
4758 C C   . ASP C 57  ? 3.03378 3.39064 2.24605 0.00227  -0.22808 -0.44830 57  ASP C C   
4759 O O   . ASP C 57  ? 3.01820 3.38322 2.27529 0.01887  -0.20842 -0.43916 57  ASP C O   
4760 C CB  . ASP C 57  ? 3.04111 3.43861 2.29036 0.04383  -0.22233 -0.43290 57  ASP C CB  
4761 C CG  . ASP C 57  ? 3.00385 3.45749 2.28727 0.05049  -0.23929 -0.42935 57  ASP C CG  
4762 O OD1 . ASP C 57  ? 3.04116 3.48130 2.27556 0.03838  -0.25493 -0.43496 57  ASP C OD1 
4763 O OD2 . ASP C 57  ? 2.94171 3.45131 2.29987 0.06697  -0.23832 -0.42049 57  ASP C OD2 
4764 N N   . GLY C 58  ? 2.95724 3.25570 2.09318 -0.02162 -0.23609 -0.45944 58  GLY C N   
4765 C CA  . GLY C 58  ? 3.00221 3.24812 2.10683 -0.03157 -0.22326 -0.46321 58  GLY C CA  
4766 C C   . GLY C 58  ? 2.94906 3.22286 2.06168 -0.06969 -0.25149 -0.47232 58  GLY C C   
4767 O O   . GLY C 58  ? 2.97820 3.21540 2.07257 -0.08016 -0.24300 -0.47491 58  GLY C O   
4768 N N   . VAL C 59  ? 2.88192 3.22099 2.02446 -0.08963 -0.28350 -0.47469 59  VAL C N   
4769 C CA  . VAL C 59  ? 2.83027 3.20158 1.98201 -0.12675 -0.31259 -0.47929 59  VAL C CA  
4770 C C   . VAL C 59  ? 2.88765 3.22769 1.97220 -0.15460 -0.34072 -0.48546 59  VAL C C   
4771 O O   . VAL C 59  ? 2.88093 3.25304 1.97232 -0.15171 -0.35497 -0.48266 59  VAL C O   
4772 C CB  . VAL C 59  ? 2.70908 3.18367 1.95192 -0.12727 -0.32675 -0.47298 59  VAL C CB  
4773 C CG1 . VAL C 59  ? 2.67230 3.18236 1.92506 -0.16437 -0.35542 -0.47366 59  VAL C CG1 
4774 C CG2 . VAL C 59  ? 2.65514 3.15333 1.95708 -0.10198 -0.30222 -0.46727 59  VAL C CG2 
4775 N N   . PRO C 60  ? 2.90695 3.18268 1.92478 -0.18246 -0.35087 -0.49292 60  PRO C N   
4776 C CA  . PRO C 60  ? 2.98710 3.22352 1.93291 -0.21130 -0.38091 -0.49821 60  PRO C CA  
4777 C C   . PRO C 60  ? 2.94248 3.26685 1.93951 -0.23721 -0.41902 -0.49037 60  PRO C C   
4778 O O   . PRO C 60  ? 2.86122 3.26888 1.94061 -0.23912 -0.42367 -0.48255 60  PRO C O   
4779 C CB  . PRO C 60  ? 3.06894 3.22552 1.94678 -0.23796 -0.38517 -0.50657 60  PRO C CB  
4780 C CG  . PRO C 60  ? 3.04947 3.17844 1.94283 -0.21046 -0.34520 -0.50653 60  PRO C CG  
4781 C CD  . PRO C 60  ? 2.93250 3.15978 1.93196 -0.18778 -0.33460 -0.49633 60  PRO C CD  
4782 N N   . ASP C 61  ? 3.00453 3.30748 1.94888 -0.25676 -0.44619 -0.49100 61  ASP C N   
4783 C CA  . ASP C 61  ? 2.97238 3.35541 1.96122 -0.28278 -0.48387 -0.47966 61  ASP C CA  
4784 C C   . ASP C 61  ? 2.96381 3.38057 1.98154 -0.31988 -0.50839 -0.47333 61  ASP C C   
4785 O O   . ASP C 61  ? 2.91593 3.41796 1.99502 -0.33637 -0.53324 -0.45901 61  ASP C O   
4786 C CB  . ASP C 61  ? 3.05247 3.39357 1.96846 -0.30048 -0.51042 -0.48045 61  ASP C CB  
4787 C CG  . ASP C 61  ? 3.02302 3.44782 1.98656 -0.32815 -0.55044 -0.46454 61  ASP C CG  
4788 O OD1 . ASP C 61  ? 2.93597 3.44963 1.98143 -0.30820 -0.54537 -0.45404 61  ASP C OD1 
4789 O OD2 . ASP C 61  ? 3.08999 3.49035 2.00915 -0.36995 -0.58735 -0.46097 61  ASP C OD2 
4790 N N   . ARG C 62  ? 2.92131 3.27405 1.89836 -0.33191 -0.50042 -0.48155 62  ARG C N   
4791 C CA  . ARG C 62  ? 2.91319 3.29617 1.91962 -0.36615 -0.52156 -0.47416 62  ARG C CA  
4792 C C   . ARG C 62  ? 2.80075 3.29621 1.91756 -0.35411 -0.51533 -0.46125 62  ARG C C   
4793 O O   . ARG C 62  ? 2.77679 3.33634 1.93911 -0.38126 -0.54156 -0.44677 62  ARG C O   
4794 C CB  . ARG C 62  ? 2.96868 3.26584 1.92215 -0.37079 -0.50433 -0.48556 62  ARG C CB  
4795 C CG  . ARG C 62  ? 3.07522 3.25064 1.91722 -0.36405 -0.49301 -0.50104 62  ARG C CG  
4796 C CD  . ARG C 62  ? 3.15558 3.23843 1.93110 -0.38213 -0.48885 -0.51042 62  ARG C CD  
4797 N NE  . ARG C 62  ? 3.11376 3.18976 1.92048 -0.35303 -0.44785 -0.51270 62  ARG C NE  
4798 C CZ  . ARG C 62  ? 3.05975 3.18324 1.92806 -0.36268 -0.44647 -0.50592 62  ARG C CZ  
4799 N NH1 . ARG C 62  ? 3.03728 3.22199 1.94691 -0.39867 -0.48128 -0.49542 62  ARG C NH1 
4800 N NH2 . ARG C 62  ? 3.02905 3.13948 1.91925 -0.33540 -0.40914 -0.50729 62  ARG C NH2 
4801 N N   . PHE C 63  ? 2.74782 3.26697 1.90728 -0.31321 -0.48113 -0.46468 63  PHE C N   
4802 C CA  . PHE C 63  ? 2.64882 3.26399 1.90333 -0.29738 -0.47273 -0.45490 63  PHE C CA  
4803 C C   . PHE C 63  ? 2.60322 3.29160 1.90307 -0.28736 -0.48498 -0.44507 63  PHE C C   
4804 O O   . PHE C 63  ? 2.61514 3.28150 1.89097 -0.26805 -0.47831 -0.44967 63  PHE C O   
4805 C CB  . PHE C 63  ? 2.60602 3.20836 1.88254 -0.26030 -0.43415 -0.46199 63  PHE C CB  
4806 C CG  . PHE C 63  ? 2.65321 3.17889 1.88383 -0.26522 -0.41770 -0.47023 63  PHE C CG  
4807 C CD1 . PHE C 63  ? 2.72600 3.15635 1.87907 -0.25646 -0.40269 -0.48054 63  PHE C CD1 
4808 C CD2 . PHE C 63  ? 2.62787 3.17584 1.89180 -0.27704 -0.41560 -0.46635 63  PHE C CD2 
4809 C CE1 . PHE C 63  ? 2.77322 3.13082 1.88354 -0.25884 -0.38520 -0.48671 63  PHE C CE1 
4810 C CE2 . PHE C 63  ? 2.67176 3.14960 1.89539 -0.28126 -0.39998 -0.47259 63  PHE C CE2 
4811 C CZ  . PHE C 63  ? 2.74476 3.12678 1.89190 -0.27185 -0.38440 -0.48273 63  PHE C CZ  
4812 N N   . SER C 64  ? 2.59725 3.37275 1.96339 -0.29879 -0.50109 -0.42983 64  SER C N   
4813 C CA  . SER C 64  ? 2.55750 3.40553 1.96925 -0.29104 -0.51355 -0.41745 64  SER C CA  
4814 C C   . SER C 64  ? 2.47948 3.42045 1.97679 -0.28105 -0.50866 -0.40436 64  SER C C   
4815 O O   . SER C 64  ? 2.46988 3.42571 1.98668 -0.29451 -0.50838 -0.39993 64  SER C O   
4816 C CB  . SER C 64  ? 2.61337 3.46138 1.99492 -0.32789 -0.55171 -0.40601 64  SER C CB  
4817 O OG  . SER C 64  ? 2.69874 3.45104 1.98933 -0.33925 -0.55761 -0.41928 64  SER C OG  
4818 N N   . GLY C 65  ? 2.51545 3.51656 2.06112 -0.25638 -0.50410 -0.39765 65  GLY C N   
4819 C CA  . GLY C 65  ? 2.44884 3.53463 2.06970 -0.24255 -0.49775 -0.38510 65  GLY C CA  
4820 C C   . GLY C 65  ? 2.43700 3.59674 2.09821 -0.25404 -0.52035 -0.36237 65  GLY C C   
4821 O O   . GLY C 65  ? 2.47278 3.62086 2.10733 -0.26821 -0.54044 -0.35755 65  GLY C O   
4822 N N   . SER C 66  ? 2.32826 3.56363 2.05296 -0.24698 -0.51625 -0.34668 66  SER C N   
4823 C CA  . SER C 66  ? 2.32034 3.63294 2.09157 -0.25657 -0.53499 -0.31974 66  SER C CA  
4824 C C   . SER C 66  ? 2.30770 3.69754 2.14772 -0.23321 -0.51804 -0.30595 66  SER C C   
4825 O O   . SER C 66  ? 2.29703 3.69932 2.15224 -0.23901 -0.51096 -0.30236 66  SER C O   
4826 C CB  . SER C 66  ? 2.36582 3.67715 2.12010 -0.30425 -0.56798 -0.30238 66  SER C CB  
4827 O OG  . SER C 66  ? 2.38943 3.65672 2.11612 -0.32279 -0.56595 -0.31133 66  SER C OG  
4828 N N   . ILE C 67  ? 2.33049 3.77004 2.20964 -0.20577 -0.51064 -0.29767 67  ILE C N   
4829 C CA  . ILE C 67  ? 2.31913 3.82890 2.25822 -0.17950 -0.49309 -0.28375 67  ILE C CA  
4830 C C   . ILE C 67  ? 2.33704 3.92377 2.32267 -0.19719 -0.51161 -0.24750 67  ILE C C   
4831 O O   . ILE C 67  ? 2.34789 3.95063 2.33657 -0.20676 -0.53018 -0.23488 67  ILE C O   
4832 C CB  . ILE C 67  ? 2.30371 3.81673 2.25658 -0.13592 -0.47181 -0.29622 67  ILE C CB  
4833 C CG1 . ILE C 67  ? 2.28347 3.73442 2.20584 -0.11633 -0.45116 -0.32568 67  ILE C CG1 
4834 C CG2 . ILE C 67  ? 2.30849 3.89802 2.32038 -0.11015 -0.45828 -0.27635 67  ILE C CG2 
4835 C CD1 . ILE C 67  ? 2.27374 3.73847 2.21322 -0.10668 -0.43409 -0.32716 67  ILE C CD1 
4836 N N   . ASP C 68  ? 2.07373 3.70974 2.09732 -0.20160 -0.50666 -0.22810 68  ASP C N   
4837 C CA  . ASP C 68  ? 2.38769 4.10463 2.46513 -0.21679 -0.52132 -0.18764 68  ASP C CA  
4838 C C   . ASP C 68  ? 2.42268 4.20577 2.55531 -0.17632 -0.49268 -0.17331 68  ASP C C   
4839 O O   . ASP C 68  ? 2.37278 4.16386 2.51521 -0.16403 -0.47310 -0.17538 68  ASP C O   
4840 C CB  . ASP C 68  ? 2.37842 4.09877 2.45504 -0.25873 -0.54111 -0.17111 68  ASP C CB  
4841 C CG  . ASP C 68  ? 2.46403 4.27178 2.60242 -0.27679 -0.55803 -0.12386 68  ASP C CG  
4842 O OD1 . ASP C 68  ? 2.47688 4.33121 2.64709 -0.26779 -0.56400 -0.10402 68  ASP C OD1 
4843 O OD2 . ASP C 68  ? 2.47347 4.30536 2.63184 -0.29982 -0.56512 -0.10407 68  ASP C OD2 
4844 N N   . ARG C 69  ? 2.34694 4.17440 2.51233 -0.15462 -0.48949 -0.15859 69  ARG C N   
4845 C CA  . ARG C 69  ? 2.37335 4.26146 2.58806 -0.11411 -0.46154 -0.14268 69  ARG C CA  
4846 C C   . ARG C 69  ? 2.39793 4.35831 2.66354 -0.12404 -0.46005 -0.10369 69  ARG C C   
4847 O O   . ARG C 69  ? 2.41989 4.41312 2.71135 -0.09074 -0.43097 -0.09681 69  ARG C O   
4848 C CB  . ARG C 69  ? 2.37501 4.29507 2.61486 -0.09252 -0.46113 -0.13146 69  ARG C CB  
4849 C CG  . ARG C 69  ? 2.40201 4.39262 2.69749 -0.05295 -0.43478 -0.10619 69  ARG C CG  
4850 C CD  . ARG C 69  ? 2.42163 4.38408 2.70103 -0.01028 -0.40014 -0.13235 69  ARG C CD  
4851 N NE  . ARG C 69  ? 2.41347 4.32383 2.66241 0.01620  -0.39186 -0.16451 69  ARG C NE  
4852 C CZ  . ARG C 69  ? 2.39880 4.23623 2.59960 0.02125  -0.38666 -0.20252 69  ARG C CZ  
4853 N NH1 . ARG C 69  ? 2.34529 4.15031 2.52003 0.00305  -0.38743 -0.21546 69  ARG C NH1 
4854 N NH2 . ARG C 69  ? 2.39198 4.18977 2.57358 0.04517  -0.38063 -0.22560 69  ARG C NH2 
4855 N N   . SER C 70  ? 2.22867 4.21158 2.50691 -0.16901 -0.49090 -0.07728 70  SER C N   
4856 C CA  . SER C 70  ? 2.24715 4.30381 2.58060 -0.18035 -0.49127 -0.03473 70  SER C CA  
4857 C C   . SER C 70  ? 2.25567 4.29422 2.57697 -0.17546 -0.47207 -0.04683 70  SER C C   
4858 O O   . SER C 70  ? 2.27789 4.36670 2.63666 -0.14679 -0.44486 -0.02855 70  SER C O   
4859 C CB  . SER C 70  ? 2.24809 4.32469 2.59385 -0.23461 -0.53409 -0.00438 70  SER C CB  
4860 O OG  . SER C 70  ? 2.24134 4.34229 2.60264 -0.23952 -0.55283 0.01183  70  SER C OG  
4861 N N   . SER C 71  ? 2.24462 4.21133 2.51274 -0.20240 -0.48494 -0.07584 71  SER C N   
4862 C CA  . SER C 71  ? 2.24993 4.19667 2.50529 -0.20208 -0.46974 -0.08664 71  SER C CA  
4863 C C   . SER C 71  ? 2.24124 4.13368 2.45829 -0.16385 -0.43980 -0.12775 71  SER C C   
4864 O O   . SER C 71  ? 2.23892 4.11026 2.44165 -0.16125 -0.42623 -0.13916 71  SER C O   
4865 C CB  . SER C 71  ? 2.24396 4.14158 2.46409 -0.25218 -0.49908 -0.09309 71  SER C CB  
4866 O OG  . SER C 71  ? 2.22541 4.03881 2.38237 -0.26101 -0.50988 -0.13070 71  SER C OG  
4867 N N   . ASN C 72  ? 2.23577 4.10574 2.43749 -0.13575 -0.43104 -0.14816 72  ASN C N   
4868 C CA  . ASN C 72  ? 2.22863 4.04801 2.39725 -0.09981 -0.40603 -0.18431 72  ASN C CA  
4869 C C   . ASN C 72  ? 2.20169 3.94634 2.32012 -0.11823 -0.40977 -0.21446 72  ASN C C   
4870 O O   . ASN C 72  ? 2.20403 3.93020 2.31088 -0.10295 -0.39087 -0.22776 72  ASN C O   
4871 C CB  . ASN C 72  ? 2.26603 4.12701 2.46176 -0.06021 -0.37457 -0.17461 72  ASN C CB  
4872 C CG  . ASN C 72  ? 2.27119 4.08733 2.43784 -0.01965 -0.35277 -0.20701 72  ASN C CG  
4873 O OD1 . ASN C 72  ? 2.25992 4.05404 2.41609 -0.00743 -0.35629 -0.22067 72  ASN C OD1 
4874 N ND2 . ASN C 72  ? 2.29189 4.09297 2.44466 0.00016  -0.33181 -0.21838 72  ASN C ND2 
4875 N N   . SER C 73  ? 2.21874 3.91814 2.30495 -0.15087 -0.43409 -0.22419 73  SER C N   
4876 C CA  . SER C 73  ? 2.19855 3.82593 2.23704 -0.16994 -0.43763 -0.24908 73  SER C CA  
4877 C C   . SER C 73  ? 2.18570 3.75093 2.17915 -0.18545 -0.45459 -0.26810 73  SER C C   
4878 O O   . SER C 73  ? 2.19759 3.77877 2.19492 -0.20379 -0.47619 -0.25403 73  SER C O   
4879 C CB  . SER C 73  ? 2.21036 3.85105 2.25626 -0.20605 -0.45071 -0.23073 73  SER C CB  
4880 O OG  . SER C 73  ? 2.19624 3.76256 2.19312 -0.22626 -0.45555 -0.25390 73  SER C OG  
4881 N N   . ALA C 74  ? 2.28197 3.77684 2.23278 -0.17737 -0.44430 -0.29797 74  ALA C N   
4882 C CA  . ALA C 74  ? 2.27603 3.70274 2.17684 -0.19289 -0.45692 -0.31559 74  ALA C CA  
4883 C C   . ALA C 74  ? 2.26287 3.65110 2.13133 -0.23340 -0.47395 -0.31430 74  ALA C C   
4884 O O   . ALA C 74  ? 2.23083 3.63611 2.11407 -0.24561 -0.47182 -0.30508 74  ALA C O   
4885 C CB  . ALA C 74  ? 2.24758 3.61713 2.12079 -0.16486 -0.43692 -0.34377 74  ALA C CB  
4886 N N   . LEU C 75  ? 2.14941 3.48203 1.97024 -0.25384 -0.49083 -0.32341 75  LEU C N   
4887 C CA  . LEU C 75  ? 2.20124 3.48707 1.98188 -0.29369 -0.50992 -0.32311 75  LEU C CA  
4888 C C   . LEU C 75  ? 2.24260 3.43549 1.95427 -0.29522 -0.50822 -0.34830 75  LEU C C   
4889 O O   . LEU C 75  ? 2.26013 3.43464 1.94858 -0.29182 -0.51641 -0.35259 75  LEU C O   
4890 C CB  . LEU C 75  ? 2.22948 3.55500 2.02420 -0.32929 -0.54316 -0.29608 75  LEU C CB  
4891 C CG  . LEU C 75  ? 2.21028 3.60959 2.06189 -0.34304 -0.54856 -0.26684 75  LEU C CG  
4892 C CD1 . LEU C 75  ? 2.21917 3.68233 2.10696 -0.36463 -0.57653 -0.23382 75  LEU C CD1 
4893 C CD2 . LEU C 75  ? 2.24420 3.60247 2.07004 -0.37384 -0.55618 -0.26865 75  LEU C CD2 
4894 N N   . LEU C 76  ? 2.23517 3.37035 1.91470 -0.29893 -0.49612 -0.36301 76  LEU C N   
4895 C CA  . LEU C 76  ? 2.28383 3.32582 1.89466 -0.30166 -0.49206 -0.38369 76  LEU C CA  
4896 C C   . LEU C 76  ? 2.35542 3.35240 1.91773 -0.34521 -0.51949 -0.37948 76  LEU C C   
4897 O O   . LEU C 76  ? 2.36818 3.36576 1.93528 -0.36834 -0.52598 -0.37226 76  LEU C O   
4898 C CB  . LEU C 76  ? 2.26811 3.26993 1.87089 -0.28147 -0.46341 -0.39911 76  LEU C CB  
4899 C CG  . LEU C 76  ? 2.32216 3.22577 1.85598 -0.28339 -0.45437 -0.41680 76  LEU C CG  
4900 C CD1 . LEU C 76  ? 2.33906 3.21038 1.84141 -0.26638 -0.45206 -0.42558 76  LEU C CD1 
4901 C CD2 . LEU C 76  ? 2.29926 3.17687 1.83889 -0.26316 -0.42614 -0.42594 76  LEU C CD2 
4902 N N   . THR C 77  ? 2.44444 3.40021 1.95802 -0.35691 -0.53671 -0.38350 77  THR C N   
4903 C CA  . THR C 77  ? 2.52363 3.42974 1.98213 -0.39985 -0.56775 -0.37991 77  THR C CA  
4904 C C   . THR C 77  ? 2.58965 3.38375 1.96200 -0.39770 -0.55637 -0.40370 77  THR C C   
4905 O O   . THR C 77  ? 2.59668 3.35603 1.93898 -0.37286 -0.54232 -0.41643 77  THR C O   
4906 C CB  . THR C 77  ? 2.54350 3.48259 2.00404 -0.41811 -0.59949 -0.36436 77  THR C CB  
4907 O OG1 . THR C 77  ? 2.47366 3.51949 2.01940 -0.40721 -0.60036 -0.34220 77  THR C OG1 
4908 C CG2 . THR C 77  ? 2.62118 3.52578 2.03930 -0.46918 -0.63863 -0.35390 77  THR C CG2 
4909 N N   . ILE C 78  ? 2.59242 3.32996 1.92577 -0.42226 -0.56102 -0.40801 78  ILE C N   
4910 C CA  . ILE C 78  ? 2.66362 3.28944 1.91208 -0.42025 -0.54775 -0.42882 78  ILE C CA  
4911 C C   . ILE C 78  ? 2.76166 3.32487 1.94042 -0.46581 -0.58384 -0.42734 78  ILE C C   
4912 O O   . ILE C 78  ? 2.78031 3.34902 1.96768 -0.49828 -0.60259 -0.41724 78  ILE C O   
4913 C CB  . ILE C 78  ? 2.64328 3.24493 1.90088 -0.40539 -0.51730 -0.43671 78  ILE C CB  
4914 C CG1 . ILE C 78  ? 2.54960 3.21469 1.87663 -0.36389 -0.48689 -0.43635 78  ILE C CG1 
4915 C CG2 . ILE C 78  ? 2.72026 3.20551 1.89058 -0.39966 -0.50012 -0.45554 78  ILE C CG2 
4916 C CD1 . ILE C 78  ? 2.52493 3.17465 1.86756 -0.34972 -0.45908 -0.44104 78  ILE C CD1 
4917 N N   . ASP C 79  ? 2.81375 3.31519 1.92154 -0.46889 -0.59473 -0.43663 79  ASP C N   
4918 C CA  . ASP C 79  ? 2.92015 3.34907 1.94791 -0.51190 -0.63136 -0.43738 79  ASP C CA  
4919 C C   . ASP C 79  ? 3.00657 3.30971 1.93939 -0.50928 -0.61323 -0.45935 79  ASP C C   
4920 O O   . ASP C 79  ? 2.99278 3.25941 1.91052 -0.46974 -0.57277 -0.47372 79  ASP C O   
4921 C CB  . ASP C 79  ? 2.95511 3.38158 1.95014 -0.51824 -0.65559 -0.43456 79  ASP C CB  
4922 C CG  . ASP C 79  ? 2.86052 3.40655 1.94954 -0.50339 -0.65879 -0.41600 79  ASP C CG  
4923 O OD1 . ASP C 79  ? 2.80869 3.44097 1.97370 -0.51995 -0.67404 -0.39453 79  ASP C OD1 
4924 O OD2 . ASP C 79  ? 2.83978 3.39268 1.92683 -0.47348 -0.64433 -0.42173 79  ASP C OD2 
4925 N N   . ASN C 80  ? 3.09484 3.33062 1.96398 -0.55177 -0.64383 -0.45987 80  ASN C N   
4926 C CA  . ASN C 80  ? 3.19511 3.30066 1.96285 -0.55360 -0.63051 -0.48006 80  ASN C CA  
4927 C C   . ASN C 80  ? 3.14568 3.24598 1.94426 -0.52066 -0.58397 -0.48729 80  ASN C C   
4928 O O   . ASN C 80  ? 3.15701 3.20143 1.91946 -0.48298 -0.54525 -0.50165 80  ASN C O   
4929 C CB  . ASN C 80  ? 3.27498 3.29134 1.94590 -0.53711 -0.62350 -0.49686 80  ASN C CB  
4930 C CG  . ASN C 80  ? 3.39723 3.26943 1.95050 -0.54076 -0.61228 -0.51658 80  ASN C CG  
4931 O OD1 . ASN C 80  ? 3.44843 3.27718 1.97594 -0.57190 -0.62782 -0.51679 80  ASN C OD1 
4932 N ND2 . ASN C 80  ? 3.44744 3.24332 1.92828 -0.50747 -0.58377 -0.53200 80  ASN C ND2 
4933 N N   . VAL C 81  ? 3.16189 3.32574 2.03204 -0.53537 -0.58853 -0.47409 81  VAL C N   
4934 C CA  . VAL C 81  ? 3.12787 3.30400 2.04097 -0.50687 -0.54838 -0.47688 81  VAL C CA  
4935 C C   . VAL C 81  ? 3.25760 3.30769 2.08053 -0.50034 -0.52557 -0.49432 81  VAL C C   
4936 O O   . VAL C 81  ? 3.36720 3.34053 2.12231 -0.53508 -0.54840 -0.49819 81  VAL C O   
4937 C CB  . VAL C 81  ? 3.06999 3.32795 2.06412 -0.52922 -0.56183 -0.45854 81  VAL C CB  
4938 C CG1 . VAL C 81  ? 3.04601 3.30963 2.07723 -0.50217 -0.52234 -0.46137 81  VAL C CG1 
4939 C CG2 . VAL C 81  ? 2.95996 3.34210 2.04323 -0.52928 -0.57835 -0.43961 81  VAL C CG2 
4940 N N   . GLN C 82  ? 3.21729 3.24396 2.03926 -0.45551 -0.48044 -0.50317 82  GLN C N   
4941 C CA  . GLN C 82  ? 3.33567 3.24575 2.07676 -0.44063 -0.45093 -0.51690 82  GLN C CA  
4942 C C   . GLN C 82  ? 3.33027 3.25207 2.11721 -0.43281 -0.42580 -0.51183 82  GLN C C   
4943 O O   . GLN C 82  ? 3.22571 3.24495 2.10418 -0.43663 -0.43000 -0.49895 82  GLN C O   
4944 C CB  . GLN C 82  ? 3.35185 3.22333 2.05946 -0.39588 -0.41638 -0.52549 82  GLN C CB  
4945 C CG  . GLN C 82  ? 3.40266 3.22822 2.03519 -0.40474 -0.43866 -0.53327 82  GLN C CG  
4946 C CD  . GLN C 82  ? 3.53960 3.26414 2.06951 -0.44585 -0.46986 -0.54233 82  GLN C CD  
4947 O OE1 . GLN C 82  ? 3.63926 3.26375 2.09987 -0.44387 -0.45163 -0.55189 82  GLN C OE1 
4948 N NE2 . GLN C 82  ? 3.52766 3.27725 2.04823 -0.48423 -0.51825 -0.53780 82  GLN C NE2 
4949 N N   . THR C 83  ? 3.37912 3.19752 2.09849 -0.42028 -0.39800 -0.52120 83  THR C N   
4950 C CA  . THR C 83  ? 3.39823 3.21323 2.14926 -0.41706 -0.37627 -0.51582 83  THR C CA  
4951 C C   . THR C 83  ? 3.29266 3.19685 2.14142 -0.38118 -0.34561 -0.50528 83  THR C C   
4952 O O   . THR C 83  ? 3.24059 3.20481 2.15714 -0.38845 -0.34509 -0.49484 83  THR C O   
4953 C CB  . THR C 83  ? 3.53688 3.21826 2.19221 -0.40539 -0.34848 -0.52682 83  THR C CB  
4954 O OG1 . THR C 83  ? 3.63629 3.22424 2.18735 -0.43584 -0.37786 -0.53917 83  THR C OG1 
4955 C CG2 . THR C 83  ? 3.57393 3.24444 2.25398 -0.41226 -0.33442 -0.52031 83  THR C CG2 
4956 N N   . GLU C 84  ? 3.37014 3.28273 2.22607 -0.34305 -0.32122 -0.50684 84  GLU C N   
4957 C CA  . GLU C 84  ? 3.26959 3.25442 2.21031 -0.30874 -0.29305 -0.49664 84  GLU C CA  
4958 C C   . GLU C 84  ? 3.11290 3.22064 2.14391 -0.31494 -0.31493 -0.48820 84  GLU C C   
4959 O O   . GLU C 84  ? 3.02905 3.19956 2.13112 -0.29069 -0.29674 -0.47998 84  GLU C O   
4960 C CB  . GLU C 84  ? 3.29618 3.24506 2.21462 -0.26615 -0.26003 -0.49829 84  GLU C CB  
4961 C CG  . GLU C 84  ? 3.21671 3.20969 2.14495 -0.25816 -0.27493 -0.50059 84  GLU C CG  
4962 C CD  . GLU C 84  ? 3.27665 3.21544 2.12306 -0.28516 -0.30469 -0.51180 84  GLU C CD  
4963 O OE1 . GLU C 84  ? 3.41356 3.25118 2.17319 -0.29771 -0.30285 -0.52049 84  GLU C OE1 
4964 O OE2 . GLU C 84  ? 3.20468 3.19971 2.07173 -0.29411 -0.33065 -0.51129 84  GLU C OE2 
4965 N N   . ASP C 85  ? 3.03152 3.17317 2.06058 -0.34631 -0.35335 -0.48849 85  ASP C N   
4966 C CA  . ASP C 85  ? 2.89597 3.15253 2.00824 -0.34972 -0.37176 -0.47858 85  ASP C CA  
4967 C C   . ASP C 85  ? 2.84067 3.16196 2.02027 -0.36206 -0.37471 -0.46706 85  ASP C C   
4968 O O   . ASP C 85  ? 2.76541 3.18075 2.01234 -0.36411 -0.38800 -0.45749 85  ASP C O   
4969 C CB  . ASP C 85  ? 2.92362 3.19816 2.01604 -0.37944 -0.41134 -0.47791 85  ASP C CB  
4970 C CG  . ASP C 85  ? 2.94449 3.19598 2.00006 -0.36056 -0.40932 -0.48553 85  ASP C CG  
4971 O OD1 . ASP C 85  ? 2.92328 3.15837 1.98087 -0.32253 -0.37690 -0.48947 85  ASP C OD1 
4972 O OD2 . ASP C 85  ? 2.98273 3.23394 2.00930 -0.38429 -0.44093 -0.48540 85  ASP C OD2 
4973 N N   . GLU C 86  ? 2.91248 3.18596 2.07501 -0.36880 -0.36144 -0.46669 86  GLU C N   
4974 C CA  . GLU C 86  ? 2.87860 3.21246 2.10476 -0.37772 -0.36126 -0.45477 86  GLU C CA  
4975 C C   . GLU C 86  ? 2.77175 3.15916 2.06081 -0.34095 -0.33337 -0.45016 86  GLU C C   
4976 O O   . GLU C 86  ? 2.82471 3.17127 2.10771 -0.32095 -0.30454 -0.45031 86  GLU C O   
4977 C CB  . GLU C 86  ? 3.00557 3.26856 2.19259 -0.39691 -0.35627 -0.45500 86  GLU C CB  
4978 C CG  . GLU C 86  ? 2.97763 3.30134 2.22584 -0.41217 -0.36072 -0.44103 86  GLU C CG  
4979 C CD  . GLU C 86  ? 3.10282 3.36072 2.30923 -0.44298 -0.36874 -0.43984 86  GLU C CD  
4980 O OE1 . GLU C 86  ? 3.20255 3.37386 2.33069 -0.46010 -0.38047 -0.45003 86  GLU C OE1 
4981 O OE2 . GLU C 86  ? 3.10925 3.39922 2.35828 -0.45023 -0.36394 -0.42865 86  GLU C OE2 
4982 N N   . ALA C 87  ? 2.80244 3.27886 2.15072 -0.33196 -0.34242 -0.44473 87  ALA C N   
4983 C CA  . ALA C 87  ? 2.69134 3.21749 2.09549 -0.29885 -0.32121 -0.44105 87  ALA C CA  
4984 C C   . ALA C 87  ? 2.57573 3.20178 2.04260 -0.30090 -0.33767 -0.43292 87  ALA C C   
4985 O O   . ALA C 87  ? 2.57216 3.23043 2.04193 -0.32531 -0.36334 -0.42830 87  ALA C O   
4986 C CB  . ALA C 87  ? 2.68319 3.17663 2.06825 -0.26701 -0.30310 -0.44821 87  ALA C CB  
4987 N N   . ALA C 88  ? 2.48853 3.16138 2.00460 -0.27454 -0.32263 -0.42955 88  ALA C N   
4988 C CA  . ALA C 88  ? 2.36894 3.13034 1.94009 -0.26897 -0.33272 -0.42275 88  ALA C CA  
4989 C C   . ALA C 88  ? 2.32801 3.10934 1.90446 -0.24856 -0.33559 -0.42820 88  ALA C C   
4990 O O   . ALA C 88  ? 2.33142 3.07389 1.89144 -0.22634 -0.32087 -0.43510 88  ALA C O   
4991 C CB  . ALA C 88  ? 2.34568 3.14201 1.96039 -0.25200 -0.31713 -0.41699 88  ALA C CB  
4992 N N   . TYR C 89  ? 2.21269 3.05643 1.81502 -0.25555 -0.35384 -0.42252 89  TYR C N   
4993 C CA  . TYR C 89  ? 2.19340 3.06247 1.80429 -0.23827 -0.35870 -0.42575 89  TYR C CA  
4994 C C   . TYR C 89  ? 2.13297 3.08030 1.79975 -0.21989 -0.35715 -0.41920 89  TYR C C   
4995 O O   . TYR C 89  ? 2.11559 3.11014 1.81166 -0.22971 -0.36121 -0.40881 89  TYR C O   
4996 C CB  . TYR C 89  ? 2.23327 3.09970 1.81826 -0.26248 -0.38277 -0.42360 89  TYR C CB  
4997 C CG  . TYR C 89  ? 2.30368 3.08201 1.82102 -0.27684 -0.38431 -0.43287 89  TYR C CG  
4998 C CD1 . TYR C 89  ? 2.35265 3.08735 1.83822 -0.30501 -0.39030 -0.43171 89  TYR C CD1 
4999 C CD2 . TYR C 89  ? 2.32591 3.06128 1.80813 -0.26097 -0.37880 -0.44234 89  TYR C CD2 
5000 C CE1 . TYR C 89  ? 2.42661 3.07228 1.84218 -0.31630 -0.39046 -0.44128 89  TYR C CE1 
5001 C CE2 . TYR C 89  ? 2.39827 3.04772 1.81137 -0.27106 -0.37762 -0.45082 89  TYR C CE2 
5002 C CZ  . TYR C 89  ? 2.45079 3.05312 1.82823 -0.29837 -0.38327 -0.45104 89  TYR C CZ  
5003 O OH  . TYR C 89  ? 2.53204 3.04077 1.83291 -0.30682 -0.38102 -0.46052 89  TYR C OH  
5004 N N   . PHE C 90  ? 2.09155 3.04949 1.77074 -0.19204 -0.35045 -0.42464 90  PHE C N   
5005 C CA  . PHE C 90  ? 2.04152 3.05684 1.76448 -0.16888 -0.34523 -0.42166 90  PHE C CA  
5006 C C   . PHE C 90  ? 2.02578 3.07032 1.76081 -0.15284 -0.35175 -0.42279 90  PHE C C   
5007 O O   . PHE C 90  ? 2.04576 3.05615 1.75586 -0.15090 -0.35440 -0.42852 90  PHE C O   
5008 C CB  . PHE C 90  ? 2.02085 3.01173 1.75039 -0.14653 -0.32739 -0.42697 90  PHE C CB  
5009 C CG  . PHE C 90  ? 2.01303 3.01259 1.75479 -0.15359 -0.32086 -0.42162 90  PHE C CG  
5010 C CD1 . PHE C 90  ? 1.98399 3.04045 1.75722 -0.14602 -0.32118 -0.41558 90  PHE C CD1 
5011 C CD2 . PHE C 90  ? 2.03783 2.98703 1.75790 -0.16594 -0.31280 -0.42175 90  PHE C CD2 
5012 C CE1 . PHE C 90  ? 1.97870 3.04346 1.76136 -0.15182 -0.31490 -0.40981 90  PHE C CE1 
5013 C CE2 . PHE C 90  ? 2.03004 2.98886 1.76311 -0.17251 -0.30696 -0.41553 90  PHE C CE2 
5014 C CZ  . PHE C 90  ? 1.99979 3.01727 1.76413 -0.16595 -0.30863 -0.40960 90  PHE C CZ  
5015 N N   . CYS C 91  ? 2.07557 3.18179 1.84749 -0.13945 -0.35261 -0.41660 91  CYS C N   
5016 C CA  . CYS C 91  ? 2.05664 3.19494 1.84591 -0.11978 -0.35606 -0.41657 91  CYS C CA  
5017 C C   . CYS C 91  ? 2.02408 3.17549 1.83476 -0.08858 -0.34380 -0.42149 91  CYS C C   
5018 O O   . CYS C 91  ? 2.01410 3.17014 1.83267 -0.08481 -0.33574 -0.42097 91  CYS C O   
5019 C CB  . CYS C 91  ? 2.05474 3.25567 1.86747 -0.13133 -0.36923 -0.40163 91  CYS C CB  
5020 S SG  . CYS C 91  ? 2.04304 3.30055 1.88655 -0.14060 -0.36695 -0.38557 91  CYS C SG  
5021 N N   . HIS C 92  ? 2.10192 3.25678 1.91970 -0.06688 -0.34383 -0.42592 92  HIS C N   
5022 C CA  . HIS C 92  ? 2.07927 3.23403 1.91087 -0.03812 -0.33533 -0.43194 92  HIS C CA  
5023 C C   . HIS C 92  ? 2.06660 3.25019 1.91463 -0.01781 -0.33888 -0.43158 92  HIS C C   
5024 O O   . HIS C 92  ? 2.07303 3.24021 1.91379 -0.01638 -0.34353 -0.43355 92  HIS C O   
5025 C CB  . HIS C 92  ? 2.08240 3.17875 1.89877 -0.03162 -0.32865 -0.43963 92  HIS C CB  
5026 C CG  . HIS C 92  ? 2.06462 3.15438 1.89396 -0.00418 -0.32589 -0.44443 92  HIS C CG  
5027 N ND1 . HIS C 92  ? 2.06313 3.12710 1.89146 0.00875  -0.32656 -0.44701 92  HIS C ND1 
5028 C CD2 . HIS C 92  ? 2.05249 3.15491 1.89356 0.01215  -0.32382 -0.44644 92  HIS C CD2 
5029 C CE1 . HIS C 92  ? 2.04922 3.11114 1.89146 0.03032  -0.32661 -0.44974 92  HIS C CE1 
5030 N NE2 . HIS C 92  ? 2.04516 3.12736 1.89211 0.03260  -0.32553 -0.45050 92  HIS C NE2 
5031 N N   . SER C 93  ? 1.98331 3.20746 1.85126 -0.00068 -0.33533 -0.42848 93  SER C N   
5032 C CA  . SER C 93  ? 1.97316 3.22331 1.85741 0.02272  -0.33602 -0.42787 93  SER C CA  
5033 C C   . SER C 93  ? 1.96637 3.19872 1.85080 0.04971  -0.32956 -0.43710 93  SER C C   
5034 O O   . SER C 93  ? 1.96888 3.19834 1.84824 0.05225  -0.32386 -0.43881 93  SER C O   
5035 C CB  . SER C 93  ? 1.97151 3.28492 1.87764 0.02223  -0.33644 -0.41335 93  SER C CB  
5036 O OG  . SER C 93  ? 1.98214 3.31193 1.88829 -0.00749 -0.34620 -0.40232 93  SER C OG  
5037 N N   . TYR C 94  ? 1.91639 3.13490 1.80497 0.06889  -0.33199 -0.44233 94  TYR C N   
5038 C CA  . TYR C 94  ? 1.91605 3.10956 1.80213 0.09254  -0.33032 -0.45098 94  TYR C CA  
5039 C C   . TYR C 94  ? 1.92315 3.14346 1.82115 0.11791  -0.32904 -0.45049 94  TYR C C   
5040 O O   . TYR C 94  ? 1.92970 3.17528 1.84139 0.11921  -0.33154 -0.44444 94  TYR C O   
5041 C CB  . TYR C 94  ? 1.91349 3.05692 1.79478 0.09368  -0.33499 -0.45611 94  TYR C CB  
5042 C CG  . TYR C 94  ? 1.91560 3.03447 1.79822 0.11687  -0.33844 -0.46244 94  TYR C CG  
5043 C CD1 . TYR C 94  ? 1.92526 3.02529 1.79666 0.12141  -0.33854 -0.46686 94  TYR C CD1 
5044 C CD2 . TYR C 94  ? 1.91185 3.02452 1.80521 0.13320  -0.34338 -0.46328 94  TYR C CD2 
5045 C CE1 . TYR C 94  ? 1.96500 3.03692 1.83271 0.14009  -0.34552 -0.47252 94  TYR C CE1 
5046 C CE2 . TYR C 94  ? 2.00458 3.09075 1.89794 0.15253  -0.34933 -0.46847 94  TYR C CE2 
5047 C CZ  . TYR C 94  ? 2.03397 3.09798 1.91292 0.15518  -0.35141 -0.47337 94  TYR C CZ  
5048 O OH  . TYR C 94  ? 2.06270 3.09447 1.93677 0.17193  -0.36104 -0.47846 94  TYR C OH  
5049 N N   . SER C 95  ? 1.92692 3.13814 1.81677 0.13843  -0.32529 -0.45652 95  SER C N   
5050 C CA  . SER C 95  ? 2.01448 3.24167 1.90962 0.16619  -0.32194 -0.45727 95  SER C CA  
5051 C C   . SER C 95  ? 2.04474 3.23372 1.91795 0.18591  -0.32230 -0.46848 95  SER C C   
5052 O O   . SER C 95  ? 2.04408 3.22870 1.90008 0.18405  -0.31744 -0.47031 95  SER C O   
5053 C CB  . SER C 95  ? 2.07533 3.36114 1.98318 0.17006  -0.31138 -0.44469 95  SER C CB  
5054 O OG  . SER C 95  ? 2.08952 3.38374 1.98487 0.16830  -0.30274 -0.44307 95  SER C OG  
5055 N N   . THR C 96  ? 1.99825 3.15771 1.87041 0.20370  -0.32950 -0.47522 96  THR C N   
5056 C CA  . THR C 96  ? 2.04592 3.16650 1.89376 0.22516  -0.33283 -0.48580 96  THR C CA  
5057 C C   . THR C 96  ? 2.00843 3.09389 1.83298 0.21404  -0.33786 -0.49116 96  THR C C   
5058 O O   . THR C 96  ? 2.05249 3.12838 1.84973 0.22557  -0.33328 -0.49627 96  THR C O   
5059 C CB  . THR C 96  ? 2.14717 3.29298 1.98489 0.25135  -0.31918 -0.48533 96  THR C CB  
5060 O OG1 . THR C 96  ? 2.15460 3.33617 1.98809 0.24461  -0.30586 -0.47816 96  THR C OG1 
5061 C CG2 . THR C 96  ? 2.18828 3.37112 2.05338 0.26244  -0.31461 -0.47705 96  THR C CG2 
5062 N N   . GLY C 97  ? 2.04249 3.10734 1.87670 0.19259  -0.34652 -0.48862 97  GLY C N   
5063 C CA  . GLY C 97  ? 1.99243 3.02431 1.81027 0.18078  -0.35261 -0.49054 97  GLY C CA  
5064 C C   . GLY C 97  ? 1.96400 3.02100 1.77519 0.16556  -0.34197 -0.48649 97  GLY C C   
5065 O O   . GLY C 97  ? 1.97928 3.01335 1.77176 0.16057  -0.34513 -0.48842 97  GLY C O   
5066 N N   . MET C 98  ? 2.07137 3.17462 1.89797 0.15670  -0.33115 -0.47937 98  MET C N   
5067 C CA  . MET C 98  ? 2.02659 3.15680 1.85107 0.14037  -0.32202 -0.47305 98  MET C CA  
5068 C C   . MET C 98  ? 1.97739 3.12111 1.82039 0.11531  -0.32210 -0.46559 98  MET C C   
5069 O O   . MET C 98  ? 1.96711 3.13966 1.82530 0.11387  -0.32091 -0.46085 98  MET C O   
5070 C CB  . MET C 98  ? 2.13448 3.30994 1.95682 0.15465  -0.30888 -0.46840 98  MET C CB  
5071 C CG  . MET C 98  ? 2.12917 3.32865 1.94630 0.14229  -0.29961 -0.46093 98  MET C CG  
5072 S SD  . MET C 98  ? 2.10776 3.26085 1.89241 0.14236  -0.30355 -0.46886 98  MET C SD  
5073 C CE  . MET C 98  ? 2.01561 3.15980 1.81451 0.10683  -0.30821 -0.46264 98  MET C CE  
5074 N N   . TYR C 99  ? 1.94770 3.06779 1.78674 0.09580  -0.32379 -0.46394 99  TYR C N   
5075 C CA  . TYR C 99  ? 1.93584 3.05652 1.78295 0.07210  -0.32292 -0.45811 99  TYR C CA  
5076 C C   . TYR C 99  ? 1.93827 3.08873 1.78389 0.05480  -0.31622 -0.45129 99  TYR C C   
5077 O O   . TYR C 99  ? 1.94324 3.07979 1.78047 0.04633  -0.31390 -0.45025 99  TYR C O   
5078 C CB  . TYR C 99  ? 1.93387 3.00657 1.77868 0.06383  -0.32663 -0.45809 99  TYR C CB  
5079 C CG  . TYR C 99  ? 1.93085 2.97447 1.78248 0.07860  -0.33400 -0.46046 99  TYR C CG  
5080 C CD1 . TYR C 99  ? 1.93963 2.96578 1.78783 0.09639  -0.34175 -0.46510 99  TYR C CD1 
5081 C CD2 . TYR C 99  ? 1.92383 2.95402 1.78297 0.07432  -0.33385 -0.45703 99  TYR C CD2 
5082 C CE1 . TYR C 99  ? 1.93805 2.93746 1.79574 0.10804  -0.35058 -0.46490 99  TYR C CE1 
5083 C CE2 . TYR C 99  ? 1.92048 2.92677 1.78965 0.08809  -0.33991 -0.45616 99  TYR C CE2 
5084 C CZ  . TYR C 99  ? 1.92586 2.91838 1.79709 0.10415  -0.34897 -0.45941 99  TYR C CZ  
5085 O OH  . TYR C 99  ? 1.99665 2.96560 1.88102 0.11622  -0.35705 -0.45636 99  TYR C OH  
5086 N N   . ILE C 100 ? 2.00938 3.20210 1.86564 0.04848  -0.31430 -0.44434 100 ILE C N   
5087 C CA  . ILE C 100 ? 2.01238 3.24009 1.87289 0.03180  -0.30963 -0.43413 100 ILE C CA  
5088 C C   . ILE C 100 ? 2.01350 3.23045 1.87274 0.00249  -0.31441 -0.42982 100 ILE C C   
5089 O O   . ILE C 100 ? 2.01333 3.22005 1.87220 -0.00235 -0.32043 -0.43122 100 ILE C O   
5090 C CB  . ILE C 100 ? 2.05220 3.33679 1.92856 0.04320  -0.30522 -0.42433 100 ILE C CB  
5091 C CG1 . ILE C 100 ? 2.15906 3.44323 2.02894 0.07632  -0.29915 -0.43075 100 ILE C CG1 
5092 C CG2 . ILE C 100 ? 2.05792 3.38142 1.94281 0.02798  -0.29984 -0.41006 100 ILE C CG2 
5093 C CD1 . ILE C 100 ? 2.23563 3.57393 2.12065 0.09304  -0.29021 -0.41903 100 ILE C CD1 
5094 N N   . PHE C 101 ? 2.01931 3.23527 1.87443 -0.01676 -0.31177 -0.42453 101 PHE C N   
5095 C CA  . PHE C 101 ? 2.02926 3.22586 1.87629 -0.04524 -0.31593 -0.42123 101 PHE C CA  
5096 C C   . PHE C 101 ? 2.03560 3.27503 1.89337 -0.06555 -0.31807 -0.40731 101 PHE C C   
5097 O O   . PHE C 101 ? 2.08357 3.36851 1.95712 -0.05627 -0.31320 -0.39854 101 PHE C O   
5098 C CB  . PHE C 101 ? 2.03433 3.18135 1.86693 -0.05224 -0.31136 -0.42574 101 PHE C CB  
5099 C CG  . PHE C 101 ? 2.03404 3.13314 1.85744 -0.04278 -0.31137 -0.43364 101 PHE C CG  
5100 C CD1 . PHE C 101 ? 2.02339 3.11134 1.85186 -0.01931 -0.31107 -0.43897 101 PHE C CD1 
5101 C CD2 . PHE C 101 ? 2.04914 3.11191 1.85711 -0.05709 -0.31174 -0.43427 101 PHE C CD2 
5102 C CE1 . PHE C 101 ? 2.02249 3.07011 1.84834 -0.01102 -0.31147 -0.44202 101 PHE C CE1 
5103 C CE2 . PHE C 101 ? 2.05036 3.07130 1.85185 -0.04601 -0.30891 -0.43806 101 PHE C CE2 
5104 C CZ  . PHE C 101 ? 2.03432 3.05078 1.84857 -0.02331 -0.30892 -0.44055 101 PHE C CZ  
5105 N N   . GLY C 102 ? 2.14054 3.36221 1.98797 -0.09331 -0.32537 -0.40399 102 GLY C N   
5106 C CA  . GLY C 102 ? 2.15114 3.40749 2.00885 -0.11804 -0.33185 -0.38889 102 GLY C CA  
5107 C C   . GLY C 102 ? 2.15951 3.40043 2.01151 -0.13476 -0.32721 -0.38524 102 GLY C C   
5108 O O   . GLY C 102 ? 2.15386 3.36615 1.99770 -0.12442 -0.31746 -0.39276 102 GLY C O   
5109 N N   . GLY C 103 ? 2.13320 3.39400 1.99126 -0.16253 -0.33603 -0.37150 103 GLY C N   
5110 C CA  . GLY C 103 ? 2.14233 3.39561 1.99934 -0.18058 -0.33276 -0.36472 103 GLY C CA  
5111 C C   . GLY C 103 ? 2.16843 3.35373 1.99395 -0.20041 -0.33478 -0.37363 103 GLY C C   
5112 O O   . GLY C 103 ? 2.17147 3.33423 1.99193 -0.20512 -0.32641 -0.37362 103 GLY C O   
5113 N N   . GLY C 104 ? 2.17990 3.33028 1.98191 -0.21101 -0.34478 -0.38038 104 GLY C N   
5114 C CA  . GLY C 104 ? 2.21411 3.29341 1.97903 -0.22708 -0.34444 -0.38878 104 GLY C CA  
5115 C C   . GLY C 104 ? 2.25115 3.32081 2.00373 -0.26341 -0.35855 -0.37918 104 GLY C C   
5116 O O   . GLY C 104 ? 2.25911 3.31913 2.01294 -0.27639 -0.35413 -0.37360 104 GLY C O   
5117 N N   . THR C 105 ? 2.18175 3.25259 1.92195 -0.28129 -0.37735 -0.37616 105 THR C N   
5118 C CA  . THR C 105 ? 2.22472 3.28236 1.94993 -0.31939 -0.39642 -0.36611 105 THR C CA  
5119 C C   . THR C 105 ? 2.27537 3.24111 1.94541 -0.33191 -0.39345 -0.37975 105 THR C C   
5120 O O   . THR C 105 ? 2.29567 3.21093 1.92956 -0.32141 -0.38985 -0.39393 105 THR C O   
5121 C CB  . THR C 105 ? 2.23896 3.32784 1.96848 -0.33522 -0.42041 -0.35644 105 THR C CB  
5122 O OG1 . THR C 105 ? 2.19219 3.36526 1.97378 -0.31763 -0.41832 -0.34273 105 THR C OG1 
5123 C CG2 . THR C 105 ? 2.28473 3.36549 2.00377 -0.37790 -0.44470 -0.34217 105 THR C CG2 
5124 N N   . LYS C 106 ? 2.40539 3.34842 2.06836 -0.35271 -0.39334 -0.37423 106 LYS C N   
5125 C CA  . LYS C 106 ? 2.46915 3.32212 2.07937 -0.36282 -0.38700 -0.38554 106 LYS C CA  
5126 C C   . LYS C 106 ? 2.53768 3.34823 2.10376 -0.39751 -0.41295 -0.38512 106 LYS C C   
5127 O O   . LYS C 106 ? 2.59156 3.42387 2.16914 -0.42882 -0.43311 -0.37044 106 LYS C O   
5128 C CB  . LYS C 106 ? 2.50150 3.34761 2.12468 -0.36784 -0.37409 -0.37932 106 LYS C CB  
5129 C CG  . LYS C 106 ? 2.58425 3.33838 2.15866 -0.36861 -0.35925 -0.39022 106 LYS C CG  
5130 C CD  . LYS C 106 ? 2.72909 3.43012 2.26221 -0.40612 -0.37706 -0.38794 106 LYS C CD  
5131 C CE  . LYS C 106 ? 2.82167 3.41854 2.29165 -0.40265 -0.36166 -0.40164 106 LYS C CE  
5132 N NZ  . LYS C 106 ? 2.93459 3.46933 2.35559 -0.43948 -0.38024 -0.40126 106 LYS C NZ  
5133 N N   . LEU C 107 ? 2.56344 3.31173 2.07761 -0.39244 -0.41341 -0.39987 107 LEU C N   
5134 C CA  . LEU C 107 ? 2.66508 3.35971 2.12421 -0.42402 -0.43881 -0.40226 107 LEU C CA  
5135 C C   . LEU C 107 ? 2.79102 3.39182 2.19283 -0.43918 -0.43252 -0.41026 107 LEU C C   
5136 O O   . LEU C 107 ? 2.82586 3.37153 2.20209 -0.41505 -0.40462 -0.42205 107 LEU C O   
5137 C CB  . LEU C 107 ? 2.63019 3.29885 2.05468 -0.40986 -0.44134 -0.41415 107 LEU C CB  
5138 C CG  . LEU C 107 ? 2.72952 3.32911 2.08311 -0.43902 -0.46671 -0.41973 107 LEU C CG  
5139 C CD1 . LEU C 107 ? 2.75530 3.39958 2.12868 -0.47989 -0.50451 -0.40123 107 LEU C CD1 
5140 C CD2 . LEU C 107 ? 2.71274 3.29548 2.03833 -0.41934 -0.46522 -0.43026 107 LEU C CD2 
5141 N N   . THR C 108 ? 2.69838 3.28071 2.08149 -0.47893 -0.45849 -0.40181 108 THR C N   
5142 C CA  . THR C 108 ? 2.81606 3.30728 2.14308 -0.49716 -0.45574 -0.40816 108 THR C CA  
5143 C C   . THR C 108 ? 2.89648 3.30316 2.14102 -0.52246 -0.47988 -0.41813 108 THR C C   
5144 O O   . THR C 108 ? 2.90537 3.34184 2.15226 -0.54889 -0.51415 -0.40929 108 THR C O   
5145 C CB  . THR C 108 ? 2.83807 3.36416 2.20323 -0.52515 -0.46766 -0.39024 108 THR C CB  
5146 O OG1 . THR C 108 ? 2.74424 3.35810 2.18600 -0.50231 -0.44888 -0.37932 108 THR C OG1 
5147 C CG2 . THR C 108 ? 2.96767 3.39984 2.28071 -0.53694 -0.45767 -0.39731 108 THR C CG2 
5148 N N   . VAL C 109 ? 2.94066 3.24097 2.11112 -0.51372 -0.46180 -0.43496 109 VAL C N   
5149 C CA  . VAL C 109 ? 3.04936 3.24998 2.12558 -0.53610 -0.48152 -0.44693 109 VAL C CA  
5150 C C   . VAL C 109 ? 3.16636 3.29793 2.20212 -0.56882 -0.49247 -0.44543 109 VAL C C   
5151 O O   . VAL C 109 ? 3.23326 3.31854 2.25754 -0.55354 -0.46267 -0.44996 109 VAL C O   
5152 C CB  . VAL C 109 ? 3.08652 3.20779 2.09891 -0.50093 -0.45168 -0.46614 109 VAL C CB  
5153 C CG1 . VAL C 109 ? 3.21285 3.21778 2.11553 -0.52327 -0.46970 -0.47960 109 VAL C CG1 
5154 C CG2 . VAL C 109 ? 3.01664 3.20580 2.06923 -0.47186 -0.44507 -0.46634 109 VAL C CG2 
5155 N N   . LEU C 110 ? 3.13400 3.25832 2.14974 -0.61459 -0.53625 -0.43715 110 LEU C N   
5156 C CA  . LEU C 110 ? 3.26805 3.33538 2.25305 -0.65169 -0.55386 -0.43234 110 LEU C CA  
5157 C C   . LEU C 110 ? 3.58803 3.50973 2.45049 -0.66261 -0.55884 -0.45298 110 LEU C C   
5158 O O   . LEU C 110 ? 3.71231 3.59176 2.51881 -0.69637 -0.59820 -0.45464 110 LEU C O   
5159 C CB  . LEU C 110 ? 3.25772 3.39772 2.29228 -0.69702 -0.60025 -0.40807 110 LEU C CB  
5160 C CG  . LEU C 110 ? 3.10326 3.38086 2.25492 -0.68748 -0.59341 -0.38482 110 LEU C CG  
5161 C CD1 . LEU C 110 ? 2.95035 3.29638 2.14818 -0.73204 -0.63911 -0.35681 110 LEU C CD1 
5162 C CD2 . LEU C 110 ? 3.07641 3.35460 2.25825 -0.67142 -0.56064 -0.38325 110 LEU C CD2 
5163 N N   . GLY C 111 ? 3.57503 3.41697 2.39335 -0.63309 -0.51820 -0.46752 111 GLY C N   
5164 C CA  . GLY C 111 ? 3.70881 3.40349 2.40734 -0.64024 -0.51647 -0.48611 111 GLY C CA  
5165 C C   . GLY C 111 ? 3.77473 3.41278 2.44901 -0.67555 -0.53155 -0.48121 111 GLY C C   
5166 O O   . GLY C 111 ? 3.90144 3.42084 2.47468 -0.70000 -0.54959 -0.49310 111 GLY C O   
5167 N N   . GLN C 112 ? 3.88794 3.60823 2.65252 -0.67817 -0.52448 -0.46346 112 GLN C N   
5168 C CA  . GLN C 112 ? 4.00112 3.69464 2.76736 -0.71244 -0.53988 -0.45313 112 GLN C CA  
5169 C C   . GLN C 112 ? 3.94498 3.71478 2.76142 -0.76153 -0.59308 -0.43147 112 GLN C C   
5170 O O   . GLN C 112 ? 3.73715 3.61004 2.61668 -0.76029 -0.60766 -0.42006 112 GLN C O   
5171 C CB  . GLN C 112 ? 3.92958 3.67361 2.76883 -0.68541 -0.50014 -0.44335 112 GLN C CB  
5172 C CG  . GLN C 112 ? 3.63785 3.31116 2.43745 -0.63791 -0.44700 -0.45853 112 GLN C CG  
5173 C CD  . GLN C 112 ? 3.72171 3.24172 2.40993 -0.64639 -0.44047 -0.47339 112 GLN C CD  
5174 O OE1 . GLN C 112 ? 3.69776 3.17376 2.36151 -0.68512 -0.46627 -0.46871 112 GLN C OE1 
5175 N NE2 . GLN C 112 ? 3.78917 3.22484 2.40805 -0.60930 -0.40527 -0.49020 112 GLN C NE2 
5176 N N   . PRO C 113 ? 3.70191 3.42344 2.49340 -0.80537 -0.62316 -0.42308 113 PRO C N   
5177 C CA  . PRO C 113 ? 3.66914 3.46508 2.51382 -0.85412 -0.67509 -0.39707 113 PRO C CA  
5178 C C   . PRO C 113 ? 3.57310 3.50490 2.54324 -0.84856 -0.66468 -0.37001 113 PRO C C   
5179 O O   . PRO C 113 ? 3.54875 3.50696 2.55830 -0.81255 -0.62114 -0.37222 113 PRO C O   
5180 C CB  . PRO C 113 ? 3.81550 3.49505 2.58011 -0.90061 -0.70765 -0.39903 113 PRO C CB  
5181 C CG  . PRO C 113 ? 3.89596 3.48592 2.61509 -0.87139 -0.66166 -0.41648 113 PRO C CG  
5182 C CD  . PRO C 113 ? 3.84923 3.43650 2.55534 -0.81366 -0.61307 -0.43625 113 PRO C CD  
5183 N N   . LYS C 114 ? 3.45563 3.47371 2.48767 -0.88526 -0.70623 -0.34204 114 LYS C N   
5184 C CA  . LYS C 114 ? 3.36843 3.51591 2.51643 -0.88285 -0.69964 -0.31277 114 LYS C CA  
5185 C C   . LYS C 114 ? 3.44195 3.55714 2.59789 -0.88914 -0.68385 -0.30747 114 LYS C C   
5186 O O   . LYS C 114 ? 3.56830 3.57301 2.65109 -0.91670 -0.69886 -0.31573 114 LYS C O   
5187 C CB  . LYS C 114 ? 3.32281 3.55542 2.52828 -0.92548 -0.74943 -0.27946 114 LYS C CB  
5188 C CG  . LYS C 114 ? 3.20711 3.52749 2.45302 -0.90965 -0.75541 -0.27350 114 LYS C CG  
5189 C CD  . LYS C 114 ? 3.15296 3.57639 2.47663 -0.94716 -0.79776 -0.23255 114 LYS C CD  
5190 C CE  . LYS C 114 ? 3.02653 3.54819 2.40194 -0.92608 -0.79766 -0.22333 114 LYS C CE  
5191 N NZ  . LYS C 114 ? 2.97450 3.60376 2.43374 -0.95877 -0.83446 -0.17852 114 LYS C NZ  
5192 N N   . SER C 115 ? 3.25915 3.46955 2.50239 -0.86311 -0.65355 -0.29331 115 SER C N   
5193 C CA  . SER C 115 ? 3.32115 3.51079 2.57935 -0.86231 -0.63250 -0.28776 115 SER C CA  
5194 C C   . SER C 115 ? 3.21999 3.54550 2.59076 -0.85238 -0.62114 -0.25890 115 SER C C   
5195 O O   . SER C 115 ? 3.11291 3.52088 2.53384 -0.81544 -0.59688 -0.25928 115 SER C O   
5196 C CB  . SER C 115 ? 3.37157 3.48013 2.57752 -0.82011 -0.58450 -0.31608 115 SER C CB  
5197 O OG  . SER C 115 ? 3.41190 3.51855 2.64666 -0.81451 -0.56055 -0.30735 115 SER C OG  
5198 N N   . THR C 116 ? 3.10008 3.44513 2.50744 -0.88535 -0.63885 -0.23334 116 THR C N   
5199 C CA  . THR C 116 ? 3.00888 3.47057 2.51561 -0.87713 -0.62587 -0.20430 116 THR C CA  
5200 C C   . THR C 116 ? 3.02620 3.46543 2.53718 -0.84662 -0.58183 -0.21339 116 THR C C   
5201 O O   . THR C 116 ? 3.14137 3.46960 2.58421 -0.84788 -0.57112 -0.23261 116 THR C O   
5202 C CB  . THR C 116 ? 3.03725 3.53259 2.58414 -0.92785 -0.66658 -0.16875 116 THR C CB  
5203 O OG1 . THR C 116 ? 3.16325 3.53627 2.63645 -0.96326 -0.68745 -0.17774 116 THR C OG1 
5204 C CG2 . THR C 116 ? 3.03092 3.59320 2.60840 -0.95210 -0.70621 -0.14813 116 THR C CG2 
5205 N N   . PRO C 117 ? 3.01308 3.55334 2.60070 -0.81806 -0.55526 -0.19907 117 PRO C N   
5206 C CA  . PRO C 117 ? 3.03412 3.55749 2.62776 -0.78801 -0.51425 -0.20638 117 PRO C CA  
5207 C C   . PRO C 117 ? 3.10317 3.61361 2.71620 -0.81500 -0.51936 -0.18574 117 PRO C C   
5208 O O   . PRO C 117 ? 3.07139 3.64303 2.73442 -0.84605 -0.54594 -0.15582 117 PRO C O   
5209 C CB  . PRO C 117 ? 2.87516 3.51395 2.54016 -0.75050 -0.49016 -0.19770 117 PRO C CB  
5210 C CG  . PRO C 117 ? 2.78009 3.51242 2.49981 -0.77222 -0.52027 -0.17070 117 PRO C CG  
5211 C CD  . PRO C 117 ? 2.86650 3.53747 2.53365 -0.80813 -0.55943 -0.17657 117 PRO C CD  
5212 N N   . THR C 118 ? 2.98931 3.42091 2.56528 -0.80192 -0.49250 -0.19955 118 THR C N   
5213 C CA  . THR C 118 ? 3.05019 3.46451 2.64372 -0.82107 -0.49024 -0.18185 118 THR C CA  
5214 C C   . THR C 118 ? 2.96639 3.46352 2.62760 -0.78831 -0.45536 -0.16892 118 THR C C   
5215 O O   . THR C 118 ? 2.95729 3.43924 2.60663 -0.74935 -0.42084 -0.18610 118 THR C O   
5216 C CB  . THR C 118 ? 3.19682 3.46990 2.70671 -0.82650 -0.48115 -0.20267 118 THR C CB  
5217 O OG1 . THR C 118 ? 3.27231 3.46314 2.71230 -0.86001 -0.51719 -0.21420 118 THR C OG1 
5218 C CG2 . THR C 118 ? 3.25626 3.51303 2.78784 -0.84349 -0.47591 -0.18370 118 THR C CG2 
5219 N N   . LEU C 119 ? 2.84577 3.42930 2.57690 -0.80442 -0.46518 -0.13697 119 LEU C N   
5220 C CA  . LEU C 119 ? 2.76087 3.43251 2.55689 -0.77555 -0.43634 -0.12175 119 LEU C CA  
5221 C C   . LEU C 119 ? 2.77920 3.41492 2.58082 -0.78023 -0.41945 -0.11163 119 LEU C C   
5222 O O   . LEU C 119 ? 2.85296 3.41639 2.62498 -0.81289 -0.43590 -0.10780 119 LEU C O   
5223 C CB  . LEU C 119 ? 2.70390 3.49915 2.57495 -0.78430 -0.45224 -0.09038 119 LEU C CB  
5224 C CG  . LEU C 119 ? 2.64973 3.51580 2.53905 -0.76118 -0.45280 -0.09576 119 LEU C CG  
5225 C CD1 . LEU C 119 ? 2.70149 3.51911 2.54369 -0.78089 -0.48215 -0.11085 119 LEU C CD1 
5226 C CD2 . LEU C 119 ? 2.59059 3.58099 2.55882 -0.76147 -0.45740 -0.06066 119 LEU C CD2 
5227 N N   . THR C 120 ? 2.81146 3.49696 2.65019 -0.74731 -0.38719 -0.10680 120 THR C N   
5228 C CA  . THR C 120 ? 2.85661 3.51800 2.70680 -0.74600 -0.36697 -0.09577 120 THR C CA  
5229 C C   . THR C 120 ? 2.73750 3.49949 2.65063 -0.71804 -0.34442 -0.07888 120 THR C C   
5230 O O   . THR C 120 ? 2.66808 3.46441 2.58467 -0.68397 -0.32779 -0.09188 120 THR C O   
5231 C CB  . THR C 120 ? 2.96439 3.51539 2.75257 -0.72851 -0.34306 -0.12109 120 THR C CB  
5232 O OG1 . THR C 120 ? 3.08402 3.53243 2.80526 -0.75533 -0.36379 -0.13627 120 THR C OG1 
5233 C CG2 . THR C 120 ? 3.00043 3.53538 2.80760 -0.72303 -0.31905 -0.10693 120 THR C CG2 
5234 N N   . MET C 121 ? 2.88386 3.68967 2.84354 -0.73263 -0.34470 -0.04978 121 MET C N   
5235 C CA  . MET C 121 ? 2.77419 3.67838 2.79174 -0.70987 -0.32675 -0.03006 121 MET C CA  
5236 C C   . MET C 121 ? 2.80577 3.68682 2.83184 -0.70033 -0.30185 -0.02188 121 MET C C   
5237 O O   . MET C 121 ? 2.90197 3.71116 2.90828 -0.72153 -0.30385 -0.01912 121 MET C O   
5238 C CB  . MET C 121 ? 2.70328 3.69912 2.77787 -0.73156 -0.34676 0.00348  121 MET C CB  
5239 C CG  . MET C 121 ? 2.64602 3.68860 2.72667 -0.73490 -0.36768 0.00196  121 MET C CG  
5240 S SD  . MET C 121 ? 2.55224 3.64042 2.62752 -0.68519 -0.34538 -0.02065 121 MET C SD  
5241 C CE  . MET C 121 ? 2.47070 3.64618 2.59836 -0.65893 -0.31860 0.00348  121 MET C CE  
5242 N N   . PHE C 122 ? 2.65092 3.59219 2.70526 -0.66833 -0.27909 -0.01712 122 PHE C N   
5243 C CA  . PHE C 122 ? 2.66476 3.59530 2.73145 -0.65547 -0.25491 -0.00753 122 PHE C CA  
5244 C C   . PHE C 122 ? 2.55460 3.58704 2.67142 -0.63768 -0.24462 0.01433  122 PHE C C   
5245 O O   . PHE C 122 ? 2.47576 3.56122 2.59697 -0.61337 -0.24145 0.00627  122 PHE C O   
5246 C CB  . PHE C 122 ? 2.70896 3.57244 2.73624 -0.62815 -0.23340 -0.03254 122 PHE C CB  
5247 C CG  . PHE C 122 ? 2.84395 3.59624 2.82568 -0.64201 -0.23079 -0.04427 122 PHE C CG  
5248 C CD1 . PHE C 122 ? 2.91444 3.63175 2.90321 -0.66612 -0.23149 -0.02648 122 PHE C CD1 
5249 C CD2 . PHE C 122 ? 2.90534 3.58529 2.83474 -0.62957 -0.22641 -0.07243 122 PHE C CD2 
5250 C CE1 . PHE C 122 ? 3.04976 3.65743 2.99029 -0.67671 -0.22726 -0.03788 122 PHE C CE1 
5251 C CE2 . PHE C 122 ? 3.04100 3.61317 2.92170 -0.63906 -0.22101 -0.08306 122 PHE C CE2 
5252 C CZ  . PHE C 122 ? 3.11571 3.64941 2.99999 -0.66228 -0.22118 -0.06642 122 PHE C CZ  
5253 N N   . PRO C 123 ? 2.59246 3.65127 2.74397 -0.64813 -0.23890 0.04181  123 PRO C N   
5254 C CA  . PRO C 123 ? 2.49890 3.64927 2.69163 -0.62969 -0.22731 0.06321  123 PRO C CA  
5255 C C   . PRO C 123 ? 2.49020 3.62727 2.67568 -0.60161 -0.20329 0.05772  123 PRO C C   
5256 O O   . PRO C 123 ? 2.56075 3.62055 2.71975 -0.59999 -0.19394 0.04471  123 PRO C O   
5257 C CB  . PRO C 123 ? 2.50572 3.68563 2.73890 -0.65840 -0.23501 0.09769  123 PRO C CB  
5258 C CG  . PRO C 123 ? 2.61342 3.69646 2.82125 -0.68229 -0.23870 0.09144  123 PRO C CG  
5259 C CD  . PRO C 123 ? 2.67669 3.68512 2.83099 -0.68037 -0.24597 0.05670  123 PRO C CD  
5260 N N   . PRO C 124 ? 2.49223 3.70107 2.69909 -0.57873 -0.19288 0.06894  124 PRO C N   
5261 C CA  . PRO C 124 ? 2.48199 3.67975 2.68195 -0.55410 -0.17413 0.06586  124 PRO C CA  
5262 C C   . PRO C 124 ? 2.53759 3.69658 2.75006 -0.56687 -0.16381 0.08321  124 PRO C C   
5263 O O   . PRO C 124 ? 2.55686 3.72649 2.79446 -0.59102 -0.16877 0.10560  124 PRO C O   
5264 C CB  . PRO C 124 ? 2.39791 3.68317 2.61740 -0.53373 -0.16933 0.07969  124 PRO C CB  
5265 C CG  . PRO C 124 ? 2.36177 3.69316 2.58610 -0.53658 -0.18243 0.07754  124 PRO C CG  
5266 C CD  . PRO C 124 ? 2.41562 3.71524 2.64813 -0.57155 -0.19789 0.08341  124 PRO C CD  
5267 N N   . SER C 125 ? 2.54982 3.66442 2.74714 -0.55010 -0.14932 0.07490  125 SER C N   
5268 C CA  . SER C 125 ? 2.60403 3.67722 2.81227 -0.55738 -0.13619 0.09119  125 SER C CA  
5269 C C   . SER C 125 ? 2.54602 3.68373 2.78916 -0.55217 -0.12869 0.12008  125 SER C C   
5270 O O   . SER C 125 ? 2.47632 3.67585 2.72324 -0.53395 -0.12946 0.12146  125 SER C O   
5271 C CB  . SER C 125 ? 2.65218 3.65905 2.83557 -0.53920 -0.12243 0.07571  125 SER C CB  
5272 O OG  . SER C 125 ? 2.71208 3.65642 2.85903 -0.54197 -0.12739 0.04941  125 SER C OG  
5273 N N   . PRO C 126 ? 2.58057 3.70192 2.84624 -0.56740 -0.12115 0.14358  126 PRO C N   
5274 C CA  . PRO C 126 ? 2.52608 3.70896 2.82463 -0.56320 -0.11409 0.17305  126 PRO C CA  
5275 C C   . PRO C 126 ? 2.48817 3.68800 2.77995 -0.53567 -0.10512 0.17164  126 PRO C C   
5276 O O   . PRO C 126 ? 2.42932 3.69490 2.73246 -0.52520 -0.10524 0.18568  126 PRO C O   
5277 C CB  . PRO C 126 ? 2.57809 3.71946 2.89681 -0.58372 -0.10628 0.19443  126 PRO C CB  
5278 C CG  . PRO C 126 ? 2.65299 3.73030 2.95221 -0.60533 -0.11560 0.17924  126 PRO C CG  
5279 C CD  . PRO C 126 ? 2.67041 3.71650 2.93038 -0.58990 -0.11953 0.14520  126 PRO C CD  
5280 N N   . GLU C 127 ? 2.59985 3.74045 2.87188 -0.52364 -0.09790 0.15652  127 GLU C N   
5281 C CA  . GLU C 127 ? 2.56895 3.72175 2.83723 -0.50047 -0.09271 0.15814  127 GLU C CA  
5282 C C   . GLU C 127 ? 2.50510 3.70565 2.75339 -0.48223 -0.10338 0.14124  127 GLU C C   
5283 O O   . GLU C 127 ? 2.45997 3.69805 2.70804 -0.46757 -0.10406 0.15012  127 GLU C O   
5284 C CB  . GLU C 127 ? 2.62871 3.70820 2.88396 -0.49161 -0.08267 0.14806  127 GLU C CB  
5285 C CG  . GLU C 127 ? 2.70616 3.72622 2.97409 -0.50601 -0.06875 0.16255  127 GLU C CG  
5286 C CD  . GLU C 127 ? 2.77102 3.74181 3.01924 -0.52377 -0.07260 0.14572  127 GLU C CD  
5287 O OE1 . GLU C 127 ? 2.75969 3.73591 2.98409 -0.52250 -0.08506 0.12118  127 GLU C OE1 
5288 O OE2 . GLU C 127 ? 2.83341 3.75805 3.08817 -0.53954 -0.06426 0.15752  127 GLU C OE2 
5289 N N   . GLU C 128 ? 2.59229 3.78945 2.82119 -0.48293 -0.11234 0.11750  128 GLU C N   
5290 C CA  . GLU C 128 ? 2.53149 3.77478 2.74215 -0.46506 -0.12104 0.10269  128 GLU C CA  
5291 C C   . GLU C 128 ? 2.48523 3.80379 2.71120 -0.46544 -0.12270 0.12215  128 GLU C C   
5292 O O   . GLU C 128 ? 2.43906 3.79823 2.64973 -0.44558 -0.12479 0.11891  128 GLU C O   
5293 C CB  . GLU C 128 ? 2.53833 3.76096 2.72829 -0.46662 -0.12964 0.07554  128 GLU C CB  
5294 C CG  . GLU C 128 ? 2.48062 3.73842 2.64854 -0.44468 -0.13683 0.05711  128 GLU C CG  
5295 C CD  . GLU C 128 ? 2.47575 3.73182 2.63186 -0.44960 -0.14627 0.03750  128 GLU C CD  
5296 O OE1 . GLU C 128 ? 2.51126 3.75475 2.67913 -0.47280 -0.15021 0.04278  128 GLU C OE1 
5297 O OE2 . GLU C 128 ? 2.43391 3.69998 2.56861 -0.43122 -0.15117 0.01778  128 GLU C OE2 
5298 N N   . LEU C 129 ? 2.47653 3.81215 2.73065 -0.48702 -0.12143 0.14329  129 LEU C N   
5299 C CA  . LEU C 129 ? 2.43916 3.84855 2.71262 -0.48672 -0.12030 0.16718  129 LEU C CA  
5300 C C   . LEU C 129 ? 2.42085 3.85508 2.69572 -0.47329 -0.11258 0.18543  129 LEU C C   
5301 O O   . LEU C 129 ? 2.38875 3.88101 2.65909 -0.45950 -0.11087 0.19598  129 LEU C O   
5302 C CB  . LEU C 129 ? 2.46083 3.87901 2.76895 -0.51522 -0.12177 0.18957  129 LEU C CB  
5303 C CG  . LEU C 129 ? 2.50020 3.87582 2.80625 -0.53657 -0.13242 0.17508  129 LEU C CG  
5304 C CD1 . LEU C 129 ? 2.52049 3.90572 2.86171 -0.56669 -0.13661 0.20168  129 LEU C CD1 
5305 C CD2 . LEU C 129 ? 2.46790 3.86908 2.75709 -0.52698 -0.14218 0.15553  129 LEU C CD2 
5306 N N   . GLN C 130 ? 2.49306 3.88306 2.77266 -0.47638 -0.10745 0.19096  130 GLN C N   
5307 C CA  . GLN C 130 ? 2.47716 3.88748 2.75789 -0.46563 -0.10306 0.20968  130 GLN C CA  
5308 C C   . GLN C 130 ? 2.44539 3.86848 2.68881 -0.44006 -0.10945 0.19269  130 GLN C C   
5309 O O   . GLN C 130 ? 2.42445 3.88374 2.65799 -0.42877 -0.10944 0.20660  130 GLN C O   
5310 C CB  . GLN C 130 ? 2.51335 3.87122 2.80998 -0.47377 -0.09649 0.22034  130 GLN C CB  
5311 C CG  . GLN C 130 ? 2.56075 3.87491 2.87998 -0.49658 -0.09076 0.22482  130 GLN C CG  
5312 C CD  . GLN C 130 ? 2.55409 3.90473 2.90631 -0.51544 -0.08753 0.25348  130 GLN C CD  
5313 O OE1 . GLN C 130 ? 2.54538 3.94038 2.91260 -0.51240 -0.08379 0.27860  130 GLN C OE1 
5314 N NE2 . GLN C 130 ? 2.55952 3.89019 2.92223 -0.53598 -0.09035 0.25097  130 GLN C NE2 
5315 N N   . GLU C 131 ? 2.54435 3.93520 2.76373 -0.43091 -0.11565 0.16289  131 GLU C N   
5316 C CA  . GLU C 131 ? 2.51522 3.90809 2.69784 -0.40782 -0.12357 0.14456  131 GLU C CA  
5317 C C   . GLU C 131 ? 2.48418 3.92431 2.64399 -0.39321 -0.12620 0.13404  131 GLU C C   
5318 O O   . GLU C 131 ? 2.46326 3.90110 2.58768 -0.37319 -0.13301 0.11556  131 GLU C O   
5319 C CB  . GLU C 131 ? 2.52764 3.86330 2.69746 -0.40364 -0.12815 0.11949  131 GLU C CB  
5320 C CG  . GLU C 131 ? 2.55683 3.84737 2.74033 -0.40729 -0.12525 0.13047  131 GLU C CG  
5321 C CD  . GLU C 131 ? 2.56734 3.80813 2.73599 -0.39810 -0.12915 0.10792  131 GLU C CD  
5322 O OE1 . GLU C 131 ? 2.56818 3.79553 2.72420 -0.39712 -0.13063 0.08440  131 GLU C OE1 
5323 O OE2 . GLU C 131 ? 2.57477 3.79188 2.74600 -0.39204 -0.13135 0.11587  131 GLU C OE2 
5324 N N   . ASN C 132 ? 2.50929 3.99111 2.68969 -0.40236 -0.12081 0.14724  132 ASN C N   
5325 C CA  . ASN C 132 ? 2.48668 4.01793 2.65270 -0.38788 -0.11992 0.14272  132 ASN C CA  
5326 C C   . ASN C 132 ? 2.47300 3.98191 2.61824 -0.37923 -0.12715 0.11099  132 ASN C C   
5327 O O   . ASN C 132 ? 2.45246 3.96959 2.56296 -0.35600 -0.12975 0.09461  132 ASN C O   
5328 C CB  . ASN C 132 ? 2.47529 4.04092 2.61023 -0.36452 -0.11686 0.15065  132 ASN C CB  
5329 C CG  . ASN C 132 ? 2.48701 4.08542 2.64292 -0.37223 -0.10870 0.18476  132 ASN C CG  
5330 O OD1 . ASN C 132 ? 2.49561 4.11671 2.69220 -0.39107 -0.10288 0.20586  132 ASN C OD1 
5331 N ND2 . ASN C 132 ? 2.48809 4.08771 2.61543 -0.35880 -0.10988 0.19131  132 ASN C ND2 
5332 N N   . LYS C 133 ? 2.44911 3.92628 2.61344 -0.39847 -0.13064 0.10270  133 LYS C N   
5333 C CA  . LYS C 133 ? 2.43747 3.88948 2.58491 -0.39383 -0.13798 0.07411  133 LYS C CA  
5334 C C   . LYS C 133 ? 2.46508 3.90037 2.63733 -0.41990 -0.14162 0.07541  133 LYS C C   
5335 O O   . LYS C 133 ? 2.50039 3.91839 2.69677 -0.44129 -0.13907 0.09212  133 LYS C O   
5336 C CB  . LYS C 133 ? 2.44103 3.83572 2.56422 -0.38401 -0.14233 0.05229  133 LYS C CB  
5337 C CG  . LYS C 133 ? 2.41932 3.78842 2.52207 -0.37592 -0.14950 0.02253  133 LYS C CG  
5338 C CD  . LYS C 133 ? 2.39684 3.80912 2.47740 -0.35384 -0.15157 0.01266  133 LYS C CD  
5339 C CE  . LYS C 133 ? 2.37537 3.76480 2.43917 -0.34674 -0.15875 -0.01519 133 LYS C CE  
5340 N NZ  . LYS C 133 ? 2.37882 3.71291 2.42355 -0.33892 -0.16350 -0.03350 133 LYS C NZ  
5341 N N   . ALA C 134 ? 2.41882 3.85712 2.58298 -0.41854 -0.14872 0.05828  134 ALA C N   
5342 C CA  . ALA C 134 ? 2.44287 3.86026 2.62300 -0.44429 -0.15658 0.05721  134 ALA C CA  
5343 C C   . ALA C 134 ? 2.43053 3.81898 2.58622 -0.43772 -0.16520 0.02753  134 ALA C C   
5344 O O   . ALA C 134 ? 2.37986 3.78983 2.51613 -0.41381 -0.16516 0.01375  134 ALA C O   
5345 C CB  . ALA C 134 ? 2.41451 3.89344 2.62742 -0.45822 -0.15865 0.08347  134 ALA C CB  
5346 N N   . THR C 135 ? 2.38756 3.72326 2.54101 -0.45874 -0.17251 0.01778  135 THR C N   
5347 C CA  . THR C 135 ? 2.38499 3.68811 2.51426 -0.45535 -0.18125 -0.00927 135 THR C CA  
5348 C C   . THR C 135 ? 2.43753 3.70353 2.57001 -0.48599 -0.19266 -0.00942 135 THR C C   
5349 O O   . THR C 135 ? 2.50678 3.72274 2.63983 -0.50346 -0.19009 -0.00408 135 THR C O   
5350 C CB  . THR C 135 ? 2.39940 3.64595 2.50044 -0.43798 -0.17579 -0.03149 135 THR C CB  
5351 O OG1 . THR C 135 ? 2.34957 3.62735 2.44441 -0.41210 -0.16974 -0.03105 135 THR C OG1 
5352 C CG2 . THR C 135 ? 2.39755 3.61161 2.47377 -0.43390 -0.18412 -0.05827 135 THR C CG2 
5353 N N   . LEU C 136 ? 2.30793 3.59551 2.44049 -0.49254 -0.20583 -0.01472 136 LEU C N   
5354 C CA  . LEU C 136 ? 2.34205 3.59458 2.47304 -0.52368 -0.22180 -0.01495 136 LEU C CA  
5355 C C   . LEU C 136 ? 2.36013 3.54236 2.45059 -0.52124 -0.22698 -0.04594 136 LEU C C   
5356 O O   . LEU C 136 ? 2.33890 3.51996 2.41063 -0.49550 -0.22176 -0.06549 136 LEU C O   
5357 C CB  . LEU C 136 ? 2.33836 3.65805 2.49769 -0.53621 -0.23595 0.00306  136 LEU C CB  
5358 C CG  . LEU C 136 ? 2.34115 3.71169 2.54345 -0.55478 -0.23681 0.03945  136 LEU C CG  
5359 C CD1 . LEU C 136 ? 2.34810 3.76894 2.57896 -0.57466 -0.25531 0.05862  136 LEU C CD1 
5360 C CD2 . LEU C 136 ? 2.37370 3.68349 2.57443 -0.57963 -0.23716 0.04574  136 LEU C CD2 
5361 N N   . VAL C 137 ? 2.42853 3.54892 2.50305 -0.54860 -0.23777 -0.04963 137 VAL C N   
5362 C CA  . VAL C 137 ? 2.45812 3.49848 2.48796 -0.54812 -0.24044 -0.07718 137 VAL C CA  
5363 C C   . VAL C 137 ? 2.49674 3.51871 2.51455 -0.57754 -0.26489 -0.07937 137 VAL C C   
5364 O O   . VAL C 137 ? 2.52883 3.54328 2.55890 -0.60818 -0.27714 -0.06176 137 VAL C O   
5365 C CB  . VAL C 137 ? 2.48909 3.44835 2.49737 -0.54935 -0.22557 -0.08140 137 VAL C CB  
5366 C CG1 . VAL C 137 ? 2.52571 3.40037 2.48431 -0.54621 -0.22556 -0.10819 137 VAL C CG1 
5367 C CG2 . VAL C 137 ? 2.45168 3.43223 2.47611 -0.52290 -0.20436 -0.07505 137 VAL C CG2 
5368 N N   . CYS C 138 ? 2.47026 3.48401 2.46424 -0.56960 -0.27376 -0.09964 138 CYS C N   
5369 C CA  . CYS C 138 ? 2.57173 3.55958 2.54675 -0.59696 -0.29905 -0.10428 138 CYS C CA  
5370 C C   . CYS C 138 ? 2.66778 3.56097 2.58453 -0.59204 -0.29675 -0.13393 138 CYS C C   
5371 O O   . CYS C 138 ? 2.55526 3.44490 2.45682 -0.56294 -0.28481 -0.15260 138 CYS C O   
5372 C CB  . CYS C 138 ? 2.44675 3.51457 2.44729 -0.59296 -0.31284 -0.09800 138 CYS C CB  
5373 S SG  . CYS C 138 ? 2.47478 3.53376 2.46887 -0.63353 -0.34989 -0.09128 138 CYS C SG  
5374 N N   . LEU C 139 ? 2.61950 3.43350 2.50167 -0.61973 -0.30772 -0.13736 139 LEU C N   
5375 C CA  . LEU C 139 ? 2.70554 3.41782 2.52510 -0.61506 -0.30234 -0.16348 139 LEU C CA  
5376 C C   . LEU C 139 ? 2.74599 3.42946 2.53131 -0.63897 -0.33150 -0.17386 139 LEU C C   
5377 O O   . LEU C 139 ? 2.82811 3.48175 2.60239 -0.67526 -0.35448 -0.16450 139 LEU C O   
5378 C CB  . LEU C 139 ? 2.83844 3.46831 2.63336 -0.62475 -0.28944 -0.16115 139 LEU C CB  
5379 C CG  . LEU C 139 ? 2.82450 3.46838 2.64712 -0.60069 -0.25944 -0.15116 139 LEU C CG  
5380 C CD1 . LEU C 139 ? 2.95763 3.51182 2.75198 -0.61093 -0.24680 -0.14856 139 LEU C CD1 
5381 C CD2 . LEU C 139 ? 2.75496 3.40687 2.57310 -0.56161 -0.23889 -0.16628 139 LEU C CD2 
5382 N N   . ILE C 140 ? 2.81608 3.50662 2.58404 -0.61973 -0.33216 -0.19222 140 ILE C N   
5383 C CA  . ILE C 140 ? 2.83365 3.49798 2.56687 -0.63887 -0.35913 -0.20316 140 ILE C CA  
5384 C C   . ILE C 140 ? 2.94625 3.49980 2.60619 -0.62983 -0.34923 -0.23025 140 ILE C C   
5385 O O   . ILE C 140 ? 2.93721 3.47933 2.58655 -0.59512 -0.32501 -0.24505 140 ILE C O   
5386 C CB  . ILE C 140 ? 2.62648 3.37631 2.39094 -0.62323 -0.36656 -0.20312 140 ILE C CB  
5387 C CG1 . ILE C 140 ? 2.41335 3.27249 2.24896 -0.61871 -0.36409 -0.17667 140 ILE C CG1 
5388 C CG2 . ILE C 140 ? 2.73042 3.46922 2.47213 -0.65034 -0.39976 -0.20553 140 ILE C CG2 
5389 C CD1 . ILE C 140 ? 2.30260 3.20634 2.16217 -0.57766 -0.33532 -0.18089 140 ILE C CD1 
5390 N N   . SER C 141 ? 2.97570 3.44523 2.58313 -0.66054 -0.36799 -0.23559 141 SER C N   
5391 C CA  . SER C 141 ? 3.08550 3.43785 2.61577 -0.65180 -0.35510 -0.25921 141 SER C CA  
5392 C C   . SER C 141 ? 3.13360 3.42481 2.60284 -0.67968 -0.38696 -0.27195 141 SER C C   
5393 O O   . SER C 141 ? 3.11152 3.43831 2.59796 -0.71454 -0.42221 -0.25849 141 SER C O   
5394 C CB  . SER C 141 ? 3.19588 3.47466 2.70572 -0.65655 -0.33694 -0.25464 141 SER C CB  
5395 O OG  . SER C 141 ? 3.22959 3.51735 2.75780 -0.69593 -0.36152 -0.23534 141 SER C OG  
5396 N N   . ASN C 142 ? 3.31370 3.51183 2.71122 -0.66333 -0.37381 -0.29603 142 ASN C N   
5397 C CA  . ASN C 142 ? 3.37359 3.48708 2.69264 -0.68521 -0.39903 -0.31270 142 ASN C CA  
5398 C C   . ASN C 142 ? 3.29360 3.47710 2.63746 -0.71084 -0.43926 -0.30507 142 ASN C C   
5399 O O   . ASN C 142 ? 3.33468 3.49645 2.66012 -0.75320 -0.47655 -0.29703 142 ASN C O   
5400 C CB  . ASN C 142 ? 3.50967 3.51365 2.76742 -0.71568 -0.40913 -0.31406 142 ASN C CB  
5401 C CG  . ASN C 142 ? 3.51837 3.57058 2.82933 -0.75098 -0.43075 -0.28785 142 ASN C CG  
5402 O OD1 . ASN C 142 ? 3.54326 3.60257 2.88584 -0.74330 -0.40849 -0.27605 142 ASN C OD1 
5403 N ND2 . ASN C 142 ? 3.49522 3.58322 2.81922 -0.79010 -0.47461 -0.27593 142 ASN C ND2 
5404 N N   . PHE C 143 ? 3.30462 3.57171 2.69117 -0.68437 -0.43173 -0.30620 143 PHE C N   
5405 C CA  . PHE C 143 ? 3.21945 3.55504 2.63049 -0.70045 -0.46395 -0.29922 143 PHE C CA  
5406 C C   . PHE C 143 ? 3.17197 3.49013 2.54737 -0.67376 -0.45638 -0.32102 143 PHE C C   
5407 O O   . PHE C 143 ? 3.15755 3.46061 2.52609 -0.63444 -0.42171 -0.33454 143 PHE C O   
5408 C CB  . PHE C 143 ? 3.09771 3.56801 2.60550 -0.69510 -0.46428 -0.27423 143 PHE C CB  
5409 C CG  . PHE C 143 ? 3.00852 3.53023 2.55591 -0.64913 -0.42625 -0.27830 143 PHE C CG  
5410 C CD1 . PHE C 143 ? 3.03499 3.55718 2.60577 -0.63625 -0.40004 -0.27139 143 PHE C CD1 
5411 C CD2 . PHE C 143 ? 2.89359 3.46241 2.45490 -0.62024 -0.41877 -0.28771 143 PHE C CD2 
5412 C CE1 . PHE C 143 ? 2.96021 3.52734 2.56542 -0.59701 -0.36926 -0.27357 143 PHE C CE1 
5413 C CE2 . PHE C 143 ? 2.80688 3.41807 2.40174 -0.58058 -0.38761 -0.29092 143 PHE C CE2 
5414 C CZ  . PHE C 143 ? 2.83840 3.44816 2.45433 -0.56975 -0.36393 -0.28368 143 PHE C CZ  
5415 N N   . SER C 144 ? 3.07523 3.39725 2.43053 -0.69648 -0.49039 -0.32182 144 SER C N   
5416 C CA  . SER C 144 ? 3.07729 3.38329 2.39710 -0.67593 -0.48839 -0.34065 144 SER C CA  
5417 C C   . SER C 144 ? 3.08526 3.43716 2.41540 -0.70527 -0.53052 -0.33021 144 SER C C   
5418 O O   . SER C 144 ? 3.15027 3.47324 2.45938 -0.74921 -0.56663 -0.31966 144 SER C O   
5419 C CB  . SER C 144 ? 3.17124 3.34218 2.39126 -0.66915 -0.47622 -0.36605 144 SER C CB  
5420 O OG  . SER C 144 ? 3.18242 3.33532 2.36405 -0.65359 -0.47840 -0.38228 144 SER C OG  
5421 N N   . PRO C 145 ? 3.14626 3.56919 2.50958 -0.68333 -0.52866 -0.33091 145 PRO C N   
5422 C CA  . PRO C 145 ? 3.05817 3.51904 2.44913 -0.63395 -0.49099 -0.34163 145 PRO C CA  
5423 C C   . PRO C 145 ? 2.92489 3.48166 2.39968 -0.61655 -0.47176 -0.32422 145 PRO C C   
5424 O O   . PRO C 145 ? 2.89590 3.48543 2.40607 -0.64072 -0.48323 -0.30391 145 PRO C O   
5425 C CB  . PRO C 145 ? 2.95931 3.46189 2.35476 -0.62676 -0.50584 -0.34481 145 PRO C CB  
5426 C CG  . PRO C 145 ? 2.95833 3.50266 2.37509 -0.66955 -0.54860 -0.32295 145 PRO C CG  
5427 C CD  . PRO C 145 ? 3.10306 3.56529 2.47261 -0.70795 -0.56693 -0.32092 145 PRO C CD  
5428 N N   . SER C 146 ? 2.84365 3.44291 2.34762 -0.57530 -0.44383 -0.33141 146 SER C N   
5429 C CA  . SER C 146 ? 2.76802 3.43869 2.33580 -0.55337 -0.42107 -0.31977 146 SER C CA  
5430 C C   . SER C 146 ? 2.65034 3.43442 2.28481 -0.54598 -0.42914 -0.30328 146 SER C C   
5431 O O   . SER C 146 ? 2.57215 3.41238 2.24886 -0.51666 -0.40741 -0.30025 146 SER C O   
5432 C CB  . SER C 146 ? 2.79566 3.43442 2.35137 -0.51317 -0.38536 -0.33621 146 SER C CB  
5433 O OG  . SER C 146 ? 2.77042 3.39739 2.30321 -0.49163 -0.38227 -0.35211 146 SER C OG  
5434 N N   . GLY C 147 ? 2.61038 3.42743 2.25377 -0.57164 -0.46000 -0.29112 147 GLY C N   
5435 C CA  . GLY C 147 ? 2.55050 3.47646 2.26031 -0.56563 -0.46630 -0.27014 147 GLY C CA  
5436 C C   . GLY C 147 ? 2.53235 3.51586 2.29414 -0.58221 -0.46921 -0.24235 147 GLY C C   
5437 O O   . GLY C 147 ? 2.54726 3.57143 2.33597 -0.61299 -0.49621 -0.21792 147 GLY C O   
5438 N N   . VAL C 148 ? 2.55190 3.54116 2.33016 -0.56243 -0.44222 -0.24331 148 VAL C N   
5439 C CA  . VAL C 148 ? 2.52049 3.54823 2.33886 -0.57839 -0.44215 -0.21880 148 VAL C CA  
5440 C C   . VAL C 148 ? 2.33627 3.45785 2.21262 -0.54814 -0.42183 -0.20481 148 VAL C C   
5441 O O   . VAL C 148 ? 2.29553 3.43560 2.17337 -0.51262 -0.40382 -0.21881 148 VAL C O   
5442 C CB  . VAL C 148 ? 2.63982 3.59036 2.42580 -0.58486 -0.42900 -0.22818 148 VAL C CB  
5443 C CG1 . VAL C 148 ? 2.74334 3.59540 2.46578 -0.61557 -0.44927 -0.24056 148 VAL C CG1 
5444 C CG2 . VAL C 148 ? 2.66536 3.59200 2.43825 -0.54489 -0.39568 -0.24873 148 VAL C CG2 
5445 N N   . THR C 149 ? 2.38776 3.56595 2.30980 -0.56264 -0.42511 -0.17598 149 THR C N   
5446 C CA  . THR C 149 ? 2.34968 3.61512 2.32312 -0.53601 -0.40574 -0.15888 149 THR C CA  
5447 C C   . THR C 149 ? 2.35419 3.63588 2.35428 -0.55113 -0.40100 -0.13695 149 THR C C   
5448 O O   . THR C 149 ? 2.43185 3.70829 2.44162 -0.58871 -0.42312 -0.11762 149 THR C O   
5449 C CB  . THR C 149 ? 2.37533 3.72600 2.39151 -0.53434 -0.41744 -0.13633 149 THR C CB  
5450 O OG1 . THR C 149 ? 2.33874 3.68269 2.33474 -0.51098 -0.41500 -0.15737 149 THR C OG1 
5451 C CG2 . THR C 149 ? 2.34269 3.78173 2.41139 -0.51225 -0.39813 -0.11147 149 THR C CG2 
5452 N N   . VAL C 150 ? 2.25224 3.55190 2.26319 -0.52329 -0.37411 -0.13905 150 VAL C N   
5453 C CA  . VAL C 150 ? 2.29439 3.60352 2.32640 -0.53395 -0.36625 -0.12074 150 VAL C CA  
5454 C C   . VAL C 150 ? 2.30340 3.71258 2.39060 -0.52149 -0.35763 -0.08983 150 VAL C C   
5455 O O   . VAL C 150 ? 2.26355 3.72798 2.36723 -0.49713 -0.35160 -0.08693 150 VAL C O   
5456 C CB  . VAL C 150 ? 2.26231 3.51761 2.26664 -0.51406 -0.34279 -0.14119 150 VAL C CB  
5457 C CG1 . VAL C 150 ? 2.24489 3.40067 2.19518 -0.52382 -0.34770 -0.16811 150 VAL C CG1 
5458 C CG2 . VAL C 150 ? 2.19376 3.48402 2.20193 -0.47141 -0.32119 -0.15209 150 VAL C CG2 
5459 N N   . ALA C 151 ? 2.19773 3.62908 2.31289 -0.53709 -0.35550 -0.06516 151 ALA C N   
5460 C CA  . ALA C 151 ? 2.16795 3.69198 2.33410 -0.52408 -0.34389 -0.03272 151 ALA C CA  
5461 C C   . ALA C 151 ? 2.18613 3.70961 2.36849 -0.53674 -0.33617 -0.01507 151 ALA C C   
5462 O O   . ALA C 151 ? 2.23728 3.74172 2.43030 -0.57444 -0.35505 0.00089  151 ALA C O   
5463 C CB  . ALA C 151 ? 2.17295 3.76107 2.38093 -0.54289 -0.36405 -0.00170 151 ALA C CB  
5464 N N   . TRP C 152 ? 2.17743 3.72000 2.36020 -0.50631 -0.31011 -0.01722 152 TRP C N   
5465 C CA  . TRP C 152 ? 2.22133 3.77696 2.42438 -0.51350 -0.29999 0.00328  152 TRP C CA  
5466 C C   . TRP C 152 ? 2.22707 3.87889 2.48382 -0.51066 -0.29560 0.04433  152 TRP C C   
5467 O O   . TRP C 152 ? 2.18841 3.89717 2.45603 -0.48076 -0.28333 0.04973  152 TRP C O   
5468 C CB  . TRP C 152 ? 2.21431 3.74553 2.39135 -0.48305 -0.27574 -0.01581 152 TRP C CB  
5469 C CG  . TRP C 152 ? 2.25090 3.69083 2.38890 -0.49201 -0.27656 -0.04248 152 TRP C CG  
5470 C CD1 . TRP C 152 ? 2.24765 3.63190 2.34548 -0.47523 -0.27300 -0.07550 152 TRP C CD1 
5471 C CD2 . TRP C 152 ? 2.31748 3.71159 2.45459 -0.51794 -0.27913 -0.03566 152 TRP C CD2 
5472 N NE1 . TRP C 152 ? 2.31435 3.62245 2.38712 -0.48772 -0.27156 -0.08819 152 TRP C NE1 
5473 C CE2 . TRP C 152 ? 2.37096 3.68172 2.46558 -0.51363 -0.27494 -0.06509 152 TRP C CE2 
5474 C CE3 . TRP C 152 ? 2.34961 3.76494 2.51904 -0.54372 -0.28385 -0.00586 152 TRP C CE3 
5475 C CZ2 . TRP C 152 ? 2.45611 3.70294 2.53771 -0.53234 -0.27343 -0.06593 152 TRP C CZ2 
5476 C CZ3 . TRP C 152 ? 2.42784 3.77810 2.58363 -0.56417 -0.28450 -0.00837 152 TRP C CZ3 
5477 C CH2 . TRP C 152 ? 2.46621 3.73225 2.57742 -0.55759 -0.27846 -0.03841 152 TRP C CH2 
5478 N N   . LYS C 153 ? 2.23871 3.90743 2.52896 -0.54060 -0.30450 0.07472  153 LYS C N   
5479 C CA  . LYS C 153 ? 2.23298 3.99445 2.58015 -0.54104 -0.30102 0.11956  153 LYS C CA  
5480 C C   . LYS C 153 ? 2.25251 4.02631 2.62075 -0.54896 -0.29038 0.14214  153 LYS C C   
5481 O O   . LYS C 153 ? 2.28706 3.99697 2.63785 -0.57217 -0.29773 0.13172  153 LYS C O   
5482 C CB  . LYS C 153 ? 2.24840 4.03604 2.63149 -0.57729 -0.33101 0.14601  153 LYS C CB  
5483 C CG  . LYS C 153 ? 2.24939 3.98745 2.59949 -0.58764 -0.35223 0.11793  153 LYS C CG  
5484 C CD  . LYS C 153 ? 2.25347 4.04547 2.64656 -0.61138 -0.37737 0.15016  153 LYS C CD  
5485 C CE  . LYS C 153 ? 2.29630 4.09067 2.72431 -0.65982 -0.40373 0.18418  153 LYS C CE  
5486 N NZ  . LYS C 153 ? 2.35603 4.05408 2.74095 -0.69986 -0.43507 0.16071  153 LYS C NZ  
5487 N N   . ALA C 154 ? 2.24057 4.09657 2.64559 -0.52784 -0.27141 0.17447  154 ALA C N   
5488 C CA  . ALA C 154 ? 2.25929 4.13984 2.68789 -0.53072 -0.25840 0.20037  154 ALA C CA  
5489 C C   . ALA C 154 ? 2.26801 4.24398 2.76123 -0.53612 -0.25764 0.25338  154 ALA C C   
5490 O O   . ALA C 154 ? 2.27823 4.32071 2.78527 -0.50235 -0.23848 0.26830  154 ALA C O   
5491 C CB  . ALA C 154 ? 2.25185 4.12884 2.64756 -0.48985 -0.22865 0.18292  154 ALA C CB  
5492 N N   . ASN C 155 ? 2.24064 4.22147 2.77307 -0.57780 -0.27790 0.28331  155 ASN C N   
5493 C CA  . ASN C 155 ? 2.24829 4.31953 2.85062 -0.58939 -0.28092 0.33987  155 ASN C CA  
5494 C C   . ASN C 155 ? 2.25490 4.38090 2.88385 -0.58355 -0.28931 0.35584  155 ASN C C   
5495 O O   . ASN C 155 ? 2.27127 4.48783 2.94865 -0.56551 -0.27469 0.39762  155 ASN C O   
5496 C CB  . ASN C 155 ? 2.25510 4.39042 2.87786 -0.55725 -0.24732 0.36701  155 ASN C CB  
5497 C CG  . ASN C 155 ? 2.26448 4.41324 2.92771 -0.58739 -0.25312 0.40219  155 ASN C CG  
5498 O OD1 . ASN C 155 ? 2.27885 4.47847 3.00197 -0.61577 -0.26990 0.44697  155 ASN C OD1 
5499 N ND2 . ASN C 155 ? 2.25742 4.36196 2.89086 -0.58199 -0.24014 0.38445  155 ASN C ND2 
5500 N N   . GLY C 156 ? 2.26841 4.33951 2.86600 -0.59791 -0.31191 0.32436  156 GLY C N   
5501 C CA  . GLY C 156 ? 2.27048 4.38444 2.88923 -0.59488 -0.32283 0.33591  156 GLY C CA  
5502 C C   . GLY C 156 ? 2.25656 4.38469 2.84366 -0.54366 -0.29606 0.31042  156 GLY C C   
5503 O O   . GLY C 156 ? 2.24543 4.36992 2.82444 -0.54198 -0.30806 0.29820  156 GLY C O   
5504 N N   . THR C 157 ? 2.32207 4.46336 2.88884 -0.50275 -0.26154 0.30241  157 THR C N   
5505 C CA  . THR C 157 ? 2.31840 4.46501 2.84853 -0.45371 -0.23674 0.27670  157 THR C CA  
5506 C C   . THR C 157 ? 2.28756 4.33881 2.75043 -0.45126 -0.24358 0.21837  157 THR C C   
5507 O O   . THR C 157 ? 2.28289 4.27190 2.71789 -0.46574 -0.24708 0.19748  157 THR C O   
5508 C CB  . THR C 157 ? 2.34376 4.53141 2.86857 -0.41184 -0.19958 0.28885  157 THR C CB  
5509 O OG1 . THR C 157 ? 2.33345 4.46949 2.83016 -0.41987 -0.19605 0.27163  157 THR C OG1 
5510 C CG2 . THR C 157 ? 2.38523 4.67129 2.97786 -0.40959 -0.18864 0.34994  157 THR C CG2 
5511 N N   . PRO C 158 ? 2.25179 4.29050 2.68999 -0.43265 -0.24476 0.19355  158 PRO C N   
5512 C CA  . PRO C 158 ? 2.21764 4.16892 2.59514 -0.42875 -0.25049 0.14094  158 PRO C CA  
5513 C C   . PRO C 158 ? 2.20813 4.13710 2.54238 -0.38947 -0.22326 0.11573  158 PRO C C   
5514 O O   . PRO C 158 ? 2.22037 4.18187 2.54332 -0.34959 -0.20268 0.11347  158 PRO C O   
5515 C CB  . PRO C 158 ? 2.20596 4.16730 2.58163 -0.42080 -0.26015 0.13163  158 PRO C CB  
5516 C CG  . PRO C 158 ? 2.23966 4.28897 2.67979 -0.43011 -0.26534 0.18194  158 PRO C CG  
5517 C CD  . PRO C 158 ? 2.26760 4.37275 2.73794 -0.41750 -0.24293 0.21634  158 PRO C CD  
5518 N N   . ILE C 159 ? 2.27379 4.14442 2.58230 -0.40102 -0.22384 0.09781  159 ILE C N   
5519 C CA  . ILE C 159 ? 2.26173 4.10307 2.52752 -0.36901 -0.20343 0.07344  159 ILE C CA  
5520 C C   . ILE C 159 ? 2.23676 4.02600 2.45751 -0.35107 -0.20629 0.03192  159 ILE C C   
5521 O O   . ILE C 159 ? 2.22235 3.95640 2.42906 -0.37300 -0.22471 0.01055  159 ILE C O   
5522 C CB  . ILE C 159 ? 2.26615 4.06294 2.52372 -0.38837 -0.20427 0.07058  159 ILE C CB  
5523 C CG1 . ILE C 159 ? 2.25882 4.01251 2.46899 -0.36034 -0.18971 0.04166  159 ILE C CG1 
5524 C CG2 . ILE C 159 ? 2.26843 4.00521 2.52568 -0.42956 -0.22870 0.05997  159 ILE C CG2 
5525 C CD1 . ILE C 159 ? 2.28012 4.08222 2.48116 -0.32196 -0.16620 0.05268  159 ILE C CD1 
5526 N N   . THR C 160 ? 2.31777 4.12185 2.51322 -0.31045 -0.18794 0.02096  160 THR C N   
5527 C CA  . THR C 160 ? 2.29095 4.05655 2.44902 -0.29020 -0.19008 -0.01388 160 THR C CA  
5528 C C   . THR C 160 ? 2.27604 3.97415 2.38835 -0.27976 -0.18726 -0.04591 160 THR C C   
5529 O O   . THR C 160 ? 2.24849 3.88854 2.34024 -0.28934 -0.19959 -0.07272 160 THR C O   
5530 C CB  . THR C 160 ? 2.32269 4.13984 2.47827 -0.25147 -0.17324 -0.00697 160 THR C CB  
5531 O OG1 . THR C 160 ? 2.35549 4.24550 2.56159 -0.25922 -0.17230 0.03160  160 THR C OG1 
5532 C CG2 . THR C 160 ? 2.29534 4.07976 2.42327 -0.23652 -0.17967 -0.03810 160 THR C CG2 
5533 N N   . GLN C 161 ? 2.34646 4.05139 2.44264 -0.26026 -0.17160 -0.04149 161 GLN C N   
5534 C CA  . GLN C 161 ? 2.33795 3.98494 2.39253 -0.24839 -0.17017 -0.06788 161 GLN C CA  
5535 C C   . GLN C 161 ? 2.33629 3.94348 2.39778 -0.27706 -0.17672 -0.06587 161 GLN C C   
5536 O O   . GLN C 161 ? 2.35260 3.98160 2.44720 -0.30201 -0.17891 -0.04197 161 GLN C O   
5537 C CB  . GLN C 161 ? 2.38657 4.05386 2.41327 -0.21371 -0.15262 -0.06479 161 GLN C CB  
5538 C CG  . GLN C 161 ? 2.41319 4.13390 2.43991 -0.18413 -0.13938 -0.05464 161 GLN C CG  
5539 C CD  . GLN C 161 ? 2.38779 4.09160 2.40186 -0.17258 -0.14664 -0.07782 161 GLN C CD  
5540 O OE1 . GLN C 161 ? 2.35471 4.00098 2.34434 -0.17564 -0.15842 -0.10676 161 GLN C OE1 
5541 N NE2 . GLN C 161 ? 2.40993 4.16629 2.44355 -0.15850 -0.13882 -0.06245 161 GLN C NE2 
5542 N N   . GLY C 162 ? 2.26189 3.80989 2.29329 -0.27288 -0.17977 -0.08936 162 GLY C N   
5543 C CA  . GLY C 162 ? 2.27722 3.78193 2.31323 -0.29612 -0.18363 -0.08809 162 GLY C CA  
5544 C C   . GLY C 162 ? 2.27970 3.74870 2.32923 -0.32627 -0.19621 -0.09309 162 GLY C C   
5545 O O   . GLY C 162 ? 2.31793 3.77444 2.38553 -0.35176 -0.19822 -0.07907 162 GLY C O   
5546 N N   . VAL C 163 ? 2.30547 3.75425 2.34322 -0.32374 -0.20489 -0.11281 163 VAL C N   
5547 C CA  . VAL C 163 ? 2.30432 3.71473 2.34569 -0.35076 -0.21794 -0.11952 163 VAL C CA  
5548 C C   . VAL C 163 ? 2.29484 3.64822 2.30553 -0.33995 -0.22158 -0.14920 163 VAL C C   
5549 O O   . VAL C 163 ? 2.25686 3.62095 2.25296 -0.31469 -0.21984 -0.16289 163 VAL C O   
5550 C CB  . VAL C 163 ? 2.26167 3.71823 2.32736 -0.36410 -0.22794 -0.10556 163 VAL C CB  
5551 C CG1 . VAL C 163 ? 2.16190 3.57063 2.21767 -0.38741 -0.24450 -0.11918 163 VAL C CG1 
5552 C CG2 . VAL C 163 ? 2.28746 3.79207 2.38934 -0.38242 -0.22670 -0.07214 163 VAL C CG2 
5553 N N   . ASP C 164 ? 2.30129 3.59217 2.30133 -0.35793 -0.22549 -0.15793 164 ASP C N   
5554 C CA  . ASP C 164 ? 2.28418 3.51783 2.25705 -0.34911 -0.22736 -0.18263 164 ASP C CA  
5555 C C   . ASP C 164 ? 2.30840 3.49308 2.27165 -0.37512 -0.23666 -0.18798 164 ASP C C   
5556 O O   . ASP C 164 ? 2.39214 3.55448 2.36126 -0.39806 -0.23689 -0.17632 164 ASP C O   
5557 C CB  . ASP C 164 ? 2.40036 3.59605 2.36217 -0.33600 -0.21720 -0.18728 164 ASP C CB  
5558 C CG  . ASP C 164 ? 2.38469 3.61940 2.34678 -0.31136 -0.21156 -0.18393 164 ASP C CG  
5559 O OD1 . ASP C 164 ? 2.33029 3.58375 2.28123 -0.29088 -0.21417 -0.19599 164 ASP C OD1 
5560 O OD2 . ASP C 164 ? 2.42872 3.67327 2.39948 -0.31254 -0.20491 -0.16898 164 ASP C OD2 
5561 N N   . THR C 165 ? 2.26712 3.43193 2.21234 -0.37147 -0.24468 -0.20554 165 THR C N   
5562 C CA  . THR C 165 ? 2.28623 3.40485 2.21456 -0.39574 -0.25629 -0.21179 165 THR C CA  
5563 C C   . THR C 165 ? 2.30113 3.35749 2.19638 -0.38288 -0.25320 -0.23511 165 THR C C   
5564 O O   . THR C 165 ? 2.26597 3.33762 2.15655 -0.36081 -0.25318 -0.24744 165 THR C O   
5565 C CB  . THR C 165 ? 2.22070 3.38559 2.16249 -0.40916 -0.27304 -0.20454 165 THR C CB  
5566 O OG1 . THR C 165 ? 2.25484 3.47802 2.23138 -0.42192 -0.27478 -0.17826 165 THR C OG1 
5567 C CG2 . THR C 165 ? 2.24032 3.35061 2.15704 -0.43568 -0.28889 -0.21241 165 THR C CG2 
5568 N N   . SER C 166 ? 2.26407 3.24922 2.13587 -0.39550 -0.24949 -0.23985 166 SER C N   
5569 C CA  . SER C 166 ? 2.35425 3.27595 2.19302 -0.38358 -0.24426 -0.25888 166 SER C CA  
5570 C C   . SER C 166 ? 2.32969 3.23222 2.14365 -0.39675 -0.26036 -0.27050 166 SER C C   
5571 O O   . SER C 166 ? 2.34148 3.24833 2.15470 -0.42433 -0.27564 -0.26293 166 SER C O   
5572 C CB  . SER C 166 ? 2.61488 3.46483 2.43572 -0.38822 -0.22996 -0.25711 166 SER C CB  
5573 O OG  . SER C 166 ? 2.78001 3.60336 2.59195 -0.41833 -0.23713 -0.24911 166 SER C OG  
5574 N N   . ASN C 167 ? 2.45547 3.33694 2.24980 -0.37780 -0.25847 -0.28733 167 ASN C N   
5575 C CA  . ASN C 167 ? 2.44955 3.30933 2.21665 -0.38824 -0.27346 -0.29896 167 ASN C CA  
5576 C C   . ASN C 167 ? 2.63008 3.40292 2.35310 -0.40741 -0.27345 -0.30475 167 ASN C C   
5577 O O   . ASN C 167 ? 2.86676 3.58857 2.57747 -0.40146 -0.25567 -0.30398 167 ASN C O   
5578 C CB  . ASN C 167 ? 2.51482 3.37536 2.27347 -0.36098 -0.26994 -0.31433 167 ASN C CB  
5579 C CG  . ASN C 167 ? 2.39994 3.33870 2.19389 -0.34193 -0.27154 -0.31070 167 ASN C CG  
5580 O OD1 . ASN C 167 ? 2.30212 3.29932 2.12422 -0.35035 -0.27742 -0.29676 167 ASN C OD1 
5581 N ND2 . ASN C 167 ? 2.34898 3.28699 2.14010 -0.31521 -0.26565 -0.32217 167 ASN C ND2 
5582 N N   . PRO C 168 ? 2.50192 3.25423 2.19868 -0.43051 -0.29344 -0.30934 168 PRO C N   
5583 C CA  . PRO C 168 ? 2.76155 3.42316 2.40675 -0.45067 -0.29569 -0.31575 168 PRO C CA  
5584 C C   . PRO C 168 ? 2.90536 3.49227 2.51036 -0.42662 -0.27414 -0.33094 168 PRO C C   
5585 O O   . PRO C 168 ? 2.84980 3.43022 2.43830 -0.41002 -0.27415 -0.34369 168 PRO C O   
5586 C CB  . PRO C 168 ? 2.80227 3.46563 2.42745 -0.47664 -0.32525 -0.31859 168 PRO C CB  
5587 C CG  . PRO C 168 ? 2.49298 3.25895 2.17436 -0.47843 -0.33800 -0.30384 168 PRO C CG  
5588 C CD  . PRO C 168 ? 2.37465 3.18675 2.08854 -0.44181 -0.31644 -0.30555 168 PRO C CD  
5589 N N   . THR C 169 ? 2.76052 3.29233 2.35225 -0.42379 -0.25444 -0.32702 169 THR C N   
5590 C CA  . THR C 169 ? 2.85374 3.31218 2.41030 -0.40001 -0.22987 -0.33580 169 THR C CA  
5591 C C   . THR C 169 ? 2.97151 3.33002 2.45947 -0.41683 -0.23107 -0.34513 169 THR C C   
5592 O O   . THR C 169 ? 3.01246 3.35478 2.48291 -0.44931 -0.25115 -0.34321 169 THR C O   
5593 C CB  . THR C 169 ? 2.89349 3.35454 2.48121 -0.38175 -0.20411 -0.32232 169 THR C CB  
5594 O OG1 . THR C 169 ? 2.94703 3.34635 2.50886 -0.35521 -0.17922 -0.32663 169 THR C OG1 
5595 C CG2 . THR C 169 ? 2.98080 3.41462 2.56680 -0.40444 -0.20200 -0.31034 169 THR C CG2 
5596 N N   . LYS C 170 ? 3.06117 3.34914 2.50796 -0.39401 -0.20934 -0.35413 170 LYS C N   
5597 C CA  . LYS C 170 ? 3.16707 3.34664 2.53812 -0.40332 -0.20445 -0.36402 170 LYS C CA  
5598 C C   . LYS C 170 ? 3.27478 3.39446 2.63657 -0.39412 -0.17493 -0.35385 170 LYS C C   
5599 O O   . LYS C 170 ? 3.28600 3.39700 2.66280 -0.36217 -0.14533 -0.34716 170 LYS C O   
5600 C CB  . LYS C 170 ? 3.14822 3.28129 2.47225 -0.38188 -0.19654 -0.37917 170 LYS C CB  
5601 C CG  . LYS C 170 ? 3.08429 3.23120 2.38296 -0.40152 -0.22910 -0.39215 170 LYS C CG  
5602 C CD  . LYS C 170 ? 3.09502 3.17168 2.32991 -0.38324 -0.21945 -0.40733 170 LYS C CD  
5603 C CE  . LYS C 170 ? 3.02914 3.12479 2.24223 -0.40178 -0.25267 -0.41857 170 LYS C CE  
5604 N NZ  . LYS C 170 ? 3.04660 3.07365 2.19497 -0.38315 -0.24303 -0.43294 170 LYS C NZ  
5605 N N   . GLU C 171 ? 3.16158 3.24088 2.50129 -0.42223 -0.18346 -0.35045 171 GLU C N   
5606 C CA  . GLU C 171 ? 3.27738 3.28186 2.59434 -0.41750 -0.15697 -0.34224 171 GLU C CA  
5607 C C   . GLU C 171 ? 3.38336 3.27913 2.61693 -0.44109 -0.16521 -0.35374 171 GLU C C   
5608 O O   . GLU C 171 ? 3.47967 3.28366 2.66596 -0.42510 -0.13641 -0.35431 171 GLU C O   
5609 C CB  . GLU C 171 ? 3.27035 3.33496 2.65166 -0.42881 -0.15677 -0.32192 171 GLU C CB  
5610 C CG  . GLU C 171 ? 3.38483 3.37724 2.74807 -0.42537 -0.13039 -0.31117 171 GLU C CG  
5611 C CD  . GLU C 171 ? 3.40404 3.37926 2.78142 -0.38487 -0.09104 -0.30134 171 GLU C CD  
5612 O OE1 . GLU C 171 ? 3.32662 3.35527 2.73668 -0.36106 -0.08626 -0.30104 171 GLU C OE1 
5613 O OE2 . GLU C 171 ? 3.49592 3.40446 2.85429 -0.37705 -0.06495 -0.29155 171 GLU C OE2 
5614 N N   . ASP C 172 ? 3.51700 3.41458 2.72639 -0.47738 -0.20357 -0.36240 172 ASP C N   
5615 C CA  . ASP C 172 ? 3.61666 3.40756 2.73912 -0.50422 -0.21950 -0.37514 172 ASP C CA  
5616 C C   . ASP C 172 ? 3.58430 3.34570 2.65034 -0.50438 -0.23650 -0.39462 172 ASP C C   
5617 O O   . ASP C 172 ? 3.48926 3.30668 2.58364 -0.48023 -0.23061 -0.39768 172 ASP C O   
5618 C CB  . ASP C 172 ? 3.64301 3.45732 2.78316 -0.55061 -0.25506 -0.36573 172 ASP C CB  
5619 C CG  . ASP C 172 ? 3.63455 3.48046 2.83077 -0.55128 -0.23920 -0.34547 172 ASP C CG  
5620 O OD1 . ASP C 172 ? 3.61220 3.41823 2.80402 -0.52090 -0.20072 -0.34195 172 ASP C OD1 
5621 O OD2 . ASP C 172 ? 3.64428 3.55837 2.89227 -0.57978 -0.26328 -0.33072 172 ASP C OD2 
5622 N N   . ASN C 173 ? 3.73047 3.39751 2.71208 -0.53170 -0.25798 -0.40771 173 ASN C N   
5623 C CA  . ASN C 173 ? 3.70027 3.34799 2.63073 -0.54161 -0.28422 -0.42400 173 ASN C CA  
5624 C C   . ASN C 173 ? 3.57763 3.34865 2.57910 -0.56118 -0.31983 -0.41617 173 ASN C C   
5625 O O   . ASN C 173 ? 3.51983 3.30586 2.50391 -0.55997 -0.33603 -0.42588 173 ASN C O   
5626 C CB  . ASN C 173 ? 3.82077 3.34822 2.64993 -0.57550 -0.30867 -0.43680 173 ASN C CB  
5627 C CG  . ASN C 173 ? 3.87347 3.40585 2.72289 -0.61758 -0.33492 -0.42389 173 ASN C CG  
5628 O OD1 . ASN C 173 ? 3.80780 3.43296 2.71908 -0.64698 -0.36953 -0.41111 173 ASN C OD1 
5629 N ND2 . ASN C 173 ? 3.98911 3.42469 2.79092 -0.61871 -0.31641 -0.42461 173 ASN C ND2 
5630 N N   . LYS C 174 ? 3.49116 3.35014 2.57172 -0.57759 -0.33065 -0.39730 174 LYS C N   
5631 C CA  . LYS C 174 ? 3.37474 3.35791 2.53163 -0.59002 -0.35693 -0.38540 174 LYS C CA  
5632 C C   . LYS C 174 ? 3.30202 3.38112 2.54782 -0.56402 -0.33208 -0.37041 174 LYS C C   
5633 O O   . LYS C 174 ? 3.35166 3.40288 2.60316 -0.54339 -0.29997 -0.36675 174 LYS C O   
5634 C CB  . LYS C 174 ? 3.40258 3.40112 2.56598 -0.64070 -0.40049 -0.37334 174 LYS C CB  
5635 C CG  . LYS C 174 ? 3.47684 3.37485 2.54736 -0.67090 -0.43055 -0.38740 174 LYS C CG  
5636 C CD  . LYS C 174 ? 3.54432 3.42857 2.61134 -0.72258 -0.46984 -0.37362 174 LYS C CD  
5637 C CE  . LYS C 174 ? 3.63046 3.40389 2.59595 -0.75400 -0.50250 -0.38859 174 LYS C CE  
5638 N NZ  . LYS C 174 ? 3.55713 3.36521 2.51419 -0.75678 -0.52666 -0.39446 174 LYS C NZ  
5639 N N   . TYR C 175 ? 3.26055 3.45159 2.57418 -0.56449 -0.34708 -0.36064 175 TYR C N   
5640 C CA  . TYR C 175 ? 3.17976 3.45909 2.56837 -0.53624 -0.32491 -0.34966 175 TYR C CA  
5641 C C   . TYR C 175 ? 3.21288 3.51871 2.64414 -0.54887 -0.31979 -0.33072 175 TYR C C   
5642 O O   . TYR C 175 ? 3.28792 3.55033 2.69693 -0.58049 -0.33463 -0.32490 175 TYR C O   
5643 C CB  . TYR C 175 ? 3.03807 3.42194 2.47917 -0.53239 -0.34181 -0.34499 175 TYR C CB  
5644 C CG  . TYR C 175 ? 2.99109 3.35738 2.39638 -0.52095 -0.34862 -0.36158 175 TYR C CG  
5645 C CD1 . TYR C 175 ? 2.95933 3.31154 2.35678 -0.48234 -0.32176 -0.37310 175 TYR C CD1 
5646 C CD2 . TYR C 175 ? 2.97690 3.34291 2.35899 -0.54965 -0.38318 -0.36315 175 TYR C CD2 
5647 C CE1 . TYR C 175 ? 2.91161 3.24927 2.27793 -0.47135 -0.32745 -0.38690 175 TYR C CE1 
5648 C CE2 . TYR C 175 ? 2.93244 3.28371 2.28195 -0.53941 -0.38983 -0.37719 175 TYR C CE2 
5649 C CZ  . TYR C 175 ? 2.89809 3.23509 2.23938 -0.49957 -0.36102 -0.38960 175 TYR C CZ  
5650 O OH  . TYR C 175 ? 2.85424 3.17775 2.16452 -0.48883 -0.36702 -0.40232 175 TYR C OH  
5651 N N   . MET C 176 ? 2.99369 3.37031 2.48570 -0.52416 -0.29964 -0.32047 176 MET C N   
5652 C CA  . MET C 176 ? 3.00564 3.41662 2.54290 -0.53112 -0.29188 -0.30127 176 MET C CA  
5653 C C   . MET C 176 ? 2.86791 3.38073 2.47288 -0.50722 -0.28202 -0.29128 176 MET C C   
5654 O O   . MET C 176 ? 2.82593 3.35164 2.43443 -0.47680 -0.26813 -0.30076 176 MET C O   
5655 C CB  . MET C 176 ? 3.11618 3.44367 2.62382 -0.52090 -0.26378 -0.30176 176 MET C CB  
5656 C CG  . MET C 176 ? 3.14222 3.49033 2.68749 -0.53447 -0.25895 -0.28145 176 MET C CG  
5657 S SD  . MET C 176 ? 3.25462 3.51491 2.77480 -0.51477 -0.22069 -0.27895 176 MET C SD  
5658 C CE  . MET C 176 ? 3.18254 3.47634 2.72747 -0.46764 -0.19317 -0.28280 176 MET C CE  
5659 N N   . ALA C 177 ? 2.87468 3.45651 2.53046 -0.52095 -0.28961 -0.27155 177 ALA C N   
5660 C CA  . ALA C 177 ? 2.63272 3.30841 2.34587 -0.49962 -0.28187 -0.26169 177 ALA C CA  
5661 C C   . ALA C 177 ? 2.62080 3.33880 2.37630 -0.51141 -0.27896 -0.23891 177 ALA C C   
5662 O O   . ALA C 177 ? 2.71677 3.40495 2.46465 -0.54023 -0.28863 -0.22917 177 ALA C O   
5663 C CB  . ALA C 177 ? 2.45489 3.20142 2.18843 -0.50008 -0.30156 -0.26239 177 ALA C CB  
5664 N N   . SER C 178 ? 2.45475 3.24057 2.25270 -0.48906 -0.26648 -0.23019 178 SER C N   
5665 C CA  . SER C 178 ? 2.43334 3.26275 2.27110 -0.49527 -0.26069 -0.20807 178 SER C CA  
5666 C C   . SER C 178 ? 2.37044 3.29402 2.25037 -0.47641 -0.25926 -0.19926 178 SER C C   
5667 O O   . SER C 178 ? 2.34056 3.28242 2.21726 -0.45158 -0.25553 -0.21215 178 SER C O   
5668 C CB  . SER C 178 ? 2.44233 3.22181 2.27400 -0.48417 -0.23715 -0.20538 178 SER C CB  
5669 O OG  . SER C 178 ? 2.41735 3.18365 2.24093 -0.45237 -0.22086 -0.21752 178 SER C OG  
5670 N N   . SER C 179 ? 2.34324 3.32355 2.26043 -0.48760 -0.26158 -0.17652 179 SER C N   
5671 C CA  . SER C 179 ? 2.27812 3.34574 2.23102 -0.46993 -0.25860 -0.16532 179 SER C CA  
5672 C C   . SER C 179 ? 2.34399 3.44128 2.32577 -0.47121 -0.24735 -0.14357 179 SER C C   
5673 O O   . SER C 179 ? 2.45191 3.51981 2.43683 -0.49411 -0.24830 -0.13170 179 SER C O   
5674 C CB  . SER C 179 ? 2.20405 3.33117 2.17671 -0.48254 -0.27709 -0.15532 179 SER C CB  
5675 O OG  . SER C 179 ? 2.15716 3.36225 2.15697 -0.45907 -0.27033 -0.14681 179 SER C OG  
5676 N N   . PHE C 180 ? 2.25045 3.40354 2.25034 -0.44641 -0.23719 -0.13829 180 PHE C N   
5677 C CA  . PHE C 180 ? 2.23724 3.41712 2.25926 -0.44284 -0.22519 -0.11919 180 PHE C CA  
5678 C C   . PHE C 180 ? 2.20972 3.47550 2.25821 -0.43079 -0.22403 -0.10298 180 PHE C C   
5679 O O   . PHE C 180 ? 2.19494 3.49567 2.24149 -0.41615 -0.22806 -0.11024 180 PHE C O   
5680 C CB  . PHE C 180 ? 2.22588 3.37011 2.23365 -0.42111 -0.21054 -0.12873 180 PHE C CB  
5681 C CG  . PHE C 180 ? 2.25566 3.31754 2.24228 -0.43017 -0.20554 -0.13753 180 PHE C CG  
5682 C CD1 . PHE C 180 ? 2.41170 3.44004 2.40125 -0.45642 -0.20626 -0.12584 180 PHE C CD1 
5683 C CD2 . PHE C 180 ? 2.25381 3.26996 2.21692 -0.41144 -0.19922 -0.15601 180 PHE C CD2 
5684 C CE1 . PHE C 180 ? 2.52070 3.46776 2.48560 -0.46168 -0.19860 -0.13367 180 PHE C CE1 
5685 C CE2 . PHE C 180 ? 2.31350 3.25355 2.25633 -0.41620 -0.19084 -0.16152 180 PHE C CE2 
5686 C CZ  . PHE C 180 ? 2.52296 3.42654 2.46435 -0.44032 -0.18947 -0.15099 180 PHE C CZ  
5687 N N   . LEU C 181 ? 2.30707 3.60536 2.37923 -0.43527 -0.21663 -0.07975 181 LEU C N   
5688 C CA  . LEU C 181 ? 2.26214 3.64056 2.35833 -0.42353 -0.21219 -0.05986 181 LEU C CA  
5689 C C   . LEU C 181 ? 2.28227 3.67379 2.38543 -0.41427 -0.19841 -0.04549 181 LEU C C   
5690 O O   . LEU C 181 ? 2.32151 3.70582 2.44297 -0.43469 -0.19700 -0.02736 181 LEU C O   
5691 C CB  . LEU C 181 ? 2.28112 3.70179 2.40954 -0.44885 -0.22313 -0.03603 181 LEU C CB  
5692 C CG  . LEU C 181 ? 2.26000 3.76287 2.42183 -0.44155 -0.21506 -0.00529 181 LEU C CG  
5693 C CD1 . LEU C 181 ? 2.21028 3.76339 2.36577 -0.40877 -0.20761 -0.00982 181 LEU C CD1 
5694 C CD2 . LEU C 181 ? 2.28273 3.81759 2.48285 -0.47362 -0.22784 0.02337  181 LEU C CD2 
5695 N N   . HIS C 182 ? 2.38723 3.79568 2.47405 -0.38450 -0.18965 -0.05296 182 HIS C N   
5696 C CA  . HIS C 182 ? 2.39377 3.81486 2.48175 -0.37455 -0.17876 -0.03952 182 HIS C CA  
5697 C C   . HIS C 182 ? 2.38497 3.87770 2.49704 -0.37297 -0.17221 -0.01118 182 HIS C C   
5698 O O   . HIS C 182 ? 2.36500 3.90545 2.48589 -0.36582 -0.17279 -0.00541 182 HIS C O   
5699 C CB  . HIS C 182 ? 2.36922 3.77700 2.42538 -0.34500 -0.17541 -0.05763 182 HIS C CB  
5700 C CG  . HIS C 182 ? 2.37284 3.72325 2.40779 -0.34121 -0.18182 -0.08451 182 HIS C CG  
5701 N ND1 . HIS C 182 ? 2.36948 3.71548 2.37861 -0.31667 -0.18435 -0.10459 182 HIS C ND1 
5702 C CD2 . HIS C 182 ? 2.39028 3.68368 2.42454 -0.35760 -0.18513 -0.09348 182 HIS C CD2 
5703 C CE1 . HIS C 182 ? 2.37636 3.66946 2.37414 -0.31876 -0.18932 -0.12336 182 HIS C CE1 
5704 N NE2 . HIS C 182 ? 2.38504 3.64491 2.39604 -0.34232 -0.18878 -0.11711 182 HIS C NE2 
5705 N N   . LEU C 183 ? 2.31280 3.81461 2.43711 -0.37830 -0.16462 0.00898  183 LEU C N   
5706 C CA  . LEU C 183 ? 2.32089 3.88887 2.47114 -0.37870 -0.15683 0.04000  183 LEU C CA  
5707 C C   . LEU C 183 ? 2.33045 3.90549 2.47327 -0.36794 -0.14618 0.05292  183 LEU C C   
5708 O O   . LEU C 183 ? 2.34858 3.87601 2.47475 -0.36723 -0.14700 0.04195  183 LEU C O   
5709 C CB  . LEU C 183 ? 2.35219 3.93023 2.54259 -0.41270 -0.16363 0.06207  183 LEU C CB  
5710 C CG  . LEU C 183 ? 2.34337 3.92093 2.54587 -0.43003 -0.17789 0.05712  183 LEU C CG  
5711 C CD1 . LEU C 183 ? 2.37461 3.93758 2.60765 -0.46864 -0.18876 0.07558  183 LEU C CD1 
5712 C CD2 . LEU C 183 ? 2.33863 3.98746 2.55417 -0.41337 -0.17471 0.06975  183 LEU C CD2 
5713 N N   . THR C 184 ? 2.33718 3.97382 2.49405 -0.35963 -0.13601 0.07925  184 THR C N   
5714 C CA  . THR C 184 ? 2.37021 4.02165 2.52407 -0.35306 -0.12607 0.09793  184 THR C CA  
5715 C C   . THR C 184 ? 2.38936 4.04825 2.58634 -0.38333 -0.12597 0.12567  184 THR C C   
5716 O O   . THR C 184 ? 2.38519 4.05454 2.61478 -0.40618 -0.13248 0.13586  184 THR C O   
5717 C CB  . THR C 184 ? 2.37968 4.09131 2.51946 -0.32422 -0.11257 0.11217  184 THR C CB  
5718 O OG1 . THR C 184 ? 2.36575 4.07183 2.46988 -0.29829 -0.11321 0.08716  184 THR C OG1 
5719 C CG2 . THR C 184 ? 2.39579 4.10945 2.51321 -0.31142 -0.10430 0.12310  184 THR C CG2 
5720 N N   . SER C 185 ? 2.39773 4.04830 2.59398 -0.38464 -0.12029 0.13850  185 SER C N   
5721 C CA  . SER C 185 ? 2.42053 4.07637 2.65702 -0.41188 -0.11904 0.16595  185 SER C CA  
5722 C C   . SER C 185 ? 2.42342 4.14953 2.69622 -0.41769 -0.11376 0.19811  185 SER C C   
5723 O O   . SER C 185 ? 2.42388 4.15318 2.73433 -0.44584 -0.12106 0.21266  185 SER C O   
5724 C CB  . SER C 185 ? 2.44036 4.08473 2.66977 -0.40812 -0.11248 0.17743  185 SER C CB  
5725 O OG  . SER C 185 ? 2.43472 4.12099 2.63921 -0.38096 -0.10329 0.18569  185 SER C OG  
5726 N N   . ASP C 186 ? 2.35987 4.14102 2.62081 -0.39113 -0.10109 0.21151  186 ASP C N   
5727 C CA  . ASP C 186 ? 2.36772 4.22135 2.66641 -0.39303 -0.09285 0.24714  186 ASP C CA  
5728 C C   . ASP C 186 ? 2.35910 4.23781 2.67314 -0.39420 -0.09884 0.24414  186 ASP C C   
5729 O O   . ASP C 186 ? 2.36251 4.29205 2.72261 -0.40854 -0.09909 0.27527  186 ASP C O   
5730 C CB  . ASP C 186 ? 2.38043 4.28177 2.65676 -0.36096 -0.07410 0.26408  186 ASP C CB  
5731 C CG  . ASP C 186 ? 2.39549 4.37574 2.71370 -0.35987 -0.06173 0.30629  186 ASP C CG  
5732 O OD1 . ASP C 186 ? 2.39370 4.39178 2.75895 -0.38651 -0.06375 0.33568  186 ASP C OD1 
5733 O OD2 . ASP C 186 ? 2.41168 4.43621 2.71648 -0.33120 -0.04896 0.31205  186 ASP C OD2 
5734 N N   . GLN C 187 ? 2.38547 4.23048 2.66466 -0.38052 -0.10489 0.20948  187 GLN C N   
5735 C CA  . GLN C 187 ? 2.37713 4.24618 2.66883 -0.37966 -0.11074 0.20626  187 GLN C CA  
5736 C C   . GLN C 187 ? 2.35087 4.19222 2.67514 -0.41891 -0.13092 0.20573  187 GLN C C   
5737 O O   . GLN C 187 ? 2.34490 4.22148 2.69758 -0.42823 -0.13826 0.21859  187 GLN C O   
5738 C CB  . GLN C 187 ? 2.36122 4.20156 2.60350 -0.35149 -0.11062 0.16948  187 GLN C CB  
5739 C CG  . GLN C 187 ? 2.35697 4.23306 2.60797 -0.34096 -0.11160 0.16904  187 GLN C CG  
5740 C CD  . GLN C 187 ? 2.34226 4.18326 2.54432 -0.31474 -0.11258 0.13132  187 GLN C CD  
5741 O OE1 . GLN C 187 ? 2.34255 4.15265 2.50052 -0.29389 -0.10709 0.11263  187 GLN C OE1 
5742 N NE2 . GLN C 187 ? 2.32874 4.17317 2.53905 -0.31733 -0.12156 0.12117  187 GLN C NE2 
5743 N N   . TRP C 188 ? 2.34360 4.12107 2.66296 -0.44193 -0.14013 0.19291  188 TRP C N   
5744 C CA  . TRP C 188 ? 2.35586 4.09745 2.69749 -0.47937 -0.15901 0.19225  188 TRP C CA  
5745 C C   . TRP C 188 ? 2.37708 4.16438 2.77190 -0.50586 -0.16267 0.23407  188 TRP C C   
5746 O O   . TRP C 188 ? 2.38026 4.19039 2.80474 -0.52641 -0.17693 0.24833  188 TRP C O   
5747 C CB  . TRP C 188 ? 2.38592 4.04183 2.70309 -0.49239 -0.16389 0.16782  188 TRP C CB  
5748 C CG  . TRP C 188 ? 2.42328 4.03033 2.75210 -0.52919 -0.18205 0.16497  188 TRP C CG  
5749 C CD1 . TRP C 188 ? 2.42876 4.00237 2.74262 -0.53942 -0.19757 0.14360  188 TRP C CD1 
5750 C CD2 . TRP C 188 ? 2.46885 4.05008 2.82168 -0.56073 -0.18738 0.18395  188 TRP C CD2 
5751 N NE1 . TRP C 188 ? 2.48015 4.00512 2.80233 -0.57556 -0.21300 0.14714  188 TRP C NE1 
5752 C CE2 . TRP C 188 ? 2.50853 4.03586 2.85466 -0.58910 -0.20691 0.17147  188 TRP C CE2 
5753 C CE3 . TRP C 188 ? 2.49017 4.08603 2.86728 -0.56768 -0.17785 0.21043  188 TRP C CE3 
5754 C CZ2 . TRP C 188 ? 2.57280 4.05604 2.93217 -0.62376 -0.21734 0.18341  188 TRP C CZ2 
5755 C CZ3 . TRP C 188 ? 2.53176 4.08856 2.92785 -0.60188 -0.18732 0.22349  188 TRP C CZ3 
5756 C CH2 . TRP C 188 ? 2.57592 4.07457 2.96131 -0.62939 -0.20695 0.20932  188 TRP C CH2 
5757 N N   . ARG C 189 ? 2.37117 4.17375 2.78057 -0.50672 -0.15131 0.25642  189 ARG C N   
5758 C CA  . ARG C 189 ? 2.38111 4.23283 2.84389 -0.52955 -0.15312 0.29974  189 ARG C CA  
5759 C C   . ARG C 189 ? 2.36709 4.31080 2.85968 -0.51282 -0.14408 0.33112  189 ARG C C   
5760 O O   . ARG C 189 ? 2.36543 4.35871 2.90944 -0.53215 -0.14709 0.37143  189 ARG C O   
5761 C CB  . ARG C 189 ? 2.37926 4.22648 2.84871 -0.53106 -0.14111 0.31619  189 ARG C CB  
5762 C CG  . ARG C 189 ? 2.40193 4.16478 2.85993 -0.55545 -0.15011 0.29873  189 ARG C CG  
5763 C CD  . ARG C 189 ? 2.41811 4.17813 2.88377 -0.55472 -0.13724 0.31597  189 ARG C CD  
5764 N NE  . ARG C 189 ? 2.45099 4.12966 2.90830 -0.57666 -0.14360 0.30198  189 ARG C NE  
5765 C CZ  . ARG C 189 ? 2.45955 4.11821 2.92187 -0.57917 -0.13413 0.31288  189 ARG C CZ  
5766 N NH1 . ARG C 189 ? 2.45136 4.16395 2.92498 -0.56295 -0.11981 0.33699  189 ARG C NH1 
5767 N NH2 . ARG C 189 ? 2.48261 4.06388 2.93666 -0.59730 -0.13819 0.30035  189 ARG C NH2 
5768 N N   . SER C 190 ? 2.37815 4.34471 2.84062 -0.47679 -0.13242 0.31555  190 SER C N   
5769 C CA  . SER C 190 ? 2.38237 4.43361 2.87047 -0.45647 -0.12042 0.34554  190 SER C CA  
5770 C C   . SER C 190 ? 2.37351 4.45088 2.90724 -0.48393 -0.13997 0.36389  190 SER C C   
5771 O O   . SER C 190 ? 2.37799 4.52400 2.96584 -0.49335 -0.13841 0.40910  190 SER C O   
5772 C CB  . SER C 190 ? 2.38474 4.44041 2.82304 -0.41200 -0.10474 0.32001  190 SER C CB  
5773 O OG  . SER C 190 ? 2.39453 4.52204 2.85609 -0.39308 -0.09479 0.34456  190 SER C OG  
5774 N N   . HIS C 191 ? 2.36447 4.38837 2.87780 -0.49762 -0.15947 0.33146  191 HIS C N   
5775 C CA  . HIS C 191 ? 2.35867 4.39739 2.90734 -0.52590 -0.18253 0.34476  191 HIS C CA  
5776 C C   . HIS C 191 ? 2.36988 4.34079 2.92422 -0.57298 -0.20919 0.33766  191 HIS C C   
5777 O O   . HIS C 191 ? 2.36550 4.26006 2.88061 -0.57713 -0.21007 0.30580  191 HIS C O   
5778 C CB  . HIS C 191 ? 2.34700 4.37425 2.86577 -0.50749 -0.18641 0.31481  191 HIS C CB  
5779 C CG  . HIS C 191 ? 2.34965 4.42614 2.84963 -0.45830 -0.15938 0.31432  191 HIS C CG  
5780 N ND1 . HIS C 191 ? 2.34461 4.37805 2.78468 -0.42656 -0.14726 0.27391  191 HIS C ND1 
5781 C CD2 . HIS C 191 ? 2.36645 4.52822 2.89735 -0.43459 -0.14162 0.35049  191 HIS C CD2 
5782 C CE1 . HIS C 191 ? 2.36107 4.44595 2.79089 -0.38618 -0.12451 0.28259  191 HIS C CE1 
5783 N NE2 . HIS C 191 ? 2.38038 4.54354 2.86379 -0.38847 -0.11867 0.32883  191 HIS C NE2 
5784 N N   . ASN C 192 ? 2.34731 4.34464 2.95018 -0.60840 -0.23113 0.36944  192 ASN C N   
5785 C CA  . ASN C 192 ? 2.37289 4.30554 2.98066 -0.65565 -0.25839 0.36759  192 ASN C CA  
5786 C C   . ASN C 192 ? 2.36718 4.26354 2.96606 -0.68215 -0.28895 0.35280  192 ASN C C   
5787 O O   . ASN C 192 ? 2.39887 4.27643 3.02193 -0.72546 -0.31727 0.37077  192 ASN C O   
5788 C CB  . ASN C 192 ? 2.37488 4.35412 3.04339 -0.68299 -0.26415 0.41826  192 ASN C CB  
5789 C CG  . ASN C 192 ? 2.35128 4.43277 3.08148 -0.68216 -0.26604 0.46661  192 ASN C CG  
5790 O OD1 . ASN C 192 ? 2.34493 4.45335 3.07535 -0.67133 -0.27076 0.46274  192 ASN C OD1 
5791 N ND2 . ASN C 192 ? 2.33957 4.48051 3.12555 -0.69305 -0.26153 0.51524  192 ASN C ND2 
5792 N N   . SER C 193 ? 2.34102 4.22360 2.90263 -0.65760 -0.28520 0.31998  193 SER C N   
5793 C CA  . SER C 193 ? 2.34744 4.19383 2.89515 -0.68013 -0.31342 0.30375  193 SER C CA  
5794 C C   . SER C 193 ? 2.33160 4.13337 2.82118 -0.64926 -0.30332 0.25530  193 SER C C   
5795 O O   . SER C 193 ? 2.29867 4.15039 2.78571 -0.61041 -0.28276 0.25239  193 SER C O   
5796 C CB  . SER C 193 ? 2.32520 4.25779 2.92947 -0.68933 -0.32648 0.34498  193 SER C CB  
5797 O OG  . SER C 193 ? 2.32794 4.23010 2.91515 -0.70603 -0.35243 0.32778  193 SER C OG  
5798 N N   . PHE C 194 ? 2.44180 4.14753 2.88335 -0.66547 -0.31685 0.21844  194 PHE C N   
5799 C CA  . PHE C 194 ? 2.42664 4.08238 2.81431 -0.64148 -0.31116 0.17355  194 PHE C CA  
5800 C C   . PHE C 194 ? 2.46291 4.05075 2.82346 -0.67318 -0.34105 0.15466  194 PHE C C   
5801 O O   . PHE C 194 ? 2.52553 4.05719 2.88002 -0.70969 -0.35958 0.15802  194 PHE C O   
5802 C CB  . PHE C 194 ? 2.44121 4.03850 2.78783 -0.62041 -0.28978 0.14437  194 PHE C CB  
5803 C CG  . PHE C 194 ? 2.42236 4.06937 2.79180 -0.60026 -0.26566 0.16562  194 PHE C CG  
5804 C CD1 . PHE C 194 ? 2.37724 4.07606 2.74240 -0.55901 -0.24328 0.16344  194 PHE C CD1 
5805 C CD2 . PHE C 194 ? 2.46023 4.09814 2.85156 -0.62253 -0.26579 0.18765  194 PHE C CD2 
5806 C CE1 . PHE C 194 ? 2.37559 4.11553 2.75460 -0.54053 -0.22207 0.18262  194 PHE C CE1 
5807 C CE2 . PHE C 194 ? 2.44935 4.13323 2.86028 -0.60419 -0.24400 0.20820  194 PHE C CE2 
5808 C CZ  . PHE C 194 ? 2.41009 4.14454 2.81309 -0.56320 -0.22238 0.20548  194 PHE C CZ  
5809 N N   . THR C 195 ? 2.33761 3.92682 2.67821 -0.65905 -0.34593 0.13467  195 THR C N   
5810 C CA  . THR C 195 ? 2.38079 3.91379 2.69532 -0.68805 -0.37569 0.11945  195 THR C CA  
5811 C C   . THR C 195 ? 2.35821 3.84877 2.62236 -0.66105 -0.36832 0.07736  195 THR C C   
5812 O O   . THR C 195 ? 2.28639 3.81689 2.55021 -0.62162 -0.34583 0.06837  195 THR C O   
5813 C CB  . THR C 195 ? 2.36748 3.96792 2.73027 -0.71197 -0.40100 0.15545  195 THR C CB  
5814 O OG1 . THR C 195 ? 2.30375 3.99412 2.69733 -0.67654 -0.38311 0.16893  195 THR C OG1 
5815 C CG2 . THR C 195 ? 2.39261 4.02524 2.80555 -0.74593 -0.41418 0.19887  195 THR C CG2 
5816 N N   . CYS C 196 ? 2.38008 3.78604 2.59895 -0.68272 -0.38794 0.05221  196 CYS C N   
5817 C CA  . CYS C 196 ? 2.35778 3.71384 2.52648 -0.66140 -0.38342 0.01299  196 CYS C CA  
5818 C C   . CYS C 196 ? 2.38786 3.72023 2.54147 -0.68973 -0.41593 0.01010  196 CYS C C   
5819 O O   . CYS C 196 ? 2.47468 3.73259 2.59767 -0.72417 -0.43752 0.00428  196 CYS C O   
5820 C CB  . CYS C 196 ? 2.43472 3.69574 2.55193 -0.65394 -0.36889 -0.01825 196 CYS C CB  
5821 S SG  . CYS C 196 ? 2.43755 3.63519 2.49529 -0.62485 -0.35955 -0.06383 196 CYS C SG  
5822 N N   . GLN C 197 ? 2.36775 3.76028 2.54021 -0.67557 -0.41999 0.01488  197 GLN C N   
5823 C CA  . GLN C 197 ? 2.39666 3.77623 2.55855 -0.70074 -0.45158 0.01479  197 GLN C CA  
5824 C C   . GLN C 197 ? 2.36002 3.69576 2.47262 -0.67555 -0.44480 -0.02404 197 GLN C C   
5825 O O   . GLN C 197 ? 2.28061 3.65251 2.39797 -0.63485 -0.41969 -0.03530 197 GLN C O   
5826 C CB  . GLN C 197 ? 2.36642 3.85110 2.59353 -0.70731 -0.46417 0.05585  197 GLN C CB  
5827 C CG  . GLN C 197 ? 2.28658 3.85507 2.54360 -0.66083 -0.43589 0.06084  197 GLN C CG  
5828 C CD  . GLN C 197 ? 2.27017 3.93570 2.58787 -0.66621 -0.44805 0.10176  197 GLN C CD  
5829 O OE1 . GLN C 197 ? 2.32085 4.00877 2.67406 -0.70523 -0.47522 0.13587  197 GLN C OE1 
5830 N NE2 . GLN C 197 ? 2.23520 3.95783 2.56594 -0.62695 -0.42825 0.10043  197 GLN C NE2 
5831 N N   . VAL C 198 ? 2.42568 3.68014 2.48815 -0.69979 -0.46755 -0.04407 198 VAL C N   
5832 C CA  . VAL C 198 ? 2.42284 3.62552 2.43390 -0.67938 -0.46282 -0.08036 198 VAL C CA  
5833 C C   . VAL C 198 ? 2.44552 3.66229 2.45608 -0.70080 -0.49466 -0.07341 198 VAL C C   
5834 O O   . VAL C 198 ? 2.53845 3.71480 2.53302 -0.74316 -0.52712 -0.06440 198 VAL C O   
5835 C CB  . VAL C 198 ? 2.52593 3.61117 2.46892 -0.68415 -0.45756 -0.11199 198 VAL C CB  
5836 C CG1 . VAL C 198 ? 2.45461 3.50288 2.35675 -0.64839 -0.43845 -0.14663 198 VAL C CG1 
5837 C CG2 . VAL C 198 ? 2.58496 3.65357 2.53688 -0.68234 -0.43786 -0.10587 198 VAL C CG2 
5838 N N   . THR C 199 ? 2.48662 3.75751 2.51281 -0.67247 -0.48679 -0.07705 199 THR C N   
5839 C CA  . THR C 199 ? 2.51059 3.80122 2.53951 -0.68847 -0.51486 -0.06969 199 THR C CA  
5840 C C   . THR C 199 ? 2.51258 3.70645 2.46740 -0.68894 -0.52182 -0.10796 199 THR C C   
5841 O O   . THR C 199 ? 2.47167 3.65712 2.40617 -0.65312 -0.50106 -0.13327 199 THR C O   
5842 C CB  . THR C 199 ? 2.44870 3.83946 2.52774 -0.65588 -0.50101 -0.05492 199 THR C CB  
5843 O OG1 . THR C 199 ? 2.41832 3.89557 2.56234 -0.65359 -0.49179 -0.01745 199 THR C OG1 
5844 C CG2 . THR C 199 ? 2.45964 3.87374 2.54568 -0.67272 -0.53014 -0.04428 199 THR C CG2 
5845 N N   . HIS C 200 ? 2.53182 3.64950 2.44372 -0.72945 -0.55130 -0.11145 200 HIS C N   
5846 C CA  . HIS C 200 ? 2.63924 3.65348 2.47171 -0.73263 -0.55831 -0.14631 200 HIS C CA  
5847 C C   . HIS C 200 ? 2.68805 3.70887 2.51217 -0.76019 -0.59652 -0.13735 200 HIS C C   
5848 O O   . HIS C 200 ? 2.76687 3.74248 2.56660 -0.80490 -0.63224 -0.12756 200 HIS C O   
5849 C CB  . HIS C 200 ? 2.72036 3.62872 2.49739 -0.75547 -0.56109 -0.15962 200 HIS C CB  
5850 C CG  . HIS C 200 ? 2.88004 3.67679 2.57136 -0.74736 -0.55575 -0.19721 200 HIS C CG  
5851 N ND1 . HIS C 200 ? 2.89577 3.65689 2.54327 -0.75829 -0.57903 -0.20935 200 HIS C ND1 
5852 C CD2 . HIS C 200 ? 2.95420 3.66739 2.59590 -0.72840 -0.52859 -0.22279 200 HIS C CD2 
5853 C CE1 . HIS C 200 ? 2.97702 3.63623 2.54896 -0.74504 -0.56513 -0.24171 200 HIS C CE1 
5854 N NE2 . HIS C 200 ? 3.03114 3.66023 2.59980 -0.72633 -0.53386 -0.24950 200 HIS C NE2 
5855 N N   . GLU C 201 ? 2.77717 3.85377 2.62131 -0.73377 -0.59008 -0.13981 201 GLU C N   
5856 C CA  . GLU C 201 ? 2.78906 3.87776 2.62750 -0.75407 -0.62325 -0.13184 201 GLU C CA  
5857 C C   . GLU C 201 ? 2.79839 3.95271 2.69281 -0.79533 -0.65906 -0.08685 201 GLU C C   
5858 O O   . GLU C 201 ? 2.83286 3.96707 2.70896 -0.83157 -0.69881 -0.07712 201 GLU C O   
5859 C CB  . GLU C 201 ? 2.88733 3.85693 2.63410 -0.77236 -0.64142 -0.16244 201 GLU C CB  
5860 C CG  . GLU C 201 ? 2.89762 3.80241 2.59061 -0.73176 -0.60672 -0.20294 201 GLU C CG  
5861 C CD  . GLU C 201 ? 3.00116 3.77968 2.59871 -0.74894 -0.62017 -0.23084 201 GLU C CD  
5862 O OE1 . GLU C 201 ? 3.11057 3.81819 2.67072 -0.77992 -0.63413 -0.23074 201 GLU C OE1 
5863 O OE2 . GLU C 201 ? 2.97854 3.72646 2.53624 -0.73073 -0.61629 -0.25233 201 GLU C OE2 
5864 N N   . GLY C 202 ? 2.55690 3.79061 2.52029 -0.79056 -0.64612 -0.05690 202 GLY C N   
5865 C CA  . GLY C 202 ? 2.56555 3.86927 2.59132 -0.82738 -0.67686 -0.00877 202 GLY C CA  
5866 C C   . GLY C 202 ? 2.59433 3.87639 2.62979 -0.85599 -0.68341 0.00727  202 GLY C C   
5867 O O   . GLY C 202 ? 2.56775 3.93423 2.67600 -0.86564 -0.68634 0.04903  202 GLY C O   
5868 N N   . ASN C 203 ? 2.67774 3.84644 2.64056 -0.86843 -0.68432 -0.02400 203 ASN C N   
5869 C CA  . ASN C 203 ? 2.74794 3.88331 2.71247 -0.89398 -0.68838 -0.01281 203 ASN C CA  
5870 C C   . ASN C 203 ? 2.69784 3.87702 2.69786 -0.85350 -0.64201 -0.01438 203 ASN C C   
5871 O O   . ASN C 203 ? 2.69961 3.83432 2.66000 -0.81738 -0.60902 -0.04981 203 ASN C O   
5872 C CB  . ASN C 203 ? 2.87633 3.86997 2.74602 -0.91708 -0.70189 -0.04645 203 ASN C CB  
5873 C CG  . ASN C 203 ? 2.94063 3.88142 2.76638 -0.96138 -0.75174 -0.04437 203 ASN C CG  
5874 O OD1 . ASN C 203 ? 2.91919 3.92092 2.79458 -0.99587 -0.78803 -0.00558 203 ASN C OD1 
5875 N ND2 . ASN C 203 ? 3.02347 3.85003 2.75515 -0.96055 -0.75405 -0.08414 203 ASN C ND2 
5876 N N   . THR C 204 ? 2.62125 3.88816 2.69626 -0.85959 -0.64001 0.02607  204 THR C N   
5877 C CA  . THR C 204 ? 2.55951 3.87104 2.66857 -0.82438 -0.59891 0.02893  204 THR C CA  
5878 C C   . THR C 204 ? 2.62521 3.88470 2.72471 -0.85081 -0.60253 0.03472  204 THR C C   
5879 O O   . THR C 204 ? 2.61897 3.93616 2.77609 -0.87033 -0.61061 0.07367  204 THR C O   
5880 C CB  . THR C 204 ? 2.47409 3.91778 2.66909 -0.80645 -0.58796 0.06966  204 THR C CB  
5881 O OG1 . THR C 204 ? 2.50827 3.99826 2.75528 -0.85002 -0.62196 0.11663  204 THR C OG1 
5882 C CG2 . THR C 204 ? 2.39677 3.88587 2.59797 -0.77787 -0.58219 0.06254  204 THR C CG2 
5883 N N   . VAL C 205 ? 2.54990 3.69775 2.57581 -0.85006 -0.59504 -0.00330 205 VAL C N   
5884 C CA  . VAL C 205 ? 2.63685 3.72504 2.64681 -0.86950 -0.59306 -0.00226 205 VAL C CA  
5885 C C   . VAL C 205 ? 2.57255 3.72383 2.63078 -0.83704 -0.55475 0.00903  205 VAL C C   
5886 O O   . VAL C 205 ? 2.50202 3.69591 2.57068 -0.79267 -0.52316 -0.00365 205 VAL C O   
5887 C CB  . VAL C 205 ? 2.75694 3.70987 2.67430 -0.86964 -0.58868 -0.04549 205 VAL C CB  
5888 C CG1 . VAL C 205 ? 2.89369 3.77300 2.78867 -0.90039 -0.59689 -0.04081 205 VAL C CG1 
5889 C CG2 . VAL C 205 ? 2.81081 3.70807 2.67320 -0.88789 -0.61894 -0.06289 205 VAL C CG2 
5890 N N   . GLU C 206 ? 2.49737 3.65213 2.58305 -0.85993 -0.55869 0.03342  206 GLU C N   
5891 C CA  . GLU C 206 ? 2.43269 3.66169 2.57291 -0.83435 -0.52750 0.05308  206 GLU C CA  
5892 C C   . GLU C 206 ? 2.51393 3.69357 2.64975 -0.85550 -0.52576 0.06076  206 GLU C C   
5893 O O   . GLU C 206 ? 2.60405 3.73200 2.72616 -0.89996 -0.55773 0.07128  206 GLU C O   
5894 C CB  . GLU C 206 ? 2.37077 3.72531 2.59208 -0.83579 -0.53456 0.09827  206 GLU C CB  
5895 C CG  . GLU C 206 ? 2.31422 3.75071 2.59082 -0.80879 -0.50278 0.12241  206 GLU C CG  
5896 C CD  . GLU C 206 ? 2.33935 3.78350 2.65200 -0.84243 -0.51459 0.15660  206 GLU C CD  
5897 O OE1 . GLU C 206 ? 2.39617 3.82841 2.72086 -0.88823 -0.55283 0.17895  206 GLU C OE1 
5898 O OE2 . GLU C 206 ? 2.31385 3.77386 2.64197 -0.82442 -0.48737 0.16184  206 GLU C OE2 
5899 N N   . LYS C 207 ? 2.49818 3.69224 2.64449 -0.82388 -0.48943 0.05605  207 LYS C N   
5900 C CA  . LYS C 207 ? 2.57359 3.73483 2.72493 -0.83746 -0.48176 0.06650  207 LYS C CA  
5901 C C   . LYS C 207 ? 2.48652 3.74090 2.69626 -0.80878 -0.45195 0.09005  207 LYS C C   
5902 O O   . LYS C 207 ? 2.38715 3.71390 2.61938 -0.77432 -0.43390 0.09065  207 LYS C O   
5903 C CB  . LYS C 207 ? 2.69773 3.74231 2.77842 -0.82878 -0.46624 0.02820  207 LYS C CB  
5904 C CG  . LYS C 207 ? 2.83105 3.76537 2.84928 -0.86545 -0.49593 0.01163  207 LYS C CG  
5905 C CD  . LYS C 207 ? 2.93890 3.76490 2.90079 -0.85908 -0.47605 -0.01339 207 LYS C CD  
5906 C CE  . LYS C 207 ? 2.93543 3.78518 2.93913 -0.86158 -0.46022 0.01093  207 LYS C CE  
5907 N NZ  . LYS C 207 ? 3.02110 3.77919 2.97916 -0.84644 -0.43332 -0.01082 207 LYS C NZ  
5908 N N   . THR C 208 ? 2.68116 3.92928 2.91141 -0.82231 -0.44632 0.10909  208 THR C N   
5909 C CA  . THR C 208 ? 2.60325 3.94385 2.89221 -0.80194 -0.42309 0.13879  208 THR C CA  
5910 C C   . THR C 208 ? 2.65759 3.95626 2.93996 -0.80064 -0.40403 0.13828  208 THR C C   
5911 O O   . THR C 208 ? 2.76587 3.96911 3.00813 -0.82278 -0.41281 0.12329  208 THR C O   
5912 C CB  . THR C 208 ? 2.34132 3.76980 2.69887 -0.82803 -0.44422 0.18803  208 THR C CB  
5913 O OG1 . THR C 208 ? 2.29587 3.81193 2.70575 -0.80458 -0.41808 0.21704  208 THR C OG1 
5914 C CG2 . THR C 208 ? 2.49518 3.86864 2.85326 -0.88066 -0.47713 0.20497  208 THR C CG2 
5915 N N   . VAL C 209 ? 2.65673 4.02722 2.97737 -0.77339 -0.37713 0.15611  209 VAL C N   
5916 C CA  . VAL C 209 ? 2.68274 4.03513 3.00979 -0.76999 -0.35767 0.16360  209 VAL C CA  
5917 C C   . VAL C 209 ? 2.60813 4.06653 3.00066 -0.76265 -0.34676 0.20615  209 VAL C C   
5918 O O   . VAL C 209 ? 2.53690 4.07947 2.96500 -0.75362 -0.34913 0.22646  209 VAL C O   
5919 C CB  . VAL C 209 ? 2.38532 3.69319 2.67052 -0.73300 -0.32808 0.12973  209 VAL C CB  
5920 C CG1 . VAL C 209 ? 2.45627 3.64898 2.67864 -0.74223 -0.33456 0.09377  209 VAL C CG1 
5921 C CG2 . VAL C 209 ? 2.25509 3.62405 2.54112 -0.69271 -0.31204 0.11857  209 VAL C CG2 
5922 N N   . SER C 210 ? 2.53942 3.99313 2.94743 -0.76469 -0.33268 0.22113  210 SER C N   
5923 C CA  . SER C 210 ? 2.47781 4.02650 2.94518 -0.75816 -0.32074 0.26320  210 SER C CA  
5924 C C   . SER C 210 ? 2.48283 4.02096 2.94775 -0.74058 -0.29415 0.26406  210 SER C C   
5925 O O   . SER C 210 ? 2.54927 4.00310 2.98409 -0.75220 -0.29348 0.24679  210 SER C O   
5926 C CB  . SER C 210 ? 2.49786 4.07327 3.01456 -0.80162 -0.34756 0.30446  210 SER C CB  
5927 O OG  . SER C 210 ? 2.57861 4.07290 3.08060 -0.83326 -0.35860 0.30250  210 SER C OG  
5928 N N   . PRO C 211 ? 2.46231 4.08197 2.95610 -0.71204 -0.27163 0.28489  211 PRO C N   
5929 C CA  . PRO C 211 ? 2.46243 4.07649 2.95519 -0.69662 -0.24826 0.28907  211 PRO C CA  
5930 C C   . PRO C 211 ? 2.50540 4.10015 3.02787 -0.72959 -0.25525 0.31655  211 PRO C C   
5931 O O   . PRO C 211 ? 2.52547 4.08464 3.03722 -0.72368 -0.24004 0.31267  211 PRO C O   
5932 C CB  . PRO C 211 ? 2.38707 4.09909 2.90405 -0.66239 -0.22723 0.31029  211 PRO C CB  
5933 C CG  . PRO C 211 ? 2.35507 4.09855 2.86317 -0.64724 -0.23269 0.29830  211 PRO C CG  
5934 C CD  . PRO C 211 ? 2.38791 4.09896 2.90414 -0.68604 -0.26359 0.29901  211 PRO C CD  
5935 N N   . THR C 212 ? 2.39277 4.01063 2.95439 -0.76450 -0.27842 0.34642  212 THR C N   
5936 C CA  . THR C 212 ? 2.42814 4.01933 3.01638 -0.79960 -0.28882 0.37199  212 THR C CA  
5937 C C   . THR C 212 ? 2.51815 3.98947 3.05779 -0.82535 -0.30570 0.34039  212 THR C C   
5938 O O   . THR C 212 ? 2.55717 3.99511 3.08861 -0.85568 -0.33485 0.33712  212 THR C O   
5939 C CB  . THR C 212 ? 2.31522 3.97854 2.96644 -0.82796 -0.30900 0.41945  212 THR C CB  
5940 O OG1 . THR C 212 ? 2.30033 3.96379 2.94664 -0.84310 -0.33469 0.41269  212 THR C OG1 
5941 C CG2 . THR C 212 ? 2.25822 4.03622 2.95669 -0.79916 -0.28585 0.45512  212 THR C CG2 
5942 N N   . GLU C 213 ? 2.59731 4.00212 3.10275 -0.81246 -0.28701 0.31844  213 GLU C N   
5943 C CA  . GLU C 213 ? 2.71137 3.99715 3.16255 -0.82697 -0.29439 0.28597  213 GLU C CA  
5944 C C   . GLU C 213 ? 2.79311 4.02830 3.25087 -0.84238 -0.28669 0.29960  213 GLU C C   
5945 O O   . GLU C 213 ? 2.73811 4.03127 3.23916 -0.83643 -0.27245 0.32978  213 GLU C O   
5946 C CB  . GLU C 213 ? 2.71417 3.95926 3.11299 -0.79134 -0.27578 0.24393  213 GLU C CB  
5947 C CG  . GLU C 213 ? 2.66114 3.94472 3.06891 -0.75486 -0.24455 0.24639  213 GLU C CG  
5948 C CD  . GLU C 213 ? 2.65148 3.90737 3.01474 -0.72051 -0.22986 0.20939  213 GLU C CD  
5949 O OE1 . GLU C 213 ? 2.70016 3.90242 3.02437 -0.72383 -0.24123 0.18075  213 GLU C OE1 
5950 O OE2 . GLU C 213 ? 2.60066 3.88793 2.96759 -0.69101 -0.20826 0.21020  213 GLU C OE2 
5951 N N   . CYS C 214 ? 2.69532 3.81856 3.10686 -0.86110 -0.29513 0.27739  214 CYS C N   
5952 C CA  . CYS C 214 ? 2.76058 3.82190 3.17087 -0.87309 -0.28538 0.28682  214 CYS C CA  
5953 C C   . CYS C 214 ? 2.73839 3.79704 3.14037 -0.83508 -0.24971 0.27710  214 CYS C C   
5954 O O   . CYS C 214 ? 2.75219 3.78609 3.11580 -0.80696 -0.23663 0.24600  214 CYS C O   
5955 C CB  . CYS C 214 ? 2.89965 3.83355 3.25351 -0.89989 -0.30201 0.26380  214 CYS C CB  
5956 S SG  . CYS C 214 ? 2.94334 3.86504 3.30687 -0.95451 -0.35014 0.28150  214 CYS C SG  
5957 N N   . VAL C 215 ? 2.75092 3.83633 3.19112 -0.83536 -0.23535 0.30609  215 VAL C N   
5958 C CA  . VAL C 215 ? 2.72203 3.81407 3.16280 -0.80284 -0.20424 0.30466  215 VAL C CA  
5959 C C   . VAL C 215 ? 2.79674 3.81007 3.23265 -0.81501 -0.19347 0.31279  215 VAL C C   
5960 O O   . VAL C 215 ? 2.85549 3.82589 3.29651 -0.84877 -0.20973 0.32556  215 VAL C O   
5961 C CB  . VAL C 215 ? 2.60394 3.81269 3.09509 -0.78484 -0.19297 0.33410  215 VAL C CB  
5962 C CG1 . VAL C 215 ? 2.54008 3.82157 3.03190 -0.76894 -0.20022 0.32582  215 VAL C CG1 
5963 C CG2 . VAL C 215 ? 2.57635 3.82831 3.12173 -0.81207 -0.20104 0.37713  215 VAL C CG2 
5964 N N   . ALA C 216 ? 2.60954 3.60374 3.03626 -0.78713 -0.16628 0.30701  216 ALA C N   
5965 C CA  . ALA C 216 ? 2.67180 3.59745 3.09752 -0.79139 -0.14979 0.31731  216 ALA C CA  
5966 C C   . ALA C 216 ? 2.80995 3.61439 3.18770 -0.81324 -0.15887 0.29776  216 ALA C C   
5967 O O   . ALA C 216 ? 2.87025 3.62244 3.19844 -0.80925 -0.16595 0.26517  216 ALA C O   
5968 C CB  . ALA C 216 ? 2.61328 3.59694 3.09722 -0.80746 -0.14956 0.35989  216 ALA C CB  
5969 N N   . GLU D 20  ? 2.89072 2.87878 3.06900 -0.01491 -0.01845 0.05691  1   GLU D N   
5970 C CA  . GLU D 20  ? 2.84862 2.74430 3.01946 -0.02564 -0.03176 0.02778  1   GLU D CA  
5971 C C   . GLU D 20  ? 2.67675 2.60645 2.85871 -0.01480 -0.02288 -0.02361 1   GLU D C   
5972 O O   . GLU D 20  ? 2.62474 2.61592 2.80802 0.01069  -0.00727 -0.04946 1   GLU D O   
5973 C CB  . GLU D 20  ? 2.86725 2.66415 3.00266 -0.00657 -0.04152 0.02179  1   GLU D CB  
5974 C CG  . GLU D 20  ? 2.97675 2.68696 3.09863 -0.02595 -0.05751 0.06461  1   GLU D CG  
5975 C CD  . GLU D 20  ? 2.94958 2.55514 3.03633 -0.00460 -0.06958 0.04964  1   GLU D CD  
5976 O OE1 . GLU D 20  ? 2.89092 2.51193 2.96080 0.03136  -0.06210 0.01826  1   GLU D OE1 
5977 O OE2 . GLU D 20  ? 2.97281 2.48342 3.04979 -0.02426 -0.08660 0.06678  1   GLU D OE2 
5978 N N   . VAL D 21  ? 2.70117 2.59001 2.89075 -0.03439 -0.03266 -0.03839 2   VAL D N   
5979 C CA  . VAL D 21  ? 2.55953 2.45596 2.75249 -0.02244 -0.02534 -0.08433 2   VAL D CA  
5980 C C   . VAL D 21  ? 2.48601 2.32033 2.65024 0.00121  -0.02415 -0.11529 2   VAL D C   
5981 O O   . VAL D 21  ? 2.52541 2.28026 2.66690 0.00097  -0.03783 -0.10688 2   VAL D O   
5982 C CB  . VAL D 21  ? 2.48056 2.34928 2.68490 -0.04596 -0.03750 -0.08812 2   VAL D CB  
5983 C CG1 . VAL D 21  ? 2.37529 2.25453 2.58170 -0.03069 -0.02782 -0.12992 2   VAL D CG1 
5984 C CG2 . VAL D 21  ? 2.56853 2.50212 2.80146 -0.07228 -0.04029 -0.05480 2   VAL D CG2 
5985 N N   . MET D 22  ? 2.70280 2.57412 2.86834 0.02131  -0.00739 -0.15272 3   MET D N   
5986 C CA  . MET D 22  ? 2.62799 2.45767 2.76883 0.04265  -0.00297 -0.18340 3   MET D CA  
5987 C C   . MET D 22  ? 2.36778 2.21098 2.51428 0.04928  0.01219  -0.22563 3   MET D C   
5988 O O   . MET D 22  ? 2.32044 2.23654 2.48527 0.05619  0.02943  -0.24165 3   MET D O   
5989 C CB  . MET D 22  ? 2.72215 2.59595 2.85473 0.06457  0.00562  -0.17913 3   MET D CB  
5990 C CG  . MET D 22  ? 2.70247 2.52500 2.80522 0.08556  0.00357  -0.19965 3   MET D CG  
5991 S SD  . MET D 22  ? 2.70387 2.60783 2.80118 0.11704  0.01909  -0.21029 3   MET D SD  
5992 C CE  . MET D 22  ? 2.54531 2.53352 2.67051 0.11568  0.04362  -0.25512 3   MET D CE  
5993 N N   . LEU D 23  ? 2.44698 2.21905 2.57693 0.04762  0.00621  -0.24355 4   LEU D N   
5994 C CA  . LEU D 23  ? 2.32173 2.08890 2.45061 0.05391  0.02122  -0.28010 4   LEU D CA  
5995 C C   . LEU D 23  ? 2.28795 2.01529 2.39089 0.06811  0.02543  -0.30479 4   LEU D C   
5996 O O   . LEU D 23  ? 2.28415 1.94297 2.36513 0.06766  0.01172  -0.30441 4   LEU D O   
5997 C CB  . LEU D 23  ? 2.27232 1.99890 2.40187 0.04214  0.01220  -0.27815 4   LEU D CB  
5998 C CG  . LEU D 23  ? 2.31398 2.07932 2.46802 0.02732  0.00474  -0.25425 4   LEU D CG  
5999 C CD1 . LEU D 23  ? 2.27532 1.99146 2.42292 0.01739  -0.01029 -0.25089 4   LEU D CD1 
6000 C CD2 . LEU D 23  ? 2.29650 2.13417 2.47367 0.03459  0.02402  -0.26846 4   LEU D CD2 
6001 N N   . VAL D 24  ? 2.37655 2.15330 2.48288 0.08074  0.04412  -0.32867 5   VAL D N   
6002 C CA  . VAL D 24  ? 2.35078 2.10823 2.43550 0.09418  0.05040  -0.35465 5   VAL D CA  
6003 C C   . VAL D 24  ? 2.24936 2.00290 2.33617 0.09093  0.07096  -0.39046 5   VAL D C   
6004 O O   . VAL D 24  ? 2.20586 2.01315 2.31340 0.08925  0.09032  -0.40971 5   VAL D O   
6005 C CB  . VAL D 24  ? 2.40508 2.22496 2.49072 0.11062  0.05668  -0.35781 5   VAL D CB  
6006 C CG1 . VAL D 24  ? 2.51480 2.30877 2.58540 0.11824  0.03550  -0.32158 5   VAL D CG1 
6007 C CG2 . VAL D 24  ? 2.40309 2.31165 2.51822 0.10919  0.07189  -0.36199 5   VAL D CG2 
6008 N N   . GLU D 25  ? 2.39469 2.08333 2.45953 0.08992  0.06725  -0.39941 6   GLU D N   
6009 C CA  . GLU D 25  ? 2.32172 1.99477 2.38376 0.08560  0.08727  -0.42756 6   GLU D CA  
6010 C C   . GLU D 25  ? 2.31011 2.00736 2.36407 0.09192  0.10437  -0.45980 6   GLU D C   
6011 O O   . GLU D 25  ? 2.34811 2.07337 2.39562 0.10395  0.09844  -0.46089 6   GLU D O   
6012 C CB  . GLU D 25  ? 2.29224 1.89234 2.33305 0.08245  0.07636  -0.42000 6   GLU D CB  
6013 C CG  . GLU D 25  ? 2.31884 1.90290 2.36957 0.07495  0.06320  -0.39535 6   GLU D CG  
6014 C CD  . GLU D 25  ? 2.35890 1.92362 2.40572 0.07228  0.03494  -0.36702 6   GLU D CD  
6015 O OE1 . GLU D 25  ? 2.39417 1.95664 2.43111 0.07883  0.02609  -0.36380 6   GLU D OE1 
6016 O OE2 . GLU D 25  ? 2.36279 1.91394 2.41619 0.06375  0.02177  -0.34861 6   GLU D OE2 
6017 N N   . SER D 26  ? 2.41861 2.10523 2.47224 0.08388  0.12639  -0.48568 7   SER D N   
6018 C CA  . SER D 26  ? 2.40895 2.12413 2.45883 0.08363  0.14631  -0.51995 7   SER D CA  
6019 C C   . SER D 26  ? 2.36988 2.04601 2.41405 0.07005  0.16798  -0.53795 7   SER D C   
6020 O O   . SER D 26  ? 2.34563 1.98896 2.39556 0.06349  0.17227  -0.52808 7   SER D O   
6021 C CB  . SER D 26  ? 2.41774 2.21753 2.49404 0.08419  0.16056  -0.54039 7   SER D CB  
6022 O OG  . SER D 26  ? 2.40338 2.23787 2.47909 0.08063  0.18083  -0.57763 7   SER D OG  
6023 N N   . GLY D 27  ? 2.41822 2.09989 2.44982 0.06699  0.18214  -0.56312 8   GLY D N   
6024 C CA  . GLY D 27  ? 2.40780 2.06011 2.43549 0.05049  0.20824  -0.58161 8   GLY D CA  
6025 C C   . GLY D 27  ? 2.43239 2.02818 2.42725 0.05205  0.20497  -0.57386 8   GLY D C   
6026 O O   . GLY D 27  ? 2.45130 1.99648 2.43708 0.04360  0.21676  -0.56706 8   GLY D O   
6027 N N   . GLY D 28  ? 2.72550 2.33083 2.70069 0.06542  0.18952  -0.57511 9   GLY D N   
6028 C CA  . GLY D 28  ? 2.75162 2.31322 2.69471 0.07018  0.18434  -0.57066 9   GLY D CA  
6029 C C   . GLY D 28  ? 2.82535 2.41843 2.76084 0.06142  0.20773  -0.60108 9   GLY D C   
6030 O O   . GLY D 28  ? 2.85881 2.51315 2.80209 0.06617  0.21026  -0.62324 9   GLY D O   
6031 N N   . ASP D 29  ? 2.95316 2.50817 2.87261 0.04919  0.22520  -0.60079 10  ASP D N   
6032 C CA  . ASP D 29  ? 2.97321 2.55597 2.88468 0.03565  0.25039  -0.62689 10  ASP D CA  
6033 C C   . ASP D 29  ? 3.00187 2.52692 2.88770 0.02790  0.26242  -0.61201 10  ASP D C   
6034 O O   . ASP D 29  ? 2.99545 2.46381 2.87277 0.03338  0.25332  -0.58455 10  ASP D O   
6035 C CB  . ASP D 29  ? 2.95165 2.58275 2.89468 0.01089  0.28103  -0.65673 10  ASP D CB  
6036 C CG  . ASP D 29  ? 2.92856 2.61922 2.86981 -0.00061 0.30061  -0.69026 10  ASP D CG  
6037 O OD1 . ASP D 29  ? 2.94039 2.60959 2.86601 -0.01726 0.32129  -0.69282 10  ASP D OD1 
6038 O OD2 . ASP D 29  ? 2.89185 2.65544 2.84640 0.00807  0.29538  -0.71296 10  ASP D OD2 
6039 N N   . LEU D 30  ? 2.90106 2.44760 2.77399 0.01600  0.28342  -0.62987 11  LEU D N   
6040 C CA  . LEU D 30  ? 2.93534 2.43640 2.78089 0.00846  0.29829  -0.61510 11  LEU D CA  
6041 C C   . LEU D 30  ? 2.94784 2.42164 2.80709 -0.02320 0.33657  -0.61687 11  LEU D C   
6042 O O   . LEU D 30  ? 2.92284 2.43474 2.81069 -0.04576 0.35829  -0.64425 11  LEU D O   
6043 C CB  . LEU D 30  ? 2.94382 2.48557 2.76652 0.01177  0.30201  -0.63158 11  LEU D CB  
6044 C CG  . LEU D 30  ? 2.98828 2.49596 2.77930 0.00515  0.31839  -0.61598 11  LEU D CG  
6045 C CD1 . LEU D 30  ? 3.00853 2.48384 2.76731 0.03704  0.28567  -0.59345 11  LEU D CD1 
6046 C CD2 . LEU D 30  ? 2.99467 2.56086 2.78012 -0.01216 0.34350  -0.64198 11  LEU D CD2 
6047 N N   . VAL D 31  ? 2.94911 2.35632 2.78710 -0.02364 0.34473  -0.58841 12  VAL D N   
6048 C CA  . VAL D 31  ? 2.98210 2.34480 2.82714 -0.04989 0.38079  -0.58410 12  VAL D CA  
6049 C C   . VAL D 31  ? 3.04932 2.37124 2.85782 -0.05413 0.39861  -0.56201 12  VAL D C   
6050 O O   . VAL D 31  ? 3.07191 2.37419 2.84973 -0.02847 0.37679  -0.53751 12  VAL D O   
6051 C CB  . VAL D 31  ? 2.98397 2.29739 2.84279 -0.04080 0.37359  -0.56549 12  VAL D CB  
6052 C CG1 . VAL D 31  ? 2.93286 2.29252 2.83149 -0.04460 0.36695  -0.59049 12  VAL D CG1 
6053 C CG2 . VAL D 31  ? 2.99027 2.27370 2.82588 -0.00792 0.33919  -0.53299 12  VAL D CG2 
6054 N N   . LYS D 32  ? 2.89733 2.20922 2.70938 -0.08770 0.43891  -0.57128 13  LYS D N   
6055 C CA  . LYS D 32  ? 2.98000 2.24393 2.75755 -0.09465 0.46175  -0.54395 13  LYS D CA  
6056 C C   . LYS D 32  ? 3.02885 2.20876 2.79125 -0.07686 0.45931  -0.50575 13  LYS D C   
6057 O O   . LYS D 32  ? 3.01301 2.16513 2.80001 -0.07744 0.45958  -0.50859 13  LYS D O   
6058 C CB  . LYS D 32  ? 3.02353 2.29056 2.81230 -0.14028 0.50839  -0.56196 13  LYS D CB  
6059 C CG  . LYS D 32  ? 3.01962 2.35289 2.79544 -0.15485 0.51970  -0.57811 13  LYS D CG  
6060 C CD  . LYS D 32  ? 3.09982 2.40090 2.82871 -0.14274 0.52460  -0.54074 13  LYS D CD  
6061 C CE  . LYS D 32  ? 3.14944 2.47662 2.86943 -0.18083 0.56496  -0.54723 13  LYS D CE  
6062 N NZ  . LYS D 32  ? 3.07336 2.50639 2.80402 -0.18639 0.55845  -0.58621 13  LYS D NZ  
6063 N N   . PRO D 33  ? 3.06447 2.20930 2.78586 -0.05767 0.45605  -0.47069 14  PRO D N   
6064 C CA  . PRO D 33  ? 3.11297 2.18429 2.81701 -0.03604 0.45345  -0.43352 14  PRO D CA  
6065 C C   . PRO D 33  ? 3.16963 2.17584 2.88600 -0.05924 0.49096  -0.42884 14  PRO D C   
6066 O O   . PRO D 33  ? 3.25658 2.23027 2.95846 -0.08448 0.52842  -0.42008 14  PRO D O   
6067 C CB  . PRO D 33  ? 3.18307 2.24197 2.83880 -0.01777 0.45253  -0.40138 14  PRO D CB  
6068 C CG  . PRO D 33  ? 3.18948 2.30423 2.83929 -0.04014 0.46752  -0.42169 14  PRO D CG  
6069 C CD  . PRO D 33  ? 3.09051 2.26973 2.77874 -0.05045 0.45238  -0.46479 14  PRO D CD  
6070 N N   . GLY D 34  ? 3.10185 2.08838 2.84514 -0.05115 0.48144  -0.43516 15  GLY D N   
6071 C CA  . GLY D 34  ? 3.15159 2.07569 2.91023 -0.06931 0.51332  -0.43704 15  GLY D CA  
6072 C C   . GLY D 34  ? 3.07691 2.03724 2.88475 -0.08607 0.51177  -0.47872 15  GLY D C   
6073 O O   . GLY D 34  ? 3.10309 2.01689 2.92909 -0.09436 0.53022  -0.48584 15  GLY D O   
6074 N N   . GLY D 35  ? 3.02313 2.06743 2.85139 -0.08820 0.48938  -0.50669 16  GLY D N   
6075 C CA  . GLY D 35  ? 2.95678 2.05139 2.82985 -0.10244 0.48718  -0.54673 16  GLY D CA  
6076 C C   . GLY D 35  ? 2.91877 2.01444 2.80871 -0.07397 0.45890  -0.54103 16  GLY D C   
6077 O O   . GLY D 35  ? 2.94565 1.99572 2.81557 -0.04558 0.44459  -0.50774 16  GLY D O   
6078 N N   . SER D 36  ? 2.91979 2.07729 2.84761 -0.08144 0.45105  -0.57483 17  SER D N   
6079 C CA  . SER D 36  ? 2.88402 2.05664 2.83326 -0.05921 0.42737  -0.57371 17  SER D CA  
6080 C C   . SER D 36  ? 2.80947 2.07290 2.78342 -0.05706 0.40405  -0.59711 17  SER D C   
6081 O O   . SER D 36  ? 2.78551 2.10075 2.76800 -0.07594 0.41281  -0.62410 17  SER D O   
6082 C CB  . SER D 36  ? 2.91104 2.04772 2.88439 -0.06957 0.45135  -0.59054 17  SER D CB  
6083 O OG  . SER D 36  ? 2.90736 2.07057 2.90631 -0.10613 0.48032  -0.63254 17  SER D OG  
6084 N N   . LEU D 37  ? 2.76948 2.05452 2.75434 -0.03304 0.37487  -0.58540 18  LEU D N   
6085 C CA  . LEU D 37  ? 2.68780 2.05158 2.69158 -0.02625 0.35043  -0.59825 18  LEU D CA  
6086 C C   . LEU D 37  ? 2.65666 2.03620 2.67953 -0.00723 0.32948  -0.58716 18  LEU D C   
6087 O O   . LEU D 37  ? 2.67577 2.00891 2.68738 0.00892  0.32135  -0.56038 18  LEU D O   
6088 C CB  . LEU D 37  ? 2.68404 2.06119 2.66160 -0.01347 0.32589  -0.58168 18  LEU D CB  
6089 C CG  . LEU D 37  ? 2.64423 2.08766 2.63363 -0.00110 0.29752  -0.58656 18  LEU D CG  
6090 C CD1 . LEU D 37  ? 2.62029 2.13413 2.63439 -0.01656 0.31250  -0.62519 18  LEU D CD1 
6091 C CD2 . LEU D 37  ? 2.65973 2.09523 2.61896 0.01414  0.27325  -0.56875 18  LEU D CD2 
6092 N N   . LYS D 38  ? 2.56842 2.02068 2.61965 -0.00805 0.32117  -0.60759 19  LYS D N   
6093 C CA  . LYS D 38  ? 2.46584 1.95059 2.53716 0.00825  0.30106  -0.59760 19  LYS D CA  
6094 C C   . LYS D 38  ? 2.44438 1.98398 2.51596 0.01924  0.27193  -0.58685 19  LYS D C   
6095 O O   . LYS D 38  ? 2.43667 2.02452 2.51258 0.01292  0.27444  -0.60719 19  LYS D O   
6096 C CB  . LYS D 38  ? 2.45847 1.98258 2.56496 -0.00095 0.31979  -0.63105 19  LYS D CB  
6097 C CG  . LYS D 38  ? 2.39487 1.96480 2.51710 -0.02395 0.34234  -0.67337 19  LYS D CG  
6098 C CD  . LYS D 38  ? 2.39687 1.99768 2.55382 -0.03402 0.36223  -0.71040 19  LYS D CD  
6099 C CE  . LYS D 38  ? 2.43297 2.05387 2.60321 -0.06437 0.39266  -0.75530 19  LYS D CE  
6100 N NZ  . LYS D 38  ? 2.47841 2.11978 2.68276 -0.07637 0.41336  -0.79606 19  LYS D NZ  
6101 N N   . VAL D 39  ? 2.31743 1.84942 2.38397 0.03581  0.24483  -0.55501 20  VAL D N   
6102 C CA  . VAL D 39  ? 2.30758 1.87632 2.37257 0.04551  0.21639  -0.53906 20  VAL D CA  
6103 C C   . VAL D 39  ? 2.29559 1.91223 2.38695 0.05247  0.20423  -0.52954 20  VAL D C   
6104 O O   . VAL D 39  ? 2.29435 1.89436 2.39264 0.05748  0.20288  -0.51731 20  VAL D O   
6105 C CB  . VAL D 39  ? 2.33405 1.85234 2.36919 0.05466  0.19357  -0.50979 20  VAL D CB  
6106 C CG1 . VAL D 39  ? 2.35611 1.85077 2.36557 0.05064  0.20132  -0.52090 20  VAL D CG1 
6107 C CG2 . VAL D 39  ? 2.33775 1.80667 2.36493 0.06064  0.19229  -0.48967 20  VAL D CG2 
6108 N N   . SER D 40  ? 2.14116 1.82135 2.24582 0.05493  0.19563  -0.53399 21  SER D N   
6109 C CA  . SER D 40  ? 2.14340 1.88046 2.27267 0.06095  0.18542  -0.52352 21  SER D CA  
6110 C C   . SER D 40  ? 2.18763 1.92167 2.30770 0.06808  0.15503  -0.48622 21  SER D C   
6111 O O   . SER D 40  ? 2.21553 1.90332 2.31096 0.06967  0.14107  -0.47279 21  SER D O   
6112 C CB  . SER D 40  ? 2.12812 1.94575 2.27959 0.05978  0.19837  -0.55244 21  SER D CB  
6113 O OG  . SER D 40  ? 2.15746 2.00178 2.29756 0.06555  0.18760  -0.54919 21  SER D OG  
6114 N N   . CYS D 41  ? 2.03978 1.82494 2.18067 0.07138  0.14524  -0.47034 22  CYS D N   
6115 C CA  . CYS D 41  ? 2.08174 1.86659 2.21854 0.07316  0.11843  -0.43321 22  CYS D CA  
6116 C C   . CYS D 41  ? 2.08444 1.95116 2.24713 0.07578  0.11666  -0.42397 22  CYS D C   
6117 O O   . CYS D 41  ? 2.08894 1.98249 2.27005 0.07480  0.11571  -0.41479 22  CYS D O   
6118 C CB  . CYS D 41  ? 2.10957 1.84426 2.23917 0.07027  0.10449  -0.41059 22  CYS D CB  
6119 S SG  . CYS D 41  ? 2.16487 1.89806 2.29444 0.06473  0.07265  -0.36790 22  CYS D SG  
6120 N N   . ALA D 42  ? 2.01376 1.92443 2.17618 0.08165  0.11617  -0.42582 23  ALA D N   
6121 C CA  . ALA D 42  ? 2.02937 2.02710 2.21384 0.08683  0.11698  -0.41779 23  ALA D CA  
6122 C C   . ALA D 42  ? 2.11525 2.11257 2.30150 0.08244  0.09512  -0.37159 23  ALA D C   
6123 O O   . ALA D 42  ? 2.19241 2.16838 2.36304 0.08393  0.07987  -0.34599 23  ALA D O   
6124 C CB  . ALA D 42  ? 2.04557 2.09215 2.22550 0.09804  0.12289  -0.43214 23  ALA D CB  
6125 N N   . ALA D 43  ? 2.02654 2.04810 2.23218 0.07682  0.09402  -0.36145 24  ALA D N   
6126 C CA  . ALA D 43  ? 2.11014 2.14394 2.32249 0.06793  0.07562  -0.31914 24  ALA D CA  
6127 C C   . ALA D 43  ? 2.18919 2.30952 2.41541 0.07301  0.07698  -0.30178 24  ALA D C   
6128 O O   . ALA D 43  ? 2.15310 2.34799 2.39570 0.08345  0.09300  -0.32581 24  ALA D O   
6129 C CB  . ALA D 43  ? 2.08002 2.12072 2.30849 0.06224  0.07438  -0.31638 24  ALA D CB  
6130 N N   . SER D 44  ? 2.15845 2.26831 2.37739 0.06561  0.06050  -0.26001 25  SER D N   
6131 C CA  . SER D 44  ? 2.25527 2.44061 2.48168 0.07171  0.06157  -0.23545 25  SER D CA  
6132 C C   . SER D 44  ? 2.43407 2.60947 2.66312 0.05321  0.04462  -0.18381 25  SER D C   
6133 O O   . SER D 44  ? 2.50596 2.59769 2.72122 0.03887  0.02890  -0.16745 25  SER D O   
6134 C CB  . SER D 44  ? 2.30982 2.48879 2.51477 0.08928  0.06391  -0.24119 25  SER D CB  
6135 O OG  . SER D 44  ? 2.39376 2.59062 2.59908 0.10214  0.08078  -0.29082 25  SER D OG  
6136 N N   . GLY D 45  ? 2.21226 2.47676 2.45976 0.05229  0.04845  -0.15959 26  GLY D N   
6137 C CA  . GLY D 45  ? 2.44854 2.71345 2.69937 0.03211  0.03556  -0.10681 26  GLY D CA  
6138 C C   . GLY D 45  ? 2.44219 2.72581 2.71573 0.00911  0.02937  -0.09454 26  GLY D C   
6139 O O   . GLY D 45  ? 2.51798 2.77021 2.79205 -0.01583 0.01556  -0.05613 26  GLY D O   
6140 N N   . PHE D 46  ? 2.46047 2.79498 2.75307 0.01686  0.03916  -0.12695 27  PHE D N   
6141 C CA  . PHE D 46  ? 2.42244 2.78793 2.73677 0.00096  0.03362  -0.11841 27  PHE D CA  
6142 C C   . PHE D 46  ? 2.24033 2.67563 2.57324 0.02113  0.04851  -0.15800 27  PHE D C   
6143 O O   . PHE D 46  ? 2.17823 2.61789 2.50632 0.04211  0.06221  -0.19506 27  PHE D O   
6144 C CB  . PHE D 46  ? 2.34554 2.61581 2.64946 -0.01583 0.01808  -0.11841 27  PHE D CB  
6145 C CG  . PHE D 46  ? 2.20268 2.40630 2.49062 0.00080  0.02287  -0.16138 27  PHE D CG  
6146 C CD1 . PHE D 46  ? 2.19051 2.32360 2.45270 0.00958  0.02365  -0.17430 27  PHE D CD1 
6147 C CD2 . PHE D 46  ? 2.10924 2.32166 2.40660 0.00873  0.02710  -0.18715 27  PHE D CD2 
6148 C CE1 . PHE D 46  ? 2.09580 2.17222 2.34346 0.02199  0.02979  -0.21129 27  PHE D CE1 
6149 C CE2 . PHE D 46  ? 2.05847 2.20610 2.33930 0.02276  0.03341  -0.22178 27  PHE D CE2 
6150 C CZ  . PHE D 46  ? 2.05560 2.13676 2.31226 0.02734  0.03531  -0.23337 27  PHE D CZ  
6151 N N   . THR D 47  ? 2.18470 2.67562 2.53958 0.01430  0.04567  -0.15145 28  THR D N   
6152 C CA  . THR D 47  ? 2.04073 2.59502 2.41354 0.03547  0.05792  -0.18816 28  THR D CA  
6153 C C   . THR D 47  ? 1.98548 2.45239 2.34485 0.04565  0.05934  -0.22385 28  THR D C   
6154 O O   . THR D 47  ? 1.99237 2.42373 2.35069 0.03798  0.04853  -0.21755 28  THR D O   
6155 C CB  . THR D 47  ? 2.17703 2.82112 2.57566 0.02753  0.05304  -0.16817 28  THR D CB  
6156 O OG1 . THR D 47  ? 2.29828 2.99965 2.70424 0.00814  0.04883  -0.12185 28  THR D OG1 
6157 C CG2 . THR D 47  ? 2.02806 2.76074 2.44634 0.05485  0.06720  -0.20439 28  THR D CG2 
6158 N N   . PHE D 48  ? 2.11497 2.55153 2.46390 0.06270  0.07348  -0.26117 29  PHE D N   
6159 C CA  . PHE D 48  ? 2.02582 2.36908 2.35729 0.06963  0.07696  -0.29011 29  PHE D CA  
6160 C C   . PHE D 48  ? 1.99218 2.34610 2.33432 0.08269  0.07983  -0.30794 29  PHE D C   
6161 O O   . PHE D 48  ? 2.00680 2.29441 2.33593 0.08134  0.07194  -0.30536 29  PHE D O   
6162 C CB  . PHE D 48  ? 1.95835 2.28097 2.28065 0.08172  0.09424  -0.32719 29  PHE D CB  
6163 C CG  . PHE D 48  ? 1.93577 2.16538 2.23982 0.08668  0.10127  -0.35529 29  PHE D CG  
6164 C CD1 . PHE D 48  ? 1.96481 2.10602 2.24539 0.07639  0.08874  -0.33899 29  PHE D CD1 
6165 C CD2 . PHE D 48  ? 1.88683 2.11721 2.19682 0.10101  0.12108  -0.39814 29  PHE D CD2 
6166 C CE1 . PHE D 48  ? 1.94580 2.00699 2.20767 0.08171  0.09633  -0.36150 29  PHE D CE1 
6167 C CE2 . PHE D 48  ? 1.87575 2.01763 2.16748 0.10359  0.12977  -0.41951 29  PHE D CE2 
6168 C CZ  . PHE D 48  ? 1.90498 1.96506 2.17184 0.09463  0.11764  -0.39945 29  PHE D CZ  
6169 N N   . SER D 49  ? 1.94801 2.38776 2.31256 0.09869  0.09068  -0.32700 30  SER D N   
6170 C CA  . SER D 49  ? 1.93668 2.38866 2.31037 0.11716  0.09370  -0.34585 30  SER D CA  
6171 C C   . SER D 49  ? 1.98440 2.46463 2.36547 0.10884  0.07571  -0.31320 30  SER D C   
6172 O O   . SER D 49  ? 1.98649 2.46267 2.36900 0.12601  0.07480  -0.32486 30  SER D O   
6173 C CB  . SER D 49  ? 1.87864 2.42204 2.27563 0.13790  0.10843  -0.37686 30  SER D CB  
6174 O OG  . SER D 49  ? 1.86160 2.51480 2.27850 0.13092  0.10317  -0.35225 30  SER D OG  
6175 N N   . ASN D 50  ? 1.93517 2.44366 2.32070 0.08314  0.06188  -0.27310 31  ASN D N   
6176 C CA  . ASN D 50  ? 1.93912 2.47983 2.33478 0.06856  0.04498  -0.24307 31  ASN D CA  
6177 C C   . ASN D 50  ? 1.97464 2.41998 2.34969 0.05956  0.03163  -0.23660 31  ASN D C   
6178 O O   . ASN D 50  ? 1.97995 2.44929 2.36242 0.05653  0.01953  -0.22575 31  ASN D O   
6179 C CB  . ASN D 50  ? 1.99712 2.59749 2.40566 0.03965  0.03669  -0.20125 31  ASN D CB  
6180 C CG  . ASN D 50  ? 2.06990 2.80251 2.50800 0.04265  0.03872  -0.19123 31  ASN D CG  
6181 O OD1 . ASN D 50  ? 1.98783 2.77111 2.43738 0.06980  0.04585  -0.21943 31  ASN D OD1 
6182 N ND2 . ASN D 50  ? 2.13299 2.92176 2.58271 0.01550  0.03301  -0.15032 31  ASN D ND2 
6183 N N   . TYR D 51  ? 1.96308 2.30972 2.31277 0.05645  0.03325  -0.24449 32  TYR D N   
6184 C CA  . TYR D 51  ? 1.98415 2.24400 2.31256 0.04748  0.01978  -0.23798 32  TYR D CA  
6185 C C   . TYR D 51  ? 1.96804 2.14459 2.27203 0.06949  0.03189  -0.26916 32  TYR D C   
6186 O O   . TYR D 51  ? 1.94189 2.09981 2.24016 0.07777  0.04812  -0.29002 32  TYR D O   
6187 C CB  . TYR D 51  ? 2.00878 2.22478 2.32739 0.01809  0.00691  -0.21149 32  TYR D CB  
6188 C CG  . TYR D 51  ? 2.02051 2.31056 2.36039 -0.00418 0.00216  -0.17936 32  TYR D CG  
6189 C CD1 . TYR D 51  ? 2.02058 2.38136 2.38323 -0.02038 -0.00833 -0.15712 32  TYR D CD1 
6190 C CD2 . TYR D 51  ? 2.02990 2.32293 2.36617 -0.00851 0.00888  -0.16984 32  TYR D CD2 
6191 C CE1 . TYR D 51  ? 2.12928 2.55821 2.51082 -0.04354 -0.01062 -0.12398 32  TYR D CE1 
6192 C CE2 . TYR D 51  ? 2.04505 2.40365 2.39754 -0.02730 0.00604  -0.13553 32  TYR D CE2 
6193 C CZ  . TYR D 51  ? 2.18167 2.60601 2.55684 -0.04644 -0.00305 -0.11152 32  TYR D CZ  
6194 O OH  . TYR D 51  ? 2.27639 2.76643 2.66725 -0.06795 -0.00392 -0.07381 32  TYR D OH  
6195 N N   . ALA D 52  ? 1.90567 2.03660 2.19528 0.07818  0.02453  -0.27172 33  ALA D N   
6196 C CA  . ALA D 52  ? 1.92414 1.97369 2.18807 0.09838  0.03659  -0.29554 33  ALA D CA  
6197 C C   . ALA D 52  ? 1.93755 1.90338 2.17589 0.08382  0.03176  -0.29226 33  ALA D C   
6198 O O   . ALA D 52  ? 1.94025 1.90051 2.17815 0.06093  0.01463  -0.27114 33  ALA D O   
6199 C CB  . ALA D 52  ? 1.94513 1.98606 2.20113 0.11945  0.03148  -0.29711 33  ALA D CB  
6200 N N   . MET D 53  ? 2.01844 1.91801 2.23521 0.09719  0.04756  -0.31420 34  MET D N   
6201 C CA  . MET D 53  ? 2.01031 1.83919 2.20292 0.08719  0.04714  -0.31693 34  MET D CA  
6202 C C   . MET D 53  ? 2.01929 1.77536 2.18265 0.09929  0.04744  -0.32178 34  MET D C   
6203 O O   . MET D 53  ? 2.03227 1.78664 2.19217 0.11862  0.05154  -0.32448 34  MET D O   
6204 C CB  . MET D 53  ? 1.97547 1.80174 2.16914 0.08810  0.06799  -0.33938 34  MET D CB  
6205 C CG  . MET D 53  ? 1.97044 1.87232 2.18911 0.07923  0.06803  -0.33391 34  MET D CG  
6206 S SD  . MET D 53  ? 2.00871 1.91791 2.22779 0.05540  0.04257  -0.29775 34  MET D SD  
6207 C CE  . MET D 53  ? 2.00248 1.81978 2.18783 0.05276  0.04082  -0.30660 34  MET D CE  
6208 N N   . SER D 54  ? 2.16486 1.86276 2.30522 0.09065  0.04326  -0.32238 35  SER D N   
6209 C CA  . SER D 54  ? 2.17749 1.81093 2.28744 0.10091  0.04211  -0.32435 35  SER D CA  
6210 C C   . SER D 54  ? 2.16308 1.74414 2.25085 0.09249  0.04404  -0.33241 35  SER D C   
6211 O O   . SER D 54  ? 2.15290 1.74630 2.24788 0.07856  0.03876  -0.33147 35  SER D O   
6212 C CB  . SER D 54  ? 2.21116 1.85379 2.31850 0.09979  0.01713  -0.30605 35  SER D CB  
6213 O OG  . SER D 54  ? 2.22630 1.81438 2.30247 0.11301  0.01576  -0.30792 35  SER D OG  
6214 N N   . TRP D 55  ? 2.34076 1.86580 2.39977 0.10356  0.05206  -0.33918 36  TRP D N   
6215 C CA  . TRP D 55  ? 2.33041 1.80858 2.36479 0.09883  0.05370  -0.34772 36  TRP D CA  
6216 C C   . TRP D 55  ? 2.35447 1.79712 2.36270 0.10480  0.03621  -0.33863 36  TRP D C   
6217 O O   . TRP D 55  ? 2.37916 1.81888 2.37976 0.11911  0.03467  -0.33066 36  TRP D O   
6218 C CB  . TRP D 55  ? 2.31556 1.76378 2.33813 0.10427  0.08429  -0.36744 36  TRP D CB  
6219 C CG  . TRP D 55  ? 2.28479 1.76734 2.33019 0.09636  0.10197  -0.38475 36  TRP D CG  
6220 C CD1 . TRP D 55  ? 2.27432 1.78510 2.34103 0.10086  0.11899  -0.39478 36  TRP D CD1 
6221 C CD2 . TRP D 55  ? 2.26018 1.75698 2.30845 0.08550  0.10417  -0.39698 36  TRP D CD2 
6222 N NE1 . TRP D 55  ? 2.24120 1.78690 2.32528 0.09149  0.13142  -0.41377 36  TRP D NE1 
6223 C CE2 . TRP D 55  ? 2.23360 1.77333 2.30628 0.08278  0.12271  -0.41423 36  TRP D CE2 
6224 C CE3 . TRP D 55  ? 2.25911 1.73939 2.29099 0.08077  0.09158  -0.39664 36  TRP D CE3 
6225 C CZ2 . TRP D 55  ? 2.20703 1.77925 2.28808 0.07555  0.12905  -0.42988 36  TRP D CZ2 
6226 C CZ3 . TRP D 55  ? 2.23721 1.74495 2.27610 0.07568  0.09795  -0.41077 36  TRP D CZ3 
6227 C CH2 . TRP D 55  ? 2.21159 1.76759 2.27481 0.07309  0.11656  -0.42660 36  TRP D CH2 
6228 N N   . VAL D 56  ? 2.33615 1.75497 2.32965 0.09682  0.02265  -0.34145 37  VAL D N   
6229 C CA  . VAL D 56  ? 2.35597 1.74182 2.32223 0.10321  0.00681  -0.33925 37  VAL D CA  
6230 C C   . VAL D 56  ? 2.34915 1.70071 2.29261 0.10230  0.01055  -0.35350 37  VAL D C   
6231 O O   . VAL D 56  ? 2.33361 1.69226 2.28611 0.09314  0.01184  -0.36078 37  VAL D O   
6232 C CB  . VAL D 56  ? 2.37848 1.78205 2.35543 0.09283  -0.02537 -0.32791 37  VAL D CB  
6233 C CG1 . VAL D 56  ? 2.40285 1.84398 2.39473 0.09868  -0.03018 -0.31550 37  VAL D CG1 
6234 C CG2 . VAL D 56  ? 2.36870 1.78827 2.36756 0.07292  -0.03637 -0.32433 37  VAL D CG2 
6235 N N   . ARG D 57  ? 2.56782 1.88776 2.48029 0.11441  0.01228  -0.35707 38  ARG D N   
6236 C CA  . ARG D 57  ? 2.56104 1.85501 2.44941 0.11621  0.01656  -0.37170 38  ARG D CA  
6237 C C   . ARG D 57  ? 2.58907 1.86640 2.45635 0.12154  -0.01052 -0.37354 38  ARG D C   
6238 O O   . ARG D 57  ? 2.61882 1.89896 2.47988 0.12869  -0.02388 -0.36468 38  ARG D O   
6239 C CB  . ARG D 57  ? 2.56671 1.84058 2.43467 0.12451  0.04795  -0.37726 38  ARG D CB  
6240 C CG  . ARG D 57  ? 2.60867 1.86318 2.45178 0.14113  0.05110  -0.36494 38  ARG D CG  
6241 C CD  . ARG D 57  ? 2.62871 1.85645 2.45090 0.14536  0.08503  -0.36763 38  ARG D CD  
6242 N NE  . ARG D 57  ? 2.69160 1.89793 2.48853 0.16422  0.09225  -0.35042 38  ARG D NE  
6243 C CZ  . ARG D 57  ? 2.73988 1.91504 2.51679 0.16914  0.12308  -0.34504 38  ARG D CZ  
6244 N NH1 . ARG D 57  ? 2.72454 1.88933 2.50647 0.15290  0.15004  -0.35887 38  ARG D NH1 
6245 N NH2 . ARG D 57  ? 2.88403 2.03919 2.63505 0.19054  0.12755  -0.32492 38  ARG D NH2 
6246 N N   . GLN D 58  ? 2.67530 1.93912 2.53153 0.12007  -0.01902 -0.38764 39  GLN D N   
6247 C CA  . GLN D 58  ? 2.70770 1.95330 2.54359 0.12601  -0.04513 -0.39614 39  GLN D CA  
6248 C C   . GLN D 58  ? 2.72262 1.95408 2.52590 0.13946  -0.03208 -0.41125 39  GLN D C   
6249 O O   . GLN D 58  ? 2.70961 1.94134 2.51068 0.13863  -0.02172 -0.42390 39  GLN D O   
6250 C CB  . GLN D 58  ? 2.71246 1.95093 2.56276 0.11498  -0.06954 -0.40006 39  GLN D CB  
6251 C CG  . GLN D 58  ? 2.75774 1.97279 2.59135 0.11899  -0.09955 -0.41189 39  GLN D CG  
6252 C CD  . GLN D 58  ? 2.77983 1.97590 2.62779 0.10685  -0.12238 -0.41328 39  GLN D CD  
6253 O OE1 . GLN D 58  ? 2.79976 1.96664 2.63169 0.11268  -0.14276 -0.42943 39  GLN D OE1 
6254 N NE2 . GLN D 58  ? 2.78929 2.00071 2.66644 0.09101  -0.11875 -0.39586 39  GLN D NE2 
6255 N N   . THR D 59  ? 2.64771 1.87382 2.42526 0.15295  -0.03221 -0.40944 40  THR D N   
6256 C CA  . THR D 59  ? 2.68308 1.90215 2.42762 0.16569  -0.01895 -0.42067 40  THR D CA  
6257 C C   . THR D 59  ? 2.69149 1.90458 2.42528 0.16993  -0.03880 -0.44316 40  THR D C   
6258 O O   . THR D 59  ? 2.68612 1.89088 2.43359 0.16473  -0.06629 -0.44800 40  THR D O   
6259 C CB  . THR D 59  ? 2.73072 1.94993 2.44842 0.18205  -0.02087 -0.41157 40  THR D CB  
6260 O OG1 . THR D 59  ? 2.75389 1.97694 2.46867 0.18696  -0.05639 -0.41955 40  THR D OG1 
6261 C CG2 . THR D 59  ? 2.73996 1.96164 2.46709 0.18316  -0.00459 -0.38835 40  THR D CG2 
6262 N N   . PRO D 60  ? 2.62164 1.83828 2.33064 0.17953  -0.02479 -0.45727 41  PRO D N   
6263 C CA  . PRO D 60  ? 2.61912 1.83206 2.31460 0.18969  -0.04504 -0.48122 41  PRO D CA  
6264 C C   . PRO D 60  ? 2.65302 1.85360 2.33693 0.19953  -0.07984 -0.48997 41  PRO D C   
6265 O O   . PRO D 60  ? 2.66205 1.84751 2.34454 0.20450  -0.10403 -0.50845 41  PRO D O   
6266 C CB  . PRO D 60  ? 2.64132 1.87166 2.30966 0.19939  -0.02068 -0.49245 41  PRO D CB  
6267 C CG  . PRO D 60  ? 2.66172 1.89465 2.32185 0.19617  0.00582  -0.47152 41  PRO D CG  
6268 C CD  . PRO D 60  ? 2.62569 1.85011 2.31772 0.18116  0.01035  -0.45271 41  PRO D CD  
6269 N N   . GLU D 61  ? 2.67842 1.88520 2.35391 0.20362  -0.08334 -0.47847 42  GLU D N   
6270 C CA  . GLU D 61  ? 2.71506 1.91973 2.38404 0.21024  -0.11626 -0.48787 42  GLU D CA  
6271 C C   . GLU D 61  ? 2.71593 1.90837 2.41830 0.19123  -0.13967 -0.48256 42  GLU D C   
6272 O O   . GLU D 61  ? 2.74864 1.94403 2.45164 0.19106  -0.16592 -0.48975 42  GLU D O   
6273 C CB  . GLU D 61  ? 2.76715 1.99314 2.41551 0.22336  -0.10920 -0.47503 42  GLU D CB  
6274 C CG  . GLU D 61  ? 2.78699 2.02505 2.40207 0.23882  -0.08088 -0.47206 42  GLU D CG  
6275 C CD  . GLU D 61  ? 2.81125 2.05313 2.42240 0.23959  -0.05100 -0.44160 42  GLU D CD  
6276 O OE1 . GLU D 61  ? 2.78651 2.01685 2.42066 0.22412  -0.03027 -0.42834 42  GLU D OE1 
6277 O OE2 . GLU D 61  ? 2.86806 2.12428 2.45211 0.25768  -0.04851 -0.43125 42  GLU D OE2 
6278 N N   . LYS D 62  ? 2.81561 2.00040 2.54534 0.17471  -0.12989 -0.47078 43  LYS D N   
6279 C CA  . LYS D 62  ? 2.81661 1.99467 2.57963 0.15370  -0.14713 -0.46037 43  LYS D CA  
6280 C C   . LYS D 62  ? 2.83103 2.03428 2.60816 0.14683  -0.14852 -0.44253 43  LYS D C   
6281 O O   . LYS D 62  ? 2.85975 2.06612 2.66055 0.12980  -0.16939 -0.43837 43  LYS D O   
6282 C CB  . LYS D 62  ? 2.86312 2.01170 2.62716 0.14937  -0.18119 -0.47941 43  LYS D CB  
6283 C CG  . LYS D 62  ? 2.86190 1.98323 2.61355 0.15964  -0.18259 -0.49603 43  LYS D CG  
6284 C CD  . LYS D 62  ? 2.88200 1.97442 2.65816 0.14281  -0.19553 -0.48809 43  LYS D CD  
6285 C CE  . LYS D 62  ? 2.94158 2.00877 2.73041 0.12614  -0.22785 -0.49313 43  LYS D CE  
6286 N NZ  . LYS D 62  ? 3.00193 2.03501 2.81314 0.10741  -0.23860 -0.48062 43  LYS D NZ  
6287 N N   . ARG D 63  ? 2.73476 1.95670 2.49737 0.16010  -0.12601 -0.43126 44  ARG D N   
6288 C CA  . ARG D 63  ? 2.75591 2.00400 2.52895 0.16034  -0.12457 -0.41306 44  ARG D CA  
6289 C C   . ARG D 63  ? 2.71901 1.97569 2.51915 0.14894  -0.10302 -0.39382 44  ARG D C   
6290 O O   . ARG D 63  ? 2.67821 1.92585 2.47415 0.15145  -0.07557 -0.39123 44  ARG D O   
6291 C CB  . ARG D 63  ? 2.79106 2.05024 2.53080 0.18519  -0.11126 -0.40784 44  ARG D CB  
6292 C CG  . ARG D 63  ? 2.87217 2.13808 2.58476 0.20008  -0.13385 -0.42639 44  ARG D CG  
6293 C CD  . ARG D 63  ? 2.91913 2.20197 2.59819 0.22648  -0.11791 -0.41393 44  ARG D CD  
6294 N NE  . ARG D 63  ? 2.97297 2.27290 2.62399 0.24404  -0.13870 -0.43208 44  ARG D NE  
6295 C CZ  . ARG D 63  ? 3.03222 2.35314 2.64927 0.27032  -0.12976 -0.42249 44  ARG D CZ  
6296 N NH1 . ARG D 63  ? 3.04770 2.36616 2.65301 0.28214  -0.09987 -0.39314 44  ARG D NH1 
6297 N NH2 . ARG D 63  ? 3.06808 2.41202 2.66125 0.28641  -0.15111 -0.44282 44  ARG D NH2 
6298 N N   . LEU D 64  ? 2.66247 1.94207 2.49124 0.13583  -0.11535 -0.38268 45  LEU D N   
6299 C CA  . LEU D 64  ? 2.62138 1.91795 2.47797 0.12617  -0.09815 -0.36638 45  LEU D CA  
6300 C C   . LEU D 64  ? 2.64073 1.95639 2.49134 0.14361  -0.08052 -0.35192 45  LEU D C   
6301 O O   . LEU D 64  ? 2.70054 2.03391 2.53983 0.15658  -0.09265 -0.34874 45  LEU D O   
6302 C CB  . LEU D 64  ? 2.63719 1.95407 2.52874 0.10216  -0.11947 -0.36038 45  LEU D CB  
6303 C CG  . LEU D 64  ? 2.62372 1.91435 2.52427 0.08453  -0.13251 -0.36811 45  LEU D CG  
6304 C CD1 . LEU D 64  ? 2.67499 1.97802 2.60309 0.05937  -0.15856 -0.36230 45  LEU D CD1 
6305 C CD2 . LEU D 64  ? 2.57072 1.86023 2.48185 0.08178  -0.10941 -0.36244 45  LEU D CD2 
6306 N N   . GLU D 65  ? 2.64276 1.95494 2.50027 0.14567  -0.05193 -0.34462 46  GLU D N   
6307 C CA  . GLU D 65  ? 2.66558 1.98642 2.51916 0.16309  -0.03259 -0.33077 46  GLU D CA  
6308 C C   . GLU D 65  ? 2.63065 1.97320 2.51796 0.15296  -0.02054 -0.32487 46  GLU D C   
6309 O O   . GLU D 65  ? 2.58284 1.92445 2.48750 0.13623  -0.01458 -0.33182 46  GLU D O   
6310 C CB  . GLU D 65  ? 2.65905 1.94405 2.48024 0.17927  -0.00369 -0.33025 46  GLU D CB  
6311 C CG  . GLU D 65  ? 2.68912 1.95568 2.47626 0.18722  -0.01104 -0.33901 46  GLU D CG  
6312 C CD  . GLU D 65  ? 2.77321 2.01136 2.52674 0.20390  0.01849  -0.33162 46  GLU D CD  
6313 O OE1 . GLU D 65  ? 2.80574 2.03218 2.56060 0.21163  0.04239  -0.31815 46  GLU D OE1 
6314 O OE2 . GLU D 65  ? 2.80654 2.03332 2.53189 0.20931  0.01833  -0.33917 46  GLU D OE2 
6315 N N   . TRP D 66  ? 2.47914 1.84659 2.37459 0.16635  -0.01742 -0.31285 47  TRP D N   
6316 C CA  . TRP D 66  ? 2.46190 1.85485 2.38730 0.16195  -0.00448 -0.30919 47  TRP D CA  
6317 C C   . TRP D 66  ? 2.45515 1.81357 2.36919 0.17335  0.03021  -0.31237 47  TRP D C   
6318 O O   . TRP D 66  ? 2.48971 1.82079 2.37742 0.19591  0.04371  -0.30507 47  TRP D O   
6319 C CB  . TRP D 66  ? 2.49339 1.93405 2.43365 0.17327  -0.01707 -0.29765 47  TRP D CB  
6320 C CG  . TRP D 66  ? 2.48220 1.94898 2.44737 0.17732  -0.00053 -0.29545 47  TRP D CG  
6321 C CD1 . TRP D 66  ? 2.44980 1.94730 2.44764 0.15697  0.00098  -0.29915 47  TRP D CD1 
6322 C CD2 . TRP D 66  ? 2.50801 1.97321 2.46596 0.20625  0.01687  -0.28994 47  TRP D CD2 
6323 N NE1 . TRP D 66  ? 2.45037 1.97102 2.46335 0.17069  0.01761  -0.29933 47  TRP D NE1 
6324 C CE2 . TRP D 66  ? 2.48572 1.98313 2.47482 0.20124  0.02740  -0.29448 47  TRP D CE2 
6325 C CE3 . TRP D 66  ? 2.64400 2.08306 2.57038 0.23850  0.02464  -0.28082 47  TRP D CE3 
6326 C CZ2 . TRP D 66  ? 2.50402 2.00502 2.49483 0.22727  0.04453  -0.29387 47  TRP D CZ2 
6327 C CZ3 . TRP D 66  ? 2.68403 2.12136 2.61036 0.26508  0.04236  -0.27639 47  TRP D CZ3 
6328 C CH2 . TRP D 66  ? 2.65384 2.12028 2.61277 0.25926  0.05176  -0.28470 47  TRP D CH2 
6329 N N   . VAL D 67  ? 2.48534 1.84538 2.41888 0.15751  0.04508  -0.32322 48  VAL D N   
6330 C CA  . VAL D 67  ? 2.47950 1.80763 2.40647 0.16117  0.07846  -0.33223 48  VAL D CA  
6331 C C   . VAL D 67  ? 2.49203 1.83587 2.43699 0.17353  0.09242  -0.33012 48  VAL D C   
6332 O O   . VAL D 67  ? 2.52625 1.83440 2.45296 0.19277  0.11170  -0.32571 48  VAL D O   
6333 C CB  . VAL D 67  ? 2.43673 1.76665 2.37568 0.13971  0.08806  -0.34989 48  VAL D CB  
6334 C CG1 . VAL D 67  ? 2.43325 1.74223 2.37431 0.13867  0.12273  -0.36355 48  VAL D CG1 
6335 C CG2 . VAL D 67  ? 2.42947 1.73665 2.34459 0.13403  0.07841  -0.35457 48  VAL D CG2 
6336 N N   . ALA D 68  ? 2.47018 1.86634 2.44958 0.16407  0.08354  -0.33275 49  ALA D N   
6337 C CA  . ALA D 68  ? 2.47800 1.89946 2.47725 0.17720  0.09489  -0.33451 49  ALA D CA  
6338 C C   . ALA D 68  ? 2.45750 1.95037 2.49338 0.16368  0.07835  -0.33348 49  ALA D C   
6339 O O   . ALA D 68  ? 2.43607 1.94735 2.48164 0.14205  0.06417  -0.33248 49  ALA D O   
6340 C CB  . ALA D 68  ? 2.46863 1.85681 2.46888 0.17722  0.12821  -0.35306 49  ALA D CB  
6341 N N   . THR D 69  ? 2.34002 1.87271 2.39475 0.17833  0.08096  -0.33265 50  THR D N   
6342 C CA  . THR D 69  ? 2.32363 1.93272 2.41408 0.16733  0.06948  -0.33090 50  THR D CA  
6343 C C   . THR D 69  ? 2.31735 1.95161 2.42587 0.18349  0.08896  -0.34552 50  THR D C   
6344 O O   . THR D 69  ? 2.34232 1.94156 2.43632 0.20909  0.10315  -0.35002 50  THR D O   
6345 C CB  . THR D 69  ? 2.35511 2.01295 2.45372 0.16729  0.04161  -0.31162 50  THR D CB  
6346 O OG1 . THR D 69  ? 2.35664 2.09160 2.49051 0.15302  0.03306  -0.30752 50  THR D OG1 
6347 C CG2 . THR D 69  ? 2.40610 2.06341 2.49148 0.20020  0.04221  -0.30648 50  THR D CG2 
6348 N N   . ILE D 70  ? 2.27785 1.97201 2.41682 0.17008  0.08979  -0.35308 51  ILE D N   
6349 C CA  . ILE D 70  ? 2.26375 1.98988 2.42288 0.18352  0.10787  -0.37296 51  ILE D CA  
6350 C C   . ILE D 70  ? 2.26660 2.08893 2.45636 0.18481  0.09293  -0.36381 51  ILE D C   
6351 O O   . ILE D 70  ? 2.27203 2.13667 2.47225 0.16505  0.07249  -0.34389 51  ILE D O   
6352 C CB  . ILE D 70  ? 2.22376 1.94193 2.39130 0.16814  0.12767  -0.39731 51  ILE D CB  
6353 C CG1 . ILE D 70  ? 2.21237 1.95055 2.39764 0.18384  0.14883  -0.42509 51  ILE D CG1 
6354 C CG2 . ILE D 70  ? 2.20135 1.97597 2.38680 0.14403  0.11424  -0.38891 51  ILE D CG2 
6355 C CD1 . ILE D 70  ? 2.18563 1.88125 2.36811 0.17420  0.17477  -0.45508 51  ILE D CD1 
6356 N N   . SER D 71  ? 2.06894 1.92504 2.27287 0.20812  0.10379  -0.37880 52  SER D N   
6357 C CA  . SER D 71  ? 2.07341 2.02937 2.30618 0.21379  0.09183  -0.37233 52  SER D CA  
6358 C C   . SER D 71  ? 2.04160 2.06638 2.30169 0.19049  0.09207  -0.37518 52  SER D C   
6359 O O   . SER D 71  ? 2.01514 2.01136 2.27163 0.17305  0.10106  -0.38402 52  SER D O   
6360 C CB  . SER D 71  ? 2.08308 2.05265 2.32051 0.25071  0.10404  -0.39134 52  SER D CB  
6361 O OG  . SER D 71  ? 2.08571 2.16227 2.35163 0.25821  0.09292  -0.38719 52  SER D OG  
6362 N N   . SER D 72  ? 2.00254 2.12617 2.28960 0.19212  0.08228  -0.36667 53  SER D N   
6363 C CA  . SER D 72  ? 1.98064 2.18086 2.29282 0.17335  0.08259  -0.36457 53  SER D CA  
6364 C C   . SER D 72  ? 1.93962 2.15226 2.26198 0.18577  0.10520  -0.40055 53  SER D C   
6365 O O   . SER D 72  ? 1.91420 2.15503 2.24594 0.16976  0.11047  -0.40503 53  SER D O   
6366 C CB  . SER D 72  ? 2.00032 2.30902 2.33843 0.17165  0.06794  -0.34480 53  SER D CB  
6367 O OG  . SER D 72  ? 2.03706 2.33751 2.36797 0.16207  0.04790  -0.31824 53  SER D OG  
6368 N N   . GLY D 73  ? 2.08896 2.28116 2.40925 0.21512  0.11855  -0.42748 54  GLY D N   
6369 C CA  . GLY D 73  ? 2.05228 2.25045 2.38357 0.22617  0.14045  -0.46766 54  GLY D CA  
6370 C C   . GLY D 73  ? 2.05871 2.14615 2.36726 0.23744  0.15949  -0.49218 54  GLY D C   
6371 O O   . GLY D 73  ? 2.04511 2.12485 2.36185 0.25322  0.17819  -0.52896 54  GLY D O   
6372 N N   . ALA D 74  ? 2.12938 2.13062 2.40915 0.22904  0.15524  -0.47214 55  ALA D N   
6373 C CA  . ALA D 74  ? 2.14289 2.03324 2.39651 0.23324  0.17377  -0.48688 55  ALA D CA  
6374 C C   . ALA D 74  ? 2.18400 2.02994 2.42658 0.26870  0.18319  -0.49681 55  ALA D C   
6375 O O   . ALA D 74  ? 2.20290 1.95802 2.42689 0.27409  0.20372  -0.51281 55  ALA D O   
6376 C CB  . ALA D 74  ? 2.10284 1.97710 2.36446 0.21611  0.19568  -0.52117 55  ALA D CB  
6377 N N   . SER D 75  ? 2.33729 2.24366 2.58931 0.29388  0.16914  -0.48622 56  SER D N   
6378 C CA  . SER D 75  ? 2.38262 2.24614 2.62053 0.33410  0.17655  -0.49364 56  SER D CA  
6379 C C   . SER D 75  ? 2.43120 2.21480 2.63204 0.34511  0.17084  -0.46480 56  SER D C   
6380 O O   . SER D 75  ? 2.48005 2.18466 2.65777 0.37334  0.18532  -0.47057 56  SER D O   
6381 C CB  . SER D 75  ? 2.12489 2.09123 2.38547 0.36170  0.16331  -0.49480 56  SER D CB  
6382 O OG  . SER D 75  ? 2.09223 2.13993 2.38613 0.35485  0.16912  -0.52228 56  SER D OG  
6383 N N   . TYR D 76  ? 2.22156 2.02229 2.41525 0.32430  0.15058  -0.43444 57  TYR D N   
6384 C CA  . TYR D 76  ? 2.26380 2.00522 2.42360 0.33471  0.14199  -0.40805 57  TYR D CA  
6385 C C   . TYR D 76  ? 2.24913 1.93852 2.39282 0.30011  0.14125  -0.39734 57  TYR D C   
6386 O O   . TYR D 76  ? 2.20993 1.94012 2.37202 0.26788  0.13415  -0.39785 57  TYR D O   
6387 C CB  . TYR D 76  ? 2.28428 2.10426 2.45029 0.34620  0.11438  -0.38403 57  TYR D CB  
6388 C CG  . TYR D 76  ? 2.29653 2.18872 2.48050 0.38140  0.11152  -0.39353 57  TYR D CG  
6389 C CD1 . TYR D 76  ? 2.34325 2.20047 2.50470 0.42851  0.11588  -0.39285 57  TYR D CD1 
6390 C CD2 . TYR D 76  ? 2.26513 2.26388 2.48686 0.37037  0.10447  -0.40206 57  TYR D CD2 
6391 C CE1 . TYR D 76  ? 2.35410 2.28070 2.53083 0.46524  0.11233  -0.40347 57  TYR D CE1 
6392 C CE2 . TYR D 76  ? 2.27334 2.34699 2.51168 0.40435  0.10153  -0.41251 57  TYR D CE2 
6393 C CZ  . TYR D 76  ? 2.31623 2.35339 2.53225 0.45248  0.10498  -0.41468 57  TYR D CZ  
6394 O OH  . TYR D 76  ? 2.32359 2.43744 2.55482 0.49081  0.10132  -0.42704 57  TYR D OH  
6395 N N   . THR D 77  ? 2.40310 2.00407 2.51070 0.30963  0.14885  -0.38683 58  THR D N   
6396 C CA  . THR D 77  ? 2.39499 1.94823 2.48271 0.28279  0.14660  -0.37589 58  THR D CA  
6397 C C   . THR D 77  ? 2.44492 1.95431 2.49659 0.30326  0.13765  -0.35128 58  THR D C   
6398 O O   . THR D 77  ? 2.56377 2.05070 2.59901 0.33995  0.14301  -0.34549 58  THR D O   
6399 C CB  . THR D 77  ? 2.37883 1.86242 2.45882 0.26565  0.17468  -0.39672 58  THR D CB  
6400 O OG1 . THR D 77  ? 2.42259 1.83383 2.48341 0.29158  0.19835  -0.40397 58  THR D OG1 
6401 C CG2 . THR D 77  ? 2.32523 1.86193 2.44044 0.24367  0.18181  -0.42311 58  THR D CG2 
6402 N N   . HIS D 78  ? 2.45206 1.95103 2.49018 0.28221  0.12364  -0.33769 59  HIS D N   
6403 C CA  . HIS D 78  ? 2.49507 1.96097 2.49865 0.29933  0.11348  -0.31648 59  HIS D CA  
6404 C C   . HIS D 78  ? 2.48661 1.89319 2.46629 0.27764  0.11948  -0.31490 59  HIS D C   
6405 O O   . HIS D 78  ? 2.44270 1.86021 2.43723 0.24575  0.11743  -0.32512 59  HIS D O   
6406 C CB  . HIS D 78  ? 2.50286 2.04410 2.51720 0.29990  0.08054  -0.30160 59  HIS D CB  
6407 C CG  . HIS D 78  ? 2.51623 2.12833 2.55312 0.32265  0.07304  -0.30194 59  HIS D CG  
6408 N ND1 . HIS D 78  ? 2.58426 2.20128 2.60294 0.36468  0.07003  -0.29177 59  HIS D ND1 
6409 C CD2 . HIS D 78  ? 2.48773 2.17502 2.56288 0.31154  0.06791  -0.31095 59  HIS D CD2 
6410 C CE1 . HIS D 78  ? 2.59633 2.28976 2.64216 0.37861  0.06291  -0.29666 59  HIS D CE1 
6411 N NE2 . HIS D 78  ? 2.54048 2.27871 2.62118 0.34571  0.06185  -0.30800 59  HIS D NE2 
6412 N N   . TYR D 79  ? 2.75595 2.10348 2.69692 0.29805  0.12712  -0.30119 60  TYR D N   
6413 C CA  . TYR D 79  ? 2.74558 2.03965 2.65887 0.28311  0.13400  -0.29798 60  TYR D CA  
6414 C C   . TYR D 79  ? 2.81487 2.09881 2.69290 0.30736  0.12009  -0.27577 60  TYR D C   
6415 O O   . TYR D 79  ? 2.87082 2.16358 2.73792 0.34206  0.11688  -0.26269 60  TYR D O   
6416 C CB  . TYR D 79  ? 2.76995 1.98834 2.66856 0.28010  0.17053  -0.30712 60  TYR D CB  
6417 C CG  . TYR D 79  ? 2.70825 1.93768 2.64073 0.25905  0.18709  -0.33382 60  TYR D CG  
6418 C CD1 . TYR D 79  ? 2.72628 1.96465 2.67713 0.27649  0.19738  -0.34387 60  TYR D CD1 
6419 C CD2 . TYR D 79  ? 2.63532 1.87062 2.58043 0.22477  0.19222  -0.35115 60  TYR D CD2 
6420 C CE1 . TYR D 79  ? 2.67492 1.93038 2.65712 0.25840  0.21194  -0.37188 60  TYR D CE1 
6421 C CE2 . TYR D 79  ? 2.50747 1.76234 2.48322 0.20742  0.20691  -0.37742 60  TYR D CE2 
6422 C CZ  . TYR D 79  ? 2.54768 1.81342 2.54238 0.22338  0.21671  -0.38841 60  TYR D CZ  
6423 O OH  . TYR D 79  ? 2.47079 1.76289 2.49654 0.20714  0.23070  -0.41807 60  TYR D OH  
6424 N N   . PRO D 80  ? 2.85052 2.12157 2.70963 0.29301  0.11097  -0.27263 61  PRO D N   
6425 C CA  . PRO D 80  ? 2.90000 2.16293 2.72249 0.31743  0.09969  -0.25395 61  PRO D CA  
6426 C C   . PRO D 80  ? 2.95785 2.14499 2.73985 0.33814  0.13000  -0.24035 61  PRO D C   
6427 O O   . PRO D 80  ? 2.95332 2.08953 2.73625 0.32544  0.15931  -0.24824 61  PRO D O   
6428 C CB  . PRO D 80  ? 2.86441 2.14424 2.68603 0.29113  0.07880  -0.26141 61  PRO D CB  
6429 C CG  . PRO D 80  ? 2.79122 2.04812 2.62923 0.25949  0.09534  -0.27903 61  PRO D CG  
6430 C CD  . PRO D 80  ? 2.77263 2.04413 2.64310 0.25671  0.10816  -0.28763 61  PRO D CD  
6431 N N   . ASP D 81  ? 3.02886 2.21175 2.77470 0.36953  0.12286  -0.21935 62  ASP D N   
6432 C CA  . ASP D 81  ? 3.09152 2.20288 2.79382 0.39339  0.15141  -0.19898 62  ASP D CA  
6433 C C   . ASP D 81  ? 3.08209 2.14567 2.76881 0.36511  0.17175  -0.20383 62  ASP D C   
6434 O O   . ASP D 81  ? 3.13616 2.13177 2.79574 0.37213  0.20383  -0.19059 62  ASP D O   
6435 C CB  . ASP D 81  ? 3.15182 2.28204 2.81681 0.43406  0.13631  -0.17462 62  ASP D CB  
6436 C CG  . ASP D 81  ? 3.15541 2.35198 2.83758 0.46068  0.11161  -0.17289 62  ASP D CG  
6437 O OD1 . ASP D 81  ? 3.13760 2.34284 2.84984 0.46018  0.11663  -0.18245 62  ASP D OD1 
6438 O OD2 . ASP D 81  ? 3.17762 2.42444 2.84423 0.48193  0.08701  -0.16415 62  ASP D OD2 
6439 N N   . SER D 82  ? 3.03566 2.13295 2.73863 0.33357  0.15453  -0.22226 63  SER D N   
6440 C CA  . SER D 82  ? 3.02476 2.08905 2.71230 0.30971  0.17136  -0.22883 63  SER D CA  
6441 C C   . SER D 82  ? 3.00040 2.02699 2.70841 0.28291  0.20250  -0.24484 63  SER D C   
6442 O O   . SER D 82  ? 3.04000 2.01175 2.72586 0.27728  0.23401  -0.23864 63  SER D O   
6443 C CB  . SER D 82  ? 2.97068 2.08214 2.66906 0.28892  0.14193  -0.24597 63  SER D CB  
6444 O OG  . SER D 82  ? 2.90998 2.06415 2.65192 0.26986  0.12279  -0.26390 63  SER D OG  
6445 N N   . VAL D 83  ? 2.95904 2.01841 2.70967 0.26483  0.19482  -0.26597 64  VAL D N   
6446 C CA  . VAL D 83  ? 2.92715 1.96707 2.70173 0.23738  0.22045  -0.28775 64  VAL D CA  
6447 C C   . VAL D 83  ? 2.94763 1.96710 2.73898 0.24965  0.23741  -0.28999 64  VAL D C   
6448 O O   . VAL D 83  ? 2.91561 1.94291 2.73852 0.22898  0.24957  -0.31393 64  VAL D O   
6449 C CB  . VAL D 83  ? 2.85241 1.94560 2.66094 0.20828  0.20287  -0.31237 64  VAL D CB  
6450 C CG1 . VAL D 83  ? 2.83688 1.94120 2.62659 0.19866  0.18823  -0.31351 64  VAL D CG1 
6451 C CG2 . VAL D 83  ? 2.82685 1.97692 2.66545 0.21462  0.17428  -0.31331 64  VAL D CG2 
6452 N N   . LYS D 84  ? 2.96227 1.95854 2.73203 0.28586  0.23808  -0.26706 65  LYS D N   
6453 C CA  . LYS D 84  ? 2.99705 1.96930 2.77918 0.30359  0.25369  -0.26997 65  LYS D CA  
6454 C C   . LYS D 84  ? 3.03158 1.92865 2.80916 0.28678  0.29453  -0.28002 65  LYS D C   
6455 O O   . LYS D 84  ? 3.07994 1.91902 2.82355 0.28401  0.31564  -0.26424 65  LYS D O   
6456 C CB  . LYS D 84  ? 3.06270 2.02291 2.81611 0.35148  0.24630  -0.24119 65  LYS D CB  
6457 C CG  . LYS D 84  ? 3.10648 2.03515 2.86746 0.37733  0.26257  -0.24357 65  LYS D CG  
6458 C CD  . LYS D 84  ? 3.18298 2.07583 2.90279 0.42864  0.26458  -0.21075 65  LYS D CD  
6459 C CE  . LYS D 84  ? 3.23411 2.08226 2.95778 0.45745  0.28341  -0.21445 65  LYS D CE  
6460 N NZ  . LYS D 84  ? 3.31646 2.11264 2.99306 0.51056  0.29106  -0.17941 65  LYS D NZ  
6461 N N   . GLY D 85  ? 3.08309 1.98491 2.89593 0.27395  0.30613  -0.30743 66  GLY D N   
6462 C CA  . GLY D 85  ? 3.11561 1.95109 2.93149 0.25402  0.34428  -0.32428 66  GLY D CA  
6463 C C   . GLY D 85  ? 3.07422 1.91457 2.89938 0.20874  0.35828  -0.34484 66  GLY D C   
6464 O O   . GLY D 85  ? 3.09084 1.89435 2.92957 0.18428  0.38831  -0.36809 66  GLY D O   
6465 N N   . ARG D 86  ? 3.04077 1.92745 2.85976 0.19725  0.33741  -0.33971 67  ARG D N   
6466 C CA  . ARG D 86  ? 3.00328 1.90255 2.82815 0.15934  0.34841  -0.35891 67  ARG D CA  
6467 C C   . ARG D 86  ? 2.91690 1.89178 2.78430 0.13804  0.33261  -0.39072 67  ARG D C   
6468 O O   . ARG D 86  ? 2.89336 1.87754 2.77942 0.10759  0.35115  -0.41897 67  ARG D O   
6469 C CB  . ARG D 86  ? 3.00789 1.91254 2.79850 0.16270  0.33547  -0.33696 67  ARG D CB  
6470 C CG  . ARG D 86  ? 3.08744 1.93931 2.83396 0.19513  0.33995  -0.29894 67  ARG D CG  
6471 C CD  . ARG D 86  ? 3.08748 1.96139 2.80253 0.20297  0.32102  -0.28046 67  ARG D CD  
6472 N NE  . ARG D 86  ? 3.08933 1.95684 2.79380 0.17349  0.33951  -0.28976 67  ARG D NE  
6473 C CZ  . ARG D 86  ? 3.02800 1.94912 2.74270 0.15586  0.32184  -0.30835 67  ARG D CZ  
6474 N NH1 . ARG D 86  ? 2.96041 1.93769 2.69509 0.16219  0.28567  -0.31752 67  ARG D NH1 
6475 N NH2 . ARG D 86  ? 3.04034 1.95823 2.74432 0.13162  0.34145  -0.31747 67  ARG D NH2 
6476 N N   . PHE D 87  ? 2.88825 1.92058 2.77092 0.15321  0.29933  -0.38587 68  PHE D N   
6477 C CA  . PHE D 87  ? 2.78597 1.89084 2.70570 0.13693  0.28270  -0.40884 68  PHE D CA  
6478 C C   . PHE D 87  ? 2.77789 1.90851 2.72869 0.14752  0.28221  -0.42080 68  PHE D C   
6479 O O   . PHE D 87  ? 2.83145 1.93306 2.77372 0.17361  0.28470  -0.40735 68  PHE D O   
6480 C CB  . PHE D 87  ? 2.74585 1.89863 2.66228 0.14161  0.24601  -0.39467 68  PHE D CB  
6481 C CG  . PHE D 87  ? 2.74844 1.88741 2.63727 0.13249  0.24291  -0.38914 68  PHE D CG  
6482 C CD1 . PHE D 87  ? 2.78592 1.87903 2.65384 0.12063  0.27217  -0.39325 68  PHE D CD1 
6483 C CD2 . PHE D 87  ? 2.69087 1.86420 2.57539 0.13493  0.21096  -0.38115 68  PHE D CD2 
6484 C CE1 . PHE D 87  ? 2.79128 1.88109 2.63377 0.11432  0.26906  -0.38925 68  PHE D CE1 
6485 C CE2 . PHE D 87  ? 2.70889 1.87239 2.56788 0.13000  0.20681  -0.37970 68  PHE D CE2 
6486 C CZ  . PHE D 87  ? 2.75441 1.88030 2.59208 0.12104  0.23564  -0.38379 68  PHE D CZ  
6487 N N   . THR D 88  ? 2.58647 1.77677 2.57225 0.13015  0.27876  -0.44649 69  THR D N   
6488 C CA  . THR D 88  ? 2.55060 1.77688 2.56851 0.13807  0.28020  -0.46335 69  THR D CA  
6489 C C   . THR D 88  ? 2.47934 1.79421 2.52663 0.12918  0.25670  -0.47034 69  THR D C   
6490 O O   . THR D 88  ? 2.43809 1.78565 2.50011 0.10725  0.26222  -0.49167 69  THR D O   
6491 C CB  . THR D 88  ? 2.63282 1.82872 2.66455 0.12351  0.31459  -0.49654 69  THR D CB  
6492 O OG1 . THR D 88  ? 2.77650 1.88023 2.77771 0.12854  0.33860  -0.48541 69  THR D OG1 
6493 C CG2 . THR D 88  ? 2.59046 1.82211 2.65314 0.13696  0.31547  -0.51614 69  THR D CG2 
6494 N N   . ILE D 89  ? 2.35841 1.71484 2.41373 0.14641  0.23131  -0.45146 70  ILE D N   
6495 C CA  . ILE D 89  ? 2.31622 1.75501 2.39930 0.13819  0.21034  -0.45277 70  ILE D CA  
6496 C C   . ILE D 89  ? 2.29326 1.78102 2.40957 0.14108  0.22147  -0.47790 70  ILE D C   
6497 O O   . ILE D 89  ? 2.31692 1.77983 2.43532 0.15772  0.23585  -0.48748 70  ILE D O   
6498 C CB  . ILE D 89  ? 2.33474 1.80077 2.41371 0.14983  0.17902  -0.42169 70  ILE D CB  
6499 C CG1 . ILE D 89  ? 2.30220 1.83889 2.40357 0.13460  0.15796  -0.41695 70  ILE D CG1 
6500 C CG2 . ILE D 89  ? 2.36431 1.84232 2.44960 0.17584  0.17674  -0.41463 70  ILE D CG2 
6501 C CD1 . ILE D 89  ? 2.32330 1.88379 2.42258 0.13773  0.12780  -0.38820 70  ILE D CD1 
6502 N N   . SER D 90  ? 2.20503 1.76321 2.34611 0.12718  0.21498  -0.48938 71  SER D N   
6503 C CA  . SER D 90  ? 2.17758 1.79617 2.35109 0.12915  0.22494  -0.51650 71  SER D CA  
6504 C C   . SER D 90  ? 2.14342 1.84873 2.33761 0.11904  0.20819  -0.51193 71  SER D C   
6505 O O   . SER D 90  ? 2.13473 1.83902 2.31816 0.10581  0.19805  -0.50011 71  SER D O   
6506 C CB  . SER D 90  ? 2.16369 1.75219 2.34241 0.11770  0.25609  -0.55582 71  SER D CB  
6507 O OG  . SER D 90  ? 2.15203 1.71098 2.31482 0.09702  0.26316  -0.55948 71  SER D OG  
6508 N N   . ARG D 91  ? 1.96616 1.74652 2.18854 0.12755  0.20575  -0.52067 72  ARG D N   
6509 C CA  . ARG D 91  ? 1.92076 1.78861 2.16228 0.12045  0.19122  -0.51159 72  ARG D CA  
6510 C C   . ARG D 91  ? 1.90479 1.84739 2.17615 0.12396  0.20547  -0.54609 72  ARG D C   
6511 O O   . ARG D 91  ? 1.92433 1.86839 2.20742 0.13781  0.21753  -0.56851 72  ARG D O   
6512 C CB  . ARG D 91  ? 1.90591 1.81022 2.15116 0.12657  0.16573  -0.47386 72  ARG D CB  
6513 C CG  . ARG D 91  ? 1.91776 1.84558 2.17523 0.14753  0.16572  -0.47558 72  ARG D CG  
6514 C CD  . ARG D 91  ? 1.90655 1.86763 2.16559 0.14924  0.14033  -0.43781 72  ARG D CD  
6515 N NE  . ARG D 91  ? 1.87028 1.91123 2.14765 0.13490  0.12707  -0.41985 72  ARG D NE  
6516 C CZ  . ARG D 91  ? 1.86079 1.92943 2.14062 0.12514  0.10512  -0.38482 72  ARG D CZ  
6517 N NH1 . ARG D 91  ? 1.87970 1.91091 2.14634 0.12821  0.09195  -0.36691 72  ARG D NH1 
6518 N NH2 . ARG D 91  ? 1.83574 1.97258 2.13146 0.11136  0.09667  -0.36720 72  ARG D NH2 
6519 N N   . ASP D 92  ? 1.95834 1.96387 2.24061 0.11396  0.20360  -0.55126 73  ASP D N   
6520 C CA  . ASP D 92  ? 1.91663 2.00997 2.22706 0.11728  0.21498  -0.58413 73  ASP D CA  
6521 C C   . ASP D 92  ? 1.91807 2.10511 2.24241 0.12147  0.19608  -0.55477 73  ASP D C   
6522 O O   . ASP D 92  ? 1.91109 2.13284 2.23227 0.11392  0.18872  -0.54065 73  ASP D O   
6523 C CB  . ASP D 92  ? 1.87947 1.97610 2.18970 0.10365  0.23115  -0.61703 73  ASP D CB  
6524 C CG  . ASP D 92  ? 1.83075 2.02543 2.17066 0.10738  0.24305  -0.65636 73  ASP D CG  
6525 O OD1 . ASP D 92  ? 1.82561 2.07907 2.18587 0.12157  0.24097  -0.66170 73  ASP D OD1 
6526 O OD2 . ASP D 92  ? 1.79461 2.01453 2.13769 0.09723  0.25422  -0.68403 73  ASP D OD2 
6527 N N   . ASN D 93  ? 1.79306 2.02231 2.13190 0.13467  0.18894  -0.54452 74  ASN D N   
6528 C CA  . ASN D 93  ? 1.80106 2.12211 2.15394 0.13608  0.17261  -0.51323 74  ASN D CA  
6529 C C   . ASN D 93  ? 1.75209 2.17865 2.12675 0.14030  0.18081  -0.53493 74  ASN D C   
6530 O O   . ASN D 93  ? 1.75655 2.26441 2.14099 0.14071  0.16943  -0.50620 74  ASN D O   
6531 C CB  . ASN D 93  ? 1.82567 2.17284 2.18917 0.14929  0.16376  -0.49901 74  ASN D CB  
6532 C CG  . ASN D 93  ? 1.87345 2.13300 2.21528 0.14712  0.15233  -0.47311 74  ASN D CG  
6533 O OD1 . ASN D 93  ? 1.87776 2.04366 2.19767 0.14296  0.15880  -0.48138 74  ASN D OD1 
6534 N ND2 . ASN D 93  ? 1.90757 2.20423 2.25570 0.14946  0.13546  -0.44193 74  ASN D ND2 
6535 N N   . ALA D 94  ? 1.87362 2.30430 2.25629 0.14253  0.20070  -0.58459 75  ALA D N   
6536 C CA  . ALA D 94  ? 1.82030 2.35570 2.22168 0.14651  0.20790  -0.60817 75  ALA D CA  
6537 C C   . ALA D 94  ? 1.82335 2.36468 2.20934 0.13651  0.20180  -0.58710 75  ALA D C   
6538 O O   . ALA D 94  ? 1.81895 2.44753 2.21087 0.14162  0.19419  -0.56603 75  ALA D O   
6539 C CB  . ALA D 94  ? 1.77360 2.31280 2.19055 0.14942  0.23096  -0.67295 75  ALA D CB  
6540 N N   . LYS D 95  ? 1.94076 2.39095 2.30516 0.12451  0.20527  -0.59106 76  LYS D N   
6541 C CA  . LYS D 95  ? 1.94905 2.39300 2.29495 0.11862  0.19838  -0.57215 76  LYS D CA  
6542 C C   . LYS D 95  ? 2.01704 2.40082 2.34045 0.11272  0.17672  -0.51624 76  LYS D C   
6543 O O   . LYS D 95  ? 2.05659 2.42765 2.36228 0.11060  0.16836  -0.49634 76  LYS D O   
6544 C CB  . LYS D 95  ? 1.78300 2.17078 2.11826 0.10885  0.21413  -0.60986 76  LYS D CB  
6545 C CG  . LYS D 95  ? 1.77951 2.22749 2.13824 0.10916  0.23636  -0.66997 76  LYS D CG  
6546 C CD  . LYS D 95  ? 1.79751 2.18854 2.14628 0.09383  0.25275  -0.70451 76  LYS D CD  
6547 C CE  . LYS D 95  ? 1.79846 2.25107 2.17370 0.08902  0.27549  -0.76835 76  LYS D CE  
6548 N NZ  . LYS D 95  ? 1.76797 2.35039 2.15819 0.10166  0.27246  -0.77954 76  LYS D NZ  
6549 N N   . ASN D 96  ? 1.86370 2.21211 2.18762 0.11112  0.16721  -0.49318 77  ASN D N   
6550 C CA  . ASN D 96  ? 1.92619 2.21994 2.23245 0.10250  0.14623  -0.44474 77  ASN D CA  
6551 C C   . ASN D 96  ? 1.93938 2.13520 2.21708 0.09445  0.14368  -0.44409 77  ASN D C   
6552 O O   . ASN D 96  ? 1.97105 2.14655 2.23218 0.09022  0.13063  -0.41782 77  ASN D O   
6553 C CB  . ASN D 96  ? 1.98531 2.34437 2.29542 0.10120  0.13200  -0.40389 77  ASN D CB  
6554 C CG  . ASN D 96  ? 2.00073 2.45729 2.33742 0.10745  0.13212  -0.39629 77  ASN D CG  
6555 O OD1 . ASN D 96  ? 1.92549 2.42592 2.28065 0.11833  0.14582  -0.43291 77  ASN D OD1 
6556 N ND2 . ASN D 96  ? 2.10630 2.59717 2.44521 0.09998  0.11724  -0.34928 77  ASN D ND2 
6557 N N   . THR D 97  ? 1.95346 2.08756 2.22459 0.09357  0.15701  -0.47346 78  THR D N   
6558 C CA  . THR D 97  ? 1.96136 2.00656 2.20541 0.08661  0.15719  -0.47565 78  THR D CA  
6559 C C   . THR D 97  ? 1.97188 1.94277 2.20661 0.08669  0.16135  -0.47909 78  THR D C   
6560 O O   . THR D 97  ? 1.95884 1.94082 2.20817 0.09338  0.17402  -0.49893 78  THR D O   
6561 C CB  . THR D 97  ? 1.91893 1.97235 2.16057 0.08448  0.17581  -0.51395 78  THR D CB  
6562 O OG1 . THR D 97  ? 1.87963 1.95887 2.14162 0.08532  0.19810  -0.55518 78  THR D OG1 
6563 C CG2 . THR D 97  ? 1.91157 2.03617 2.15614 0.08949  0.17008  -0.50812 78  THR D CG2 
6564 N N   . LEU D 98  ? 2.00929 1.90544 2.21820 0.08205  0.15029  -0.45990 79  LEU D N   
6565 C CA  . LEU D 98  ? 2.02364 1.84610 2.21691 0.08461  0.15364  -0.45946 79  LEU D CA  
6566 C C   . LEU D 98  ? 2.00789 1.77165 2.18166 0.07915  0.17132  -0.48329 79  LEU D C   
6567 O O   . LEU D 98  ? 1.99136 1.76379 2.15858 0.07281  0.17338  -0.49282 79  LEU D O   
6568 C CB  . LEU D 98  ? 2.06366 1.85164 2.24173 0.08336  0.12848  -0.42258 79  LEU D CB  
6569 C CG  . LEU D 98  ? 2.08477 1.80536 2.24345 0.08985  0.12717  -0.41588 79  LEU D CG  
6570 C CD1 . LEU D 98  ? 2.09124 1.83125 2.26477 0.10358  0.13453  -0.42042 79  LEU D CD1 
6571 C CD2 . LEU D 98  ? 2.11702 1.81174 2.26065 0.08518  0.10067  -0.38547 79  LEU D CD2 
6572 N N   . TYR D 99  ? 2.14744 1.85353 2.31106 0.08275  0.18492  -0.49184 80  TYR D N   
6573 C CA  . TYR D 99  ? 2.14151 1.79132 2.28726 0.07481  0.20537  -0.51250 80  TYR D CA  
6574 C C   . TYR D 99  ? 2.18009 1.75062 2.29763 0.08105  0.20347  -0.49346 80  TYR D C   
6575 O O   . TYR D 99  ? 2.20737 1.77047 2.32151 0.09307  0.18732  -0.46900 80  TYR D O   
6576 C CB  . TYR D 99  ? 2.11889 1.78096 2.28353 0.06990  0.23443  -0.55167 80  TYR D CB  
6577 C CG  . TYR D 99  ? 2.07753 1.82788 2.27024 0.06573  0.23755  -0.57527 80  TYR D CG  
6578 C CD1 . TYR D 99  ? 2.04727 1.82522 2.23936 0.05422  0.24455  -0.59506 80  TYR D CD1 
6579 C CD2 . TYR D 99  ? 2.06903 1.88332 2.28805 0.07582  0.23325  -0.57813 80  TYR D CD2 
6580 C CE1 . TYR D 99  ? 2.00972 1.87618 2.22578 0.05400  0.24699  -0.61645 80  TYR D CE1 
6581 C CE2 . TYR D 99  ? 2.03148 1.93421 2.27461 0.07450  0.23610  -0.59894 80  TYR D CE2 
6582 C CZ  . TYR D 99  ? 2.00175 1.93004 2.24288 0.06414  0.24289  -0.61775 80  TYR D CZ  
6583 O OH  . TYR D 99  ? 1.96360 1.98734 2.22713 0.06628  0.24537  -0.63834 80  TYR D OH  
6584 N N   . LEU D 100 ? 2.24008 1.75798 2.33715 0.07285  0.22085  -0.50521 81  LEU D N   
6585 C CA  . LEU D 100 ? 2.28169 1.72508 2.34829 0.07940  0.22383  -0.48837 81  LEU D CA  
6586 C C   . LEU D 100 ? 2.31463 1.71372 2.36702 0.06552  0.25261  -0.50864 81  LEU D C   
6587 O O   . LEU D 100 ? 2.30436 1.71393 2.34888 0.05326  0.25386  -0.51806 81  LEU D O   
6588 C CB  . LEU D 100 ? 2.27515 1.70765 2.32014 0.08447  0.19563  -0.46027 81  LEU D CB  
6589 C CG  . LEU D 100 ? 2.31624 1.68284 2.32645 0.09302  0.19590  -0.44294 81  LEU D CG  
6590 C CD1 . LEU D 100 ? 2.34641 1.68568 2.35348 0.11084  0.20097  -0.43033 81  LEU D CD1 
6591 C CD2 . LEU D 100 ? 2.30711 1.67388 2.30043 0.09635  0.16597  -0.42295 81  LEU D CD2 
6592 N N   . GLN D 101 ? 2.51822 1.86792 2.56692 0.06746  0.27644  -0.51524 82  GLN D N   
6593 C CA  . GLN D 101 ? 2.56650 1.87012 2.60441 0.04960  0.30808  -0.53387 82  GLN D CA  
6594 C C   . GLN D 101 ? 2.69112 1.92069 2.68978 0.05846  0.31158  -0.50542 82  GLN D C   
6595 O O   . GLN D 101 ? 2.75133 1.93744 2.73824 0.07804  0.31242  -0.48620 82  GLN D O   
6596 C CB  . GLN D 101 ? 2.64718 1.93931 2.70795 0.04306  0.33522  -0.56243 82  GLN D CB  
6597 C CG  . GLN D 101 ? 2.73741 1.96798 2.78716 0.02152  0.37093  -0.57889 82  GLN D CG  
6598 C CD  . GLN D 101 ? 2.70378 1.97330 2.75965 -0.00699 0.38147  -0.60440 82  GLN D CD  
6599 O OE1 . GLN D 101 ? 2.65664 1.98873 2.74345 -0.02089 0.38697  -0.63940 82  GLN D OE1 
6600 N NE2 . GLN D 101 ? 2.73165 1.97162 2.75755 -0.01369 0.38411  -0.58821 82  GLN D NE2 
6601 N N   . MET D 102 ? 2.75579 1.97645 2.73308 0.04691  0.31366  -0.50310 83  MET D N   
6602 C CA  . MET D 102 ? 2.80683 1.96976 2.74470 0.05544  0.31590  -0.47630 83  MET D CA  
6603 C C   . MET D 102 ? 2.88625 2.00019 2.81190 0.03467  0.35404  -0.48724 83  MET D C   
6604 O O   . MET D 102 ? 2.88143 2.02313 2.82481 0.00843  0.37164  -0.51796 83  MET D O   
6605 C CB  . MET D 102 ? 2.78570 1.97596 2.70617 0.05904  0.28979  -0.46568 83  MET D CB  
6606 C CG  . MET D 102 ? 2.74311 1.97328 2.67456 0.07518  0.25269  -0.45255 83  MET D CG  
6607 S SD  . MET D 102 ? 2.64520 1.92519 2.57713 0.06958  0.22678  -0.46018 83  MET D SD  
6608 C CE  . MET D 102 ? 2.66133 1.99227 2.62537 0.04852  0.24730  -0.49708 83  MET D CE  
6609 N N   . SER D 103 ? 2.91649 1.96035 2.81156 0.04609  0.36746  -0.46138 84  SER D N   
6610 C CA  . SER D 103 ? 2.97870 1.96377 2.86109 0.02548  0.40694  -0.46589 84  SER D CA  
6611 C C   . SER D 103 ? 3.04217 1.97497 2.87790 0.03837  0.41162  -0.42922 84  SER D C   
6612 O O   . SER D 103 ? 3.04285 1.97633 2.85737 0.06836  0.38557  -0.40111 84  SER D O   
6613 C CB  . SER D 103 ? 3.02188 1.95831 2.92028 0.02575  0.43009  -0.47554 84  SER D CB  
6614 O OG  . SER D 103 ? 2.96537 1.95818 2.90676 0.01683  0.42479  -0.51073 84  SER D OG  
6615 N N   . SER D 104 ? 3.13474 2.02660 2.95534 0.01398  0.44625  -0.43053 85  SER D N   
6616 C CA  . SER D 104 ? 3.20842 2.05198 2.98294 0.02243  0.45773  -0.39525 85  SER D CA  
6617 C C   . SER D 104 ? 3.17122 2.06349 2.92417 0.04174  0.42396  -0.38071 85  SER D C   
6618 O O   . SER D 104 ? 3.21494 2.08485 2.93436 0.07109  0.41132  -0.34724 85  SER D O   
6619 C CB  . SER D 104 ? 3.29003 2.05419 3.04057 0.05035  0.46790  -0.36159 85  SER D CB  
6620 O OG  . SER D 104 ? 3.26087 2.04712 3.00666 0.08973  0.43167  -0.34363 85  SER D OG  
6621 N N   . LEU D 105 ? 3.14153 2.10218 2.91367 0.02649  0.40919  -0.40816 86  LEU D N   
6622 C CA  . LEU D 105 ? 3.09805 2.10663 2.85837 0.04576  0.37182  -0.40235 86  LEU D CA  
6623 C C   . LEU D 105 ? 3.15402 2.15043 2.87086 0.05345  0.37532  -0.38055 86  LEU D C   
6624 O O   . LEU D 105 ? 3.20948 2.18598 2.91146 0.03295  0.40763  -0.37955 86  LEU D O   
6625 C CB  . LEU D 105 ? 3.02410 2.10216 2.81344 0.02962  0.35837  -0.43704 86  LEU D CB  
6626 C CG  . LEU D 105 ? 2.96931 2.07380 2.79985 0.02745  0.34873  -0.45589 86  LEU D CG  
6627 C CD1 . LEU D 105 ? 2.91878 2.08582 2.77738 0.00579  0.35094  -0.49246 86  LEU D CD1 
6628 C CD2 . LEU D 105 ? 2.93606 2.05602 2.76822 0.05523  0.30972  -0.43885 86  LEU D CD2 
6629 N N   . ARG D 106 ? 3.30835 2.32105 3.00563 0.08214  0.34184  -0.36400 87  ARG D N   
6630 C CA  . ARG D 106 ? 3.35161 2.36797 3.00829 0.09523  0.33719  -0.34695 87  ARG D CA  
6631 C C   . ARG D 106 ? 3.28908 2.36559 2.94942 0.09823  0.30582  -0.36869 87  ARG D C   
6632 O O   . ARG D 106 ? 3.21771 2.32637 2.90919 0.09411  0.28528  -0.39008 87  ARG D O   
6633 C CB  . ARG D 106 ? 2.91968 1.90644 2.54701 0.12991  0.32357  -0.31172 87  ARG D CB  
6634 C CG  . ARG D 106 ? 2.98123 1.90188 2.59927 0.13544  0.35274  -0.28649 87  ARG D CG  
6635 C CD  . ARG D 106 ? 3.05062 1.93037 2.63985 0.11958  0.39404  -0.27099 87  ARG D CD  
6636 N NE  . ARG D 106 ? 3.12174 1.92608 2.69894 0.12677  0.42267  -0.24450 87  ARG D NE  
6637 C CZ  . ARG D 106 ? 3.14352 1.90601 2.74536 0.10172  0.45209  -0.25761 87  ARG D CZ  
6638 N NH1 . ARG D 106 ? 3.09665 1.89282 2.73740 0.06693  0.45768  -0.29718 87  ARG D NH1 
6639 N NH2 . ARG D 106 ? 3.21817 1.90389 2.80460 0.11383  0.47610  -0.23179 87  ARG D NH2 
6640 N N   . SER D 107 ? 3.23536 2.32625 2.86163 0.10753  0.30249  -0.36227 88  SER D N   
6641 C CA  . SER D 107 ? 3.18446 2.32631 2.80956 0.11485  0.27229  -0.38405 88  SER D CA  
6642 C C   . SER D 107 ? 3.13958 2.29013 2.77217 0.13772  0.22925  -0.38206 88  SER D C   
6643 O O   . SER D 107 ? 3.08870 2.27068 2.73745 0.13804  0.20336  -0.40401 88  SER D O   
6644 C CB  . SER D 107 ? 3.23968 2.39771 2.82486 0.12299  0.27821  -0.37845 88  SER D CB  
6645 O OG  . SER D 107 ? 3.30652 2.43731 2.85847 0.14634  0.27657  -0.34580 88  SER D OG  
6646 N N   . GLU D 108 ? 3.16161 2.28546 2.78263 0.15682  0.22157  -0.35590 89  GLU D N   
6647 C CA  . GLU D 108 ? 3.13269 2.26965 2.76401 0.17419  0.18225  -0.35472 89  GLU D CA  
6648 C C   . GLU D 108 ? 3.06623 2.21239 2.74100 0.16069  0.17209  -0.36790 89  GLU D C   
6649 O O   . GLU D 108 ? 3.02858 2.19419 2.71771 0.16640  0.13881  -0.37390 89  GLU D O   
6650 C CB  . GLU D 108 ? 3.18540 2.30054 2.79638 0.19808  0.17956  -0.32462 89  GLU D CB  
6651 C CG  . GLU D 108 ? 3.25240 2.36424 2.81694 0.21660  0.18742  -0.30712 89  GLU D CG  
6652 C CD  . GLU D 108 ? 3.32134 2.40677 2.86360 0.24139  0.19470  -0.27325 89  GLU D CD  
6653 O OE1 . GLU D 108 ? 3.31583 2.37833 2.87858 0.24172  0.20079  -0.26421 89  GLU D OE1 
6654 O OE2 . GLU D 108 ? 3.38628 2.47754 2.88924 0.26348  0.19418  -0.25586 89  GLU D OE2 
6655 N N   . ASP D 109 ? 3.06778 2.20205 2.76396 0.14182  0.20055  -0.37305 90  ASP D N   
6656 C CA  . ASP D 109 ? 2.98831 2.13901 2.72509 0.13009  0.19381  -0.38588 90  ASP D CA  
6657 C C   . ASP D 109 ? 2.93788 2.12696 2.69103 0.12058  0.17663  -0.41072 90  ASP D C   
6658 O O   . ASP D 109 ? 2.89845 2.10773 2.68375 0.11131  0.17154  -0.42080 90  ASP D O   
6659 C CB  . ASP D 109 ? 3.00700 2.13768 2.76083 0.11314  0.23015  -0.38975 90  ASP D CB  
6660 C CG  . ASP D 109 ? 3.08851 2.16990 2.82180 0.12475  0.25082  -0.36404 90  ASP D CG  
6661 O OD1 . ASP D 109 ? 3.12259 2.19324 2.82826 0.14813  0.23619  -0.34184 90  ASP D OD1 
6662 O OD2 . ASP D 109 ? 3.11566 2.16882 2.85974 0.11174  0.28168  -0.36691 90  ASP D OD2 
6663 N N   . THR D 110 ? 2.83246 2.03391 2.56283 0.12551  0.16786  -0.42036 91  THR D N   
6664 C CA  . THR D 110 ? 2.79866 2.03205 2.53906 0.12334  0.14933  -0.44297 91  THR D CA  
6665 C C   . THR D 110 ? 2.76957 2.00410 2.51785 0.13494  0.10985  -0.43791 91  THR D C   
6666 O O   . THR D 110 ? 2.79257 2.01704 2.51933 0.14968  0.08928  -0.43077 91  THR D O   
6667 C CB  . THR D 110 ? 2.83050 2.07753 2.54184 0.12831  0.15333  -0.45640 91  THR D CB  
6668 O OG1 . THR D 110 ? 2.87610 2.12364 2.58175 0.11228  0.19251  -0.45934 91  THR D OG1 
6669 C CG2 . THR D 110 ? 2.80177 2.08028 2.52149 0.13128  0.13448  -0.48073 91  THR D CG2 
6670 N N   . ALA D 111 ? 2.56089 1.81040 2.34023 0.12710  0.09974  -0.44193 92  ALA D N   
6671 C CA  . ALA D 111 ? 2.55736 1.80661 2.34815 0.13200  0.06500  -0.43513 92  ALA D CA  
6672 C C   . ALA D 111 ? 2.52547 1.79769 2.34612 0.12239  0.06069  -0.44180 92  ALA D C   
6673 O O   . ALA D 111 ? 2.50261 1.79608 2.33454 0.11437  0.08315  -0.45414 92  ALA D O   
6674 C CB  . ALA D 111 ? 2.58355 1.82158 2.37983 0.13528  0.05794  -0.41349 92  ALA D CB  
6675 N N   . MET D 112 ? 2.59079 1.86152 2.42412 0.12252  0.03188  -0.43342 93  MET D N   
6676 C CA  . MET D 112 ? 2.57614 1.86807 2.43629 0.11490  0.02536  -0.43224 93  MET D CA  
6677 C C   . MET D 112 ? 2.55404 1.85996 2.44149 0.10549  0.02784  -0.41444 93  MET D C   
6678 O O   . MET D 112 ? 2.56067 1.85773 2.45143 0.10471  0.00866  -0.39986 93  MET D O   
6679 C CB  . MET D 112 ? 2.60238 1.87883 2.45765 0.11960  -0.00669 -0.43230 93  MET D CB  
6680 C CG  . MET D 112 ? 2.60859 1.90173 2.48970 0.11199  -0.01558 -0.42212 93  MET D CG  
6681 S SD  . MET D 112 ? 2.62308 1.94928 2.50705 0.11878  0.00063  -0.43816 93  MET D SD  
6682 C CE  . MET D 112 ? 2.69223 1.98464 2.55439 0.13465  -0.02937 -0.44370 93  MET D CE  
6683 N N   . TYR D 113 ? 2.49168 1.82538 2.39954 0.09878  0.05096  -0.41839 94  TYR D N   
6684 C CA  . TYR D 113 ? 2.47643 1.82768 2.40854 0.09341  0.05781  -0.40582 94  TYR D CA  
6685 C C   . TYR D 113 ? 2.48207 1.86629 2.44142 0.08622  0.04304  -0.39549 94  TYR D C   
6686 O O   . TYR D 113 ? 2.48732 1.89943 2.45772 0.08396  0.04990  -0.40407 94  TYR D O   
6687 C CB  . TYR D 113 ? 2.45881 1.81973 2.39809 0.09029  0.09182  -0.41868 94  TYR D CB  
6688 C CG  . TYR D 113 ? 2.47338 1.79655 2.38735 0.09577  0.10832  -0.41915 94  TYR D CG  
6689 C CD1 . TYR D 113 ? 2.49094 1.79717 2.37922 0.09688  0.11713  -0.43130 94  TYR D CD1 
6690 C CD2 . TYR D 113 ? 2.48403 1.79099 2.39800 0.10202  0.11528  -0.40564 94  TYR D CD2 
6691 C CE1 . TYR D 113 ? 2.52158 1.79502 2.38487 0.10131  0.13378  -0.42737 94  TYR D CE1 
6692 C CE2 . TYR D 113 ? 2.51632 1.78538 2.40376 0.10962  0.13138  -0.40125 94  TYR D CE2 
6693 C CZ  . TYR D 113 ? 2.53678 1.78869 2.39884 0.10787  0.14120  -0.41078 94  TYR D CZ  
6694 O OH  . TYR D 113 ? 2.58703 1.80285 2.42087 0.11479  0.15891  -0.40232 94  TYR D OH  
6695 N N   . TYR D 114 ? 2.40402 1.79024 2.37375 0.08270  0.02339  -0.37643 95  TYR D N   
6696 C CA  . TYR D 114 ? 2.42714 1.84386 2.42184 0.07276  0.00857  -0.36116 95  TYR D CA  
6697 C C   . TYR D 114 ? 2.42046 1.88176 2.44276 0.06974  0.02126  -0.35430 95  TYR D C   
6698 O O   . TYR D 114 ? 2.40889 1.86709 2.43034 0.07583  0.02991  -0.35411 95  TYR D O   
6699 C CB  . TYR D 114 ? 2.45999 1.85646 2.45196 0.06588  -0.02178 -0.34597 95  TYR D CB  
6700 C CG  . TYR D 114 ? 2.48228 1.83821 2.45234 0.06835  -0.03914 -0.35298 95  TYR D CG  
6701 C CD1 . TYR D 114 ? 2.51928 1.87541 2.49295 0.06629  -0.04561 -0.35003 95  TYR D CD1 
6702 C CD2 . TYR D 114 ? 2.48033 1.79945 2.42462 0.07595  -0.04961 -0.36262 95  TYR D CD2 
6703 C CE1 . TYR D 114 ? 2.55204 1.86691 2.50416 0.07277  -0.06215 -0.35784 95  TYR D CE1 
6704 C CE2 . TYR D 114 ? 2.50744 1.79098 2.43162 0.08088  -0.06651 -0.37280 95  TYR D CE2 
6705 C CZ  . TYR D 114 ? 2.54275 1.82131 2.47097 0.07971  -0.07292 -0.37096 95  TYR D CZ  
6706 O OH  . TYR D 114 ? 2.58195 1.82080 2.48856 0.08873  -0.09030 -0.38246 95  TYR D OH  
6707 N N   . CYS D 115 ? 2.26691 1.77140 2.31206 0.06322  0.02187  -0.34810 96  CYS D N   
6708 C CA  . CYS D 115 ? 2.26469 1.82319 2.33824 0.06130  0.03201  -0.34296 96  CYS D CA  
6709 C C   . CYS D 115 ? 2.30667 1.89255 2.39837 0.04897  0.01006  -0.31643 96  CYS D C   
6710 O O   . CYS D 115 ? 2.35277 1.95041 2.45001 0.04105  0.00063  -0.30431 96  CYS D O   
6711 C CB  . CYS D 115 ? 2.24605 1.84527 2.33222 0.06366  0.05224  -0.35885 96  CYS D CB  
6712 S SG  . CYS D 115 ? 2.25693 1.93947 2.38007 0.06146  0.05937  -0.35208 96  CYS D SG  
6713 N N   . GLY D 116 ? 2.13707 1.73411 2.23721 0.04753  0.00254  -0.30648 97  GLY D N   
6714 C CA  . GLY D 116 ? 2.17084 1.79464 2.28843 0.03144  -0.01880 -0.28245 97  GLY D CA  
6715 C C   . GLY D 116 ? 2.17424 1.86749 2.32012 0.03179  -0.01248 -0.27459 97  GLY D C   
6716 O O   . GLY D 116 ? 2.15810 1.86142 2.30445 0.04797  0.00145  -0.28718 97  GLY D O   
6717 N N   . ARG D 117 ? 2.09907 1.83928 2.26744 0.01480  -0.02239 -0.25296 98  ARG D N   
6718 C CA  . ARG D 117 ? 2.10328 1.92236 2.30044 0.01380  -0.01812 -0.24370 98  ARG D CA  
6719 C C   . ARG D 117 ? 2.12952 1.96739 2.33671 0.00145  -0.03727 -0.22873 98  ARG D C   
6720 O O   . ARG D 117 ? 2.15820 1.97482 2.36496 -0.02115 -0.05656 -0.21296 98  ARG D O   
6721 C CB  . ARG D 117 ? 2.11811 1.99044 2.33439 0.00239  -0.01526 -0.22681 98  ARG D CB  
6722 C CG  . ARG D 117 ? 2.11877 2.08390 2.36555 0.00106  -0.01098 -0.21654 98  ARG D CG  
6723 C CD  . ARG D 117 ? 2.15977 2.16015 2.42418 -0.02759 -0.02818 -0.18224 98  ARG D CD  
6724 N NE  . ARG D 117 ? 2.20185 2.25705 2.48044 -0.03460 -0.02140 -0.16325 98  ARG D NE  
6725 C CZ  . ARG D 117 ? 2.30096 2.38429 2.59316 -0.06106 -0.03197 -0.12862 98  ARG D CZ  
6726 N NH1 . ARG D 117 ? 2.44108 2.50269 2.73762 -0.08694 -0.05037 -0.11219 98  ARG D NH1 
6727 N NH2 . ARG D 117 ? 2.39191 2.52813 2.69355 -0.06251 -0.02327 -0.10998 98  ARG D NH2 
6728 N N   . GLN D 118 ? 2.12293 2.00154 2.33943 0.01681  -0.03202 -0.23548 99  GLN D N   
6729 C CA  . GLN D 118 ? 2.14652 2.05522 2.37260 0.00946  -0.04942 -0.22521 99  GLN D CA  
6730 C C   . GLN D 118 ? 2.16327 2.15138 2.42194 -0.01555 -0.05815 -0.20167 99  GLN D C   
6731 O O   . GLN D 118 ? 2.15754 2.19295 2.43257 -0.01796 -0.04698 -0.19441 99  GLN D O   
6732 C CB  . GLN D 118 ? 2.14033 2.06776 2.36251 0.04029  -0.04060 -0.23965 99  GLN D CB  
6733 C CG  . GLN D 118 ? 2.14935 2.01130 2.34081 0.05627  -0.04512 -0.25033 99  GLN D CG  
6734 C CD  . GLN D 118 ? 2.16665 2.05959 2.35631 0.08446  -0.04366 -0.25496 99  GLN D CD  
6735 O OE1 . GLN D 118 ? 2.17813 2.14914 2.39249 0.08549  -0.04806 -0.24814 99  GLN D OE1 
6736 N NE2 . GLN D 118 ? 2.17169 2.00621 2.33067 0.10945  -0.03703 -0.26533 99  GLN D NE2 
6737 N N   . VAL D 119 ? 2.19503 2.20306 2.46342 -0.03511 -0.07795 -0.19021 100 VAL D N   
6738 C CA  . VAL D 119 ? 2.20752 2.29478 2.50817 -0.06391 -0.08664 -0.16663 100 VAL D CA  
6739 C C   . VAL D 119 ? 2.20899 2.39092 2.53007 -0.04367 -0.07767 -0.17071 100 VAL D C   
6740 O O   . VAL D 119 ? 2.18284 2.36653 2.49401 -0.01383 -0.07548 -0.18862 100 VAL D O   
6741 C CB  . VAL D 119 ? 2.31334 2.38967 2.61901 -0.09529 -0.11084 -0.15779 100 VAL D CB  
6742 C CG1 . VAL D 119 ? 2.33300 2.49809 2.67462 -0.12916 -0.11815 -0.13337 100 VAL D CG1 
6743 C CG2 . VAL D 119 ? 2.37320 2.35360 2.65886 -0.11348 -0.12026 -0.15583 100 VAL D CG2 
6744 N N   . ASN D 120 ? 2.24945 2.51191 2.59759 -0.05717 -0.07216 -0.15331 101 ASN D N   
6745 C CA  . ASN D 120 ? 2.20317 2.56592 2.57265 -0.03717 -0.06419 -0.15820 101 ASN D CA  
6746 C C   . ASN D 120 ? 2.20847 2.67221 2.61147 -0.06869 -0.07415 -0.13302 101 ASN D C   
6747 O O   . ASN D 120 ? 2.15440 2.71636 2.57849 -0.05505 -0.06648 -0.13357 101 ASN D O   
6748 C CB  . ASN D 120 ? 2.17509 2.55841 2.54580 -0.01277 -0.04222 -0.16958 101 ASN D CB  
6749 C CG  . ASN D 120 ? 2.21208 2.64954 2.60192 -0.03748 -0.03805 -0.14454 101 ASN D CG  
6750 O OD1 . ASN D 120 ? 2.25196 2.65263 2.63921 -0.06974 -0.04681 -0.12086 101 ASN D OD1 
6751 N ND2 . ASN D 120 ? 2.22500 2.75039 2.63296 -0.02052 -0.02455 -0.14939 101 ASN D ND2 
6752 N N   . ARG D 121 ? 2.27102 2.71452 2.68015 -0.11136 -0.09034 -0.11215 102 ARG D N   
6753 C CA  . ARG D 121 ? 2.26396 2.80068 2.70613 -0.14818 -0.09968 -0.08795 102 ARG D CA  
6754 C C   . ARG D 121 ? 2.19027 2.82044 2.64747 -0.12617 -0.10326 -0.10287 102 ARG D C   
6755 O O   . ARG D 121 ? 2.13892 2.87586 2.61925 -0.11828 -0.09520 -0.09756 102 ARG D O   
6756 C CB  . ARG D 121 ? 2.32746 2.81098 2.77105 -0.19539 -0.11863 -0.07304 102 ARG D CB  
6757 C CG  . ARG D 121 ? 2.41339 2.80432 2.84193 -0.21692 -0.11697 -0.05540 102 ARG D CG  
6758 C CD  . ARG D 121 ? 2.47513 2.80731 2.90552 -0.26287 -0.13666 -0.04455 102 ARG D CD  
6759 N NE  . ARG D 121 ? 2.50182 2.91423 2.96738 -0.31031 -0.14281 -0.01754 102 ARG D NE  
6760 C CZ  . ARG D 121 ? 2.51717 2.98323 3.00332 -0.33298 -0.15750 -0.02497 102 ARG D CZ  
6761 N NH1 . ARG D 121 ? 2.50970 2.95902 2.98318 -0.30960 -0.16873 -0.05732 102 ARG D NH1 
6762 N NH2 . ARG D 121 ? 2.53787 3.08062 3.05793 -0.38071 -0.16053 0.00131  102 ARG D NH2 
6763 N N   . HIS D 122 ? 2.38284 2.97669 2.82524 -0.11267 -0.11555 -0.12207 103 HIS D N   
6764 C CA  . HIS D 122 ? 2.32591 2.99048 2.77233 -0.07748 -0.11807 -0.14029 103 HIS D CA  
6765 C C   . HIS D 122 ? 2.31499 2.92362 2.73254 -0.02144 -0.10253 -0.16472 103 HIS D C   
6766 O O   . HIS D 122 ? 2.35111 2.85166 2.73834 -0.01139 -0.10090 -0.17499 103 HIS D O   
6767 C CB  . HIS D 122 ? 2.33654 3.00032 2.78142 -0.09038 -0.13958 -0.14711 103 HIS D CB  
6768 C CG  . HIS D 122 ? 2.37073 3.07602 2.84445 -0.15159 -0.15469 -0.12676 103 HIS D CG  
6769 N ND1 . HIS D 122 ? 2.40576 3.02657 2.87510 -0.19424 -0.16037 -0.11282 103 HIS D ND1 
6770 C CD2 . HIS D 122 ? 2.37771 3.19844 2.88527 -0.17839 -0.16481 -0.11885 103 HIS D CD2 
6771 C CE1 . HIS D 122 ? 2.43676 3.11127 2.93600 -0.24671 -0.17266 -0.09644 103 HIS D CE1 
6772 N NE2 . HIS D 122 ? 2.41818 3.21788 2.94218 -0.24035 -0.17526 -0.09982 103 HIS D NE2 
6773 N N   . ASP D 123 ? 2.24228 2.92419 2.66967 0.01365  -0.09045 -0.17463 104 ASP D N   
6774 C CA  . ASP D 123 ? 2.22760 2.85904 2.63274 0.06170  -0.07232 -0.19747 104 ASP D CA  
6775 C C   . ASP D 123 ? 2.24341 2.81424 2.61882 0.09722  -0.07665 -0.21457 104 ASP D C   
6776 O O   . ASP D 123 ? 2.21949 2.84905 2.59697 0.12950  -0.08054 -0.22327 104 ASP D O   
6777 C CB  . ASP D 123 ? 2.16960 2.90188 2.59575 0.08922  -0.06010 -0.20581 104 ASP D CB  
6778 C CG  . ASP D 123 ? 2.15405 2.94554 2.60528 0.05921  -0.05266 -0.18856 104 ASP D CG  
6779 O OD1 . ASP D 123 ? 2.19200 2.96550 2.64934 0.01368  -0.05997 -0.16417 104 ASP D OD1 
6780 O OD2 . ASP D 123 ? 2.10923 2.96551 2.57281 0.08388  -0.03917 -0.19996 104 ASP D OD2 
6781 N N   . ARG D 124 ? 2.32071 2.77763 2.66667 0.09474  -0.07543 -0.21873 105 ARG D N   
6782 C CA  . ARG D 124 ? 2.34118 2.73344 2.65450 0.12827  -0.07728 -0.23159 105 ARG D CA  
6783 C C   . ARG D 124 ? 2.33868 2.61739 2.62205 0.14204  -0.05949 -0.24286 105 ARG D C   
6784 O O   . ARG D 124 ? 2.31795 2.55852 2.60348 0.11594  -0.05342 -0.23926 105 ARG D O   
6785 C CB  . ARG D 124 ? 2.36208 2.74478 2.66959 0.10514  -0.10052 -0.22443 105 ARG D CB  
6786 C CG  . ARG D 124 ? 2.38470 2.73193 2.66055 0.14529  -0.10453 -0.23524 105 ARG D CG  
6787 C CD  . ARG D 124 ? 2.38934 2.76798 2.66803 0.12521  -0.12995 -0.23203 105 ARG D CD  
6788 N NE  . ARG D 124 ? 2.40748 2.77542 2.65677 0.17008  -0.13414 -0.24071 105 ARG D NE  
6789 C CZ  . ARG D 124 ? 2.43767 2.71985 2.65142 0.18159  -0.13561 -0.24512 105 ARG D CZ  
6790 N NH1 . ARG D 124 ? 2.44588 2.64536 2.64945 0.15203  -0.13440 -0.24473 105 ARG D NH1 
6791 N NH2 . ARG D 124 ? 2.46095 2.74423 2.64723 0.22645  -0.13831 -0.24932 105 ARG D NH2 
6792 N N   . ALA D 125 ? 2.45612 2.68419 2.71107 0.18431  -0.05026 -0.25574 106 ALA D N   
6793 C CA  . ALA D 125 ? 2.39147 2.51431 2.61780 0.19693  -0.03123 -0.26704 106 ALA D CA  
6794 C C   . ALA D 125 ? 2.34769 2.39202 2.55045 0.17532  -0.04000 -0.26199 106 ALA D C   
6795 O O   . ALA D 125 ? 2.28730 2.26010 2.47585 0.16737  -0.02700 -0.26824 106 ALA D O   
6796 C CB  . ALA D 125 ? 2.41118 2.50059 2.61354 0.24791  -0.01700 -0.27895 106 ALA D CB  
6797 N N   . LEU D 126 ? 2.42609 2.48751 2.62484 0.16672  -0.06198 -0.25375 107 LEU D N   
6798 C CA  . LEU D 126 ? 2.42307 2.41762 2.59981 0.14859  -0.07315 -0.25230 107 LEU D CA  
6799 C C   . LEU D 126 ? 2.46876 2.50205 2.67072 0.10224  -0.09504 -0.24206 107 LEU D C   
6800 O O   . LEU D 126 ? 2.50738 2.61579 2.72909 0.09309  -0.11205 -0.23668 107 LEU D O   
6801 C CB  . LEU D 126 ? 2.47210 2.44697 2.61881 0.17970  -0.08045 -0.25468 107 LEU D CB  
6802 C CG  . LEU D 126 ? 2.48178 2.40439 2.60580 0.16490  -0.09560 -0.25592 107 LEU D CG  
6803 C CD1 . LEU D 126 ? 2.38934 2.22140 2.49359 0.15521  -0.08134 -0.26099 107 LEU D CD1 
6804 C CD2 . LEU D 126 ? 2.53189 2.45118 2.62577 0.20235  -0.10122 -0.25709 107 LEU D CD2 
6805 N N   . ASP D 127 ? 2.43093 2.41312 2.63207 0.07321  -0.09418 -0.23964 108 ASP D N   
6806 C CA  . ASP D 127 ? 2.49493 2.49574 2.71741 0.02825  -0.11263 -0.22801 108 ASP D CA  
6807 C C   . ASP D 127 ? 2.39654 2.30717 2.59818 0.01249  -0.11483 -0.23135 108 ASP D C   
6808 O O   . ASP D 127 ? 2.30430 2.15026 2.47797 0.03459  -0.10112 -0.24251 108 ASP D O   
6809 C CB  . ASP D 127 ? 2.53348 2.60317 2.79073 0.00781  -0.10688 -0.21376 108 ASP D CB  
6810 C CG  . ASP D 127 ? 2.54221 2.71704 2.82868 0.00184  -0.11747 -0.20619 108 ASP D CG  
6811 O OD1 . ASP D 127 ? 2.54836 2.74198 2.83524 -0.00577 -0.13632 -0.20850 108 ASP D OD1 
6812 O OD2 . ASP D 127 ? 2.52520 2.77098 2.83487 0.00509  -0.10722 -0.19978 108 ASP D OD2 
6813 N N   . ALA D 128 ? 2.48254 2.38946 2.69811 -0.02635 -0.13188 -0.22179 109 ALA D N   
6814 C CA  . ALA D 128 ? 2.37858 2.20322 2.57609 -0.04056 -0.13593 -0.22467 109 ALA D CA  
6815 C C   . ALA D 128 ? 2.29075 2.09744 2.48934 -0.03921 -0.11683 -0.21862 109 ALA D C   
6816 O O   . ALA D 128 ? 2.28029 2.14381 2.49834 -0.03461 -0.10303 -0.21082 109 ALA D O   
6817 C CB  . ALA D 128 ? 2.55332 2.37390 2.76581 -0.08203 -0.15987 -0.21659 109 ALA D CB  
6818 N N   . MET D 129 ? 2.38460 2.11763 2.56174 -0.04112 -0.11666 -0.22444 110 MET D N   
6819 C CA  . MET D 129 ? 2.34839 2.06425 2.52291 -0.03723 -0.09986 -0.22180 110 MET D CA  
6820 C C   . MET D 129 ? 2.41087 2.12631 2.60077 -0.06877 -0.11050 -0.20028 110 MET D C   
6821 O O   . MET D 129 ? 2.43288 2.09004 2.61091 -0.08365 -0.12630 -0.19993 110 MET D O   
6822 C CB  . MET D 129 ? 2.28737 1.93114 2.42847 -0.01710 -0.09157 -0.24122 110 MET D CB  
6823 C CG  . MET D 129 ? 2.26349 1.90368 2.38867 0.01326  -0.07495 -0.25801 110 MET D CG  
6824 S SD  . MET D 129 ? 2.23311 1.79980 2.32213 0.03226  -0.06024 -0.27886 110 MET D SD  
6825 C CE  . MET D 129 ? 2.22085 1.79192 2.29836 0.06190  -0.03890 -0.28980 110 MET D CE  
6826 N N   . ASP D 130 ? 2.27077 2.05066 2.48596 -0.07750 -0.10140 -0.18200 111 ASP D N   
6827 C CA  . ASP D 130 ? 2.38405 2.16862 2.61358 -0.10703 -0.10851 -0.15496 111 ASP D CA  
6828 C C   . ASP D 130 ? 2.34937 2.06056 2.55514 -0.10186 -0.10742 -0.15580 111 ASP D C   
6829 O O   . ASP D 130 ? 2.48931 2.14750 2.68934 -0.12252 -0.12323 -0.14473 111 ASP D O   
6830 C CB  . ASP D 130 ? 2.46005 2.33439 2.71659 -0.10947 -0.09457 -0.13659 111 ASP D CB  
6831 C CG  . ASP D 130 ? 2.64679 2.55212 2.92630 -0.14742 -0.10444 -0.10227 111 ASP D CG  
6832 O OD1 . ASP D 130 ? 2.72740 2.56705 2.99774 -0.16894 -0.11729 -0.09002 111 ASP D OD1 
6833 O OD2 . ASP D 130 ? 2.69159 2.68683 2.99816 -0.15579 -0.09877 -0.08740 111 ASP D OD2 
6834 N N   . TYR D 131 ? 2.30155 2.00922 2.49344 -0.07385 -0.08894 -0.17085 112 TYR D N   
6835 C CA  . TYR D 131 ? 2.30394 1.95587 2.47301 -0.06341 -0.08618 -0.17483 112 TYR D CA  
6836 C C   . TYR D 131 ? 2.24313 1.86084 2.38773 -0.03553 -0.07505 -0.20739 112 TYR D C   
6837 O O   . TYR D 131 ? 2.20670 1.85944 2.35593 -0.02010 -0.05902 -0.22243 112 TYR D O   
6838 C CB  . TYR D 131 ? 2.37349 2.07223 2.55298 -0.06016 -0.07247 -0.15717 112 TYR D CB  
6839 C CG  . TYR D 131 ? 2.60160 2.34088 2.80485 -0.08833 -0.07991 -0.12020 112 TYR D CG  
6840 C CD1 . TYR D 131 ? 2.73483 2.41979 2.93194 -0.10980 -0.09550 -0.09635 112 TYR D CD1 
6841 C CD2 . TYR D 131 ? 2.62546 2.45665 2.85696 -0.09373 -0.07069 -0.10905 112 TYR D CD2 
6842 C CE1 . TYR D 131 ? 2.87112 2.58987 3.08989 -0.13970 -0.10019 -0.05936 112 TYR D CE1 
6843 C CE2 . TYR D 131 ? 2.77095 2.64641 3.02454 -0.12176 -0.07594 -0.07330 112 TYR D CE2 
6844 C CZ  . TYR D 131 ? 2.88574 2.70358 3.13304 -0.14659 -0.08993 -0.04702 112 TYR D CZ  
6845 O OH  . TYR D 131 ? 2.97579 2.83448 3.24504 -0.17847 -0.09309 -0.00834 112 TYR D OH  
6846 N N   . TRP D 132 ? 2.51023 2.05855 2.62853 -0.02934 -0.08312 -0.21810 113 TRP D N   
6847 C CA  . TRP D 132 ? 2.42278 1.93805 2.51595 -0.00579 -0.07253 -0.24704 113 TRP D CA  
6848 C C   . TRP D 132 ? 2.42610 1.94103 2.50884 0.00920  -0.05938 -0.25338 113 TRP D C   
6849 O O   . TRP D 132 ? 2.50536 2.02738 2.59291 0.00424  -0.06355 -0.23421 113 TRP D O   
6850 C CB  . TRP D 132 ? 2.40894 1.85724 2.47834 -0.00579 -0.09093 -0.25934 113 TRP D CB  
6851 C CG  . TRP D 132 ? 2.40387 1.85888 2.47956 -0.01475 -0.10255 -0.26008 113 TRP D CG  
6852 C CD1 . TRP D 132 ? 2.46038 1.95202 2.56156 -0.03678 -0.11392 -0.24183 113 TRP D CD1 
6853 C CD2 . TRP D 132 ? 2.35534 1.78657 2.41060 -0.00066 -0.10394 -0.27973 113 TRP D CD2 
6854 N NE1 . TRP D 132 ? 2.44938 1.94494 2.54786 -0.03558 -0.12314 -0.25127 113 TRP D NE1 
6855 C CE2 . TRP D 132 ? 2.38932 1.84655 2.45848 -0.01221 -0.11723 -0.27315 113 TRP D CE2 
6856 C CE3 . TRP D 132 ? 2.31913 1.71524 2.34529 0.02075  -0.09448 -0.30114 113 TRP D CE3 
6857 C CZ2 . TRP D 132 ? 2.37501 1.82365 2.42795 0.00058  -0.12200 -0.28660 113 TRP D CZ2 
6858 C CZ3 . TRP D 132 ? 2.31708 1.70142 2.32691 0.03115  -0.09805 -0.31200 113 TRP D CZ3 
6859 C CH2 . TRP D 132 ? 2.34079 1.75093 2.36307 0.02284  -0.11202 -0.30440 113 TRP D CH2 
6860 N N   . GLY D 133 ? 2.39566 1.90468 2.46339 0.02782  -0.04270 -0.27989 114 GLY D N   
6861 C CA  . GLY D 133 ? 2.39940 1.91851 2.45796 0.04278  -0.02885 -0.29233 114 GLY D CA  
6862 C C   . GLY D 133 ? 2.40212 1.86305 2.43007 0.05450  -0.03766 -0.30662 114 GLY D C   
6863 O O   . GLY D 133 ? 2.39116 1.80151 2.40374 0.05194  -0.05353 -0.31006 114 GLY D O   
6864 N N   . GLN D 134 ? 2.50881 1.98550 2.52823 0.06964  -0.02722 -0.31731 115 GLN D N   
6865 C CA  . GLN D 134 ? 2.52332 1.95558 2.51354 0.08538  -0.03488 -0.33242 115 GLN D CA  
6866 C C   . GLN D 134 ? 2.44869 1.85366 2.42080 0.09024  -0.02900 -0.35817 115 GLN D C   
6867 O O   . GLN D 134 ? 2.46029 1.81608 2.40873 0.09749  -0.04398 -0.36646 115 GLN D O   
6868 C CB  . GLN D 134 ? 2.56171 2.03365 2.54822 0.10324  -0.02193 -0.34178 115 GLN D CB  
6869 C CG  . GLN D 134 ? 2.60118 2.11262 2.60439 0.10191  -0.02364 -0.31445 115 GLN D CG  
6870 C CD  . GLN D 134 ? 2.64073 2.21379 2.64441 0.12088  -0.00652 -0.32792 115 GLN D CD  
6871 O OE1 . GLN D 134 ? 2.61320 2.22069 2.61911 0.12527  0.01323  -0.35872 115 GLN D OE1 
6872 N NE2 . GLN D 134 ? 2.71356 2.30205 2.71481 0.13190  -0.01352 -0.30479 115 GLN D NE2 
6873 N N   . GLY D 135 ? 2.60398 2.03922 2.58585 0.08717  -0.00689 -0.37075 116 GLY D N   
6874 C CA  . GLY D 135 ? 2.55157 1.96220 2.51523 0.09123  0.00264  -0.39051 116 GLY D CA  
6875 C C   . GLY D 135 ? 2.54231 1.96752 2.49210 0.10250  0.02121  -0.41701 116 GLY D C   
6876 O O   . GLY D 135 ? 2.58563 2.01017 2.52285 0.11475  0.01332  -0.42321 116 GLY D O   
6877 N N   . THR D 136 ? 2.60342 2.04229 2.55534 0.09856  0.04648  -0.43299 117 THR D N   
6878 C CA  . THR D 136 ? 2.60062 2.05688 2.54149 0.10327  0.06733  -0.46022 117 THR D CA  
6879 C C   . THR D 136 ? 2.58362 2.00398 2.50350 0.10160  0.07712  -0.46783 117 THR D C   
6880 O O   . THR D 136 ? 2.56104 1.96742 2.48662 0.09399  0.08745  -0.46019 117 THR D O   
6881 C CB  . THR D 136 ? 2.58985 2.10222 2.55586 0.09591  0.09319  -0.47484 117 THR D CB  
6882 O OG1 . THR D 136 ? 2.59297 2.12217 2.55026 0.09451  0.11599  -0.50369 117 THR D OG1 
6883 C CG2 . THR D 136 ? 2.55810 2.07082 2.54434 0.08435  0.10486  -0.46676 117 THR D CG2 
6884 N N   . SER D 137 ? 2.71974 2.12706 2.61362 0.11143  0.07369  -0.48156 118 SER D N   
6885 C CA  . SER D 137 ? 2.72647 2.10222 2.59577 0.11242  0.08008  -0.48532 118 SER D CA  
6886 C C   . SER D 137 ? 2.72272 2.11945 2.59065 0.10295  0.11469  -0.50497 118 SER D C   
6887 O O   . SER D 137 ? 2.72588 2.16558 2.60420 0.10007  0.12851  -0.52476 118 SER D O   
6888 C CB  . SER D 137 ? 2.76741 2.12103 2.60814 0.12873  0.05718  -0.49105 118 SER D CB  
6889 O OG  . SER D 137 ? 2.79939 2.12992 2.61507 0.13142  0.06268  -0.49328 118 SER D OG  
6890 N N   . VAL D 138 ? 2.71882 2.08612 2.57345 0.09771  0.12917  -0.49897 119 VAL D N   
6891 C CA  . VAL D 138 ? 2.73526 2.10979 2.58581 0.08468  0.16384  -0.51356 119 VAL D CA  
6892 C C   . VAL D 138 ? 2.79963 2.15314 2.61476 0.09184  0.16495  -0.51334 119 VAL D C   
6893 O O   . VAL D 138 ? 2.77640 2.10677 2.57176 0.10746  0.13939  -0.50188 119 VAL D O   
6894 C CB  . VAL D 138 ? 2.72197 2.07689 2.58810 0.07146  0.18658  -0.50428 119 VAL D CB  
6895 C CG1 . VAL D 138 ? 2.67922 2.05632 2.57825 0.06947  0.17883  -0.50080 119 VAL D CG1 
6896 C CG2 . VAL D 138 ? 2.73681 2.04208 2.58052 0.08001  0.18184  -0.47974 119 VAL D CG2 
6897 N N   . THR D 139 ? 2.91072 2.27658 2.71883 0.07870  0.19572  -0.52747 120 THR D N   
6898 C CA  . THR D 139 ? 2.94731 2.30386 2.72184 0.08332  0.20232  -0.52740 120 THR D CA  
6899 C C   . THR D 139 ? 2.98992 2.33314 2.76166 0.06135  0.24261  -0.52576 120 THR D C   
6900 O O   . THR D 139 ? 2.98320 2.34289 2.78012 0.04003  0.26739  -0.54023 120 THR D O   
6901 C CB  . THR D 139 ? 2.94971 2.35100 2.71288 0.09290  0.19414  -0.55210 120 THR D CB  
6902 O OG1 . THR D 139 ? 2.93243 2.38197 2.72230 0.08265  0.20512  -0.57488 120 THR D OG1 
6903 C CG2 . THR D 139 ? 2.94432 2.33474 2.69389 0.11943  0.15339  -0.54835 120 THR D CG2 
6904 N N   . VAL D 140 ? 3.04408 2.35686 2.78453 0.06655  0.24936  -0.50811 121 VAL D N   
6905 C CA  . VAL D 140 ? 3.08763 2.37517 2.81874 0.04701  0.28813  -0.49904 121 VAL D CA  
6906 C C   . VAL D 140 ? 3.12888 2.43524 2.82705 0.04854  0.29766  -0.50153 121 VAL D C   
6907 O O   . VAL D 140 ? 3.15468 2.44742 2.82208 0.07054  0.28030  -0.48465 121 VAL D O   
6908 C CB  . VAL D 140 ? 3.11923 2.34672 2.84112 0.05496  0.29077  -0.46634 121 VAL D CB  
6909 C CG1 . VAL D 140 ? 3.18197 2.37330 2.89445 0.03443  0.33343  -0.45542 121 VAL D CG1 
6910 C CG2 . VAL D 140 ? 3.07821 2.29737 2.83172 0.05808  0.27619  -0.46451 121 VAL D CG2 
6911 N N   . SER D 141 ? 3.13447 2.47951 2.83970 0.02520  0.32505  -0.52429 122 SER D N   
6912 C CA  . SER D 141 ? 3.17398 2.54947 2.85022 0.02408  0.33702  -0.52887 122 SER D CA  
6913 C C   . SER D 141 ? 3.18554 2.59245 2.87705 -0.01353 0.37844  -0.54894 122 SER D C   
6914 O O   . SER D 141 ? 3.14403 2.57008 2.87094 -0.03228 0.38768  -0.57115 122 SER D O   
6915 C CB  . SER D 141 ? 3.14308 2.56791 2.80812 0.05138  0.30281  -0.54872 122 SER D CB  
6916 O OG  . SER D 141 ? 3.14865 2.54225 2.79248 0.08209  0.26883  -0.53004 122 SER D OG  
6917 N N   . PRO D 142 ? 3.21579 2.63156 2.88233 -0.02697 0.40492  -0.54181 123 PRO D N   
6918 C CA  . PRO D 142 ? 3.34441 2.79492 3.02622 -0.06818 0.44622  -0.56213 123 PRO D CA  
6919 C C   . PRO D 142 ? 3.29368 2.83979 2.98433 -0.07034 0.44249  -0.60184 123 PRO D C   
6920 O O   . PRO D 142 ? 3.40386 2.99119 3.10955 -0.10671 0.47656  -0.62257 123 PRO D O   
6921 C CB  . PRO D 142 ? 3.01126 2.42869 2.65780 -0.07971 0.47551  -0.53054 123 PRO D CB  
6922 C CG  . PRO D 142 ? 3.02816 2.37939 2.64840 -0.04692 0.45379  -0.49196 123 PRO D CG  
6923 C CD  . PRO D 142 ? 2.97166 2.34968 2.59666 -0.01050 0.40507  -0.50652 123 PRO D CD  
6924 N N   . ALA D 143 ? 3.29962 2.88251 2.98113 -0.03307 0.40341  -0.61400 124 ALA D N   
6925 C CA  . ALA D 143 ? 3.26416 2.93802 2.95057 -0.02715 0.39746  -0.65143 124 ALA D CA  
6926 C C   . ALA D 143 ? 3.13267 2.83983 2.85867 -0.03199 0.39093  -0.67976 124 ALA D C   
6927 O O   . ALA D 143 ? 2.96363 2.64247 2.69884 -0.00830 0.36047  -0.67371 124 ALA D O   
6928 C CB  . ALA D 143 ? 3.17971 2.87158 2.83538 0.01873  0.35840  -0.65245 124 ALA D CB  
6929 N N   . LYS D 144 ? 3.10577 2.87839 2.85532 -0.06329 0.41986  -0.71075 125 LYS D N   
6930 C CA  . LYS D 144 ? 3.03385 2.85027 2.82118 -0.06829 0.41644  -0.74013 125 LYS D CA  
6931 C C   . LYS D 144 ? 2.98548 2.85030 2.76695 -0.02325 0.37673  -0.75573 125 LYS D C   
6932 O O   . LYS D 144 ? 2.98566 2.87901 2.73856 0.00388  0.36041  -0.75940 125 LYS D O   
6933 C CB  . LYS D 144 ? 2.98855 2.87679 2.80152 -0.11181 0.45583  -0.77471 125 LYS D CB  
6934 C CG  . LYS D 144 ? 3.04954 2.88200 2.87040 -0.16044 0.49809  -0.76086 125 LYS D CG  
6935 C CD  . LYS D 144 ? 3.07985 2.83124 2.92042 -0.16530 0.49628  -0.74396 125 LYS D CD  
6936 C CE  . LYS D 144 ? 3.16873 2.84004 3.00605 -0.20238 0.53342  -0.72059 125 LYS D CE  
6937 N NZ  . LYS D 144 ? 3.24927 2.86629 3.04185 -0.18674 0.53124  -0.67907 125 LYS D NZ  
6938 N N   . THR D 145 ? 3.03116 2.90455 2.83905 -0.01407 0.36170  -0.76475 126 THR D N   
6939 C CA  . THR D 145 ? 3.00491 2.90322 2.80612 0.03057  0.32275  -0.77074 126 THR D CA  
6940 C C   . THR D 145 ? 2.94471 2.94270 2.73929 0.04567  0.32252  -0.80606 126 THR D C   
6941 O O   . THR D 145 ? 2.88491 2.96030 2.70319 0.02159  0.34778  -0.83722 126 THR D O   
6942 C CB  . THR D 145 ? 2.98381 2.87918 2.81590 0.03307  0.31260  -0.77121 126 THR D CB  
6943 O OG1 . THR D 145 ? 2.92052 2.89106 2.78491 0.00540  0.34018  -0.80495 126 THR D OG1 
6944 C CG2 . THR D 145 ? 3.03506 2.84001 2.87425 0.02016  0.31279  -0.73834 126 THR D CG2 
6945 N N   . THR D 146 ? 3.03309 3.03210 2.79585 0.08663  0.29340  -0.80380 127 THR D N   
6946 C CA  . THR D 146 ? 2.97804 3.06891 2.72929 0.11173  0.28753  -0.83641 127 THR D CA  
6947 C C   . THR D 146 ? 2.97202 3.06366 2.71678 0.16125  0.24839  -0.83852 127 THR D C   
6948 O O   . THR D 146 ? 3.02872 3.04200 2.75523 0.18688  0.21805  -0.81331 127 THR D O   
6949 C CB  . THR D 146 ? 3.00267 3.10017 2.71835 0.12182  0.28782  -0.83601 127 THR D CB  
6950 O OG1 . THR D 146 ? 3.06669 3.07916 2.75523 0.15155  0.25565  -0.80830 127 THR D OG1 
6951 C CG2 . THR D 146 ? 3.02399 3.12146 2.74376 0.07178  0.32965  -0.82972 127 THR D CG2 
6952 N N   . PRO D 147 ? 3.07028 3.24823 2.82899 0.17582  0.24821  -0.86739 128 PRO D N   
6953 C CA  . PRO D 147 ? 3.07934 3.25015 2.83207 0.22269  0.21330  -0.86351 128 PRO D CA  
6954 C C   . PRO D 147 ? 3.10688 3.26449 2.82039 0.27232  0.18232  -0.86601 128 PRO D C   
6955 O O   . PRO D 147 ? 3.08653 3.28400 2.78077 0.27506  0.19052  -0.88359 128 PRO D O   
6956 C CB  . PRO D 147 ? 3.00025 3.28262 2.77698 0.22383  0.22702  -0.89663 128 PRO D CB  
6957 C CG  . PRO D 147 ? 2.94070 3.30375 2.72349 0.19184  0.26083  -0.92709 128 PRO D CG  
6958 C CD  . PRO D 147 ? 2.99114 3.27852 2.77308 0.14855  0.28103  -0.90424 128 PRO D CD  
6959 N N   . PRO D 148 ? 3.02859 3.12936 2.72953 0.31112  0.14716  -0.84898 129 PRO D N   
6960 C CA  . PRO D 148 ? 3.06664 3.13930 2.73016 0.35888  0.11556  -0.85247 129 PRO D CA  
6961 C C   . PRO D 148 ? 3.02256 3.18765 2.67306 0.40205  0.10879  -0.88596 129 PRO D C   
6962 O O   . PRO D 148 ? 2.96875 3.21638 2.63944 0.40037  0.12314  -0.90294 129 PRO D O   
6963 C CB  . PRO D 148 ? 3.14264 3.11388 2.80303 0.37664  0.08375  -0.82017 129 PRO D CB  
6964 C CG  . PRO D 148 ? 3.12545 3.11807 2.81862 0.35940  0.09502  -0.81027 129 PRO D CG  
6965 C CD  . PRO D 148 ? 3.06330 3.11363 2.78363 0.30977  0.13516  -0.82319 129 PRO D CD  
6966 N N   . SER D 149 ? 3.01320 3.16633 2.62870 0.44401  0.08535  -0.89724 130 SER D N   
6967 C CA  . SER D 149 ? 2.98451 3.21348 2.57997 0.49655  0.07254  -0.92827 130 SER D CA  
6968 C C   . SER D 149 ? 3.07244 3.21616 2.64290 0.54971  0.03098  -0.91402 130 SER D C   
6969 O O   . SER D 149 ? 3.13839 3.19951 2.68609 0.56252  0.00880  -0.90541 130 SER D O   
6970 C CB  . SER D 149 ? 2.94339 3.23925 2.51739 0.50393  0.08161  -0.95854 130 SER D CB  
6971 O OG  . SER D 149 ? 3.00581 3.21938 2.55544 0.50821  0.06493  -0.94618 130 SER D OG  
6972 N N   . VAL D 150 ? 3.07482 3.23896 2.64910 0.58035  0.02096  -0.91182 131 VAL D N   
6973 C CA  . VAL D 150 ? 3.15529 3.23179 2.70739 0.62813  -0.01567 -0.89313 131 VAL D CA  
6974 C C   . VAL D 150 ? 3.15674 3.27370 2.67272 0.69384  -0.03533 -0.92422 131 VAL D C   
6975 O O   . VAL D 150 ? 3.10184 3.33137 2.61778 0.71806  -0.02457 -0.95069 131 VAL D O   
6976 C CB  . VAL D 150 ? 3.17775 3.25037 2.74982 0.62921  -0.01583 -0.86834 131 VAL D CB  
6977 C CG1 . VAL D 150 ? 3.27089 3.25557 2.81657 0.68128  -0.05177 -0.84770 131 VAL D CG1 
6978 C CG2 . VAL D 150 ? 3.18378 3.21098 2.78999 0.56826  0.00059  -0.83846 131 VAL D CG2 
6979 N N   . TYR D 151 ? 3.26926 3.29800 2.75487 0.72412  -0.06475 -0.92366 132 TYR D N   
6980 C CA  . TYR D 151 ? 3.28306 3.33482 2.73106 0.79087  -0.08702 -0.95450 132 TYR D CA  
6981 C C   . TYR D 151 ? 3.39819 3.32931 2.82262 0.83649  -0.12430 -0.93449 132 TYR D C   
6982 O O   . TYR D 151 ? 3.46581 3.27981 2.88792 0.81886  -0.14136 -0.91382 132 TYR D O   
6983 C CB  . TYR D 151 ? 3.25701 3.32411 2.68698 0.78842  -0.08717 -0.98146 132 TYR D CB  
6984 C CG  . TYR D 151 ? 3.15985 3.34305 2.60997 0.74296  -0.04868 -0.99922 132 TYR D CG  
6985 C CD1 . TYR D 151 ? 3.07430 3.38353 2.54168 0.74007  -0.02397 -1.01762 132 TYR D CD1 
6986 C CD2 . TYR D 151 ? 3.14998 3.31717 2.60193 0.70187  -0.03629 -0.99701 132 TYR D CD2 
6987 C CE1 . TYR D 151 ? 2.99462 3.40534 2.48237 0.69327  0.01271  -1.03451 132 TYR D CE1 
6988 C CE2 . TYR D 151 ? 3.06919 3.33383 2.53814 0.65820  0.00084  -1.00930 132 TYR D CE2 
6989 C CZ  . TYR D 151 ? 2.99946 3.38282 2.48729 0.65180  0.02563  -1.02852 132 TYR D CZ  
6990 O OH  . TYR D 151 ? 2.94486 3.42094 2.45148 0.60326  0.06403  -1.04153 132 TYR D OH  
6991 N N   . PRO D 152 ? 3.29491 3.24823 2.70132 0.89441  -0.13750 -0.93914 133 PRO D N   
6992 C CA  . PRO D 152 ? 3.42662 3.25478 2.80910 0.93703  -0.17128 -0.91625 133 PRO D CA  
6993 C C   . PRO D 152 ? 3.48256 3.24026 2.82896 0.97719  -0.20078 -0.94069 133 PRO D C   
6994 O O   . PRO D 152 ? 3.41871 3.24848 2.75120 0.99229  -0.19756 -0.98024 133 PRO D O   
6995 C CB  . PRO D 152 ? 3.44446 3.33900 2.81509 0.99205  -0.17249 -0.91757 133 PRO D CB  
6996 C CG  . PRO D 152 ? 3.31820 3.37483 2.69168 1.00042  -0.15038 -0.96111 133 PRO D CG  
6997 C CD  . PRO D 152 ? 3.22190 3.31816 2.62913 0.92348  -0.12123 -0.96475 133 PRO D CD  
6998 N N   . LEU D 153 ? 3.32942 2.94508 2.66119 0.99358  -0.22972 -0.91742 134 LEU D N   
6999 C CA  . LEU D 153 ? 3.40781 2.93484 2.70789 1.02767  -0.26087 -0.94010 134 LEU D CA  
7000 C C   . LEU D 153 ? 3.51429 2.93911 2.78533 1.08716  -0.29038 -0.92638 134 LEU D C   
7001 O O   . LEU D 153 ? 3.60909 2.91834 2.88859 1.06650  -0.30092 -0.88674 134 LEU D O   
7002 C CB  . LEU D 153 ? 3.39626 2.83474 2.71244 0.97094  -0.26594 -0.92756 134 LEU D CB  
7003 C CG  . LEU D 153 ? 3.30288 2.81845 2.64938 0.90575  -0.23528 -0.92766 134 LEU D CG  
7004 C CD1 . LEU D 153 ? 3.29889 2.71582 2.66118 0.85449  -0.24289 -0.90626 134 LEU D CD1 
7005 C CD2 . LEU D 153 ? 3.28716 2.91074 2.61815 0.92306  -0.22555 -0.97307 134 LEU D CD2 
7006 N N   . ALA D 154 ? 3.34723 2.81484 2.58328 1.16143  -0.30306 -0.95836 135 ALA D N   
7007 C CA  . ALA D 154 ? 3.45552 2.82586 2.65736 1.22794  -0.33122 -0.94845 135 ALA D CA  
7008 C C   . ALA D 154 ? 3.54676 2.84326 2.71222 1.27610  -0.36291 -0.98822 135 ALA D C   
7009 O O   . ALA D 154 ? 3.52439 2.90382 2.68189 1.28594  -0.36066 -1.03363 135 ALA D O   
7010 C CB  . ALA D 154 ? 3.46089 2.93544 2.64685 1.28762  -0.32317 -0.95234 135 ALA D CB  
7011 N N   . PRO D 155 ? 3.49713 2.63711 2.63995 1.30602  -0.39251 -0.97308 136 PRO D N   
7012 C CA  . PRO D 155 ? 3.59492 2.65251 2.70342 1.35292  -0.42484 -1.01403 136 PRO D CA  
7013 C C   . PRO D 155 ? 3.66450 2.77234 2.72933 1.44945  -0.43841 -1.04956 136 PRO D C   
7014 O O   . PRO D 155 ? 3.78218 2.77747 2.81557 1.49930  -0.46825 -1.05607 136 PRO D O   
7015 C CB  . PRO D 155 ? 3.68569 2.55279 2.79190 1.33957  -0.44750 -0.97866 136 PRO D CB  
7016 C CG  . PRO D 155 ? 3.67527 2.53768 2.79159 1.33478  -0.43274 -0.92270 136 PRO D CG  
7017 C CD  . PRO D 155 ? 3.53745 2.56494 2.68750 1.29201  -0.39635 -0.91606 136 PRO D CD  
7018 N N   . ASN D 162 ? 4.48958 2.39108 3.43756 1.53712  -0.60753 -0.90375 143 ASN D N   
7019 C CA  . ASN D 162 ? 4.43333 2.37232 3.38036 1.54805  -0.58668 -0.85778 143 ASN D CA  
7020 C C   . ASN D 162 ? 4.48741 2.26925 3.44877 1.50040  -0.58554 -0.79830 143 ASN D C   
7021 O O   . ASN D 162 ? 4.56622 2.27895 3.50471 1.53567  -0.58347 -0.74885 143 ASN D O   
7022 C CB  . ASN D 162 ? 4.48737 2.48117 3.39170 1.63916  -0.58609 -0.84902 143 ASN D CB  
7023 C CG  . ASN D 162 ? 4.37986 2.50461 3.28704 1.65918  -0.56097 -0.82878 143 ASN D CG  
7024 O OD1 . ASN D 162 ? 4.31129 2.42303 3.24490 1.61193  -0.54539 -0.79598 143 ASN D OD1 
7025 N ND2 . ASN D 162 ? 4.36503 2.62462 3.24660 1.72833  -0.55679 -0.84994 143 ASN D ND2 
7026 N N   . SER D 163 ? 4.44656 2.17813 3.44554 1.41948  -0.58657 -0.80162 144 SER D N   
7027 C CA  . SER D 163 ? 4.49426 2.08265 3.51249 1.36192  -0.58638 -0.74887 144 SER D CA  
7028 C C   . SER D 163 ? 4.35569 2.00753 3.42096 1.27893  -0.57035 -0.74302 144 SER D C   
7029 O O   . SER D 163 ? 4.28581 1.99785 3.36987 1.24907  -0.57384 -0.79172 144 SER D O   
7030 C CB  . SER D 163 ? 4.62877 2.06595 3.65063 1.33450  -0.60698 -0.75479 144 SER D CB  
7031 O OG  . SER D 163 ? 4.66049 1.97586 3.70921 1.26436  -0.60501 -0.70900 144 SER D OG  
7032 N N   . MET D 164 ? 4.39398 2.05451 3.48416 1.23270  -0.54847 -0.67620 145 MET D N   
7033 C CA  . MET D 164 ? 4.25473 2.00080 3.39759 1.14414  -0.52614 -0.65585 145 MET D CA  
7034 C C   . MET D 164 ? 4.11064 2.03858 3.26688 1.14396  -0.51081 -0.69906 145 MET D C   
7035 O O   . MET D 164 ? 4.04830 2.01042 3.22779 1.10030  -0.51290 -0.73479 145 MET D O   
7036 C CB  . MET D 164 ? 4.28912 1.92191 3.46071 1.07106  -0.54017 -0.66028 145 MET D CB  
7037 C CG  . MET D 164 ? 4.43189 1.88373 3.59608 1.05790  -0.55215 -0.61450 145 MET D CG  
7038 S SD  . MET D 164 ? 4.41622 1.88570 3.58698 1.04674  -0.52456 -0.52235 145 MET D SD  
7039 C CE  . MET D 164 ? 4.59857 1.94089 3.70565 1.14551  -0.54105 -0.50530 145 MET D CE  
7040 N N   . VAL D 165 ? 4.12729 2.17432 3.26765 1.19427  -0.49457 -0.69435 146 VAL D N   
7041 C CA  . VAL D 165 ? 4.01092 2.22858 3.15730 1.20496  -0.48007 -0.73817 146 VAL D CA  
7042 C C   . VAL D 165 ? 3.86939 2.17856 3.06600 1.12072  -0.45491 -0.72395 146 VAL D C   
7043 O O   . VAL D 165 ? 3.82770 2.14259 3.05029 1.07792  -0.43724 -0.67140 146 VAL D O   
7044 C CB  . VAL D 165 ? 3.99913 2.32424 3.11953 1.27525  -0.46792 -0.73460 146 VAL D CB  
7045 C CG1 . VAL D 165 ? 3.88355 2.38751 3.01230 1.28125  -0.45144 -0.78144 146 VAL D CG1 
7046 C CG2 . VAL D 165 ? 4.14867 2.37707 3.21601 1.36464  -0.49390 -0.74704 146 VAL D CG2 
7047 N N   . THR D 166 ? 3.82310 2.20453 3.03191 1.09899  -0.45311 -0.77028 147 THR D N   
7048 C CA  . THR D 166 ? 3.69259 2.16620 2.94430 1.02677  -0.42907 -0.76288 147 THR D CA  
7049 C C   . THR D 166 ? 3.58954 2.23504 2.84515 1.04250  -0.40202 -0.77665 147 THR D C   
7050 O O   . THR D 166 ? 3.60192 2.31293 2.83014 1.09844  -0.40625 -0.81880 147 THR D O   
7051 C CB  . THR D 166 ? 3.68328 2.13227 2.94500 0.99208  -0.44201 -0.80191 147 THR D CB  
7052 O OG1 . THR D 166 ? 3.75642 2.06099 3.02861 0.95535  -0.46123 -0.78286 147 THR D OG1 
7053 C CG2 . THR D 166 ? 3.54883 2.11652 2.84550 0.93462  -0.41544 -0.80303 147 THR D CG2 
7054 N N   . LEU D 167 ? 3.73052 2.45084 3.02105 0.99262  -0.37416 -0.74290 148 LEU D N   
7055 C CA  . LEU D 167 ? 3.62620 2.50667 2.92678 0.99734  -0.34570 -0.75290 148 LEU D CA  
7056 C C   . LEU D 167 ? 3.48849 2.44270 2.82382 0.93199  -0.32489 -0.76330 148 LEU D C   
7057 O O   . LEU D 167 ? 3.48464 2.38636 2.84808 0.87301  -0.32229 -0.73656 148 LEU D O   
7058 C CB  . LEU D 167 ? 3.66199 2.57787 2.97298 0.99947  -0.32867 -0.70697 148 LEU D CB  
7059 C CG  . LEU D 167 ? 3.81157 2.64900 3.08742 1.06294  -0.34664 -0.68450 148 LEU D CG  
7060 C CD1 . LEU D 167 ? 3.85676 2.70028 3.14939 1.04539  -0.33131 -0.62680 148 LEU D CD1 
7061 C CD2 . LEU D 167 ? 3.81366 2.73255 3.05364 1.14206  -0.35037 -0.72272 148 LEU D CD2 
7062 N N   . GLY D 168 ? 3.59041 2.66775 2.92316 0.94310  -0.30929 -0.80083 149 GLY D N   
7063 C CA  . GLY D 168 ? 3.47308 2.61865 2.83342 0.88646  -0.28828 -0.81129 149 GLY D CA  
7064 C C   . GLY D 168 ? 3.36460 2.64890 2.74756 0.86666  -0.25307 -0.80943 149 GLY D C   
7065 O O   . GLY D 168 ? 3.35304 2.71339 2.72478 0.90776  -0.24572 -0.81768 149 GLY D O   
7066 N N   . CYS D 169 ? 3.40561 2.72388 2.82050 0.80431  -0.23127 -0.80009 150 CYS D N   
7067 C CA  . CYS D 169 ? 3.30087 2.74302 2.74088 0.77644  -0.19611 -0.80149 150 CYS D CA  
7068 C C   . CYS D 169 ? 3.21661 2.68744 2.67286 0.72668  -0.17936 -0.81268 150 CYS D C   
7069 O O   . CYS D 169 ? 3.22925 2.62824 2.70074 0.68592  -0.18366 -0.79095 150 CYS D O   
7070 C CB  . CYS D 169 ? 3.32232 2.76354 2.79078 0.74892  -0.18270 -0.75978 150 CYS D CB  
7071 S SG  . CYS D 169 ? 3.19758 2.78139 2.70232 0.70784  -0.13959 -0.76368 150 CYS D SG  
7072 N N   . LEU D 170 ? 3.28383 2.86167 2.73629 0.73024  -0.15969 -0.84503 151 LEU D N   
7073 C CA  . LEU D 170 ? 3.21957 2.82823 2.68046 0.68994  -0.14269 -0.85610 151 LEU D CA  
7074 C C   . LEU D 170 ? 3.14414 2.83659 2.63828 0.64146  -0.10404 -0.84662 151 LEU D C   
7075 O O   . LEU D 170 ? 3.10290 2.88263 2.60529 0.65155  -0.08713 -0.85630 151 LEU D O   
7076 C CB  . LEU D 170 ? 3.18835 2.85452 2.61936 0.72532  -0.14719 -0.89928 151 LEU D CB  
7077 C CG  . LEU D 170 ? 3.13235 2.84286 2.56658 0.68894  -0.12747 -0.91056 151 LEU D CG  
7078 C CD1 . LEU D 170 ? 3.15770 2.82767 2.56061 0.71724  -0.15345 -0.93451 151 LEU D CD1 
7079 C CD2 . LEU D 170 ? 3.04943 2.89563 2.48958 0.68251  -0.09457 -0.93308 151 LEU D CD2 
7080 N N   . VAL D 171 ? 3.13913 2.80480 2.65198 0.59020  -0.09060 -0.82932 152 VAL D N   
7081 C CA  . VAL D 171 ? 3.07663 2.80582 2.61996 0.54071  -0.05358 -0.82122 152 VAL D CA  
7082 C C   . VAL D 171 ? 3.04390 2.79304 2.58033 0.51606  -0.03868 -0.83237 152 VAL D C   
7083 O O   . VAL D 171 ? 3.05396 2.73210 2.58755 0.49861  -0.04878 -0.81640 152 VAL D O   
7084 C CB  . VAL D 171 ? 3.07068 2.74337 2.64435 0.50253  -0.04934 -0.78281 152 VAL D CB  
7085 C CG1 . VAL D 171 ? 3.02086 2.74832 2.62368 0.45200  -0.01180 -0.77808 152 VAL D CG1 
7086 C CG2 . VAL D 171 ? 3.11359 2.77924 2.69363 0.52617  -0.06028 -0.76888 152 VAL D CG2 
7087 N N   . LYS D 172 ? 2.98762 2.83724 2.52104 0.51441  -0.01421 -0.85887 153 LYS D N   
7088 C CA  . LYS D 172 ? 2.96571 2.84437 2.48803 0.49510  0.00190  -0.86899 153 LYS D CA  
7089 C C   . LYS D 172 ? 2.89960 2.84937 2.44772 0.44603  0.04544  -0.86714 153 LYS D C   
7090 O O   . LYS D 172 ? 2.84673 2.86714 2.41353 0.44138  0.06281  -0.87908 153 LYS D O   
7091 C CB  . LYS D 172 ? 2.95438 2.88983 2.44343 0.54033  -0.00968 -0.90595 153 LYS D CB  
7092 C CG  . LYS D 172 ? 2.95627 2.91536 2.42842 0.52586  0.00216  -0.91339 153 LYS D CG  
7093 C CD  . LYS D 172 ? 2.96945 3.03810 2.42150 0.55305  0.01094  -0.95157 153 LYS D CD  
7094 C CE  . LYS D 172 ? 2.95079 3.08375 2.40560 0.51061  0.04822  -0.95004 153 LYS D CE  
7095 N NZ  . LYS D 172 ? 2.96304 3.21423 2.40007 0.53268  0.05936  -0.98680 153 LYS D NZ  
7096 N N   . GLY D 173 ? 3.02872 2.95894 2.57712 0.41020  0.06297  -0.85275 154 GLY D N   
7097 C CA  . GLY D 173 ? 2.98445 2.97176 2.55241 0.36278  0.10568  -0.85135 154 GLY D CA  
7098 C C   . GLY D 173 ? 2.97116 2.94348 2.57669 0.32536  0.12451  -0.83303 154 GLY D C   
7099 O O   . GLY D 173 ? 2.91654 2.95985 2.54258 0.31802  0.14158  -0.85040 154 GLY D O   
7100 N N   . TYR D 174 ? 3.03179 2.91906 2.64701 0.30282  0.12136  -0.80047 155 TYR D N   
7101 C CA  . TYR D 174 ? 3.02265 2.89449 2.67301 0.26813  0.13916  -0.78352 155 TYR D CA  
7102 C C   . TYR D 174 ? 3.06113 2.86378 2.71548 0.23555  0.15017  -0.75276 155 TYR D C   
7103 O O   . TYR D 174 ? 3.10149 2.85649 2.73194 0.24593  0.13516  -0.74026 155 TYR D O   
7104 C CB  . TYR D 174 ? 3.03708 2.87769 2.69975 0.29006  0.11291  -0.77452 155 TYR D CB  
7105 C CG  . TYR D 174 ? 3.09121 2.83288 2.74516 0.30121  0.08156  -0.74658 155 TYR D CG  
7106 C CD1 . TYR D 174 ? 3.12512 2.83133 2.75030 0.34014  0.04781  -0.75225 155 TYR D CD1 
7107 C CD2 . TYR D 174 ? 3.10240 2.78921 2.77819 0.27264  0.08550  -0.71729 155 TYR D CD2 
7108 C CE1 . TYR D 174 ? 3.12928 2.74791 2.74954 0.34568  0.01966  -0.73011 155 TYR D CE1 
7109 C CE2 . TYR D 174 ? 3.06696 2.67323 2.73734 0.27992  0.05748  -0.69370 155 TYR D CE2 
7110 C CZ  . TYR D 174 ? 3.09474 2.66717 2.73835 0.31424  0.02495  -0.70050 155 TYR D CZ  
7111 O OH  . TYR D 174 ? 3.08822 2.58285 2.72933 0.31692  -0.00244 -0.68017 155 TYR D OH  
7112 N N   . PHE D 175 ? 2.97204 2.77276 2.65653 0.19851  0.17608  -0.74250 156 PHE D N   
7113 C CA  . PHE D 175 ? 3.00891 2.74593 2.69973 0.16906  0.18933  -0.71319 156 PHE D CA  
7114 C C   . PHE D 175 ? 2.99285 2.72758 2.72106 0.14099  0.20695  -0.70741 156 PHE D C   
7115 O O   . PHE D 175 ? 2.95014 2.74973 2.69876 0.12425  0.23028  -0.73060 156 PHE D O   
7116 C CB  . PHE D 175 ? 3.02739 2.77905 2.70246 0.14661  0.21934  -0.71241 156 PHE D CB  
7117 C CG  . PHE D 175 ? 3.07860 2.75925 2.75101 0.12586  0.23002  -0.67910 156 PHE D CG  
7118 C CD1 . PHE D 175 ? 3.11776 2.74515 2.76435 0.14678  0.20551  -0.65877 156 PHE D CD1 
7119 C CD2 . PHE D 175 ? 3.08848 2.75698 2.78365 0.08748  0.26415  -0.67005 156 PHE D CD2 
7120 C CE1 . PHE D 175 ? 3.15964 2.72885 2.80182 0.13255  0.21455  -0.62793 156 PHE D CE1 
7121 C CE2 . PHE D 175 ? 3.13606 2.73704 2.82570 0.07412  0.27353  -0.63834 156 PHE D CE2 
7122 C CZ  . PHE D 175 ? 3.16969 2.72409 2.83211 0.09806  0.24862  -0.61625 156 PHE D CZ  
7123 N N   . PRO D 176 ? 3.01289 2.68116 2.75204 0.13535  0.19643  -0.67971 157 PRO D N   
7124 C CA  . PRO D 176 ? 3.05215 2.65008 2.77200 0.15164  0.16902  -0.65412 157 PRO D CA  
7125 C C   . PRO D 176 ? 3.04312 2.61309 2.76838 0.17570  0.13256  -0.64584 157 PRO D C   
7126 O O   . PRO D 176 ? 3.02241 2.62808 2.76182 0.18527  0.12738  -0.65801 157 PRO D O   
7127 C CB  . PRO D 176 ? 3.07502 2.62685 2.80698 0.12358  0.18876  -0.62940 157 PRO D CB  
7128 C CG  . PRO D 176 ? 3.04861 2.63454 2.81606 0.09800  0.21478  -0.64100 157 PRO D CG  
7129 C CD  . PRO D 176 ? 3.00492 2.66750 2.77803 0.10746  0.21583  -0.67335 157 PRO D CD  
7130 N N   . GLU D 177 ? 3.06137 2.56989 2.77502 0.18467  0.10833  -0.62456 158 GLU D N   
7131 C CA  . GLU D 177 ? 3.03327 2.50555 2.75461 0.19938  0.07605  -0.61200 158 GLU D CA  
7132 C C   . GLU D 177 ? 3.02348 2.49939 2.77947 0.17995  0.08641  -0.59820 158 GLU D C   
7133 O O   . GLU D 177 ? 3.05908 2.53526 2.82976 0.15536  0.11150  -0.59069 158 GLU D O   
7134 C CB  . GLU D 177 ? 3.04528 2.45760 2.75103 0.20540  0.05202  -0.59440 158 GLU D CB  
7135 C CG  . GLU D 177 ? 3.05990 2.43414 2.76076 0.22642  0.01335  -0.59149 158 GLU D CG  
7136 C CD  . GLU D 177 ? 3.07357 2.46304 2.75012 0.25736  -0.00243 -0.61728 158 GLU D CD  
7137 O OE1 . GLU D 177 ? 3.07573 2.49401 2.73016 0.26550  0.00762  -0.63539 158 GLU D OE1 
7138 O OE2 . GLU D 177 ? 3.09341 2.46644 2.77180 0.27493  -0.02440 -0.61852 158 GLU D OE2 
7139 N N   . PRO D 178 ? 2.99174 2.46951 2.76028 0.19184  0.06778  -0.59383 159 PRO D N   
7140 C CA  . PRO D 178 ? 3.01097 2.47634 2.76382 0.22191  0.03766  -0.59837 159 PRO D CA  
7141 C C   . PRO D 178 ? 3.01288 2.53775 2.76750 0.23994  0.04275  -0.61845 159 PRO D C   
7142 O O   . PRO D 178 ? 3.00725 2.59293 2.77619 0.22688  0.07061  -0.63402 159 PRO D O   
7143 C CB  . PRO D 178 ? 3.03968 2.45831 2.80813 0.21725  0.01634  -0.57006 159 PRO D CB  
7144 C CG  . PRO D 178 ? 3.02777 2.46998 2.82779 0.18959  0.04057  -0.55803 159 PRO D CG  
7145 C CD  . PRO D 178 ? 2.99487 2.47592 2.79518 0.17505  0.07405  -0.57715 159 PRO D CD  
7146 N N   . VAL D 179 ? 2.99327 2.49951 2.73305 0.27054  0.01548  -0.61868 160 VAL D N   
7147 C CA  . VAL D 179 ? 3.05520 2.61391 2.79195 0.29683  0.01498  -0.63425 160 VAL D CA  
7148 C C   . VAL D 179 ? 3.15689 2.66881 2.89086 0.31789  -0.01367 -0.61230 160 VAL D C   
7149 O O   . VAL D 179 ? 3.19574 2.63701 2.91275 0.32869  -0.04011 -0.60322 160 VAL D O   
7150 C CB  . VAL D 179 ? 3.07878 2.67220 2.78713 0.32366  0.01412  -0.66624 160 VAL D CB  
7151 C CG1 . VAL D 179 ? 3.12137 2.74217 2.81727 0.36467  -0.00082 -0.67657 160 VAL D CG1 
7152 C CG2 . VAL D 179 ? 3.03276 2.69864 2.74959 0.30141  0.04926  -0.68897 160 VAL D CG2 
7153 N N   . THR D 180 ? 3.02470 2.57652 2.77528 0.32274  -0.00785 -0.60386 161 THR D N   
7154 C CA  . THR D 180 ? 3.11810 2.63014 2.86582 0.34197  -0.03101 -0.57801 161 THR D CA  
7155 C C   . THR D 180 ? 3.16674 2.69072 2.88618 0.38918  -0.04540 -0.59302 161 THR D C   
7156 O O   . THR D 180 ? 3.13247 2.73642 2.84830 0.40567  -0.03024 -0.61975 161 THR D O   
7157 C CB  . THR D 180 ? 3.13076 2.68524 2.90839 0.32691  -0.01748 -0.55826 161 THR D CB  
7158 O OG1 . THR D 180 ? 3.11622 2.65576 2.91882 0.28718  -0.00616 -0.54470 161 THR D OG1 
7159 C CG2 . THR D 180 ? 3.21440 2.73043 2.98696 0.34670  -0.03927 -0.52664 161 THR D CG2 
7160 N N   . VAL D 181 ? 3.13867 2.58285 2.83818 0.41105  -0.07473 -0.57713 162 VAL D N   
7161 C CA  . VAL D 181 ? 3.20889 2.64557 2.87767 0.46120  -0.09226 -0.58817 162 VAL D CA  
7162 C C   . VAL D 181 ? 3.32454 2.69772 2.98988 0.47510  -0.11204 -0.55111 162 VAL D C   
7163 O O   . VAL D 181 ? 3.36675 2.66217 3.04067 0.45023  -0.12533 -0.52492 162 VAL D O   
7164 C CB  . VAL D 181 ? 3.19564 2.58591 2.83475 0.48049  -0.11023 -0.61388 162 VAL D CB  
7165 C CG1 . VAL D 181 ? 3.27285 2.64648 2.87883 0.53693  -0.13072 -0.62494 162 VAL D CG1 
7166 C CG2 . VAL D 181 ? 3.09784 2.55694 2.73783 0.46749  -0.08844 -0.64711 162 VAL D CG2 
7167 N N   . THR D 182 ? 3.24505 2.65470 2.89756 0.51456  -0.11320 -0.54804 163 THR D N   
7168 C CA  . THR D 182 ? 3.37821 2.72792 3.02116 0.53470  -0.13060 -0.51027 163 THR D CA  
7169 C C   . THR D 182 ? 3.44434 2.79769 3.05067 0.59740  -0.14361 -0.52308 163 THR D C   
7170 O O   . THR D 182 ? 3.37575 2.80208 2.96986 0.62330  -0.13571 -0.56121 163 THR D O   
7171 C CB  . THR D 182 ? 3.39340 2.79664 3.06420 0.51574  -0.11389 -0.47882 163 THR D CB  
7172 O OG1 . THR D 182 ? 3.28839 2.81383 2.97423 0.51552  -0.08771 -0.50587 163 THR D OG1 
7173 C CG2 . THR D 182 ? 3.37916 2.74151 3.08006 0.46154  -0.11138 -0.45310 163 THR D CG2 
7174 N N   . TRP D 183 ? 3.43495 2.70882 3.02307 0.62236  -0.16323 -0.49004 164 TRP D N   
7175 C CA  . TRP D 183 ? 3.51025 2.77065 3.05978 0.68757  -0.17807 -0.49553 164 TRP D CA  
7176 C C   . TRP D 183 ? 3.59973 2.88210 3.14728 0.70975  -0.17384 -0.45459 164 TRP D C   
7177 O O   . TRP D 183 ? 3.68494 2.89777 3.24157 0.68711  -0.17945 -0.40921 164 TRP D O   
7178 C CB  . TRP D 183 ? 3.59298 2.71920 3.11401 0.70556  -0.20834 -0.49572 164 TRP D CB  
7179 C CG  . TRP D 183 ? 3.51662 2.64237 3.02582 0.71019  -0.21527 -0.54463 164 TRP D CG  
7180 C CD1 . TRP D 183 ? 3.46596 2.54577 2.98800 0.66840  -0.22042 -0.55696 164 TRP D CD1 
7181 C CD2 . TRP D 183 ? 3.48082 2.66398 2.96217 0.76127  -0.21740 -0.58765 164 TRP D CD2 
7182 N NE1 . TRP D 183 ? 3.40829 2.51179 2.91115 0.69028  -0.22527 -0.60336 164 TRP D NE1 
7183 C CE2 . TRP D 183 ? 3.41443 2.58209 2.89292 0.74613  -0.22328 -0.62337 164 TRP D CE2 
7184 C CE3 . TRP D 183 ? 3.49391 2.74750 2.95203 0.82009  -0.21494 -0.59976 164 TRP D CE3 
7185 C CZ2 . TRP D 183 ? 3.36497 2.58469 2.81873 0.78593  -0.22619 -0.66975 164 TRP D CZ2 
7186 C CZ3 . TRP D 183 ? 3.43635 2.74289 2.87096 0.85979  -0.21835 -0.64766 164 TRP D CZ3 
7187 C CH2 . TRP D 183 ? 3.37393 2.66336 2.80685 0.84158  -0.22356 -0.68181 164 TRP D CH2 
7188 N N   . ASN D 184 ? 3.43589 2.82136 2.97144 0.75404  -0.16357 -0.47069 165 ASN D N   
7189 C CA  . ASN D 184 ? 3.52085 2.94895 3.05075 0.78410  -0.15836 -0.43543 165 ASN D CA  
7190 C C   . ASN D 184 ? 3.51439 2.98210 3.08390 0.73254  -0.14003 -0.40374 165 ASN D C   
7191 O O   . ASN D 184 ? 3.62956 3.06158 3.19742 0.73494  -0.14332 -0.35436 165 ASN D O   
7192 C CB  . ASN D 184 ? 3.68224 2.99171 3.17428 0.82787  -0.18276 -0.39765 165 ASN D CB  
7193 C CG  . ASN D 184 ? 3.69865 2.97612 3.14858 0.88912  -0.20140 -0.43069 165 ASN D CG  
7194 O OD1 . ASN D 184 ? 3.60030 2.90704 3.05051 0.88596  -0.20145 -0.47946 165 ASN D OD1 
7195 N ND2 . ASN D 184 ? 3.82717 3.04501 3.23911 0.94732  -0.21695 -0.40330 165 ASN D ND2 
7196 N N   . SER D 185 ? 3.44734 2.98901 3.05173 0.68642  -0.12003 -0.43196 166 SER D N   
7197 C CA  . SER D 185 ? 3.41727 3.00870 3.06120 0.63876  -0.10118 -0.41134 166 SER D CA  
7198 C C   . SER D 185 ? 3.52084 3.00325 3.17436 0.60309  -0.11277 -0.36370 166 SER D C   
7199 O O   . SER D 185 ? 3.57401 3.07964 3.24644 0.58518  -0.10463 -0.32718 166 SER D O   
7200 C CB  . SER D 185 ? 3.42278 3.12795 3.07075 0.66627  -0.08686 -0.40103 166 SER D CB  
7201 O OG  . SER D 185 ? 3.30281 3.12221 2.94775 0.69251  -0.07440 -0.44965 166 SER D OG  
7202 N N   . GLY D 186 ? 3.46637 2.83547 3.10754 0.59226  -0.13194 -0.36589 167 GLY D N   
7203 C CA  . GLY D 186 ? 3.53833 2.80666 3.19100 0.55365  -0.14349 -0.32702 167 GLY D CA  
7204 C C   . GLY D 186 ? 3.69536 2.87460 3.32362 0.57865  -0.16072 -0.28012 167 GLY D C   
7205 O O   . GLY D 186 ? 3.75602 2.87267 3.39894 0.54280  -0.16541 -0.24019 167 GLY D O   
7206 N N   . SER D 187 ? 3.62403 2.79535 3.21475 0.63956  -0.16976 -0.28269 168 SER D N   
7207 C CA  . SER D 187 ? 3.76725 2.84050 3.33019 0.66686  -0.18576 -0.23538 168 SER D CA  
7208 C C   . SER D 187 ? 3.80417 2.72978 3.34764 0.66410  -0.21156 -0.24090 168 SER D C   
7209 O O   . SER D 187 ? 3.90769 2.72568 3.44601 0.64992  -0.22354 -0.19845 168 SER D O   
7210 C CB  . SER D 187 ? 3.81889 2.94389 3.34684 0.73910  -0.18499 -0.23283 168 SER D CB  
7211 O OG  . SER D 187 ? 3.81733 2.90037 3.31038 0.78642  -0.20155 -0.27017 168 SER D OG  
7212 N N   . LEU D 188 ? 3.75213 2.67315 3.28527 0.67604  -0.21989 -0.29361 169 LEU D N   
7213 C CA  . LEU D 188 ? 3.77965 2.57212 3.29412 0.67704  -0.24524 -0.30895 169 LEU D CA  
7214 C C   . LEU D 188 ? 3.69666 2.46570 3.24436 0.61133  -0.24601 -0.32221 169 LEU D C   
7215 O O   . LEU D 188 ? 3.57635 2.43240 3.14486 0.58971  -0.23157 -0.35393 169 LEU D O   
7216 C CB  . LEU D 188 ? 3.75311 2.55898 3.23399 0.73346  -0.25551 -0.35996 169 LEU D CB  
7217 C CG  . LEU D 188 ? 3.84615 2.65427 3.28605 0.80881  -0.26137 -0.35076 169 LEU D CG  
7218 C CD1 . LEU D 188 ? 3.81057 2.63905 3.22003 0.86158  -0.27225 -0.40660 169 LEU D CD1 
7219 C CD2 . LEU D 188 ? 3.98446 2.65007 3.40207 0.82152  -0.27913 -0.30226 169 LEU D CD2 
7220 N N   . SER D 189 ? 3.81219 2.46418 3.36433 0.57992  -0.26238 -0.29760 170 SER D N   
7221 C CA  . SER D 189 ? 3.74662 2.37107 3.32809 0.52064  -0.26663 -0.30975 170 SER D CA  
7222 C C   . SER D 189 ? 3.80059 2.28661 3.36948 0.51158  -0.29446 -0.31665 170 SER D C   
7223 O O   . SER D 189 ? 3.73318 2.20538 3.31597 0.48007  -0.30236 -0.34675 170 SER D O   
7224 C CB  . SER D 189 ? 3.74814 2.40935 3.36887 0.46579  -0.25077 -0.26790 170 SER D CB  
7225 O OG  . SER D 189 ? 3.85775 2.45434 3.47323 0.46465  -0.25486 -0.21442 170 SER D OG  
7226 N N   . SER D 190 ? 3.90982 2.29282 3.45251 0.53848  -0.30944 -0.29107 171 SER D N   
7227 C CA  . SER D 190 ? 3.96037 2.20447 3.49205 0.52840  -0.33612 -0.30095 171 SER D CA  
7228 C C   . SER D 190 ? 3.92791 2.15900 3.43387 0.56683  -0.35267 -0.36334 171 SER D C   
7229 O O   . SER D 190 ? 3.94772 2.20819 3.42147 0.62888  -0.35306 -0.38265 171 SER D O   
7230 C CB  . SER D 190 ? 4.09486 2.22705 3.60133 0.55218  -0.34586 -0.25663 171 SER D CB  
7231 O OG  . SER D 190 ? 4.13883 2.28830 3.60514 0.62707  -0.34572 -0.26176 171 SER D OG  
7232 N N   . GLY D 191 ? 3.98843 2.18332 3.50850 0.53127  -0.36649 -0.39566 172 GLY D N   
7233 C CA  . GLY D 191 ? 3.96031 2.14200 3.45728 0.56362  -0.38367 -0.45533 172 GLY D CA  
7234 C C   . GLY D 191 ? 3.87033 2.18245 3.35994 0.59474  -0.36751 -0.48919 172 GLY D C   
7235 O O   . GLY D 191 ? 3.88683 2.20539 3.34302 0.65186  -0.37594 -0.52357 172 GLY D O   
7236 N N   . VAL D 192 ? 3.69217 2.10910 3.21293 0.55743  -0.34377 -0.48052 173 VAL D N   
7237 C CA  . VAL D 192 ? 3.57063 2.11279 3.09007 0.57553  -0.32447 -0.50997 173 VAL D CA  
7238 C C   . VAL D 192 ? 3.47505 2.05619 3.01771 0.53138  -0.32001 -0.53350 173 VAL D C   
7239 O O   . VAL D 192 ? 3.45759 2.03103 3.03162 0.47870  -0.31531 -0.50900 173 VAL D O   
7240 C CB  . VAL D 192 ? 3.55096 2.18969 3.08436 0.57649  -0.29671 -0.47882 173 VAL D CB  
7241 C CG1 . VAL D 192 ? 3.44449 2.20768 2.97568 0.59526  -0.27691 -0.51383 173 VAL D CG1 
7242 C CG2 . VAL D 192 ? 3.67128 2.26915 3.18153 0.61897  -0.30150 -0.44750 173 VAL D CG2 
7243 N N   . HIS D 193 ? 3.49456 2.12166 3.02058 0.55481  -0.32108 -0.57963 174 HIS D N   
7244 C CA  . HIS D 193 ? 3.39533 2.06270 2.93627 0.52153  -0.31648 -0.60287 174 HIS D CA  
7245 C C   . HIS D 193 ? 3.28383 2.07391 2.82659 0.52892  -0.28873 -0.61891 174 HIS D C   
7246 O O   . HIS D 193 ? 3.29055 2.12770 2.81112 0.57319  -0.28349 -0.63783 174 HIS D O   
7247 C CB  . HIS D 193 ? 3.41355 2.02153 2.93244 0.53816  -0.34373 -0.64513 174 HIS D CB  
7248 C CG  . HIS D 193 ? 3.52107 2.00271 3.03872 0.52852  -0.37181 -0.63657 174 HIS D CG  
7249 N ND1 . HIS D 193 ? 3.51915 1.95501 3.05551 0.48528  -0.38582 -0.64158 174 HIS D ND1 
7250 C CD2 . HIS D 193 ? 3.64173 2.03205 3.14163 0.55568  -0.38786 -0.62354 174 HIS D CD2 
7251 C CE1 . HIS D 193 ? 3.64675 1.96877 3.17961 0.48185  -0.40894 -0.63416 174 HIS D CE1 
7252 N NE2 . HIS D 193 ? 3.72569 2.01253 3.23547 0.52437  -0.41022 -0.62138 174 HIS D NE2 
7253 N N   . THR D 194 ? 3.37650 2.21820 2.94584 0.48529  -0.27060 -0.61159 175 THR D N   
7254 C CA  . THR D 194 ? 3.27124 2.21957 2.84514 0.48286  -0.24250 -0.62634 175 THR D CA  
7255 C C   . THR D 194 ? 3.20154 2.15967 2.77685 0.46052  -0.24304 -0.64668 175 THR D C   
7256 O O   . THR D 194 ? 3.18347 2.11966 2.78100 0.42052  -0.24345 -0.62836 175 THR D O   
7257 C CB  . THR D 194 ? 3.23780 2.24403 2.84219 0.45396  -0.21521 -0.59417 175 THR D CB  
7258 O OG1 . THR D 194 ? 3.31016 2.32365 2.90909 0.48162  -0.21355 -0.57817 175 THR D OG1 
7259 C CG2 . THR D 194 ? 3.13426 2.23876 2.74633 0.44319  -0.18560 -0.61107 175 THR D CG2 
7260 N N   . PHE D 195 ? 3.22428 2.22161 2.77498 0.48823  -0.24272 -0.68369 176 PHE D N   
7261 C CA  . PHE D 195 ? 3.17701 2.17960 2.72077 0.47697  -0.24750 -0.70526 176 PHE D CA  
7262 C C   . PHE D 195 ? 3.08223 2.16045 2.64299 0.44489  -0.21553 -0.69568 176 PHE D C   
7263 O O   . PHE D 195 ? 3.01918 2.16475 2.58705 0.44444  -0.18878 -0.69136 176 PHE D O   
7264 C CB  . PHE D 195 ? 3.18687 2.20279 2.69515 0.52238  -0.26087 -0.74856 176 PHE D CB  
7265 C CG  . PHE D 195 ? 3.28181 2.21205 2.77033 0.55692  -0.29432 -0.76248 176 PHE D CG  
7266 C CD1 . PHE D 195 ? 3.33985 2.25999 2.81683 0.59258  -0.29697 -0.75863 176 PHE D CD1 
7267 C CD2 . PHE D 195 ? 3.32075 2.17925 2.80190 0.55453  -0.32313 -0.77996 176 PHE D CD2 
7268 C CE1 . PHE D 195 ? 3.45422 2.28476 2.91056 0.62654  -0.32708 -0.76917 176 PHE D CE1 
7269 C CE2 . PHE D 195 ? 3.42032 2.19003 2.88384 0.58448  -0.35350 -0.79454 176 PHE D CE2 
7270 C CZ  . PHE D 195 ? 3.49648 2.24737 2.94655 0.62117  -0.35514 -0.78770 176 PHE D CZ  
7271 N N   . PRO D 196 ? 3.10275 2.17035 2.66989 0.41853  -0.21779 -0.69301 177 PRO D N   
7272 C CA  . PRO D 196 ? 2.97996 2.10278 2.56370 0.38694  -0.18789 -0.67716 177 PRO D CA  
7273 C C   . PRO D 196 ? 2.92214 2.12268 2.48912 0.40014  -0.16338 -0.69777 177 PRO D C   
7274 O O   . PRO D 196 ? 2.97175 2.19171 2.51249 0.43427  -0.17141 -0.72779 177 PRO D O   
7275 C CB  . PRO D 196 ? 2.97897 2.06845 2.56528 0.36690  -0.20235 -0.67410 177 PRO D CB  
7276 C CG  . PRO D 196 ? 3.08996 2.10048 2.67591 0.37297  -0.23737 -0.67801 177 PRO D CG  
7277 C CD  . PRO D 196 ? 3.14259 2.14205 2.70519 0.41418  -0.24853 -0.70139 177 PRO D CD  
7278 N N   . ALA D 197 ? 3.06668 2.31192 2.64968 0.37143  -0.13240 -0.68127 178 ALA D N   
7279 C CA  . ALA D 197 ? 3.01924 2.33825 2.59192 0.37297  -0.10302 -0.69510 178 ALA D CA  
7280 C C   . ALA D 197 ? 3.01569 2.34389 2.56920 0.37001  -0.10100 -0.70178 178 ALA D C   
7281 O O   . ALA D 197 ? 3.01006 2.30444 2.57054 0.35128  -0.10693 -0.68400 178 ALA D O   
7282 C CB  . ALA D 197 ? 2.94275 2.30005 2.54301 0.34220  -0.06871 -0.67493 178 ALA D CB  
7283 N N   . VAL D 198 ? 3.05447 2.43546 2.58304 0.39016  -0.09236 -0.72709 179 VAL D N   
7284 C CA  . VAL D 198 ? 3.06012 2.46303 2.56615 0.39121  -0.08750 -0.73328 179 VAL D CA  
7285 C C   . VAL D 198 ? 3.05684 2.53027 2.56124 0.37493  -0.04628 -0.73021 179 VAL D C   
7286 O O   . VAL D 198 ? 3.04511 2.56335 2.55794 0.37489  -0.02845 -0.73964 179 VAL D O   
7287 C CB  . VAL D 198 ? 3.08437 2.48764 2.55864 0.43114  -0.11685 -0.76826 179 VAL D CB  
7288 C CG1 . VAL D 198 ? 3.11386 2.43791 2.59099 0.44019  -0.15660 -0.77136 179 VAL D CG1 
7289 C CG2 . VAL D 198 ? 3.08357 2.53179 2.54673 0.46074  -0.11503 -0.79567 179 VAL D CG2 
7290 N N   . LEU D 199 ? 3.06151 2.54588 2.55458 0.36081  -0.03075 -0.71682 180 LEU D N   
7291 C CA  . LEU D 199 ? 3.07834 2.61241 2.57234 0.33623  0.01170  -0.70498 180 LEU D CA  
7292 C C   . LEU D 199 ? 3.08442 2.68770 2.54887 0.35531  0.02127  -0.73004 180 LEU D C   
7293 O O   . LEU D 199 ? 3.12201 2.73099 2.55830 0.37623  0.00590  -0.73899 180 LEU D O   
7294 C CB  . LEU D 199 ? 3.10223 2.60566 2.59735 0.31287  0.02486  -0.67180 180 LEU D CB  
7295 C CG  . LEU D 199 ? 3.07410 2.60256 2.57432 0.28133  0.07024  -0.65055 180 LEU D CG  
7296 C CD1 . LEU D 199 ? 3.05801 2.53363 2.57673 0.25817  0.07772  -0.61632 180 LEU D CD1 
7297 C CD2 . LEU D 199 ? 3.12477 2.69535 2.59083 0.28830  0.08589  -0.65130 180 LEU D CD2 
7298 N N   . GLN D 200 ? 3.14824 2.81159 2.61999 0.34765  0.04697  -0.74274 181 GLN D N   
7299 C CA  . GLN D 200 ? 3.14217 2.88502 2.59022 0.36725  0.05534  -0.77160 181 GLN D CA  
7300 C C   . GLN D 200 ? 3.15589 2.95117 2.60300 0.33308  0.10142  -0.75781 181 GLN D C   
7301 O O   . GLN D 200 ? 3.16372 3.01021 2.62792 0.31343  0.12884  -0.76636 181 GLN D O   
7302 C CB  . GLN D 200 ? 3.09059 2.87128 2.54826 0.38725  0.04782  -0.80043 181 GLN D CB  
7303 C CG  . GLN D 200 ? 3.10820 2.87636 2.54602 0.43737  0.00644  -0.82993 181 GLN D CG  
7304 C CD  . GLN D 200 ? 3.05724 2.88889 2.49694 0.46066  0.00804  -0.85927 181 GLN D CD  
7305 O OE1 . GLN D 200 ? 3.00232 2.88061 2.46448 0.43651  0.03655  -0.85658 181 GLN D OE1 
7306 N NE2 . GLN D 200 ? 3.07739 2.90880 2.49452 0.50934  -0.02408 -0.88869 181 GLN D NE2 
7307 N N   . SER D 201 ? 3.09493 2.88008 2.52091 0.32665  0.10999  -0.73729 182 SER D N   
7308 C CA  . SER D 201 ? 3.12459 2.95166 2.54281 0.29610  0.15385  -0.71961 182 SER D CA  
7309 C C   . SER D 201 ? 3.09843 2.92485 2.55103 0.25257  0.18965  -0.70796 182 SER D C   
7310 O O   . SER D 201 ? 3.05866 2.95310 2.51881 0.23572  0.21704  -0.72431 182 SER D O   
7311 C CB  . SER D 201 ? 3.12456 3.04426 2.51640 0.31394  0.16179  -0.74663 182 SER D CB  
7312 O OG  . SER D 201 ? 3.16050 3.08247 2.51735 0.34754  0.13738  -0.75084 182 SER D OG  
7313 N N   . ASP D 202 ? 3.19159 2.94430 2.66659 0.23526  0.18748  -0.68283 183 ASP D N   
7314 C CA  . ASP D 202 ? 3.17105 2.90859 2.68112 0.19573  0.21698  -0.67138 183 ASP D CA  
7315 C C   . ASP D 202 ? 3.09896 2.86094 2.63747 0.20060  0.20584  -0.69830 183 ASP D C   
7316 O O   . ASP D 202 ? 3.05940 2.83533 2.62744 0.17022  0.23126  -0.70035 183 ASP D O   
7317 C CB  . ASP D 202 ? 3.20047 2.97777 2.70902 0.15837  0.26590  -0.66336 183 ASP D CB  
7318 C CG  . ASP D 202 ? 3.20896 2.95527 2.75221 0.11562  0.29695  -0.64995 183 ASP D CG  
7319 O OD1 . ASP D 202 ? 3.23335 2.90616 2.78521 0.10992  0.29253  -0.62300 183 ASP D OD1 
7320 O OD2 . ASP D 202 ? 3.18908 2.98918 2.75206 0.08849  0.32509  -0.66955 183 ASP D OD2 
7321 N N   . LEU D 203 ? 3.11184 2.87919 2.64127 0.23995  0.16805  -0.71976 184 LEU D N   
7322 C CA  . LEU D 203 ? 3.06138 2.83797 2.61391 0.25138  0.15258  -0.73788 184 LEU D CA  
7323 C C   . LEU D 203 ? 3.08845 2.80298 2.63342 0.28523  0.10711  -0.73543 184 LEU D C   
7324 O O   . LEU D 203 ? 3.12989 2.80649 2.65279 0.29976  0.08772  -0.72708 184 LEU D O   
7325 C CB  . LEU D 203 ? 3.01022 2.87999 2.55923 0.26578  0.15993  -0.77462 184 LEU D CB  
7326 C CG  . LEU D 203 ? 2.95508 2.89165 2.53058 0.22870  0.20055  -0.78541 184 LEU D CG  
7327 C CD1 . LEU D 203 ? 2.91675 2.88990 2.48242 0.19579  0.23924  -0.77958 184 LEU D CD1 
7328 C CD2 . LEU D 203 ? 2.95496 2.97420 2.53560 0.25247  0.19440  -0.82238 184 LEU D CD2 
7329 N N   . TYR D 204 ? 3.10688 2.81128 2.67123 0.29590  0.09097  -0.74194 185 TYR D N   
7330 C CA  . TYR D 204 ? 3.13475 2.77491 2.69574 0.32269  0.05027  -0.73757 185 TYR D CA  
7331 C C   . TYR D 204 ? 3.12518 2.79345 2.67807 0.36125  0.02911  -0.76532 185 TYR D C   
7332 O O   . TYR D 204 ? 3.08485 2.82620 2.64239 0.36467  0.04663  -0.78543 185 TYR D O   
7333 C CB  . TYR D 204 ? 3.13420 2.71844 2.72546 0.29954  0.04851  -0.70915 185 TYR D CB  
7334 C CG  . TYR D 204 ? 3.11166 2.65552 2.70773 0.27079  0.06146  -0.68055 185 TYR D CG  
7335 C CD1 . TYR D 204 ? 3.10601 2.59247 2.68981 0.27950  0.03574  -0.66677 185 TYR D CD1 
7336 C CD2 . TYR D 204 ? 3.09931 2.66274 2.71208 0.23612  0.09925  -0.66875 185 TYR D CD2 
7337 C CE1 . TYR D 204 ? 3.08426 2.54036 2.67049 0.25821  0.04710  -0.64036 185 TYR D CE1 
7338 C CE2 . TYR D 204 ? 3.08173 2.60438 2.69578 0.21511  0.11119  -0.64127 185 TYR D CE2 
7339 C CZ  . TYR D 204 ? 3.07304 2.54520 2.67295 0.22819  0.08487  -0.62632 185 TYR D CZ  
7340 O OH  . TYR D 204 ? 3.08834 2.52630 2.68768 0.21210  0.09625  -0.59879 185 TYR D OH  
7341 N N   . THR D 205 ? 3.07418 2.68287 2.61517 0.39074  -0.00894 -0.76666 186 THR D N   
7342 C CA  . THR D 205 ? 3.07749 2.69574 2.60427 0.43445  -0.03315 -0.79120 186 THR D CA  
7343 C C   . THR D 205 ? 3.10620 2.63118 2.63053 0.45122  -0.07116 -0.78025 186 THR D C   
7344 O O   . THR D 205 ? 3.12012 2.59130 2.63762 0.44430  -0.08661 -0.77185 186 THR D O   
7345 C CB  . THR D 205 ? 3.09207 2.76469 2.58621 0.46612  -0.03702 -0.82493 186 THR D CB  
7346 O OG1 . THR D 205 ? 3.07128 2.83856 2.57016 0.44885  -0.00036 -0.83616 186 THR D OG1 
7347 C CG2 . THR D 205 ? 3.10743 2.77457 2.58269 0.51851  -0.06747 -0.85066 186 THR D CG2 
7348 N N   . LEU D 206 ? 3.09205 2.60047 2.62218 0.47215  -0.08516 -0.77971 187 LEU D N   
7349 C CA  . LEU D 206 ? 3.13420 2.55134 2.66153 0.48764  -0.11991 -0.76877 187 LEU D CA  
7350 C C   . LEU D 206 ? 3.18125 2.60112 2.69447 0.53314  -0.13623 -0.78389 187 LEU D C   
7351 O O   . LEU D 206 ? 3.15831 2.65814 2.66451 0.55360  -0.12159 -0.80441 187 LEU D O   
7352 C CB  . LEU D 206 ? 3.08839 2.45760 2.64731 0.44955  -0.11618 -0.73063 187 LEU D CB  
7353 C CG  . LEU D 206 ? 3.09934 2.50781 2.68545 0.43376  -0.09393 -0.71308 187 LEU D CG  
7354 C CD1 . LEU D 206 ? 3.15732 2.53271 2.74257 0.46089  -0.11377 -0.70424 187 LEU D CD1 
7355 C CD2 . LEU D 206 ? 3.03849 2.43102 2.65452 0.38754  -0.07789 -0.68291 187 LEU D CD2 
7356 N N   . SER D 207 ? 3.05152 2.38350 2.56029 0.54906  -0.16640 -0.77308 188 SER D N   
7357 C CA  . SER D 207 ? 3.11045 2.42611 2.60265 0.59557  -0.18419 -0.78139 188 SER D CA  
7358 C C   . SER D 207 ? 3.18883 2.40603 2.69179 0.58857  -0.20449 -0.74908 188 SER D C   
7359 O O   . SER D 207 ? 3.18696 2.35408 2.70977 0.54878  -0.20693 -0.72555 188 SER D O   
7360 C CB  . SER D 207 ? 3.13592 2.44556 2.59121 0.64447  -0.20688 -0.82083 188 SER D CB  
7361 O OG  . SER D 207 ? 3.17181 2.40223 2.61860 0.63812  -0.23147 -0.82610 188 SER D OG  
7362 N N   . SER D 208 ? 3.09612 2.28821 2.58476 0.62874  -0.21864 -0.74705 189 SER D N   
7363 C CA  . SER D 208 ? 3.18710 2.28505 2.68276 0.62474  -0.23642 -0.71335 189 SER D CA  
7364 C C   . SER D 208 ? 3.32009 2.35885 2.78243 0.68238  -0.26343 -0.72606 189 SER D C   
7365 O O   . SER D 208 ? 3.31572 2.41116 2.75415 0.72924  -0.26252 -0.75474 189 SER D O   
7366 C CB  . SER D 208 ? 3.18643 2.32335 2.70928 0.60300  -0.21471 -0.67736 189 SER D CB  
7367 O OG  . SER D 208 ? 3.29925 2.34944 2.82596 0.60169  -0.23108 -0.64219 189 SER D OG  
7368 N N   . SER D 209 ? 3.28380 2.20782 2.74487 0.67843  -0.28700 -0.70441 190 SER D N   
7369 C CA  . SER D 209 ? 3.39487 2.23712 2.82395 0.73048  -0.31421 -0.71221 190 SER D CA  
7370 C C   . SER D 209 ? 3.49456 2.25437 2.93266 0.72071  -0.32050 -0.66409 190 SER D C   
7371 O O   . SER D 209 ? 3.49637 2.20873 2.96146 0.66896  -0.32043 -0.63540 190 SER D O   
7372 C CB  . SER D 209 ? 3.41850 2.18252 2.82953 0.73904  -0.34270 -0.74593 190 SER D CB  
7373 O OG  . SER D 209 ? 3.54185 2.19060 2.93024 0.77319  -0.37044 -0.74277 190 SER D OG  
7374 N N   . VAL D 210 ? 3.49479 2.24152 2.90919 0.77172  -0.32557 -0.65425 191 VAL D N   
7375 C CA  . VAL D 210 ? 3.55290 2.21874 2.96861 0.77117  -0.33156 -0.60571 191 VAL D CA  
7376 C C   . VAL D 210 ? 3.68014 2.24368 3.05492 0.83089  -0.35923 -0.61505 191 VAL D C   
7377 O O   . VAL D 210 ? 3.70337 2.30962 3.04736 0.89135  -0.36346 -0.64718 191 VAL D O   
7378 C CB  . VAL D 210 ? 3.49521 2.25384 2.92301 0.77540  -0.30587 -0.57372 191 VAL D CB  
7379 C CG1 . VAL D 210 ? 3.46471 2.33830 2.87302 0.82667  -0.29477 -0.60800 191 VAL D CG1 
7380 C CG2 . VAL D 210 ? 3.57426 2.25198 2.99188 0.79200  -0.31384 -0.52456 191 VAL D CG2 
7381 N N   . THR D 211 ? 3.70392 2.13271 3.07851 0.81382  -0.37771 -0.58810 192 THR D N   
7382 C CA  . THR D 211 ? 3.83251 2.13967 3.16924 0.86527  -0.40468 -0.59368 192 THR D CA  
7383 C C   . THR D 211 ? 3.94330 2.20537 3.26900 0.88682  -0.40034 -0.53791 192 THR D C   
7384 O O   . THR D 211 ? 3.96816 2.21912 3.32177 0.83778  -0.38790 -0.48900 192 THR D O   
7385 C CB  . THR D 211 ? 3.88985 2.06691 3.23227 0.83096  -0.42947 -0.60597 192 THR D CB  
7386 O OG1 . THR D 211 ? 3.76695 2.00352 3.12878 0.79587  -0.42805 -0.64559 192 THR D OG1 
7387 C CG2 . THR D 211 ? 3.99645 2.06088 3.29627 0.89161  -0.45889 -0.63394 192 THR D CG2 
7388 N N   . VAL D 212 ? 4.00856 2.24928 3.29220 0.96257  -0.41041 -0.54466 193 VAL D N   
7389 C CA  . VAL D 212 ? 4.12327 2.33250 3.38856 0.99656  -0.40566 -0.49195 193 VAL D CA  
7390 C C   . VAL D 212 ? 4.25433 2.32498 3.47254 1.06034  -0.43281 -0.49681 193 VAL D C   
7391 O O   . VAL D 212 ? 4.25541 2.29206 3.45180 1.09334  -0.45302 -0.55034 193 VAL D O   
7392 C CB  . VAL D 212 ? 4.05713 2.42499 3.31765 1.03551  -0.38284 -0.49017 193 VAL D CB  
7393 C CG1 . VAL D 212 ? 3.93833 2.43238 3.24610 0.97125  -0.35482 -0.48247 193 VAL D CG1 
7394 C CG2 . VAL D 212 ? 4.01641 2.45220 3.24617 1.10144  -0.39070 -0.54970 193 VAL D CG2 
7395 N N   . PRO D 213 ? 4.33324 2.31927 3.53368 1.08007  -0.43363 -0.44057 194 PRO D N   
7396 C CA  . PRO D 213 ? 4.45879 2.30900 3.60958 1.14896  -0.45771 -0.44121 194 PRO D CA  
7397 C C   . PRO D 213 ? 4.46411 2.40206 3.57500 1.24083  -0.46101 -0.47932 194 PRO D C   
7398 O O   . PRO D 213 ? 4.40815 2.49825 3.52315 1.26078  -0.44034 -0.47519 194 PRO D O   
7399 C CB  . PRO D 213 ? 4.55839 2.32793 3.70220 1.14505  -0.45004 -0.36249 194 PRO D CB  
7400 C CG  . PRO D 213 ? 4.49361 2.31228 3.69043 1.05401  -0.42970 -0.32796 194 PRO D CG  
7401 C CD  . PRO D 213 ? 4.35389 2.34535 3.57978 1.03365  -0.41412 -0.37199 194 PRO D CD  
7402 N N   . SER D 214 ? 4.42221 2.26533 3.49488 1.29734  -0.48779 -0.51946 195 SER D N   
7403 C CA  . SER D 214 ? 4.42546 2.35853 3.46164 1.38377  -0.49377 -0.56742 195 SER D CA  
7404 C C   . SER D 214 ? 4.46161 2.44303 3.46545 1.45459  -0.48407 -0.52848 195 SER D C   
7405 O O   . SER D 214 ? 4.41907 2.53453 3.40438 1.51497  -0.47916 -0.56071 195 SER D O   
7406 C CB  . SER D 214 ? 4.55329 2.36271 3.55375 1.43214  -0.52648 -0.61746 195 SER D CB  
7407 O OG  . SER D 214 ? 4.56466 2.46235 3.52748 1.52099  -0.53328 -0.66351 195 SER D OG  
7408 N N   . SER D 215 ? 4.64312 2.52463 3.63969 1.44840  -0.48054 -0.45902 196 SER D N   
7409 C CA  . SER D 215 ? 4.70808 2.63559 3.67116 1.51869  -0.47139 -0.41739 196 SER D CA  
7410 C C   . SER D 215 ? 4.59236 2.72031 3.58716 1.49516  -0.44078 -0.40379 196 SER D C   
7411 O O   . SER D 215 ? 4.58116 2.81693 3.55135 1.56229  -0.43270 -0.39906 196 SER D O   
7412 C CB  . SER D 215 ? 4.84544 2.60283 3.78940 1.51792  -0.47548 -0.34290 196 SER D CB  
7413 O OG  . SER D 215 ? 4.80746 2.55662 3.79864 1.42300  -0.45803 -0.29580 196 SER D OG  
7414 N N   . THR D 216 ? 4.65837 2.84223 3.70749 1.40269  -0.42405 -0.40115 197 THR D N   
7415 C CA  . THR D 216 ? 4.54906 2.90698 3.63170 1.37280  -0.39454 -0.38569 197 THR D CA  
7416 C C   . THR D 216 ? 4.41564 2.95386 3.50608 1.39376  -0.38477 -0.44901 197 THR D C   
7417 O O   . THR D 216 ? 4.34532 3.03802 3.45344 1.39141  -0.36173 -0.44294 197 THR D O   
7418 C CB  . THR D 216 ? 4.50140 2.84813 3.63814 1.26873  -0.38037 -0.35943 197 THR D CB  
7419 O OG1 . THR D 216 ? 4.41549 2.74941 3.57631 1.22103  -0.38816 -0.41125 197 THR D OG1 
7420 C CG2 . THR D 216 ? 4.62897 2.80906 3.76089 1.24293  -0.38750 -0.29431 197 THR D CG2 
7421 N N   . TRP D 217 ? 4.64860 3.17453 3.72731 1.41228  -0.40099 -0.51024 198 TRP D N   
7422 C CA  . TRP D 217 ? 4.52109 3.21415 3.60373 1.43447  -0.39200 -0.57047 198 TRP D CA  
7423 C C   . TRP D 217 ? 4.56561 3.23467 3.59682 1.52743  -0.41551 -0.61287 198 TRP D C   
7424 O O   . TRP D 217 ? 4.65929 3.17206 3.66559 1.54604  -0.44127 -0.62014 198 TRP D O   
7425 C CB  . TRP D 217 ? 4.39888 3.13143 3.52335 1.35733  -0.38459 -0.60883 198 TRP D CB  
7426 C CG  . TRP D 217 ? 4.23287 3.16189 3.38155 1.34447  -0.36018 -0.64588 198 TRP D CG  
7427 C CD1 . TRP D 217 ? 4.13926 3.18315 3.32711 1.29451  -0.33141 -0.62645 198 TRP D CD1 
7428 C CD2 . TRP D 217 ? 4.12703 3.15995 3.26325 1.37990  -0.36164 -0.70977 198 TRP D CD2 
7429 N NE1 . TRP D 217 ? 3.98063 3.18663 3.18183 1.29415  -0.31434 -0.67419 198 TRP D NE1 
7430 C CE2 . TRP D 217 ? 3.96675 3.17244 3.13688 1.34509  -0.33174 -0.72421 198 TRP D CE2 
7431 C CE3 . TRP D 217 ? 4.15002 3.14899 3.24984 1.43773  -0.38500 -0.75721 198 TRP D CE3 
7432 C CZ2 . TRP D 217 ? 3.82627 3.17009 2.99586 1.36204  -0.32312 -0.78132 198 TRP D CZ2 
7433 C CZ3 . TRP D 217 ? 4.00932 3.15311 3.10774 1.45795  -0.37715 -0.81417 198 TRP D CZ3 
7434 C CH2 . TRP D 217 ? 3.84754 3.16146 2.98097 1.41831  -0.34576 -0.82432 198 TRP D CH2 
7435 N N   . PRO D 218 ? 4.50690 3.33118 3.52195 1.58745  -0.40776 -0.64486 199 PRO D N   
7436 C CA  . PRO D 218 ? 4.36486 3.38540 3.40944 1.56847  -0.37804 -0.64832 199 PRO D CA  
7437 C C   . PRO D 218 ? 4.41978 3.48112 3.45403 1.60154  -0.36670 -0.59491 199 PRO D C   
7438 O O   . PRO D 218 ? 4.31332 3.54840 3.35800 1.61673  -0.34748 -0.60852 199 PRO D O   
7439 C CB  . PRO D 218 ? 4.24945 3.40343 3.27523 1.62586  -0.38044 -0.71539 199 PRO D CB  
7440 C CG  . PRO D 218 ? 4.38048 3.41819 3.34901 1.71582  -0.41136 -0.72321 199 PRO D CG  
7441 C CD  . PRO D 218 ? 4.53319 3.35333 3.49932 1.68031  -0.42994 -0.69051 199 PRO D CD  
7442 N N   . SER D 219 ? 4.31127 3.21870 3.32565 1.61133  -0.37772 -0.53538 200 SER D N   
7443 C CA  . SER D 219 ? 4.37508 3.31782 3.37477 1.64772  -0.36740 -0.47981 200 SER D CA  
7444 C C   . SER D 219 ? 4.28302 3.34149 3.33396 1.57477  -0.33774 -0.45468 200 SER D C   
7445 O O   . SER D 219 ? 4.23755 3.42412 3.28647 1.60573  -0.32253 -0.43878 200 SER D O   
7446 C CB  . SER D 219 ? 4.57057 3.31080 3.53655 1.66998  -0.38465 -0.41808 200 SER D CB  
7447 O OG  . SER D 219 ? 4.59383 3.20710 3.59265 1.58165  -0.38533 -0.39303 200 SER D OG  
7448 N N   . GLU D 220 ? 4.31224 3.33245 3.40858 1.48119  -0.32974 -0.45293 201 GLU D N   
7449 C CA  . GLU D 220 ? 4.22964 3.34819 3.37586 1.40945  -0.30271 -0.43198 201 GLU D CA  
7450 C C   . GLU D 220 ? 4.06471 3.27319 3.25378 1.34567  -0.28971 -0.48633 201 GLU D C   
7451 O O   . GLU D 220 ? 4.03855 3.19210 3.22356 1.33748  -0.30311 -0.52618 201 GLU D O   
7452 C CB  . GLU D 220 ? 4.33866 3.32472 3.50029 1.35419  -0.30251 -0.36602 201 GLU D CB  
7453 C CG  . GLU D 220 ? 4.48906 3.39649 3.61029 1.41149  -0.30983 -0.30290 201 GLU D CG  
7454 C CD  . GLU D 220 ? 4.57872 3.34525 3.71340 1.35495  -0.31031 -0.23769 201 GLU D CD  
7455 O OE1 . GLU D 220 ? 4.54157 3.24296 3.71028 1.27965  -0.31190 -0.24685 201 GLU D OE1 
7456 O OE2 . GLU D 220 ? 4.67960 3.40504 3.79024 1.38637  -0.30862 -0.17630 201 GLU D OE2 
7457 N N   . THR D 221 ? 4.00977 3.35735 3.23908 1.30153  -0.26299 -0.48736 202 THR D N   
7458 C CA  . THR D 221 ? 3.84337 3.30498 3.11011 1.25143  -0.24569 -0.53963 202 THR D CA  
7459 C C   . THR D 221 ? 3.82257 3.22655 3.13311 1.15849  -0.23673 -0.52427 202 THR D C   
7460 O O   . THR D 221 ? 3.86851 3.25389 3.20067 1.12149  -0.22711 -0.47737 202 THR D O   
7461 C CB  . THR D 221 ? 3.71688 3.37358 3.00166 1.26134  -0.22096 -0.55840 202 THR D CB  
7462 O OG1 . THR D 221 ? 3.70225 3.43341 2.94811 1.34730  -0.22946 -0.58648 202 THR D OG1 
7463 C CG2 . THR D 221 ? 3.54493 3.30551 2.87460 1.19473  -0.19873 -0.60325 202 THR D CG2 
7464 N N   . VAL D 222 ? 3.82271 3.20570 3.14503 1.12384  -0.23981 -0.56392 203 VAL D N   
7465 C CA  . VAL D 222 ? 3.77215 3.12574 3.13603 1.03914  -0.22956 -0.55952 203 VAL D CA  
7466 C C   . VAL D 222 ? 3.59490 3.09036 2.98754 1.00719  -0.20576 -0.60627 203 VAL D C   
7467 O O   . VAL D 222 ? 3.52017 3.08378 2.89612 1.04166  -0.20676 -0.65298 203 VAL D O   
7468 C CB  . VAL D 222 ? 3.83339 3.03516 3.18677 1.02183  -0.25317 -0.56293 203 VAL D CB  
7469 C CG1 . VAL D 222 ? 3.99424 3.04846 3.33260 1.02772  -0.27097 -0.50911 203 VAL D CG1 
7470 C CG2 . VAL D 222 ? 3.81736 3.01654 3.13556 1.07652  -0.27033 -0.61311 203 VAL D CG2 
7471 N N   . THR D 223 ? 3.60213 3.14208 3.03770 0.94140  -0.18370 -0.59369 204 THR D N   
7472 C CA  . THR D 223 ? 3.43261 3.10223 2.89840 0.90553  -0.15746 -0.63267 204 THR D CA  
7473 C C   . THR D 223 ? 3.37925 3.00113 2.87731 0.83134  -0.14927 -0.62985 204 THR D C   
7474 O O   . THR D 223 ? 3.43145 2.99481 2.95035 0.79219  -0.14803 -0.59045 204 THR D O   
7475 C CB  . THR D 223 ? 3.37301 3.17323 2.86083 0.90425  -0.13401 -0.62689 204 THR D CB  
7476 O OG1 . THR D 223 ? 3.42815 3.27558 2.88329 0.97837  -0.14285 -0.62652 204 THR D OG1 
7477 C CG2 . THR D 223 ? 3.19617 3.12720 2.71453 0.86746  -0.10640 -0.67233 204 THR D CG2 
7478 N N   . CYS D 224 ? 3.39856 3.05045 2.89941 0.81423  -0.14332 -0.67059 205 CYS D N   
7479 C CA  . CYS D 224 ? 3.34113 2.96355 2.87043 0.74807  -0.13280 -0.67057 205 CYS D CA  
7480 C C   . CYS D 224 ? 3.24998 2.96985 2.81963 0.70190  -0.10114 -0.66905 205 CYS D C   
7481 O O   . CYS D 224 ? 3.16184 3.00290 2.73854 0.71107  -0.08179 -0.69833 205 CYS D O   
7482 C CB  . CYS D 224 ? 3.27169 2.90377 2.78780 0.74866  -0.13468 -0.71270 205 CYS D CB  
7483 S SG  . CYS D 224 ? 3.23858 2.80030 2.77486 0.68285  -0.13185 -0.70864 205 CYS D SG  
7484 N N   . ASN D 225 ? 3.26425 2.93395 2.86120 0.65247  -0.09605 -0.63730 206 ASN D N   
7485 C CA  . ASN D 225 ? 3.19065 2.93855 2.82650 0.60918  -0.06807 -0.63345 206 ASN D CA  
7486 C C   . ASN D 225 ? 3.11128 2.83848 2.76876 0.55355  -0.05506 -0.64275 206 ASN D C   
7487 O O   . ASN D 225 ? 3.14427 2.78675 2.81152 0.52323  -0.06345 -0.61515 206 ASN D O   
7488 C CB  . ASN D 225 ? 3.27222 2.99174 2.92176 0.60230  -0.07132 -0.58743 206 ASN D CB  
7489 C CG  . ASN D 225 ? 3.37510 3.08733 2.99590 0.66083  -0.08791 -0.56834 206 ASN D CG  
7490 O OD1 . ASN D 225 ? 3.49816 3.11689 3.10823 0.66833  -0.10596 -0.52749 206 ASN D OD1 
7491 N ND2 . ASN D 225 ? 3.32798 3.13973 2.93549 0.70288  -0.08133 -0.59719 206 ASN D ND2 
7492 N N   . VAL D 226 ? 3.20322 3.01088 2.86782 0.54033  -0.03372 -0.68064 207 VAL D N   
7493 C CA  . VAL D 226 ? 3.13295 2.92567 2.81277 0.49273  -0.01885 -0.69019 207 VAL D CA  
7494 C C   . VAL D 226 ? 3.06700 2.92972 2.78504 0.44980  0.01235  -0.69309 207 VAL D C   
7495 O O   . VAL D 226 ? 3.03375 2.99009 2.76423 0.45884  0.02693  -0.70754 207 VAL D O   
7496 C CB  . VAL D 226 ? 3.08764 2.91280 2.74619 0.50556  -0.01569 -0.72834 207 VAL D CB  
7497 C CG1 . VAL D 226 ? 3.05290 2.84310 2.71937 0.46192  -0.00452 -0.73012 207 VAL D CG1 
7498 C CG2 . VAL D 226 ? 3.15913 2.93181 2.77868 0.55881  -0.04712 -0.73271 207 VAL D CG2 
7499 N N   . ALA D 227 ? 3.09463 2.91321 2.83124 0.40451  0.02224  -0.68107 208 ALA D N   
7500 C CA  . ALA D 227 ? 3.05281 2.92234 2.82522 0.36297  0.05121  -0.68427 208 ALA D CA  
7501 C C   . ALA D 227 ? 3.03434 2.86326 2.81376 0.32272  0.06475  -0.68538 208 ALA D C   
7502 O O   . ALA D 227 ? 3.03375 2.77600 2.80411 0.31648  0.04799  -0.66237 208 ALA D O   
7503 C CB  . ALA D 227 ? 3.08788 2.94113 2.88124 0.35559  0.04638  -0.65131 208 ALA D CB  
7504 N N   . HIS D 228 ? 3.06027 2.95267 2.85549 0.29553  0.09544  -0.71193 209 HIS D N   
7505 C CA  . HIS D 228 ? 3.04493 2.90250 2.84638 0.25723  0.11325  -0.71083 209 HIS D CA  
7506 C C   . HIS D 228 ? 3.01447 2.89597 2.85227 0.21976  0.13897  -0.70949 209 HIS D C   
7507 O O   . HIS D 228 ? 2.95244 2.91599 2.80887 0.20737  0.16316  -0.73793 209 HIS D O   
7508 C CB  . HIS D 228 ? 2.99939 2.90031 2.78576 0.25404  0.12979  -0.74156 209 HIS D CB  
7509 C CG  . HIS D 228 ? 3.00487 2.85855 2.78764 0.22242  0.14449  -0.73416 209 HIS D CG  
7510 N ND1 . HIS D 228 ? 2.97225 2.86611 2.74762 0.20642  0.16836  -0.75666 209 HIS D ND1 
7511 C CD2 . HIS D 228 ? 3.04369 2.81685 2.82773 0.20552  0.13911  -0.70512 209 HIS D CD2 
7512 C CE1 . HIS D 228 ? 3.00027 2.83559 2.77053 0.18235  0.17751  -0.73911 209 HIS D CE1 
7513 N NE2 . HIS D 228 ? 3.03827 2.80160 2.81351 0.18302  0.15942  -0.70895 209 HIS D NE2 
7514 N N   . PRO D 229 ? 3.05650 2.87359 2.90629 0.20147  0.13463  -0.68043 210 PRO D N   
7515 C CA  . PRO D 229 ? 3.03378 2.87599 2.91833 0.17215  0.15644  -0.68080 210 PRO D CA  
7516 C C   . PRO D 229 ? 2.98773 2.85357 2.88536 0.13703  0.19145  -0.70485 210 PRO D C   
7517 O O   . PRO D 229 ? 2.93806 2.86427 2.86347 0.11880  0.21392  -0.72659 210 PRO D O   
7518 C CB  . PRO D 229 ? 3.08905 2.85252 2.97762 0.16540  0.14032  -0.64327 210 PRO D CB  
7519 C CG  . PRO D 229 ? 3.12329 2.83503 2.98425 0.19456  0.10678  -0.62392 210 PRO D CG  
7520 C CD  . PRO D 229 ? 3.10930 2.83633 2.94339 0.21016  0.10713  -0.64800 210 PRO D CD  
7521 N N   . ALA D 230 ? 3.03877 2.85872 2.91691 0.12650  0.19735  -0.70170 211 ALA D N   
7522 C CA  . ALA D 230 ? 3.01466 2.83925 2.90352 0.08995  0.23215  -0.71617 211 ALA D CA  
7523 C C   . ALA D 230 ? 2.94865 2.86571 2.84983 0.07784  0.25723  -0.75700 211 ALA D C   
7524 O O   . ALA D 230 ? 2.92000 2.85682 2.84400 0.04252  0.28876  -0.77466 211 ALA D O   
7525 C CB  . ALA D 230 ? 3.05261 2.81595 2.91266 0.08631  0.23238  -0.70130 211 ALA D CB  
7526 N N   . SER D 231 ? 3.08161 3.05686 2.96859 0.10665  0.24398  -0.77414 212 SER D N   
7527 C CA  . SER D 231 ? 3.00908 3.08558 2.90687 0.09827  0.26574  -0.81545 212 SER D CA  
7528 C C   . SER D 231 ? 2.96520 3.12261 2.87703 0.12376  0.25501  -0.83207 212 SER D C   
7529 O O   . SER D 231 ? 2.89815 3.15140 2.81427 0.12821  0.26597  -0.86735 212 SER D O   
7530 C CB  . SER D 231 ? 3.00308 3.09970 2.87030 0.11178  0.26411  -0.82764 212 SER D CB  
7531 O OG  . SER D 231 ? 3.03291 3.10930 2.87146 0.15969  0.22796  -0.81443 212 SER D OG  
7532 N N   . SER D 232 ? 2.97204 3.09926 2.89045 0.14125  0.23442  -0.80682 213 SER D N   
7533 C CA  . SER D 232 ? 2.94436 3.14377 2.87385 0.16816  0.22370  -0.81479 213 SER D CA  
7534 C C   . SER D 232 ? 2.93422 3.18242 2.83657 0.21310  0.20523  -0.82587 213 SER D C   
7535 O O   . SER D 232 ? 2.89424 3.23259 2.80441 0.23477  0.20461  -0.84503 213 SER D O   
7536 C CB  . SER D 232 ? 2.86281 3.15366 2.83022 0.13991  0.25285  -0.85087 213 SER D CB  
7537 O OG  . SER D 232 ? 2.79130 3.15469 2.76191 0.12308  0.27614  -0.89170 213 SER D OG  
7538 N N   . THR D 233 ? 2.93967 3.13276 2.80908 0.23082  0.18944  -0.81528 214 THR D N   
7539 C CA  . THR D 233 ? 2.93699 3.16951 2.77767 0.27692  0.17112  -0.82789 214 THR D CA  
7540 C C   . THR D 233 ? 3.00869 3.20200 2.83347 0.32126  0.13798  -0.79802 214 THR D C   
7541 O O   . THR D 233 ? 3.07916 3.18328 2.90372 0.31635  0.12287  -0.76160 214 THR D O   
7542 C CB  . THR D 233 ? 2.95642 3.14545 2.76746 0.28038  0.16629  -0.83022 214 THR D CB  
7543 O OG1 . THR D 233 ? 2.90515 3.12237 2.73030 0.23518  0.19959  -0.85092 214 THR D OG1 
7544 C CG2 . THR D 233 ? 2.94635 3.18842 2.72845 0.32935  0.14989  -0.85095 214 THR D CG2 
7545 N N   . LYS D 234 ? 2.86082 3.12399 2.67190 0.36505  0.12750  -0.81320 215 LYS D N   
7546 C CA  . LYS D 234 ? 2.94155 3.17052 2.73457 0.41068  0.09814  -0.78393 215 LYS D CA  
7547 C C   . LYS D 234 ? 2.93138 3.21846 2.69477 0.46497  0.08521  -0.80579 215 LYS D C   
7548 O O   . LYS D 234 ? 2.85977 3.26216 2.63233 0.47958  0.09724  -0.83378 215 LYS D O   
7549 C CB  . LYS D 234 ? 2.93781 3.20872 2.75795 0.40484  0.10444  -0.77099 215 LYS D CB  
7550 C CG  . LYS D 234 ? 3.02954 3.28242 2.83065 0.45318  0.07851  -0.73979 215 LYS D CG  
7551 C CD  . LYS D 234 ? 3.01124 3.33501 2.83973 0.44870  0.08899  -0.73301 215 LYS D CD  
7552 C CE  . LYS D 234 ? 3.10342 3.42487 2.90991 0.50080  0.06649  -0.70146 215 LYS D CE  
7553 N NZ  . LYS D 234 ? 3.07203 3.48290 2.90330 0.50098  0.07787  -0.69788 215 LYS D NZ  
7554 N N   . VAL D 235 ? 2.96642 3.17714 2.69482 0.49589  0.06037  -0.79545 216 VAL D N   
7555 C CA  . VAL D 235 ? 2.96685 3.21920 2.66253 0.55225  0.04533  -0.81661 216 VAL D CA  
7556 C C   . VAL D 235 ? 3.07571 3.24980 2.74387 0.60200  0.01267  -0.78231 216 VAL D C   
7557 O O   . VAL D 235 ? 3.15819 3.21473 2.82129 0.59106  -0.00402 -0.74770 216 VAL D O   
7558 C CB  . VAL D 235 ? 2.94441 3.17930 2.61926 0.55135  0.04404  -0.83975 216 VAL D CB  
7559 C CG1 . VAL D 235 ? 2.91609 3.22607 2.56217 0.60802  0.03426  -0.87144 216 VAL D CG1 
7560 C CG2 . VAL D 235 ? 2.85820 3.13730 2.56023 0.49183  0.07744  -0.86056 216 VAL D CG2 
7561 N N   . ASP D 236 ? 2.97381 3.21427 2.62384 0.65686  0.00407  -0.79181 217 ASP D N   
7562 C CA  . ASP D 236 ? 3.09593 3.26571 2.71528 0.71102  -0.02536 -0.75921 217 ASP D CA  
7563 C C   . ASP D 236 ? 3.10259 3.30382 2.68319 0.77496  -0.04098 -0.78681 217 ASP D C   
7564 O O   . ASP D 236 ? 3.09010 3.38389 2.66041 0.82091  -0.04061 -0.79945 217 ASP D O   
7565 C CB  . ASP D 236 ? 3.12167 3.33934 2.75470 0.72211  -0.02086 -0.73459 217 ASP D CB  
7566 C CG  . ASP D 236 ? 3.14909 3.31559 2.81455 0.66784  -0.01213 -0.70081 217 ASP D CG  
7567 O OD1 . ASP D 236 ? 3.18857 3.24603 2.85550 0.63635  -0.02022 -0.68202 217 ASP D OD1 
7568 O OD2 . ASP D 236 ? 3.12234 3.36377 2.81168 0.65870  0.00225  -0.69477 217 ASP D OD2 
7569 N N   . LYS D 237 ? 3.07874 3.20781 2.63708 0.78077  -0.05538 -0.79751 218 LYS D N   
7570 C CA  . LYS D 237 ? 3.09141 3.24112 2.61121 0.84270  -0.07240 -0.82591 218 LYS D CA  
7571 C C   . LYS D 237 ? 3.24012 3.25765 2.72393 0.89089  -0.10704 -0.79505 218 LYS D C   
7572 O O   . LYS D 237 ? 3.30659 3.19863 2.78807 0.86686  -0.12116 -0.77336 218 LYS D O   
7573 C CB  . LYS D 237 ? 3.01774 3.18338 2.53408 0.82234  -0.06585 -0.86204 218 LYS D CB  
7574 C CG  . LYS D 237 ? 2.91773 3.22457 2.46299 0.78435  -0.03116 -0.89834 218 LYS D CG  
7575 C CD  . LYS D 237 ? 2.91761 3.24972 2.45195 0.77503  -0.02554 -0.93276 218 LYS D CD  
7576 C CE  . LYS D 237 ? 2.97513 3.34122 2.46887 0.84802  -0.04675 -0.96122 218 LYS D CE  
7577 N NZ  . LYS D 237 ? 2.97217 3.38401 2.45616 0.83952  -0.03897 -0.99712 218 LYS D NZ  
7578 N N   . LYS D 238 ? 3.15091 3.19721 2.60668 0.95876  -0.12026 -0.79375 219 LYS D N   
7579 C CA  . LYS D 238 ? 3.30518 3.22486 2.72358 1.01009  -0.15194 -0.76456 219 LYS D CA  
7580 C C   . LYS D 238 ? 3.32463 3.20193 2.70680 1.05263  -0.17344 -0.79752 219 LYS D C   
7581 O O   . LYS D 238 ? 3.21505 3.18768 2.59629 1.05649  -0.16366 -0.84341 219 LYS D O   
7582 C CB  . LYS D 238 ? 3.35666 3.32238 2.75678 1.06976  -0.15633 -0.74538 219 LYS D CB  
7583 C CG  . LYS D 238 ? 3.24723 3.37387 2.63709 1.11731  -0.14669 -0.79027 219 LYS D CG  
7584 C CD  . LYS D 238 ? 3.28883 3.47500 2.66392 1.17325  -0.14849 -0.76872 219 LYS D CD  
7585 C CE  . LYS D 238 ? 3.20661 3.56656 2.57346 1.22045  -0.13904 -0.81734 219 LYS D CE  
7586 N NZ  . LYS D 238 ? 3.23577 3.66721 2.58720 1.27878  -0.14057 -0.79749 219 LYS D NZ  
7587 N N   . ILE D 239 ? 3.37695 3.11020 2.72943 1.08390  -0.20268 -0.77443 220 ILE D N   
7588 C CA  . ILE D 239 ? 3.41081 3.08836 2.72697 1.12851  -0.22687 -0.80573 220 ILE D CA  
7589 C C   . ILE D 239 ? 3.45117 3.17268 2.72657 1.21923  -0.24068 -0.82115 220 ILE D C   
7590 O O   . ILE D 239 ? 3.54923 3.23946 2.80981 1.25644  -0.24778 -0.78618 220 ILE D O   
7591 C CB  . ILE D 239 ? 3.53910 3.03492 2.84474 1.11479  -0.25241 -0.77993 220 ILE D CB  
7592 C CG1 . ILE D 239 ? 3.48462 2.94665 2.83052 1.02807  -0.23896 -0.76413 220 ILE D CG1 
7593 C CG2 . ILE D 239 ? 3.57032 3.01326 2.83958 1.16103  -0.27791 -0.81885 220 ILE D CG2 
7594 C CD1 . ILE D 239 ? 3.34375 2.88814 2.70493 0.99333  -0.22289 -0.80533 220 ILE D CD1 
7595 N N   . ASP E 21  ? 2.97841 2.81195 2.50578 0.63668  -0.88018 -0.31555 1   ASP E N   
7596 C CA  . ASP E 21  ? 3.01255 2.82941 2.52110 0.61576  -0.84805 -0.31828 1   ASP E CA  
7597 C C   . ASP E 21  ? 3.06362 2.92480 2.58551 0.60185  -0.84460 -0.37187 1   ASP E C   
7598 O O   . ASP E 21  ? 3.09599 3.00403 2.63086 0.61351  -0.87120 -0.40301 1   ASP E O   
7599 C CB  . ASP E 21  ? 3.06044 2.85545 2.51225 0.63027  -0.84763 -0.28072 1   ASP E CB  
7600 C CG  . ASP E 21  ? 3.00825 2.75466 2.45057 0.63874  -0.84515 -0.22602 1   ASP E CG  
7601 O OD1 . ASP E 21  ? 2.92865 2.65274 2.40658 0.63107  -0.84063 -0.21805 1   ASP E OD1 
7602 O OD2 . ASP E 21  ? 3.05128 2.78123 2.45050 0.65328  -0.84776 -0.19105 1   ASP E OD2 
7603 N N   . ILE E 22  ? 2.95827 2.80353 2.47909 0.57707  -0.81296 -0.38321 2   ILE E N   
7604 C CA  . ILE E 22  ? 3.00522 2.88522 2.53522 0.56153  -0.80694 -0.43162 2   ILE E CA  
7605 C C   . ILE E 22  ? 3.05193 2.90572 2.54394 0.55147  -0.78220 -0.42285 2   ILE E C   
7606 O O   . ILE E 22  ? 3.02416 2.83157 2.50995 0.54048  -0.75661 -0.39378 2   ILE E O   
7607 C CB  . ILE E 22  ? 2.96477 2.85636 2.55166 0.53461  -0.79124 -0.46764 2   ILE E CB  
7608 C CG1 . ILE E 22  ? 2.93050 2.85819 2.55741 0.54600  -0.81637 -0.48362 2   ILE E CG1 
7609 C CG2 . ILE E 22  ? 3.00728 2.92640 2.60358 0.51468  -0.78099 -0.51419 2   ILE E CG2 
7610 C CD1 . ILE E 22  ? 2.90227 2.85178 2.58563 0.52046  -0.80128 -0.52424 2   ILE E CD1 
7611 N N   . VAL E 23  ? 3.02131 2.90476 2.48783 0.55686  -0.79124 -0.44901 3   VAL E N   
7612 C CA  . VAL E 23  ? 3.07350 2.93866 2.50413 0.54849  -0.76931 -0.44885 3   VAL E CA  
7613 C C   . VAL E 23  ? 3.05939 2.93506 2.52299 0.51884  -0.75138 -0.49491 3   VAL E C   
7614 O O   . VAL E 23  ? 3.06334 2.98191 2.55774 0.51411  -0.76708 -0.53784 3   VAL E O   
7615 C CB  . VAL E 23  ? 3.16727 3.05431 2.54371 0.57404  -0.78990 -0.44924 3   VAL E CB  
7616 C CG1 . VAL E 23  ? 3.23050 3.11054 2.57699 0.56395  -0.76968 -0.46560 3   VAL E CG1 
7617 C CG2 . VAL E 23  ? 3.18067 3.04354 2.51644 0.59932  -0.79798 -0.39537 3   VAL E CG2 
7618 N N   . MET E 24  ? 3.09698 2.93310 2.55610 0.49876  -0.71911 -0.48648 4   MET E N   
7619 C CA  . MET E 24  ? 3.08113 2.91630 2.56900 0.46854  -0.69884 -0.52527 4   MET E CA  
7620 C C   . MET E 24  ? 3.14283 2.97373 2.59204 0.46709  -0.68913 -0.53832 4   MET E C   
7621 O O   . MET E 24  ? 3.14070 2.93074 2.57075 0.45865  -0.66373 -0.51941 4   MET E O   
7622 C CB  . MET E 24  ? 3.01308 2.80200 2.52750 0.44629  -0.67063 -0.50843 4   MET E CB  
7623 C CG  . MET E 24  ? 2.95396 2.74666 2.50662 0.44732  -0.67915 -0.49989 4   MET E CG  
7624 S SD  . MET E 24  ? 2.95298 2.81204 2.55103 0.44500  -0.70299 -0.55084 4   MET E SD  
7625 C CE  . MET E 24  ? 2.95300 2.81141 2.57866 0.40727  -0.67654 -0.59721 4   MET E CE  
7626 N N   . SER E 25  ? 3.16080 3.03472 2.59901 0.47678  -0.71107 -0.57271 5   SER E N   
7627 C CA  . SER E 25  ? 3.22328 3.09784 2.62472 0.47719  -0.70566 -0.59206 5   SER E CA  
7628 C C   . SER E 25  ? 3.18616 3.04766 2.61906 0.44377  -0.68289 -0.62653 5   SER E C   
7629 O O   . SER E 25  ? 3.16039 3.05043 2.63773 0.42705  -0.69022 -0.66666 5   SER E O   
7630 C CB  . SER E 25  ? 3.29403 3.21746 2.67540 0.49874  -0.73956 -0.62105 5   SER E CB  
7631 O OG  . SER E 25  ? 3.26092 3.22560 2.69426 0.49140  -0.75983 -0.65720 5   SER E OG  
7632 N N   . GLN E 26  ? 3.33684 3.15488 2.74810 0.43392  -0.65520 -0.61108 6   GLN E N   
7633 C CA  . GLN E 26  ? 3.30558 3.09971 2.74162 0.40246  -0.63146 -0.63726 6   GLN E CA  
7634 C C   . GLN E 26  ? 3.35908 3.14070 2.75363 0.40508  -0.62236 -0.64902 6   GLN E C   
7635 O O   . GLN E 26  ? 3.38820 3.14147 2.74362 0.41823  -0.60937 -0.61525 6   GLN E O   
7636 C CB  . GLN E 26  ? 3.24250 2.98685 2.69791 0.38619  -0.60521 -0.60642 6   GLN E CB  
7637 C CG  . GLN E 26  ? 3.21360 2.92303 2.68686 0.35508  -0.57917 -0.62761 6   GLN E CG  
7638 C CD  . GLN E 26  ? 3.16231 2.81753 2.64503 0.34396  -0.55552 -0.59385 6   GLN E CD  
7639 O OE1 . GLN E 26  ? 3.14627 2.78897 2.62079 0.36024  -0.55806 -0.55344 6   GLN E OE1 
7640 N NE2 . GLN E 26  ? 3.13927 2.75976 2.63859 0.31656  -0.53373 -0.61055 6   GLN E NE2 
7641 N N   . SER E 27  ? 3.32505 3.12823 2.73024 0.39273  -0.62912 -0.69746 7   SER E N   
7642 C CA  . SER E 27  ? 3.38252 3.17650 2.75041 0.39520  -0.62347 -0.71625 7   SER E CA  
7643 C C   . SER E 27  ? 3.35393 3.12720 2.75385 0.36151  -0.60651 -0.75178 7   SER E C   
7644 O O   . SER E 27  ? 3.31301 3.09843 2.76417 0.33866  -0.60793 -0.77534 7   SER E O   
7645 C CB  . SER E 27  ? 3.45868 3.29962 2.79888 0.41804  -0.65441 -0.74440 7   SER E CB  
7646 O OG  . SER E 27  ? 3.44216 3.31929 2.82745 0.40238  -0.67235 -0.79304 7   SER E OG  
7647 N N   . PRO E 28  ? 3.39867 3.13983 2.76952 0.35771  -0.58964 -0.75655 8   PRO E N   
7648 C CA  . PRO E 28  ? 3.45650 3.18304 2.76873 0.38290  -0.58347 -0.73154 8   PRO E CA  
7649 C C   . PRO E 28  ? 3.42387 3.10586 2.72763 0.38459  -0.55844 -0.68117 8   PRO E C   
7650 O O   . PRO E 28  ? 3.35415 3.00588 2.69347 0.36269  -0.54299 -0.67190 8   PRO E O   
7651 C CB  . PRO E 28  ? 3.49175 3.20522 2.78969 0.37273  -0.57698 -0.76936 8   PRO E CB  
7652 C CG  . PRO E 28  ? 3.43090 3.12027 2.78006 0.33588  -0.56336 -0.79094 8   PRO E CG  
7653 C CD  . PRO E 28  ? 3.38618 3.10506 2.78267 0.32668  -0.57598 -0.79290 8   PRO E CD  
7654 N N   . SER E 29  ? 3.48608 3.16371 2.74300 0.41070  -0.55442 -0.64930 9   SER E N   
7655 C CA  . SER E 29  ? 3.46555 3.10295 2.71766 0.41302  -0.53146 -0.60238 9   SER E CA  
7656 C C   . SER E 29  ? 3.44813 3.04057 2.70166 0.39586  -0.50597 -0.61036 9   SER E C   
7657 O O   . SER E 29  ? 3.39470 2.94734 2.66589 0.38587  -0.48776 -0.58334 9   SER E O   
7658 C CB  . SER E 29  ? 3.55093 3.19892 2.75564 0.44484  -0.53301 -0.56571 9   SER E CB  
7659 O OG  . SER E 29  ? 3.56128 3.24118 2.76592 0.46062  -0.55577 -0.55022 9   SER E OG  
7660 N N   . SER E 30  ? 3.47088 3.06716 2.70554 0.39343  -0.50620 -0.64788 10  SER E N   
7661 C CA  . SER E 30  ? 3.45484 3.00866 2.68995 0.37762  -0.48506 -0.66116 10  SER E CA  
7662 C C   . SER E 30  ? 3.43618 2.99445 2.69235 0.35461  -0.49309 -0.71431 10  SER E C   
7663 O O   . SER E 30  ? 3.46640 3.06644 2.72124 0.35914  -0.51542 -0.74480 10  SER E O   
7664 C CB  . SER E 30  ? 3.53139 3.07910 2.71754 0.39990  -0.47394 -0.65231 10  SER E CB  
7665 O OG  . SER E 30  ? 3.60490 3.19210 2.75557 0.41815  -0.49201 -0.67894 10  SER E OG  
7666 N N   . LEU E 31  ? 3.40589 2.91929 2.68214 0.32990  -0.47565 -0.72553 11  LEU E N   
7667 C CA  . LEU E 31  ? 3.39760 2.90885 2.69925 0.30366  -0.48068 -0.77334 11  LEU E CA  
7668 C C   . LEU E 31  ? 3.38351 2.83789 2.68419 0.28611  -0.45973 -0.78205 11  LEU E C   
7669 O O   . LEU E 31  ? 3.34078 2.75244 2.64783 0.28060  -0.44134 -0.75142 11  LEU E O   
7670 C CB  . LEU E 31  ? 3.35264 2.87638 2.70380 0.28178  -0.48670 -0.77877 11  LEU E CB  
7671 C CG  . LEU E 31  ? 3.35581 2.89684 2.73963 0.25686  -0.49717 -0.82951 11  LEU E CG  
7672 C CD1 . LEU E 31  ? 3.41278 2.98858 2.77043 0.27172  -0.51717 -0.86563 11  LEU E CD1 
7673 C CD2 . LEU E 31  ? 3.32365 2.89966 2.75043 0.24752  -0.50843 -0.83098 11  LEU E CD2 
7674 N N   . ALA E 32  ? 3.35935 2.81174 2.65192 0.27834  -0.46456 -0.82467 12  ALA E N   
7675 C CA  . ALA E 32  ? 3.35191 2.75004 2.64155 0.26216  -0.44805 -0.83894 12  ALA E CA  
7676 C C   . ALA E 32  ? 3.33926 2.73343 2.65923 0.23181  -0.45506 -0.88603 12  ALA E C   
7677 O O   . ALA E 32  ? 3.37195 2.80538 2.69031 0.23515  -0.47493 -0.92183 12  ALA E O   
7678 C CB  . ALA E 32  ? 3.39723 2.79046 2.63976 0.28669  -0.44499 -0.84300 12  ALA E CB  
7679 N N   . VAL E 33  ? 3.38438 2.72990 2.73163 0.20233  -0.43919 -0.88607 13  VAL E N   
7680 C CA  . VAL E 33  ? 3.38368 2.71914 2.76419 0.16904  -0.44147 -0.92649 13  VAL E CA  
7681 C C   . VAL E 33  ? 3.37504 2.63937 2.74938 0.15035  -0.42318 -0.93252 13  VAL E C   
7682 O O   . VAL E 33  ? 3.36280 2.58672 2.71387 0.16172  -0.40880 -0.90334 13  VAL E O   
7683 C CB  . VAL E 33  ? 3.35233 2.70409 2.77967 0.14684  -0.44053 -0.92188 13  VAL E CB  
7684 C CG1 . VAL E 33  ? 3.35668 2.77492 2.78903 0.16835  -0.45930 -0.91145 13  VAL E CG1 
7685 C CG2 . VAL E 33  ? 3.31564 2.61383 2.74999 0.13511  -0.41764 -0.88526 13  VAL E CG2 
7686 N N   . SER E 34  ? 3.32128 2.56985 2.71865 0.12119  -0.42472 -0.97138 14  SER E N   
7687 C CA  . SER E 34  ? 3.32108 2.49903 2.71424 0.10009  -0.40936 -0.98107 14  SER E CA  
7688 C C   . SER E 34  ? 3.29463 2.43345 2.71952 0.06837  -0.39173 -0.96737 14  SER E C   
7689 O O   . SER E 34  ? 3.27666 2.44666 2.72965 0.06194  -0.39158 -0.95436 14  SER E O   
7690 C CB  . SER E 34  ? 3.35601 2.53324 2.75141 0.08727  -0.42162 -1.03235 14  SER E CB  
7691 O OG  . SER E 34  ? 3.38878 2.59394 2.74722 0.11882  -0.43635 -1.04484 14  SER E OG  
7692 N N   . VAL E 35  ? 3.15196 2.21990 2.56959 0.04959  -0.37688 -0.97080 15  VAL E N   
7693 C CA  . VAL E 35  ? 3.14071 2.15846 2.57719 0.02169  -0.35754 -0.95471 15  VAL E CA  
7694 C C   . VAL E 35  ? 3.16134 2.18506 2.63721 -0.01555 -0.35685 -0.99006 15  VAL E C   
7695 O O   . VAL E 35  ? 3.20251 2.21460 2.68038 -0.02915 -0.36326 -1.02727 15  VAL E O   
7696 C CB  . VAL E 35  ? 3.16011 2.09406 2.56730 0.01990  -0.34273 -0.94087 15  VAL E CB  
7697 C CG1 . VAL E 35  ? 3.15386 2.03195 2.57365 -0.00675 -0.32322 -0.92267 15  VAL E CG1 
7698 C CG2 . VAL E 35  ? 3.14079 2.07386 2.51520 0.05676  -0.34354 -0.90848 15  VAL E CG2 
7699 N N   . GLY E 36  ? 3.23941 2.28114 2.74842 -0.03218 -0.34874 -0.97888 16  GLY E N   
7700 C CA  . GLY E 36  ? 3.25700 2.30259 2.80865 -0.07016 -0.34298 -1.00819 16  GLY E CA  
7701 C C   . GLY E 36  ? 3.25062 2.37951 2.84132 -0.07152 -0.36227 -1.03829 16  GLY E C   
7702 O O   . GLY E 36  ? 3.27801 2.41449 2.90347 -0.10063 -0.36375 -1.07516 16  GLY E O   
7703 N N   . GLU E 37  ? 3.43110 2.62160 3.01872 -0.04127 -0.37783 -1.02388 17  GLU E N   
7704 C CA  . GLU E 37  ? 3.43719 2.70726 3.05728 -0.03738 -0.40055 -1.05331 17  GLU E CA  
7705 C C   . GLU E 37  ? 3.41538 2.73525 3.06174 -0.02983 -0.40191 -1.03162 17  GLU E C   
7706 O O   . GLU E 37  ? 3.39947 2.68978 3.04139 -0.03107 -0.38372 -0.99557 17  GLU E O   
7707 C CB  . GLU E 37  ? 3.44129 2.74443 3.02665 -0.00311 -0.42517 -1.06498 17  GLU E CB  
7708 C CG  . GLU E 37  ? 3.41844 2.72537 2.96154 0.03479  -0.42591 -1.02177 17  GLU E CG  
7709 C CD  . GLU E 37  ? 3.43324 2.79986 2.95421 0.06914  -0.45209 -1.03094 17  GLU E CD  
7710 O OE1 . GLU E 37  ? 3.46027 2.81895 2.94996 0.08186  -0.46108 -1.05055 17  GLU E OE1 
7711 O OE2 . GLU E 37  ? 3.42311 2.84327 2.95592 0.08432  -0.46408 -1.01895 17  GLU E OE2 
7712 N N   . LYS E 38  ? 3.45439 2.84851 3.12712 -0.02045 -0.42526 -1.05457 18  LYS E N   
7713 C CA  . LYS E 38  ? 3.43580 2.88437 3.13232 -0.00818 -0.43232 -1.03796 18  LYS E CA  
7714 C C   . LYS E 38  ? 3.42491 2.91573 3.08616 0.03479  -0.45652 -1.02400 18  LYS E C   
7715 O O   . LYS E 38  ? 3.44368 2.95757 3.08704 0.04924  -0.47700 -1.04955 18  LYS E O   
7716 C CB  . LYS E 38  ? 3.44996 2.95393 3.21008 -0.03132 -0.44120 -1.07620 18  LYS E CB  
7717 C CG  . LYS E 38  ? 3.47612 2.94431 3.27591 -0.07682 -0.41694 -1.09491 18  LYS E CG  
7718 C CD  . LYS E 38  ? 3.49574 3.02580 3.36100 -0.09787 -0.42981 -1.13990 18  LYS E CD  
7719 C CE  . LYS E 38  ? 3.53283 3.02624 3.43758 -0.14522 -0.40540 -1.16176 18  LYS E CE  
7720 N NZ  . LYS E 38  ? 3.55128 3.10308 3.52052 -0.16609 -0.42115 -1.21201 18  LYS E NZ  
7721 N N   . VAL E 39  ? 3.30215 2.80102 2.95169 0.05543  -0.45424 -0.98339 19  VAL E N   
7722 C CA  . VAL E 39  ? 3.29808 2.83685 2.91611 0.09514  -0.47545 -0.96513 19  VAL E CA  
7723 C C   . VAL E 39  ? 3.28197 2.86677 2.92920 0.10324  -0.48355 -0.94950 19  VAL E C   
7724 O O   . VAL E 39  ? 3.26587 2.83132 2.93766 0.08691  -0.46550 -0.93188 19  VAL E O   
7725 C CB  . VAL E 39  ? 3.29085 2.78359 2.85441 0.11797  -0.46476 -0.92501 19  VAL E CB  
7726 C CG1 . VAL E 39  ? 3.26849 2.71780 2.83515 0.11154  -0.44249 -0.88393 19  VAL E CG1 
7727 C CG2 . VAL E 39  ? 3.29122 2.82503 2.81941 0.15747  -0.48572 -0.91002 19  VAL E CG2 
7728 N N   . THR E 40  ? 3.29049 2.93489 2.93334 0.12938  -0.51152 -0.95724 20  THR E N   
7729 C CA  . THR E 40  ? 3.27841 2.97499 2.95356 0.13793  -0.52537 -0.95203 20  THR E CA  
7730 C C   . THR E 40  ? 3.26945 2.97259 2.90474 0.17490  -0.53469 -0.90819 20  THR E C   
7731 O O   . THR E 40  ? 3.29398 3.02932 2.89894 0.20336  -0.55783 -0.91042 20  THR E O   
7732 C CB  . THR E 40  ? 3.29675 3.05845 3.00437 0.13789  -0.55356 -0.99894 20  THR E CB  
7733 O OG1 . THR E 40  ? 3.32683 3.10323 2.98953 0.16458  -0.57564 -1.00977 20  THR E OG1 
7734 C CG2 . THR E 40  ? 3.30359 3.05986 3.05986 0.09788  -0.54300 -1.04139 20  THR E CG2 
7735 N N   . MET E 41  ? 3.28265 2.95337 2.91709 0.17451  -0.51697 -0.86829 21  MET E N   
7736 C CA  . MET E 41  ? 3.26826 2.94706 2.87537 0.20651  -0.52629 -0.82618 21  MET E CA  
7737 C C   . MET E 41  ? 3.26484 3.01037 2.89495 0.22260  -0.55436 -0.83744 21  MET E C   
7738 O O   . MET E 41  ? 3.25556 3.02889 2.93590 0.20517  -0.55601 -0.85938 21  MET E O   
7739 C CB  . MET E 41  ? 3.22210 2.85455 2.83322 0.19998  -0.50413 -0.78673 21  MET E CB  
7740 C CG  . MET E 41  ? 3.21227 2.77465 2.80448 0.18328  -0.47699 -0.77552 21  MET E CG  
7741 S SD  . MET E 41  ? 3.23500 2.76857 2.76712 0.20981  -0.47630 -0.74956 21  MET E SD  
7742 C CE  . MET E 41  ? 3.28040 2.81257 2.80451 0.19488  -0.47683 -0.79794 21  MET E CE  
7743 N N   . SER E 42  ? 3.26016 3.03102 2.85344 0.25628  -0.57609 -0.82247 22  SER E N   
7744 C CA  . SER E 42  ? 3.26537 3.09729 2.87294 0.27585  -0.60679 -0.83342 22  SER E CA  
7745 C C   . SER E 42  ? 3.24629 3.07694 2.82928 0.30457  -0.61425 -0.78580 22  SER E C   
7746 O O   . SER E 42  ? 3.25659 3.05476 2.79342 0.32090  -0.60627 -0.75053 22  SER E O   
7747 C CB  . SER E 42  ? 3.32404 3.19241 2.90787 0.29191  -0.63256 -0.86598 22  SER E CB  
7748 O OG  . SER E 42  ? 3.33818 3.26535 2.93981 0.30950  -0.66455 -0.88180 22  SER E OG  
7749 N N   . CYS E 43  ? 3.25246 3.11895 2.86895 0.31042  -0.62960 -0.78562 23  CYS E N   
7750 C CA  . CYS E 43  ? 3.23608 3.10456 2.83433 0.33772  -0.64091 -0.74363 23  CYS E CA  
7751 C C   . CYS E 43  ? 3.23437 3.16195 2.86477 0.35027  -0.67088 -0.76273 23  CYS E C   
7752 O O   . CYS E 43  ? 3.21384 3.16843 2.89840 0.32988  -0.67062 -0.79595 23  CYS E O   
7753 C CB  . CYS E 43  ? 3.18720 3.00828 2.79539 0.32737  -0.61624 -0.70647 23  CYS E CB  
7754 S SG  . CYS E 43  ? 3.16469 2.98428 2.75490 0.35952  -0.63123 -0.65484 23  CYS E SG  
7755 N N   . LYS E 44  ? 3.10167 3.04853 2.69914 0.38393  -0.69619 -0.74138 24  LYS E N   
7756 C CA  . LYS E 44  ? 3.10754 3.10856 2.72874 0.40151  -0.72897 -0.75693 24  LYS E CA  
7757 C C   . LYS E 44  ? 3.09342 3.08447 2.69358 0.42812  -0.73957 -0.70982 24  LYS E C   
7758 O O   . LYS E 44  ? 3.11658 3.07563 2.66516 0.44519  -0.73531 -0.67083 24  LYS E O   
7759 C CB  . LYS E 44  ? 3.17023 3.21241 2.76887 0.41953  -0.75929 -0.78934 24  LYS E CB  
7760 C CG  . LYS E 44  ? 3.17530 3.27700 2.80620 0.43526  -0.79555 -0.81540 24  LYS E CG  
7761 C CD  . LYS E 44  ? 3.23619 3.37722 2.85486 0.44615  -0.82394 -0.85855 24  LYS E CD  
7762 C CE  . LYS E 44  ? 3.23736 3.43970 2.89764 0.45936  -0.86085 -0.89065 24  LYS E CE  
7763 N NZ  . LYS E 44  ? 3.28543 3.52703 2.94655 0.46453  -0.88824 -0.94108 24  LYS E NZ  
7764 N N   . SER E 45  ? 3.11263 3.13140 2.75473 0.43139  -0.75306 -0.71409 25  SER E N   
7765 C CA  . SER E 45  ? 3.09536 3.10522 2.72464 0.45560  -0.76549 -0.67263 25  SER E CA  
7766 C C   . SER E 45  ? 3.14969 3.19989 2.75567 0.48980  -0.80608 -0.67595 25  SER E C   
7767 O O   . SER E 45  ? 3.18244 3.27660 2.79754 0.49351  -0.82752 -0.71719 25  SER E O   
7768 C CB  . SER E 45  ? 3.02932 3.04369 2.71389 0.44293  -0.75818 -0.67426 25  SER E CB  
7769 O OG  . SER E 45  ? 3.01235 3.01910 2.68621 0.46783  -0.77383 -0.63694 25  SER E OG  
7770 N N   . SER E 46  ? 3.12853 3.16090 2.70359 0.51540  -0.81778 -0.63163 26  SER E N   
7771 C CA  . SER E 46  ? 3.18373 3.24727 2.73158 0.54980  -0.85699 -0.62940 26  SER E CA  
7772 C C   . SER E 46  ? 3.15281 3.26656 2.75454 0.55528  -0.88386 -0.66061 26  SER E C   
7773 O O   . SER E 46  ? 3.19299 3.35129 2.79399 0.57221  -0.91636 -0.69130 26  SER E O   
7774 C CB  . SER E 46  ? 3.18802 3.21412 2.68870 0.57371  -0.86031 -0.57110 26  SER E CB  
7775 O OG  . SER E 46  ? 3.11800 3.12761 2.65163 0.57115  -0.85583 -0.54753 26  SER E OG  
7776 N N   . GLN E 47  ? 3.22235 3.32985 2.87077 0.54253  -0.87144 -0.65428 27  GLN E N   
7777 C CA  . GLN E 47  ? 3.18591 3.34119 2.89217 0.54530  -0.89151 -0.68461 27  GLN E CA  
7778 C C   . GLN E 47  ? 3.13725 3.30363 2.90516 0.50833  -0.86296 -0.71921 27  GLN E C   
7779 O O   . GLN E 47  ? 3.12362 3.25054 2.88646 0.48245  -0.82764 -0.71069 27  GLN E O   
7780 C CB  . GLN E 47  ? 3.15216 3.29341 2.86110 0.56536  -0.90349 -0.64846 27  GLN E CB  
7781 C CG  . GLN E 47  ? 3.17828 3.28088 2.82142 0.59262  -0.91494 -0.59636 27  GLN E CG  
7782 C CD  . GLN E 47  ? 3.24026 3.37050 2.84230 0.62266  -0.95201 -0.60375 27  GLN E CD  
7783 O OE1 . GLN E 47  ? 3.26023 3.44258 2.88939 0.63173  -0.98019 -0.64452 27  GLN E OE1 
7784 N NE2 . GLN E 47  ? 3.27162 3.36658 2.80756 0.63879  -0.95208 -0.56438 27  GLN E NE2 
7785 N N   . SER E 48  ? 2.98434 3.20455 2.81111 0.50628  -0.87839 -0.75850 28  SER E N   
7786 C CA  . SER E 48  ? 2.95123 3.18660 2.84071 0.47113  -0.85103 -0.79227 28  SER E CA  
7787 C C   . SER E 48  ? 2.90537 3.09654 2.80567 0.45718  -0.81946 -0.76109 28  SER E C   
7788 O O   . SER E 48  ? 2.88700 3.05211 2.76435 0.47813  -0.82723 -0.72160 28  SER E O   
7789 C CB  . SER E 48  ? 2.93998 3.24687 2.89397 0.47440  -0.87523 -0.83992 28  SER E CB  
7790 O OG  . SER E 48  ? 2.91302 3.23394 2.93034 0.43980  -0.84534 -0.86874 28  SER E OG  
7791 N N   . LEU E 49  ? 2.87759 3.05807 2.81209 0.42153  -0.78423 -0.77957 29  LEU E N   
7792 C CA  . LEU E 49  ? 2.84505 2.98054 2.78828 0.40538  -0.75157 -0.75477 29  LEU E CA  
7793 C C   . LEU E 49  ? 2.83657 3.00348 2.84765 0.37886  -0.73203 -0.79180 29  LEU E C   
7794 O O   . LEU E 49  ? 2.83723 2.96809 2.85747 0.35028  -0.69508 -0.78901 29  LEU E O   
7795 C CB  . LEU E 49  ? 2.85045 2.91996 2.75147 0.38711  -0.72035 -0.72897 29  LEU E CB  
7796 C CG  . LEU E 49  ? 2.87414 2.91420 2.71080 0.40457  -0.73056 -0.70039 29  LEU E CG  
7797 C CD1 . LEU E 49  ? 2.87372 2.85410 2.68312 0.38146  -0.69576 -0.68413 29  LEU E CD1 
7798 C CD2 . LEU E 49  ? 2.86331 2.88706 2.66613 0.43832  -0.75234 -0.65630 29  LEU E CD2 
7799 N N   . PHE E 50  ? 2.77547 3.00954 2.83537 0.38806  -0.75593 -0.82705 30  PHE E N   
7800 C CA  . PHE E 50  ? 2.77959 3.05381 2.91081 0.36191  -0.73749 -0.86759 30  PHE E CA  
7801 C C   . PHE E 50  ? 2.74973 3.06476 2.92017 0.38304  -0.75559 -0.87238 30  PHE E C   
7802 O O   . PHE E 50  ? 2.74492 3.11470 2.93397 0.40710  -0.79349 -0.89315 30  PHE E O   
7803 C CB  . PHE E 50  ? 2.81319 3.13848 2.97967 0.34613  -0.74648 -0.91808 30  PHE E CB  
7804 C CG  . PHE E 50  ? 2.82974 3.18889 3.06963 0.31150  -0.71991 -0.95861 30  PHE E CG  
7805 C CD1 . PHE E 50  ? 2.85329 3.16960 3.09520 0.27376  -0.67614 -0.95749 30  PHE E CD1 
7806 C CD2 . PHE E 50  ? 2.83051 3.26407 3.13815 0.31660  -0.73849 -0.99807 30  PHE E CD2 
7807 C CE1 . PHE E 50  ? 2.88228 3.22755 3.19058 0.24040  -0.64936 -0.99296 30  PHE E CE1 
7808 C CE2 . PHE E 50  ? 2.85582 3.32284 3.23481 0.28331  -0.71147 -1.03507 30  PHE E CE2 
7809 C CZ  . PHE E 50  ? 2.88533 3.30736 3.26374 0.24445  -0.66587 -1.03161 30  PHE E CZ  
7810 N N   . TYR E 51  ? 2.85002 3.13674 3.03088 0.37558  -0.72963 -0.85389 31  TYR E N   
7811 C CA  . TYR E 51  ? 2.82290 3.14932 3.04783 0.39151  -0.74065 -0.86364 31  TYR E CA  
7812 C C   . TYR E 51  ? 2.83983 3.24424 3.14210 0.37670  -0.74257 -0.92037 31  TYR E C   
7813 O O   . TYR E 51  ? 2.87708 3.29127 3.20631 0.34309  -0.71890 -0.94876 31  TYR E O   
7814 C CB  . TYR E 51  ? 2.81532 3.09502 3.03828 0.38070  -0.70601 -0.83898 31  TYR E CB  
7815 C CG  . TYR E 51  ? 2.77930 3.00681 2.95187 0.40939  -0.71811 -0.78890 31  TYR E CG  
7816 C CD1 . TYR E 51  ? 2.77040 2.95595 2.88123 0.42609  -0.73535 -0.75295 31  TYR E CD1 
7817 C CD2 . TYR E 51  ? 2.75853 2.97733 2.94635 0.41889  -0.71062 -0.77778 31  TYR E CD2 
7818 C CE1 . TYR E 51  ? 2.74181 2.87941 2.81171 0.45032  -0.74592 -0.70718 31  TYR E CE1 
7819 C CE2 . TYR E 51  ? 2.72637 2.89565 2.87091 0.44457  -0.72319 -0.73323 31  TYR E CE2 
7820 C CZ  . TYR E 51  ? 2.71750 2.84648 2.80517 0.45933  -0.74102 -0.69790 31  TYR E CZ  
7821 O OH  . TYR E 51  ? 2.68615 2.76607 2.73539 0.48330  -0.75365 -0.65357 31  TYR E OH  
7822 N N   . SER E 52  ? 2.71127 3.17146 3.05232 0.40202  -0.77146 -0.93750 32  SER E N   
7823 C CA  . SER E 52  ? 2.72686 3.26674 3.14929 0.39035  -0.77509 -0.99258 32  SER E CA  
7824 C C   . SER E 52  ? 2.74900 3.29303 3.22254 0.35903  -0.72873 -1.00644 32  SER E C   
7825 O O   . SER E 52  ? 2.78991 3.36194 3.31246 0.32460  -0.70436 -1.04212 32  SER E O   
7826 C CB  . SER E 52  ? 2.69370 3.29179 3.14124 0.42980  -0.82262 -1.00716 32  SER E CB  
7827 O OG  . SER E 52  ? 2.69084 3.28322 3.08720 0.45905  -0.86518 -0.99417 32  SER E OG  
7828 N N   . SER E 53  ? 2.74904 3.26368 3.21075 0.37057  -0.71577 -0.97844 33  SER E N   
7829 C CA  . SER E 53  ? 2.78038 3.29583 3.28372 0.34418  -0.67093 -0.98916 33  SER E CA  
7830 C C   . SER E 53  ? 2.82389 3.26580 3.28880 0.30962  -0.62492 -0.96644 33  SER E C   
7831 O O   . SER E 53  ? 2.87680 3.32761 3.38097 0.27282  -0.58658 -0.99034 33  SER E O   
7832 C CB  . SER E 53  ? 2.74657 3.25752 3.24916 0.37221  -0.67619 -0.96980 33  SER E CB  
7833 O OG  . SER E 53  ? 2.77212 3.20342 3.19936 0.38787  -0.67722 -0.91710 33  SER E OG  
7834 N N   . ASN E 54  ? 2.80699 3.17508 3.19633 0.32103  -0.62817 -0.92021 34  ASN E N   
7835 C CA  . ASN E 54  ? 2.84656 3.13997 3.19525 0.29208  -0.58794 -0.89664 34  ASN E CA  
7836 C C   . ASN E 54  ? 2.89231 3.19559 3.25961 0.25587  -0.57029 -0.92581 34  ASN E C   
7837 O O   . ASN E 54  ? 2.94544 3.21393 3.31524 0.22140  -0.52826 -0.92771 34  ASN E O   
7838 C CB  . ASN E 54  ? 2.81226 3.03503 3.08245 0.31364  -0.60241 -0.84620 34  ASN E CB  
7839 C CG  . ASN E 54  ? 2.83889 2.97823 3.06495 0.29128  -0.56353 -0.81634 34  ASN E CG  
7840 O OD1 . ASN E 54  ? 2.87652 2.95679 3.04871 0.30895  -0.56936 -0.77421 34  ASN E OD1 
7841 N ND2 . ASN E 54  ? 2.82796 2.96060 3.07703 0.25282  -0.52499 -0.83778 34  ASN E ND2 
7842 N N   . GLN E 55  ? 2.74901 3.09645 3.12699 0.26398  -0.60302 -0.94873 35  GLN E N   
7843 C CA  . GLN E 55  ? 2.78744 3.14801 3.18406 0.23314  -0.59326 -0.97967 35  GLN E CA  
7844 C C   . GLN E 55  ? 2.80682 3.08667 3.14384 0.21302  -0.56724 -0.95158 35  GLN E C   
7845 O O   . GLN E 55  ? 2.85473 3.12289 3.20879 0.17659  -0.53813 -0.97084 35  GLN E O   
7846 C CB  . GLN E 55  ? 2.83750 3.24906 3.31488 0.19966  -0.56596 -1.02455 35  GLN E CB  
7847 C CG  . GLN E 55  ? 2.84378 3.35000 3.39140 0.21226  -0.59832 -1.06970 35  GLN E CG  
7848 C CD  . GLN E 55  ? 2.88869 3.44159 3.50940 0.17308  -0.57778 -1.11882 35  GLN E CD  
7849 O OE1 . GLN E 55  ? 2.91584 3.49299 3.59267 0.15088  -0.54562 -1.13662 35  GLN E OE1 
7850 N NE2 . GLN E 55  ? 2.89075 3.45476 3.51069 0.16383  -0.59516 -1.14082 35  GLN E NE2 
7851 N N   . LYS E 56  ? 2.78855 3.01208 3.05728 0.23670  -0.57815 -0.90630 36  LYS E N   
7852 C CA  . LYS E 56  ? 2.79673 2.94490 3.00756 0.22271  -0.55802 -0.87842 36  LYS E CA  
7853 C C   . LYS E 56  ? 2.75935 2.88747 2.91170 0.25422  -0.59082 -0.84902 36  LYS E C   
7854 O O   . LYS E 56  ? 2.72514 2.88400 2.87410 0.28766  -0.62528 -0.84115 36  LYS E O   
7855 C CB  . LYS E 56  ? 2.80921 2.89007 2.99588 0.21193  -0.52223 -0.84666 36  LYS E CB  
7856 C CG  . LYS E 56  ? 2.85953 2.95319 3.09684 0.18000  -0.48471 -0.87198 36  LYS E CG  
7857 C CD  . LYS E 56  ? 2.90366 2.91583 3.10461 0.15818  -0.44379 -0.84607 36  LYS E CD  
7858 C CE  . LYS E 56  ? 2.88519 2.85185 3.04755 0.18412  -0.44551 -0.80474 36  LYS E CE  
7859 N NZ  . LYS E 56  ? 2.93312 2.81974 3.06009 0.16372  -0.40693 -0.78224 36  LYS E NZ  
7860 N N   . ASN E 57  ? 2.88784 2.96327 2.99370 0.24338  -0.57919 -0.83279 37  ASN E N   
7861 C CA  . ASN E 57  ? 2.86550 2.91923 2.91448 0.26943  -0.60420 -0.80512 37  ASN E CA  
7862 C C   . ASN E 57  ? 2.84315 2.82020 2.83954 0.27604  -0.58890 -0.75520 37  ASN E C   
7863 O O   . ASN E 57  ? 2.85760 2.78582 2.84953 0.25229  -0.55511 -0.74718 37  ASN E O   
7864 C CB  . ASN E 57  ? 2.89064 2.94875 2.92655 0.25631  -0.60691 -0.82720 37  ASN E CB  
7865 C CG  . ASN E 57  ? 2.89917 3.03389 2.97437 0.26266  -0.63671 -0.87099 37  ASN E CG  
7866 O OD1 . ASN E 57  ? 2.88699 3.04966 2.94316 0.29443  -0.67279 -0.86615 37  ASN E OD1 
7867 N ND2 . ASN E 57  ? 2.92906 3.09667 3.05937 0.23247  -0.62233 -0.91407 37  ASN E ND2 
7868 N N   . TYR E 58  ? 2.83361 2.79914 2.79044 0.30850  -0.61455 -0.72182 38  TYR E N   
7869 C CA  . TYR E 58  ? 2.80599 2.70447 2.71919 0.31897  -0.60557 -0.67352 38  TYR E CA  
7870 C C   . TYR E 58  ? 2.81051 2.66965 2.67295 0.32061  -0.60410 -0.65297 38  TYR E C   
7871 O O   . TYR E 58  ? 2.79306 2.64273 2.61983 0.34680  -0.62459 -0.62322 38  TYR E O   
7872 C CB  . TYR E 58  ? 2.76888 2.67817 2.67717 0.35337  -0.63349 -0.64760 38  TYR E CB  
7873 C CG  . TYR E 58  ? 2.75950 2.69835 2.71308 0.35528  -0.63324 -0.66199 38  TYR E CG  
7874 C CD1 . TYR E 58  ? 2.77689 2.78580 2.78222 0.35049  -0.64247 -0.70569 38  TYR E CD1 
7875 C CD2 . TYR E 58  ? 2.73341 2.63142 2.67885 0.36385  -0.62534 -0.63264 38  TYR E CD2 
7876 C CE1 . TYR E 58  ? 2.77046 2.80950 2.81925 0.35333  -0.64100 -0.71971 38  TYR E CE1 
7877 C CE2 . TYR E 58  ? 2.72880 2.65400 2.71316 0.36776  -0.62472 -0.64629 38  TYR E CE2 
7878 C CZ  . TYR E 58  ? 2.74792 2.74469 2.78431 0.36239  -0.63149 -0.68970 38  TYR E CZ  
7879 O OH  . TYR E 58  ? 2.74505 2.77186 2.82254 0.36694  -0.62930 -0.70440 38  TYR E OH  
7880 N N   . LEU E 59  ? 2.81312 2.64809 2.67288 0.29181  -0.57828 -0.66910 39  LEU E N   
7881 C CA  . LEU E 59  ? 2.81947 2.61617 2.63398 0.29112  -0.57316 -0.65357 39  LEU E CA  
7882 C C   . LEU E 59  ? 2.82235 2.55332 2.62470 0.26542  -0.53804 -0.64391 39  LEU E C   
7883 O O   . LEU E 59  ? 2.84360 2.57119 2.67551 0.23840  -0.51571 -0.66731 39  LEU E O   
7884 C CB  . LEU E 59  ? 2.85370 2.69114 2.67042 0.28588  -0.58443 -0.68886 39  LEU E CB  
7885 C CG  . LEU E 59  ? 2.86487 2.67386 2.62926 0.29638  -0.58744 -0.67004 39  LEU E CG  
7886 C CD1 . LEU E 59  ? 2.86819 2.70076 2.60461 0.33274  -0.61904 -0.64731 39  LEU E CD1 
7887 C CD2 . LEU E 59  ? 2.90185 2.72447 2.66753 0.27785  -0.58265 -0.70746 39  LEU E CD2 
7888 N N   . ALA E 60  ? 2.84907 2.52743 2.60799 0.27410  -0.53318 -0.60944 40  ALA E N   
7889 C CA  . ALA E 60  ? 2.84124 2.45168 2.58274 0.25434  -0.50376 -0.59687 40  ALA E CA  
7890 C C   . ALA E 60  ? 2.84873 2.43317 2.55355 0.25429  -0.50035 -0.59057 40  ALA E C   
7891 O O   . ALA E 60  ? 2.84351 2.43937 2.52291 0.27812  -0.51865 -0.57176 40  ALA E O   
7892 C CB  . ALA E 60  ? 2.79323 2.35550 2.52179 0.26661  -0.49980 -0.55713 40  ALA E CB  
7893 N N   . TRP E 61  ? 2.90298 2.45158 2.60429 0.22778  -0.47623 -0.60634 41  TRP E N   
7894 C CA  . TRP E 61  ? 2.88013 2.39741 2.54772 0.22580  -0.46959 -0.60247 41  TRP E CA  
7895 C C   . TRP E 61  ? 2.81268 2.25428 2.45721 0.22093  -0.44954 -0.57282 41  TRP E C   
7896 O O   . TRP E 61  ? 2.81150 2.21905 2.46770 0.20354  -0.43159 -0.57391 41  TRP E O   
7897 C CB  . TRP E 61  ? 2.96197 2.49372 2.64178 0.20047  -0.46058 -0.64563 41  TRP E CB  
7898 C CG  . TRP E 61  ? 2.99368 2.59928 2.69946 0.20417  -0.48185 -0.67939 41  TRP E CG  
7899 C CD1 . TRP E 61  ? 2.99992 2.65276 2.74883 0.19923  -0.48897 -0.70011 41  TRP E CD1 
7900 C CD2 . TRP E 61  ? 3.01761 2.65798 2.70800 0.21478  -0.49967 -0.69803 41  TRP E CD2 
7901 N NE1 . TRP E 61  ? 3.02050 2.73551 2.78419 0.20611  -0.51188 -0.73090 41  TRP E NE1 
7902 C CE2 . TRP E 61  ? 3.03368 2.74083 2.75955 0.21609  -0.51929 -0.73006 41  TRP E CE2 
7903 C CE3 . TRP E 61  ? 3.03117 2.65297 2.68069 0.22456  -0.50111 -0.69160 41  TRP E CE3 
7904 C CZ2 . TRP E 61  ? 3.06217 2.81485 2.78121 0.22739  -0.54209 -0.75561 41  TRP E CZ2 
7905 C CZ3 . TRP E 61  ? 3.06461 2.73191 2.70520 0.23576  -0.52161 -0.71634 41  TRP E CZ3 
7906 C CH2 . TRP E 61  ? 3.07971 2.81033 2.75357 0.23736  -0.54278 -0.74796 41  TRP E CH2 
7907 N N   . TYR E 62  ? 2.90697 2.32231 2.51853 0.23712  -0.45265 -0.54656 42  TYR E N   
7908 C CA  . TYR E 62  ? 2.86595 2.21150 2.45667 0.23648  -0.43775 -0.51758 42  TYR E CA  
7909 C C   . TYR E 62  ? 2.87506 2.19272 2.44010 0.23093  -0.42756 -0.52315 42  TYR E C   
7910 O O   . TYR E 62  ? 2.91867 2.27198 2.47337 0.23861  -0.43685 -0.53594 42  TYR E O   
7911 C CB  . TYR E 62  ? 2.81082 2.14637 2.39145 0.26400  -0.45145 -0.47448 42  TYR E CB  
7912 C CG  . TYR E 62  ? 2.79496 2.15530 2.39851 0.27338  -0.46422 -0.46689 42  TYR E CG  
7913 C CD1 . TYR E 62  ? 2.81383 2.23842 2.43049 0.28786  -0.48608 -0.47527 42  TYR E CD1 
7914 C CD2 . TYR E 62  ? 2.75780 2.07577 2.36774 0.26968  -0.45577 -0.45200 42  TYR E CD2 
7915 C CE1 . TYR E 62  ? 2.79566 2.24317 2.43411 0.29798  -0.49900 -0.46971 42  TYR E CE1 
7916 C CE2 . TYR E 62  ? 2.74495 2.08562 2.37508 0.27989  -0.46766 -0.44642 42  TYR E CE2 
7917 C CZ  . TYR E 62  ? 2.76116 2.16736 2.40691 0.29391  -0.48923 -0.45552 42  TYR E CZ  
7918 O OH  . TYR E 62  ? 2.74699 2.17604 2.41370 0.30554  -0.50227 -0.45125 42  TYR E OH  
7919 N N   . GLN E 63  ? 3.04933 2.30143 2.60220 0.21906  -0.40924 -0.51413 43  GLN E N   
7920 C CA  . GLN E 63  ? 3.02761 2.24462 2.55663 0.21425  -0.39862 -0.51834 43  GLN E CA  
7921 C C   . GLN E 63  ? 2.94631 2.11972 2.45663 0.23285  -0.39849 -0.47869 43  GLN E C   
7922 O O   . GLN E 63  ? 2.90504 2.02803 2.41554 0.23014  -0.39148 -0.46037 43  GLN E O   
7923 C CB  . GLN E 63  ? 3.06054 2.23452 2.59135 0.18410  -0.37824 -0.54401 43  GLN E CB  
7924 C CG  . GLN E 63  ? 3.03825 2.15587 2.54291 0.18069  -0.36647 -0.54097 43  GLN E CG  
7925 C CD  . GLN E 63  ? 3.11376 2.20356 2.61836 0.15124  -0.35059 -0.57496 43  GLN E CD  
7926 O OE1 . GLN E 63  ? 3.12566 2.24269 2.62974 0.14456  -0.35288 -0.60357 43  GLN E OE1 
7927 N NE2 . GLN E 63  ? 3.17073 2.20327 2.67383 0.13388  -0.33489 -0.57183 43  GLN E NE2 
7928 N N   . GLN E 64  ? 3.03797 2.23099 2.53262 0.25212  -0.40625 -0.46584 44  GLN E N   
7929 C CA  . GLN E 64  ? 3.01418 2.17297 2.49585 0.26984  -0.40565 -0.42941 44  GLN E CA  
7930 C C   . GLN E 64  ? 3.05180 2.17706 2.51444 0.26422  -0.39204 -0.43962 44  GLN E C   
7931 O O   . GLN E 64  ? 3.10605 2.25937 2.55433 0.27391  -0.39363 -0.44569 44  GLN E O   
7932 C CB  . GLN E 64  ? 3.02874 2.23192 2.50701 0.29590  -0.42162 -0.40434 44  GLN E CB  
7933 C CG  . GLN E 64  ? 3.01369 2.18352 2.48804 0.31307  -0.42164 -0.36317 44  GLN E CG  
7934 C CD  . GLN E 64  ? 3.06540 2.26367 2.52352 0.33246  -0.42427 -0.34755 44  GLN E CD  
7935 O OE1 . GLN E 64  ? 3.07993 2.25164 2.52781 0.33594  -0.41306 -0.33898 44  GLN E OE1 
7936 N NE2 . GLN E 64  ? 3.10712 2.35890 2.56195 0.34605  -0.43883 -0.34358 44  GLN E NE2 
7937 N N   . LYS E 65  ? 3.14485 2.20828 2.60518 0.24962  -0.37902 -0.44212 45  LYS E N   
7938 C CA  . LYS E 65  ? 3.18176 2.20616 2.62477 0.24543  -0.36730 -0.45088 45  LYS E CA  
7939 C C   . LYS E 65  ? 3.20094 2.22602 2.63599 0.26952  -0.37007 -0.42163 45  LYS E C   
7940 O O   . LYS E 65  ? 3.15496 2.17848 2.59950 0.28469  -0.37773 -0.38834 45  LYS E O   
7941 C CB  . LYS E 65  ? 3.17121 2.12221 2.61101 0.22920  -0.35548 -0.45232 45  LYS E CB  
7942 C CG  . LYS E 65  ? 3.17857 2.12143 2.62571 0.20320  -0.34815 -0.47863 45  LYS E CG  
7943 C CD  . LYS E 65  ? 3.28416 2.23741 2.72587 0.18440  -0.34069 -0.51776 45  LYS E CD  
7944 C CE  . LYS E 65  ? 3.31193 2.21875 2.75410 0.15557  -0.32621 -0.53814 45  LYS E CE  
7945 N NZ  . LYS E 65  ? 3.29528 2.12037 2.71715 0.15337  -0.31664 -0.52575 45  LYS E NZ  
7946 N N   . PRO E 66  ? 3.19366 2.22172 2.61295 0.27368  -0.36370 -0.43329 46  PRO E N   
7947 C CA  . PRO E 66  ? 3.23342 2.26245 2.64751 0.29573  -0.36269 -0.40572 46  PRO E CA  
7948 C C   . PRO E 66  ? 3.18467 2.15335 2.60801 0.29898  -0.35934 -0.37995 46  PRO E C   
7949 O O   . PRO E 66  ? 3.14705 2.06095 2.56670 0.28536  -0.35217 -0.39258 46  PRO E O   
7950 C CB  . PRO E 66  ? 3.28309 2.31875 2.67738 0.29559  -0.35389 -0.43148 46  PRO E CB  
7951 C CG  . PRO E 66  ? 3.26261 2.27451 2.65365 0.27057  -0.34923 -0.46903 46  PRO E CG  
7952 C CD  . PRO E 66  ? 3.24680 2.27863 2.65359 0.25876  -0.35701 -0.47298 46  PRO E CD  
7953 N N   . GLY E 67  ? 3.26370 2.24102 2.69891 0.31749  -0.36581 -0.34364 47  GLY E N   
7954 C CA  . GLY E 67  ? 3.21872 2.14293 2.66739 0.32274  -0.36689 -0.31767 47  GLY E CA  
7955 C C   . GLY E 67  ? 3.12991 2.01850 2.58529 0.31106  -0.37267 -0.31745 47  GLY E C   
7956 O O   . GLY E 67  ? 3.09992 1.92708 2.55306 0.30432  -0.36905 -0.31875 47  GLY E O   
7957 N N   . GLN E 68  ? 3.06633 1.99219 2.52825 0.30985  -0.38185 -0.31622 48  GLN E N   
7958 C CA  . GLN E 68  ? 3.00410 1.90379 2.47119 0.29860  -0.38536 -0.31956 48  GLN E CA  
7959 C C   . GLN E 68  ? 2.97857 1.93076 2.45782 0.30533  -0.39850 -0.31129 48  GLN E C   
7960 O O   . GLN E 68  ? 3.01303 2.02186 2.49194 0.31412  -0.40386 -0.31146 48  GLN E O   
7961 C CB  . GLN E 68  ? 3.01972 1.89809 2.47434 0.27404  -0.37294 -0.35604 48  GLN E CB  
7962 C CG  . GLN E 68  ? 2.98292 1.82043 2.43838 0.26102  -0.37100 -0.35893 48  GLN E CG  
7963 C CD  . GLN E 68  ? 3.00192 1.79702 2.44181 0.23716  -0.35546 -0.38840 48  GLN E CD  
7964 O OE1 . GLN E 68  ? 3.01120 1.80640 2.45221 0.21936  -0.34918 -0.40612 48  GLN E OE1 
7965 N NE2 . GLN E 68  ? 3.05026 1.80815 2.47648 0.23659  -0.34871 -0.39376 48  GLN E NE2 
7966 N N   . SER E 69  ? 2.95142 1.88217 2.43914 0.30263  -0.40430 -0.30427 49  SER E N   
7967 C CA  . SER E 69  ? 2.92552 1.90050 2.42600 0.30802  -0.41713 -0.30013 49  SER E CA  
7968 C C   . SER E 69  ? 2.95137 1.96371 2.45203 0.29010  -0.41155 -0.33647 49  SER E C   
7969 O O   . SER E 69  ? 2.97361 1.96183 2.46569 0.27014  -0.39682 -0.36260 49  SER E O   
7970 C CB  . SER E 69  ? 2.86112 1.79654 2.36988 0.31274  -0.42477 -0.28122 49  SER E CB  
7971 O OG  . SER E 69  ? 2.85280 1.73380 2.35083 0.29561  -0.41180 -0.29720 49  SER E OG  
7972 N N   . PRO E 70  ? 2.77585 1.84668 2.28786 0.29679  -0.42401 -0.33932 50  PRO E N   
7973 C CA  . PRO E 70  ? 2.80558 1.91617 2.32470 0.28032  -0.42079 -0.37511 50  PRO E CA  
7974 C C   . PRO E 70  ? 2.78412 1.87138 2.31420 0.26587  -0.41434 -0.38510 50  PRO E C   
7975 O O   . PRO E 70  ? 2.73823 1.79005 2.27013 0.27381  -0.41799 -0.36245 50  PRO E O   
7976 C CB  . PRO E 70  ? 2.83835 2.01686 2.36602 0.29724  -0.43986 -0.37066 50  PRO E CB  
7977 C CG  . PRO E 70  ? 2.82617 1.99901 2.34571 0.32049  -0.44924 -0.33309 50  PRO E CG  
7978 C CD  . PRO E 70  ? 2.77006 1.87594 2.28904 0.32031  -0.44245 -0.31105 50  PRO E CD  
7979 N N   . LYS E 71  ? 2.73073 1.83883 2.26851 0.24441  -0.40434 -0.42031 51  LYS E N   
7980 C CA  . LYS E 71  ? 2.77668 1.86856 2.32577 0.22781  -0.39388 -0.43348 51  LYS E CA  
7981 C C   . LYS E 71  ? 2.86589 2.02104 2.43844 0.21467  -0.39432 -0.46762 51  LYS E C   
7982 O O   . LYS E 71  ? 2.92307 2.11284 2.49672 0.20852  -0.39555 -0.49011 51  LYS E O   
7983 C CB  . LYS E 71  ? 2.72936 1.75047 2.26092 0.20737  -0.37213 -0.44087 51  LYS E CB  
7984 C CG  . LYS E 71  ? 2.69060 1.64350 2.20263 0.22036  -0.37305 -0.40874 51  LYS E CG  
7985 C CD  . LYS E 71  ? 2.69273 1.57278 2.18400 0.20115  -0.35332 -0.41741 51  LYS E CD  
7986 C CE  . LYS E 71  ? 2.74375 1.61595 2.22341 0.18937  -0.34459 -0.43625 51  LYS E CE  
7987 N NZ  . LYS E 71  ? 2.72472 1.59404 2.19639 0.21016  -0.35532 -0.41578 51  LYS E NZ  
7988 N N   . LEU E 72  ? 2.70728 1.87712 2.29964 0.21110  -0.39372 -0.47261 52  LEU E N   
7989 C CA  . LEU E 72  ? 2.80103 2.03719 2.42347 0.20186  -0.39704 -0.50351 52  LEU E CA  
7990 C C   . LEU E 72  ? 2.87221 2.10454 2.50259 0.16969  -0.37608 -0.53986 52  LEU E C   
7991 O O   . LEU E 72  ? 2.89375 2.06543 2.50869 0.15179  -0.35514 -0.54030 52  LEU E O   
7992 C CB  . LEU E 72  ? 2.79549 2.04592 2.43847 0.20770  -0.40036 -0.49847 52  LEU E CB  
7993 C CG  . LEU E 72  ? 2.84647 2.16360 2.52738 0.19736  -0.40160 -0.53143 52  LEU E CG  
7994 C CD1 . LEU E 72  ? 2.83349 2.22143 2.52754 0.21576  -0.42851 -0.53834 52  LEU E CD1 
7995 C CD2 . LEU E 72  ? 2.90357 2.21839 2.60049 0.20009  -0.39733 -0.52632 52  LEU E CD2 
7996 N N   . LEU E 73  ? 2.83672 2.13314 2.49142 0.16273  -0.38329 -0.57093 53  LEU E N   
7997 C CA  . LEU E 73  ? 2.91581 2.21812 2.58608 0.13159  -0.36643 -0.60872 53  LEU E CA  
7998 C C   . LEU E 73  ? 3.00978 2.36224 2.72312 0.11826  -0.36296 -0.63440 53  LEU E C   
7999 O O   . LEU E 73  ? 3.05924 2.38286 2.78179 0.09707  -0.33992 -0.64063 53  LEU E O   
8000 C CB  . LEU E 73  ? 2.92661 2.25887 2.59100 0.13249  -0.37745 -0.62847 53  LEU E CB  
8001 C CG  . LEU E 73  ? 2.88153 2.17561 2.50629 0.14926  -0.38194 -0.60393 53  LEU E CG  
8002 C CD1 . LEU E 73  ? 2.90709 2.23667 2.52530 0.15187  -0.39283 -0.62638 53  LEU E CD1 
8003 C CD2 . LEU E 73  ? 2.88576 2.09845 2.48722 0.13439  -0.35967 -0.59336 53  LEU E CD2 
8004 N N   . ILE E 74  ? 2.89634 2.32317 2.63622 0.13058  -0.38491 -0.64995 54  ILE E N   
8005 C CA  . ILE E 74  ? 2.93651 2.41912 2.72350 0.11964  -0.38406 -0.67752 54  ILE E CA  
8006 C C   . ILE E 74  ? 2.89514 2.42107 2.69337 0.14996  -0.40843 -0.66136 54  ILE E C   
8007 O O   . ILE E 74  ? 2.85638 2.40376 2.63812 0.17627  -0.43387 -0.64697 54  ILE E O   
8008 C CB  . ILE E 74  ? 2.97797 2.51442 2.79497 0.10288  -0.38949 -0.72100 54  ILE E CB  
8009 C CG1 . ILE E 74  ? 2.94681 2.52261 2.74885 0.12825  -0.42022 -0.72125 54  ILE E CG1 
8010 C CG2 . ILE E 74  ? 3.02983 2.52073 2.83988 0.07015  -0.36430 -0.73887 54  ILE E CG2 
8011 C CD1 . ILE E 74  ? 2.97427 2.61966 2.81278 0.12081  -0.43522 -0.76460 54  ILE E CD1 
8012 N N   . TYR E 75  ? 2.85555 2.39204 2.67990 0.14671  -0.40001 -0.66315 55  TYR E N   
8013 C CA  . TYR E 75  ? 2.82371 2.40820 2.66728 0.17298  -0.42320 -0.65566 55  TYR E CA  
8014 C C   . TYR E 75  ? 2.85360 2.51512 2.75159 0.16303  -0.42855 -0.69675 55  TYR E C   
8015 O O   . TYR E 75  ? 2.90595 2.57664 2.83094 0.13232  -0.40795 -0.72814 55  TYR E O   
8016 C CB  . TYR E 75  ? 2.80561 2.34935 2.63977 0.18194  -0.41361 -0.62795 55  TYR E CB  
8017 C CG  . TYR E 75  ? 2.86917 2.37389 2.70988 0.15323  -0.37778 -0.63752 55  TYR E CG  
8018 C CD1 . TYR E 75  ? 2.87935 2.30784 2.68390 0.13726  -0.35522 -0.62410 55  TYR E CD1 
8019 C CD2 . TYR E 75  ? 2.91930 2.46176 2.80078 0.14327  -0.36617 -0.65909 55  TYR E CD2 
8020 C CE1 . TYR E 75  ? 2.94953 2.33720 2.75405 0.11176  -0.32233 -0.63097 55  TYR E CE1 
8021 C CE2 . TYR E 75  ? 2.98974 2.49461 2.87364 0.11693  -0.33070 -0.66596 55  TYR E CE2 
8022 C CZ  . TYR E 75  ? 3.01064 2.43619 2.85362 0.10124  -0.30905 -0.65109 55  TYR E CZ  
8023 O OH  . TYR E 75  ? 3.09003 2.47331 2.92974 0.07554  -0.27359 -0.65639 55  TYR E OH  
8024 N N   . TRP E 76  ? 2.81407 2.53086 2.72955 0.18964  -0.45769 -0.69660 56  TRP E N   
8025 C CA  . TRP E 76  ? 2.83167 2.62867 2.79984 0.18716  -0.47105 -0.73552 56  TRP E CA  
8026 C C   . TRP E 76  ? 2.85456 2.68348 2.83353 0.17289  -0.47791 -0.76880 56  TRP E C   
8027 O O   . TRP E 76  ? 2.88313 2.76769 2.91230 0.15759  -0.47850 -0.80872 56  TRP E O   
8028 C CB  . TRP E 76  ? 2.87692 2.68853 2.89038 0.16508  -0.44520 -0.75656 56  TRP E CB  
8029 C CG  . TRP E 76  ? 2.85920 2.65125 2.86681 0.18268  -0.44262 -0.73016 56  TRP E CG  
8030 C CD1 . TRP E 76  ? 2.88897 2.62207 2.87996 0.17077  -0.41257 -0.71262 56  TRP E CD1 
8031 C CD2 . TRP E 76  ? 2.81285 2.64139 2.82837 0.21697  -0.47296 -0.71869 56  TRP E CD2 
8032 N NE1 . TRP E 76  ? 2.86255 2.59452 2.85141 0.19589  -0.42250 -0.69205 56  TRP E NE1 
8033 C CE2 . TRP E 76  ? 2.81341 2.60348 2.81847 0.22412  -0.45956 -0.69527 56  TRP E CE2 
8034 C CE3 . TRP E 76  ? 2.77492 2.66231 2.80293 0.24328  -0.51131 -0.72619 56  TRP E CE3 
8035 C CZ2 . TRP E 76  ? 2.77334 2.58274 2.78275 0.25607  -0.48347 -0.67995 56  TRP E CZ2 
8036 C CZ3 . TRP E 76  ? 2.73697 2.64214 2.76830 0.27453  -0.53468 -0.70981 56  TRP E CZ3 
8037 C CH2 . TRP E 76  ? 2.73384 2.60067 2.75732 0.28045  -0.52084 -0.68729 56  TRP E CH2 
8038 N N   . ALA E 77  ? 2.86986 2.66518 2.80428 0.17803  -0.48333 -0.75435 57  ALA E N   
8039 C CA  . ALA E 77  ? 2.89066 2.70952 2.82426 0.17003  -0.49317 -0.78228 57  ALA E CA  
8040 C C   . ALA E 77  ? 2.94535 2.76381 2.91218 0.13031  -0.46782 -0.81946 57  ALA E C   
8041 O O   . ALA E 77  ? 2.96448 2.81009 2.94115 0.12146  -0.47754 -0.85021 57  ALA E O   
8042 C CB  . ALA E 77  ? 2.87820 2.77164 2.83108 0.19357  -0.53076 -0.80234 57  ALA E CB  
8043 N N   . SER E 78  ? 2.81582 2.60172 2.79835 0.10621  -0.43567 -0.81734 58  SER E N   
8044 C CA  . SER E 78  ? 2.87833 2.65950 2.89281 0.06628  -0.40871 -0.85007 58  SER E CA  
8045 C C   . SER E 78  ? 2.91523 2.62368 2.91127 0.04510  -0.37083 -0.82942 58  SER E C   
8046 O O   . SER E 78  ? 2.96842 2.62473 2.94387 0.02193  -0.35061 -0.83158 58  SER E O   
8047 C CB  . SER E 78  ? 2.92386 2.78216 3.00885 0.05500  -0.41294 -0.89007 58  SER E CB  
8048 O OG  . SER E 78  ? 2.98226 2.83331 3.10203 0.01385  -0.38309 -0.91902 58  SER E OG  
8049 N N   . THR E 79  ? 2.91163 2.61444 2.91287 0.05411  -0.36221 -0.81022 59  THR E N   
8050 C CA  . THR E 79  ? 2.95095 2.58235 2.92889 0.03825  -0.32820 -0.78884 59  THR E CA  
8051 C C   . THR E 79  ? 2.91838 2.47257 2.83231 0.04878  -0.32797 -0.75376 59  THR E C   
8052 O O   . THR E 79  ? 2.85216 2.40728 2.73832 0.07942  -0.35377 -0.73036 59  THR E O   
8053 C CB  . THR E 79  ? 2.94540 2.58711 2.93504 0.05365  -0.32501 -0.77314 59  THR E CB  
8054 O OG1 . THR E 79  ? 2.94466 2.67159 2.99485 0.05474  -0.33618 -0.80450 59  THR E OG1 
8055 C CG2 . THR E 79  ? 3.01773 2.59881 2.99583 0.03036  -0.28521 -0.76378 59  THR E CG2 
8056 N N   . ARG E 80  ? 2.99267 2.47930 2.88401 0.02321  -0.29863 -0.75020 60  ARG E N   
8057 C CA  . ARG E 80  ? 2.96306 2.37520 2.79771 0.03088  -0.29729 -0.72107 60  ARG E CA  
8058 C C   . ARG E 80  ? 2.96660 2.31142 2.76910 0.03670  -0.28062 -0.68765 60  ARG E C   
8059 O O   . ARG E 80  ? 3.01806 2.35918 2.83695 0.02451  -0.25996 -0.69132 60  ARG E O   
8060 C CB  . ARG E 80  ? 3.02448 2.40044 2.84934 0.00158  -0.28099 -0.74027 60  ARG E CB  
8061 C CG  . ARG E 80  ? 3.11918 2.45036 2.95018 -0.03390 -0.24397 -0.75011 60  ARG E CG  
8062 C CD  . ARG E 80  ? 3.14215 2.42491 2.95392 -0.05854 -0.23150 -0.76306 60  ARG E CD  
8063 N NE  . ARG E 80  ? 3.11827 2.45649 2.95541 -0.06176 -0.25093 -0.79442 60  ARG E NE  
8064 C CZ  . ARG E 80  ? 3.15603 2.53942 3.04192 -0.08864 -0.24462 -0.83316 60  ARG E CZ  
8065 N NH1 . ARG E 80  ? 3.22662 2.60842 3.14382 -0.11702 -0.21639 -0.84530 60  ARG E NH1 
8066 N NH2 . ARG E 80  ? 3.12734 2.55851 3.03136 -0.08682 -0.26697 -0.86076 60  ARG E NH2 
8067 N N   . GLU E 81  ? 3.09216 2.38380 2.84859 0.05640  -0.29005 -0.65549 61  GLU E N   
8068 C CA  . GLU E 81  ? 3.08517 2.30686 2.80650 0.06538  -0.27932 -0.62281 61  GLU E CA  
8069 C C   . GLU E 81  ? 3.15797 2.30698 2.85691 0.03561  -0.24690 -0.62689 61  GLU E C   
8070 O O   . GLU E 81  ? 3.20489 2.34642 2.90654 0.01169  -0.23655 -0.64867 61  GLU E O   
8071 C CB  . GLU E 81  ? 2.99308 2.18478 2.67837 0.09556  -0.30161 -0.58898 61  GLU E CB  
8072 C CG  . GLU E 81  ? 2.95204 2.08078 2.60646 0.11175  -0.29916 -0.55429 61  GLU E CG  
8073 C CD  . GLU E 81  ? 2.95418 2.11382 2.62961 0.12419  -0.30294 -0.55004 61  GLU E CD  
8074 O OE1 . GLU E 81  ? 2.90169 2.11915 2.59739 0.14666  -0.32826 -0.54655 61  GLU E OE1 
8075 O OE2 . GLU E 81  ? 3.01131 2.13657 2.68132 0.11209  -0.28041 -0.55065 61  GLU E OE2 
8076 N N   . SER E 82  ? 3.12218 2.21502 2.79690 0.03797  -0.23173 -0.60598 62  SER E N   
8077 C CA  . SER E 82  ? 3.20742 2.21881 2.84971 0.01437  -0.20287 -0.60363 62  SER E CA  
8078 C C   . SER E 82  ? 3.16675 2.11934 2.76891 0.02053  -0.21131 -0.58876 62  SER E C   
8079 O O   . SER E 82  ? 3.06843 2.00977 2.65146 0.04960  -0.23359 -0.56307 62  SER E O   
8080 C CB  . SER E 82  ? 3.23268 2.19497 2.85131 0.02138  -0.18852 -0.58236 62  SER E CB  
8081 O OG  . SER E 82  ? 3.12227 2.05736 2.71334 0.05569  -0.21169 -0.54945 62  SER E OG  
8082 N N   . GLY E 83  ? 3.36477 2.28031 2.95643 -0.00695 -0.19349 -0.60540 63  GLY E N   
8083 C CA  . GLY E 83  ? 3.32848 2.19305 2.88635 -0.00271 -0.20086 -0.59685 63  GLY E CA  
8084 C C   . GLY E 83  ? 3.28198 2.20108 2.85795 0.00256  -0.22089 -0.61302 63  GLY E C   
8085 O O   . GLY E 83  ? 3.24480 2.12971 2.79410 0.01176  -0.22979 -0.60429 63  GLY E O   
8086 N N   . VAL E 84  ? 3.29227 2.29437 2.91170 -0.00162 -0.22868 -0.63694 64  VAL E N   
8087 C CA  . VAL E 84  ? 3.25626 2.31380 2.89144 0.00436  -0.24884 -0.65516 64  VAL E CA  
8088 C C   . VAL E 84  ? 3.31488 2.37484 2.96699 -0.02977 -0.23411 -0.69177 64  VAL E C   
8089 O O   . VAL E 84  ? 3.38048 2.45321 3.06111 -0.05553 -0.21502 -0.71091 64  VAL E O   
8090 C CB  . VAL E 84  ? 3.20613 2.35231 2.87688 0.02336  -0.27089 -0.66020 64  VAL E CB  
8091 C CG1 . VAL E 84  ? 3.20486 2.41164 2.89601 0.02224  -0.28767 -0.68879 64  VAL E CG1 
8092 C CG2 . VAL E 84  ? 3.11200 2.25395 2.76242 0.05948  -0.29071 -0.62330 64  VAL E CG2 
8093 N N   . PRO E 85  ? 3.35351 2.40114 2.99037 -0.03121 -0.24164 -0.70263 65  PRO E N   
8094 C CA  . PRO E 85  ? 3.40060 2.44294 3.05207 -0.06408 -0.22886 -0.73769 65  PRO E CA  
8095 C C   . PRO E 85  ? 3.41701 2.54294 3.12346 -0.07787 -0.23367 -0.77202 65  PRO E C   
8096 O O   . PRO E 85  ? 3.36929 2.56503 3.09524 -0.05639 -0.25759 -0.77624 65  PRO E O   
8097 C CB  . PRO E 85  ? 3.35820 2.38419 2.98245 -0.05247 -0.24363 -0.74071 65  PRO E CB  
8098 C CG  . PRO E 85  ? 3.30742 2.29835 2.89434 -0.02091 -0.25296 -0.70141 65  PRO E CG  
8099 C CD  . PRO E 85  ? 3.28909 2.32109 2.89329 -0.00321 -0.26038 -0.68248 65  PRO E CD  
8100 N N   . ASP E 86  ? 3.39915 2.51596 3.13116 -0.11433 -0.21077 -0.79685 66  ASP E N   
8101 C CA  . ASP E 86  ? 3.42015 2.61443 3.21171 -0.13156 -0.21293 -0.83246 66  ASP E CA  
8102 C C   . ASP E 86  ? 3.37611 2.62467 3.18382 -0.12465 -0.23987 -0.86110 66  ASP E C   
8103 O O   . ASP E 86  ? 3.37039 2.69530 3.22670 -0.12775 -0.25205 -0.88848 66  ASP E O   
8104 C CB  . ASP E 86  ? 3.50880 2.67474 3.32369 -0.17506 -0.18063 -0.85299 66  ASP E CB  
8105 C CG  . ASP E 86  ? 3.56862 2.73683 3.40104 -0.18359 -0.15722 -0.84130 66  ASP E CG  
8106 O OD1 . ASP E 86  ? 3.53882 2.72139 3.36027 -0.15469 -0.16689 -0.81564 66  ASP E OD1 
8107 O OD2 . ASP E 86  ? 3.64651 2.80213 3.50398 -0.21921 -0.12872 -0.85805 66  ASP E OD2 
8108 N N   . ARG E 87  ? 3.34944 2.56054 3.11737 -0.11423 -0.25001 -0.85669 67  ARG E N   
8109 C CA  . ARG E 87  ? 3.31465 2.57394 3.09088 -0.10469 -0.27579 -0.88344 67  ARG E CA  
8110 C C   . ARG E 87  ? 3.26417 2.59408 3.04654 -0.06909 -0.30450 -0.87517 67  ARG E C   
8111 O O   . ARG E 87  ? 3.25258 2.64471 3.05833 -0.06359 -0.32642 -0.90368 67  ARG E O   
8112 C CB  . ARG E 87  ? 3.30067 2.50128 3.02916 -0.09869 -0.27837 -0.87830 67  ARG E CB  
8113 C CG  . ARG E 87  ? 3.26877 2.41429 2.94704 -0.07331 -0.27614 -0.83447 67  ARG E CG  
8114 C CD  . ARG E 87  ? 3.26321 2.35172 2.90031 -0.06996 -0.27688 -0.83399 67  ARG E CD  
8115 N NE  . ARG E 87  ? 3.22401 2.26684 2.81854 -0.04359 -0.27766 -0.79429 67  ARG E NE  
8116 C CZ  . ARG E 87  ? 3.23507 2.19836 2.80161 -0.05062 -0.25987 -0.77314 67  ARG E CZ  
8117 N NH1 . ARG E 87  ? 3.23281 2.14832 2.80358 -0.08328 -0.23794 -0.78523 67  ARG E NH1 
8118 N NH2 . ARG E 87  ? 3.25259 2.18219 2.78606 -0.02415 -0.26454 -0.73902 67  ARG E NH2 
8119 N N   . PHE E 88  ? 3.27839 2.59780 3.03933 -0.04440 -0.30612 -0.83706 68  PHE E N   
8120 C CA  . PHE E 88  ? 3.23435 2.61439 2.99856 -0.01036 -0.33267 -0.82490 68  PHE E CA  
8121 C C   . PHE E 88  ? 3.24798 2.69488 3.06639 -0.01759 -0.33610 -0.84418 68  PHE E C   
8122 O O   . PHE E 88  ? 3.25988 2.69877 3.09074 -0.02133 -0.32178 -0.82865 68  PHE E O   
8123 C CB  . PHE E 88  ? 3.20196 2.54397 2.92830 0.01640  -0.33307 -0.77793 68  PHE E CB  
8124 C CG  . PHE E 88  ? 3.17895 2.46801 2.85682 0.02955  -0.33437 -0.75883 68  PHE E CG  
8125 C CD1 . PHE E 88  ? 3.14953 2.46891 2.80779 0.05684  -0.35704 -0.75446 68  PHE E CD1 
8126 C CD2 . PHE E 88  ? 3.19257 2.40114 2.84366 0.01569  -0.31268 -0.74520 68  PHE E CD2 
8127 C CE1 . PHE E 88  ? 3.13471 2.40893 2.75168 0.06927  -0.35626 -0.73759 68  PHE E CE1 
8128 C CE2 . PHE E 88  ? 3.17027 2.33253 2.78080 0.02890  -0.31461 -0.72930 68  PHE E CE2 
8129 C CZ  . PHE E 88  ? 3.14024 2.33727 2.73574 0.05540  -0.33553 -0.72579 68  PHE E CZ  
8130 N N   . THR E 89  ? 3.19424 2.70786 3.04519 -0.01810 -0.35612 -0.87936 69  THR E N   
8131 C CA  . THR E 89  ? 3.20372 2.78941 3.11199 -0.02319 -0.36366 -0.90315 69  THR E CA  
8132 C C   . THR E 89  ? 3.16587 2.81663 3.07329 0.01232  -0.40064 -0.90440 69  THR E C   
8133 O O   . THR E 89  ? 3.16509 2.85284 3.07864 0.01614  -0.42171 -0.93314 69  THR E O   
8134 C CB  . THR E 89  ? 3.24541 2.85303 3.20246 -0.05989 -0.35424 -0.94931 69  THR E CB  
8135 O OG1 . THR E 89  ? 3.23697 2.84696 3.17944 -0.05913 -0.37099 -0.97252 69  THR E OG1 
8136 C CG2 . THR E 89  ? 3.29827 2.84211 3.25785 -0.09598 -0.31533 -0.94553 69  THR E CG2 
8137 N N   . GLY E 90  ? 3.04452 2.70640 2.94203 0.03898  -0.40946 -0.87335 70  GLY E N   
8138 C CA  . GLY E 90  ? 3.01421 2.73510 2.91040 0.07277  -0.44403 -0.87189 70  GLY E CA  
8139 C C   . GLY E 90  ? 3.02453 2.82392 2.98086 0.06725  -0.45987 -0.91138 70  GLY E C   
8140 O O   . GLY E 90  ? 3.05197 2.86450 3.05713 0.03824  -0.44153 -0.93520 70  GLY E O   
8141 N N   . SER E 91  ? 3.11655 2.96919 3.06934 0.09632  -0.49476 -0.91839 71  SER E N   
8142 C CA  . SER E 91  ? 3.12275 3.05308 3.13097 0.09565  -0.51644 -0.95881 71  SER E CA  
8143 C C   . SER E 91  ? 3.10187 3.07631 3.09119 0.13722  -0.55461 -0.94838 71  SER E C   
8144 O O   . SER E 91  ? 3.07431 3.01867 3.00805 0.16345  -0.56211 -0.91122 71  SER E O   
8145 C CB  . SER E 91  ? 3.15006 3.09723 3.18138 0.07240  -0.51977 -1.00484 71  SER E CB  
8146 O OG  . SER E 91  ? 3.15172 3.06770 3.12737 0.08483  -0.52912 -0.99814 71  SER E OG  
8147 N N   . GLY E 92  ? 3.11062 3.15617 3.14796 0.14275  -0.57867 -0.98174 72  GLY E N   
8148 C CA  . GLY E 92  ? 3.09816 3.18932 3.12153 0.18156  -0.61785 -0.97753 72  GLY E CA  
8149 C C   . GLY E 92  ? 3.05620 3.18287 3.11517 0.19439  -0.62513 -0.96929 72  GLY E C   
8150 O O   . GLY E 92  ? 3.04190 3.14526 3.11912 0.17974  -0.59794 -0.95333 72  GLY E O   
8151 N N   . SER E 93  ? 3.04034 3.22302 3.10656 0.22400  -0.66378 -0.98112 73  SER E N   
8152 C CA  . SER E 93  ? 3.00755 3.22888 3.10630 0.24154  -0.67739 -0.97602 73  SER E CA  
8153 C C   . SER E 93  ? 2.99743 3.24986 3.06465 0.28438  -0.72175 -0.96782 73  SER E C   
8154 O O   . SER E 93  ? 3.02453 3.29842 3.07425 0.29505  -0.74663 -0.98924 73  SER E O   
8155 C CB  . SER E 93  ? 3.03327 3.31380 3.21691 0.21864  -0.67390 -1.02321 73  SER E CB  
8156 O OG  . SER E 93  ? 2.99235 3.31141 3.20804 0.23745  -0.68710 -1.01940 73  SER E OG  
8157 N N   . GLY E 94  ? 2.90711 3.15904 2.96481 0.30943  -0.73201 -0.93667 74  GLY E N   
8158 C CA  . GLY E 94  ? 2.92032 3.19828 2.94823 0.35060  -0.77385 -0.92559 74  GLY E CA  
8159 C C   . GLY E 94  ? 2.93465 3.16233 2.88145 0.37210  -0.77834 -0.88223 74  GLY E C   
8160 O O   . GLY E 94  ? 2.91851 3.10753 2.83390 0.38609  -0.77215 -0.83669 74  GLY E O   
8161 N N   . THR E 95  ? 3.02630 3.25434 2.93981 0.37500  -0.78882 -0.89657 75  THR E N   
8162 C CA  . THR E 95  ? 3.05090 3.23733 2.88745 0.39632  -0.79283 -0.85900 75  THR E CA  
8163 C C   . THR E 95  ? 3.06520 3.20463 2.87433 0.37283  -0.76233 -0.85614 75  THR E C   
8164 O O   . THR E 95  ? 3.05530 3.14046 2.82051 0.37565  -0.74294 -0.81377 75  THR E O   
8165 C CB  . THR E 95  ? 3.09771 3.32199 2.90343 0.42904  -0.83533 -0.87307 75  THR E CB  
8166 O OG1 . THR E 95  ? 3.12082 3.38728 2.96023 0.41562  -0.84719 -0.92846 75  THR E OG1 
8167 C CG2 . THR E 95  ? 3.08492 3.34353 2.90309 0.45859  -0.86743 -0.86488 75  THR E CG2 
8168 N N   . ASP E 96  ? 3.07159 3.23000 2.90740 0.35004  -0.75866 -0.90091 76  ASP E N   
8169 C CA  . ASP E 96  ? 3.08880 3.20360 2.89926 0.32858  -0.73275 -0.90274 76  ASP E CA  
8170 C C   . ASP E 96  ? 3.05770 3.13965 2.90624 0.29070  -0.69352 -0.90311 76  ASP E C   
8171 O O   . ASP E 96  ? 3.04798 3.16036 2.95853 0.27112  -0.68838 -0.92972 76  ASP E O   
8172 C CB  . ASP E 96  ? 3.13717 3.28450 2.95297 0.32431  -0.75093 -0.95136 76  ASP E CB  
8173 C CG  . ASP E 96  ? 3.15921 3.26166 2.95018 0.30263  -0.72591 -0.95666 76  ASP E CG  
8174 O OD1 . ASP E 96  ? 3.17284 3.23435 2.90125 0.31764  -0.71885 -0.92397 76  ASP E OD1 
8175 O OD2 . ASP E 96  ? 3.16308 3.27106 2.99847 0.27050  -0.71310 -0.99371 76  ASP E OD2 
8176 N N   . PHE E 97  ? 3.18122 3.20034 2.99159 0.28112  -0.66555 -0.87346 77  PHE E N   
8177 C CA  . PHE E 97  ? 3.16431 3.14070 2.99802 0.24732  -0.62802 -0.86950 77  PHE E CA  
8178 C C   . PHE E 97  ? 3.18559 3.11166 2.98316 0.23280  -0.60812 -0.86821 77  PHE E C   
8179 O O   . PHE E 97  ? 3.19268 3.09576 2.93526 0.25384  -0.61364 -0.84421 77  PHE E O   
8180 C CB  . PHE E 97  ? 3.12369 3.06497 2.94943 0.25431  -0.61350 -0.82403 77  PHE E CB  
8181 C CG  . PHE E 97  ? 3.10099 3.08706 2.95685 0.27255  -0.63417 -0.82149 77  PHE E CG  
8182 C CD1 . PHE E 97  ? 3.09269 3.10584 3.00882 0.25323  -0.62477 -0.84476 77  PHE E CD1 
8183 C CD2 . PHE E 97  ? 3.09459 3.09470 2.91815 0.30929  -0.66232 -0.79559 77  PHE E CD2 
8184 C CE1 . PHE E 97  ? 3.07160 3.12710 3.01667 0.27160  -0.64427 -0.84412 77  PHE E CE1 
8185 C CE2 . PHE E 97  ? 3.07439 3.11337 2.92489 0.32736  -0.68332 -0.79392 77  PHE E CE2 
8186 C CZ  . PHE E 97  ? 3.05930 3.12697 2.97132 0.30920  -0.67487 -0.81911 77  PHE E CZ  
8187 N N   . THR E 98  ? 3.15559 3.06393 2.98427 0.19695  -0.58432 -0.89382 78  THR E N   
8188 C CA  . THR E 98  ? 3.18659 3.04898 2.98596 0.18157  -0.56759 -0.89941 78  THR E CA  
8189 C C   . THR E 98  ? 3.17935 2.98616 2.99296 0.14843  -0.53039 -0.89178 78  THR E C   
8190 O O   . THR E 98  ? 3.18263 3.00333 3.04718 0.12266  -0.51787 -0.91280 78  THR E O   
8191 C CB  . THR E 98  ? 3.21360 3.11204 3.03010 0.17213  -0.58389 -0.95010 78  THR E CB  
8192 O OG1 . THR E 98  ? 3.21340 3.15660 3.09876 0.14976  -0.58584 -0.98729 78  THR E OG1 
8193 C CG2 . THR E 98  ? 3.23563 3.17272 3.01710 0.20847  -0.61959 -0.95372 78  THR E CG2 
8194 N N   . LEU E 99  ? 3.18134 2.92515 2.94940 0.14974  -0.51273 -0.86210 79  LEU E N   
8195 C CA  . LEU E 99  ? 3.18202 2.86279 2.95125 0.12113  -0.47932 -0.85387 79  LEU E CA  
8196 C C   . LEU E 99  ? 3.20785 2.86179 2.96532 0.10189  -0.47121 -0.88089 79  LEU E C   
8197 O O   . LEU E 99  ? 3.21588 2.87970 2.94261 0.11879  -0.48750 -0.88875 79  LEU E O   
8198 C CB  . LEU E 99  ? 3.15039 2.77559 2.87929 0.13643  -0.46693 -0.80322 79  LEU E CB  
8199 C CG  . LEU E 99  ? 3.15823 2.70733 2.87332 0.11398  -0.43565 -0.78887 79  LEU E CG  
8200 C CD1 . LEU E 99  ? 3.17401 2.71489 2.92980 0.08492  -0.41502 -0.79998 79  LEU E CD1 
8201 C CD2 . LEU E 99  ? 3.11071 2.61296 2.78546 0.13565  -0.43119 -0.74052 79  LEU E CD2 
8202 N N   . THR E 100 ? 3.23332 2.85113 3.01345 0.06684  -0.44562 -0.89496 80  THR E N   
8203 C CA  . THR E 100 ? 3.25661 2.84740 3.03287 0.04428  -0.43769 -0.92436 80  THR E CA  
8204 C C   . THR E 100 ? 3.26343 2.77473 3.02456 0.02082  -0.40533 -0.90730 80  THR E C   
8205 O O   . THR E 100 ? 3.26873 2.76076 3.04931 0.00537  -0.38564 -0.89416 80  THR E O   
8206 C CB  . THR E 100 ? 3.27791 2.91851 3.11069 0.01975  -0.44488 -0.97439 80  THR E CB  
8207 O OG1 . THR E 100 ? 3.27471 2.97444 3.10628 0.04238  -0.47856 -0.99790 80  THR E OG1 
8208 C CG2 . THR E 100 ? 3.30944 2.90580 3.15102 -0.01609 -0.42541 -1.00026 80  THR E CG2 
8209 N N   . ILE E 101 ? 3.24116 2.70538 2.96521 0.01992  -0.40059 -0.90792 81  ILE E N   
8210 C CA  . ILE E 101 ? 3.25249 2.63720 2.95854 -0.00184 -0.37318 -0.89667 81  ILE E CA  
8211 C C   . ILE E 101 ? 3.28570 2.66044 3.01357 -0.03441 -0.36712 -0.93936 81  ILE E C   
8212 O O   . ILE E 101 ? 3.28769 2.67346 3.00265 -0.02832 -0.38249 -0.96328 81  ILE E O   
8213 C CB  . ILE E 101 ? 3.23272 2.56765 2.88320 0.02121  -0.37217 -0.86605 81  ILE E CB  
8214 C CG1 . ILE E 101 ? 3.20274 2.57354 2.83401 0.05950  -0.39022 -0.83565 81  ILE E CG1 
8215 C CG2 . ILE E 101 ? 3.23724 2.49268 2.87017 0.00743  -0.34593 -0.83981 81  ILE E CG2 
8216 C CD1 . ILE E 101 ? 3.18792 2.51784 2.77023 0.08291  -0.38901 -0.80585 81  ILE E CD1 
8217 N N   . SER E 102 ? 3.33979 2.69211 3.09984 -0.06899 -0.34433 -0.94893 82  SER E N   
8218 C CA  . SER E 102 ? 3.37812 2.72362 3.16699 -0.10357 -0.33785 -0.99003 82  SER E CA  
8219 C C   . SER E 102 ? 3.38559 2.66568 3.13328 -0.10773 -0.33352 -0.99384 82  SER E C   
8220 O O   . SER E 102 ? 3.39961 2.68994 3.15655 -0.11790 -0.34479 -1.03014 82  SER E O   
8221 C CB  . SER E 102 ? 3.42045 2.74722 3.24724 -0.14007 -0.30933 -0.99319 82  SER E CB  
8222 O OG  . SER E 102 ? 3.41656 2.80535 3.28313 -0.13499 -0.31278 -0.99099 82  SER E OG  
8223 N N   . SER E 103 ? 3.46791 2.68014 3.17103 -0.09900 -0.31890 -0.95822 83  SER E N   
8224 C CA  . SER E 103 ? 3.47366 2.61977 3.13640 -0.10042 -0.31454 -0.95952 83  SER E CA  
8225 C C   . SER E 103 ? 3.43677 2.55120 3.05100 -0.06722 -0.31574 -0.91772 83  SER E C   
8226 O O   . SER E 103 ? 3.43392 2.50315 3.03480 -0.06792 -0.29914 -0.88546 83  SER E O   
8227 C CB  . SER E 103 ? 3.52037 2.59631 3.18800 -0.13876 -0.28814 -0.96643 83  SER E CB  
8228 O OG  . SER E 103 ? 3.53333 2.57962 3.20169 -0.14660 -0.26643 -0.93610 83  SER E OG  
8229 N N   . VAL E 104 ? 3.40097 2.53914 2.98939 -0.03802 -0.33528 -0.91903 84  VAL E N   
8230 C CA  . VAL E 104 ? 3.36837 2.48498 2.91628 -0.00582 -0.33695 -0.88059 84  VAL E CA  
8231 C C   . VAL E 104 ? 3.37382 2.40208 2.89102 -0.01387 -0.31916 -0.86605 84  VAL E C   
8232 O O   . VAL E 104 ? 3.40144 2.39084 2.91271 -0.03266 -0.31424 -0.89133 84  VAL E O   
8233 C CB  . VAL E 104 ? 3.36020 2.52129 2.88657 0.02496  -0.35895 -0.88840 84  VAL E CB  
8234 C CG1 . VAL E 104 ? 3.33663 2.46998 2.82261 0.05519  -0.35717 -0.85061 84  VAL E CG1 
8235 C CG2 . VAL E 104 ? 3.35528 2.59963 2.90624 0.03777  -0.37856 -0.89668 84  VAL E CG2 
8236 N N   . LYS E 105 ? 3.40230 2.39669 2.90030 0.00095  -0.31116 -0.82579 85  LYS E N   
8237 C CA  . LYS E 105 ? 3.40169 2.31243 2.86864 -0.00092 -0.29748 -0.80821 85  LYS E CA  
8238 C C   . LYS E 105 ? 3.36640 2.27304 2.80298 0.03445  -0.30584 -0.78176 85  LYS E C   
8239 O O   . LYS E 105 ? 3.34817 2.31299 2.78633 0.05940  -0.31934 -0.77093 85  LYS E O   
8240 C CB  . LYS E 105 ? 3.41082 2.27449 2.88131 -0.01582 -0.27969 -0.78442 85  LYS E CB  
8241 C CG  . LYS E 105 ? 3.46214 2.31233 2.95774 -0.05439 -0.26462 -0.80862 85  LYS E CG  
8242 C CD  . LYS E 105 ? 3.49129 2.25735 2.96755 -0.06983 -0.24343 -0.78848 85  LYS E CD  
8243 C CE  . LYS E 105 ? 3.48655 2.17718 2.92267 -0.06353 -0.24198 -0.78322 85  LYS E CE  
8244 N NZ  . LYS E 105 ? 3.50160 2.10712 2.91180 -0.07124 -0.22538 -0.75887 85  LYS E NZ  
8245 N N   . ALA E 106 ? 3.43843 2.27420 2.84764 0.03633  -0.29734 -0.77130 86  ALA E N   
8246 C CA  . ALA E 106 ? 3.40040 2.22547 2.78433 0.06748  -0.30241 -0.74764 86  ALA E CA  
8247 C C   . ALA E 106 ? 3.32896 2.13659 2.71071 0.08295  -0.29944 -0.70457 86  ALA E C   
8248 O O   . ALA E 106 ? 3.28312 2.07568 2.64846 0.10698  -0.30195 -0.68191 86  ALA E O   
8249 C CB  . ALA E 106 ? 3.38909 2.14782 2.74756 0.06425  -0.29701 -0.75975 86  ALA E CB  
8250 N N   . GLU E 107 ? 3.45755 2.26752 2.85713 0.07014  -0.29432 -0.69372 87  GLU E N   
8251 C CA  . GLU E 107 ? 3.39726 2.18906 2.79515 0.08463  -0.29333 -0.65473 87  GLU E CA  
8252 C C   . GLU E 107 ? 3.41267 2.27609 2.82979 0.10207  -0.30517 -0.63861 87  GLU E C   
8253 O O   . GLU E 107 ? 3.33643 2.19344 2.75120 0.12134  -0.30896 -0.60466 87  GLU E O   
8254 C CB  . GLU E 107 ? 3.41449 2.14927 2.81269 0.06141  -0.27876 -0.65006 87  GLU E CB  
8255 C CG  . GLU E 107 ? 3.48778 2.26339 2.91441 0.03935  -0.27393 -0.66691 87  GLU E CG  
8256 C CD  . GLU E 107 ? 3.54686 2.27158 2.97233 0.00457  -0.25602 -0.68854 87  GLU E CD  
8257 O OE1 . GLU E 107 ? 3.55805 2.21756 2.95840 -0.00227 -0.24983 -0.69392 87  GLU E OE1 
8258 O OE2 . GLU E 107 ? 3.58746 2.33713 3.03784 -0.01595 -0.24777 -0.70018 87  GLU E OE2 
8259 N N   . ASP E 108 ? 3.31480 2.24425 2.75124 0.09647  -0.31279 -0.66258 88  ASP E N   
8260 C CA  . ASP E 108 ? 3.30515 2.30115 2.75945 0.11249  -0.32565 -0.64943 88  ASP E CA  
8261 C C   . ASP E 108 ? 3.30358 2.35872 2.75117 0.13433  -0.34107 -0.65617 88  ASP E C   
8262 O O   . ASP E 108 ? 3.31857 2.43476 2.78251 0.13346  -0.35222 -0.67603 88  ASP E O   
8263 C CB  . ASP E 108 ? 3.32652 2.35479 2.81182 0.09037  -0.32355 -0.66962 88  ASP E CB  
8264 C CG  . ASP E 108 ? 3.36444 2.39877 2.86056 0.06387  -0.31911 -0.71278 88  ASP E CG  
8265 O OD1 . ASP E 108 ? 3.37146 2.39825 2.85026 0.06688  -0.32246 -0.72930 88  ASP E OD1 
8266 O OD2 . ASP E 108 ? 3.38975 2.43636 2.91334 0.03987  -0.31198 -0.73075 88  ASP E OD2 
8267 N N   . LEU E 109 ? 3.25624 2.29405 2.67950 0.15479  -0.34180 -0.64022 89  LEU E N   
8268 C CA  . LEU E 109 ? 3.25011 2.33999 2.66057 0.17834  -0.35382 -0.64208 89  LEU E CA  
8269 C C   . LEU E 109 ? 3.21776 2.33724 2.62904 0.20423  -0.36236 -0.60350 89  LEU E C   
8270 O O   . LEU E 109 ? 3.20101 2.31500 2.59582 0.22568  -0.36177 -0.57970 89  LEU E O   
8271 C CB  . LEU E 109 ? 3.24686 2.30563 2.63115 0.18606  -0.34790 -0.64913 89  LEU E CB  
8272 C CG  . LEU E 109 ? 3.22218 2.21407 2.59343 0.19104  -0.33630 -0.62653 89  LEU E CG  
8273 C CD1 . LEU E 109 ? 3.16467 2.17154 2.52527 0.22147  -0.33855 -0.59349 89  LEU E CD1 
8274 C CD2 . LEU E 109 ? 3.29654 2.24406 2.65243 0.17867  -0.32869 -0.65559 89  LEU E CD2 
8275 N N   . ALA E 110 ? 3.27298 2.42430 2.70564 0.20193  -0.37015 -0.59744 90  ALA E N   
8276 C CA  . ALA E 110 ? 3.16697 2.33626 2.60295 0.22372  -0.37849 -0.55932 90  ALA E CA  
8277 C C   . ALA E 110 ? 3.21394 2.45545 2.65380 0.23846  -0.39645 -0.56364 90  ALA E C   
8278 O O   . ALA E 110 ? 3.25827 2.53758 2.70630 0.22870  -0.40361 -0.59773 90  ALA E O   
8279 C CB  . ALA E 110 ? 3.08179 2.21914 2.53634 0.21395  -0.37412 -0.54138 90  ALA E CB  
8280 N N   . VAL E 111 ? 3.04621 2.30471 2.48003 0.26278  -0.40478 -0.52842 91  VAL E N   
8281 C CA  . VAL E 111 ? 3.10476 2.42574 2.53894 0.27976  -0.42349 -0.52611 91  VAL E CA  
8282 C C   . VAL E 111 ? 3.06798 2.40778 2.53247 0.27027  -0.43194 -0.53062 91  VAL E C   
8283 O O   . VAL E 111 ? 3.00045 2.31391 2.47758 0.27075  -0.42954 -0.50471 91  VAL E O   
8284 C CB  . VAL E 111 ? 3.11112 2.43882 2.52867 0.30757  -0.42825 -0.48454 91  VAL E CB  
8285 C CG1 . VAL E 111 ? 3.16348 2.55279 2.57178 0.32677  -0.44789 -0.48420 91  VAL E CG1 
8286 C CG2 . VAL E 111 ? 3.14302 2.44351 2.53620 0.31513  -0.41458 -0.47674 91  VAL E CG2 
8287 N N   . TYR E 112 ? 3.05941 2.44530 2.53700 0.26235  -0.44244 -0.56494 92  TYR E N   
8288 C CA  . TYR E 112 ? 3.03887 2.45060 2.54923 0.25361  -0.45030 -0.57399 92  TYR E CA  
8289 C C   . TYR E 112 ? 3.04191 2.50221 2.55183 0.27949  -0.47278 -0.55565 92  TYR E C   
8290 O O   . TYR E 112 ? 3.09285 2.58967 2.58232 0.29686  -0.48644 -0.56018 92  TYR E O   
8291 C CB  . TYR E 112 ? 3.08244 2.52061 2.61459 0.23052  -0.45050 -0.62202 92  TYR E CB  
8292 C CG  . TYR E 112 ? 3.08908 2.47608 2.62373 0.20235  -0.42840 -0.64033 92  TYR E CG  
8293 C CD1 . TYR E 112 ? 3.06238 2.40783 2.61419 0.18329  -0.41219 -0.63338 92  TYR E CD1 
8294 C CD2 . TYR E 112 ? 3.13257 2.50997 2.64935 0.19585  -0.42422 -0.66445 92  TYR E CD2 
8295 C CE1 . TYR E 112 ? 3.08469 2.37853 2.63457 0.15783  -0.39217 -0.64852 92  TYR E CE1 
8296 C CE2 . TYR E 112 ? 3.14956 2.47635 2.66728 0.17036  -0.40536 -0.68083 92  TYR E CE2 
8297 C CZ  . TYR E 112 ? 3.12744 2.41160 2.66112 0.15107  -0.38926 -0.67204 92  TYR E CZ  
8298 O OH  . TYR E 112 ? 3.16312 2.39237 2.69369 0.12594  -0.37064 -0.68690 92  TYR E OH  
8299 N N   . TYR E 113 ? 2.91455 2.37276 2.44421 0.28307  -0.47719 -0.53512 93  TYR E N   
8300 C CA  . TYR E 113 ? 2.91488 2.41074 2.44425 0.30826  -0.49912 -0.51354 93  TYR E CA  
8301 C C   . TYR E 113 ? 2.93104 2.47095 2.49471 0.30315  -0.51249 -0.53673 93  TYR E C   
8302 O O   . TYR E 113 ? 2.91467 2.44095 2.50606 0.28205  -0.50058 -0.55143 93  TYR E O   
8303 C CB  . TYR E 113 ? 2.86256 2.32040 2.38590 0.32216  -0.49717 -0.46656 93  TYR E CB  
8304 C CG  . TYR E 113 ? 2.88428 2.32142 2.37554 0.33751  -0.49247 -0.43897 93  TYR E CG  
8305 C CD1 . TYR E 113 ? 2.94023 2.41276 2.40931 0.36132  -0.50760 -0.42492 93  TYR E CD1 
8306 C CD2 . TYR E 113 ? 2.85653 2.23893 2.33928 0.32864  -0.47245 -0.42761 93  TYR E CD2 
8307 C CE1 . TYR E 113 ? 2.97948 2.43546 2.42032 0.37479  -0.50016 -0.39944 93  TYR E CE1 
8308 C CE2 . TYR E 113 ? 2.87896 2.24640 2.33718 0.34273  -0.46684 -0.40387 93  TYR E CE2 
8309 C CZ  . TYR E 113 ? 2.95540 2.36084 2.39351 0.36520  -0.47932 -0.38954 93  TYR E CZ  
8310 O OH  . TYR E 113 ? 3.00584 2.39813 2.42061 0.37865  -0.47058 -0.36531 93  TYR E OH  
8311 N N   . CYS E 114 ? 2.98634 2.57857 2.54697 0.32351  -0.53703 -0.53956 94  CYS E N   
8312 C CA  . CYS E 114 ? 2.98598 2.62976 2.57959 0.32317  -0.55448 -0.56488 94  CYS E CA  
8313 C C   . CYS E 114 ? 2.96154 2.61458 2.55828 0.34659  -0.57209 -0.53231 94  CYS E C   
8314 O O   . CYS E 114 ? 2.98135 2.64927 2.55163 0.37216  -0.58984 -0.51044 94  CYS E O   
8315 C CB  . CYS E 114 ? 3.03339 2.72974 2.62042 0.32975  -0.57297 -0.59825 94  CYS E CB  
8316 S SG  . CYS E 114 ? 3.04019 2.80787 2.66468 0.33829  -0.60249 -0.62710 94  CYS E SG  
8317 N N   . GLN E 115 ? 2.92279 2.56520 2.54984 0.33834  -0.56702 -0.52890 95  GLN E N   
8318 C CA  . GLN E 115 ? 2.89171 2.53464 2.52341 0.35939  -0.58262 -0.49780 95  GLN E CA  
8319 C C   . GLN E 115 ? 2.89002 2.58079 2.56108 0.35955  -0.59711 -0.52319 95  GLN E C   
8320 O O   . GLN E 115 ? 2.89134 2.59110 2.59397 0.33603  -0.58308 -0.55492 95  GLN E O   
8321 C CB  . GLN E 115 ? 2.83677 2.41732 2.46580 0.35456  -0.56511 -0.46563 95  GLN E CB  
8322 C CG  . GLN E 115 ? 2.79570 2.36943 2.42584 0.37800  -0.58249 -0.42992 95  GLN E CG  
8323 C CD  . GLN E 115 ? 2.75552 2.32458 2.41734 0.37151  -0.57982 -0.43629 95  GLN E CD  
8324 O OE1 . GLN E 115 ? 2.78214 2.36757 2.46917 0.35097  -0.56771 -0.47061 95  GLN E OE1 
8325 N NE2 . GLN E 115 ? 2.71249 2.25851 2.37346 0.38903  -0.59056 -0.40325 95  GLN E NE2 
8326 N N   . GLN E 116 ? 2.81613 2.53699 2.48593 0.38620  -0.62476 -0.50887 96  GLN E N   
8327 C CA  . GLN E 116 ? 2.80479 2.57145 2.51196 0.39201  -0.64216 -0.52906 96  GLN E CA  
8328 C C   . GLN E 116 ? 2.75929 2.49889 2.47546 0.40287  -0.64442 -0.49872 96  GLN E C   
8329 O O   . GLN E 116 ? 2.73992 2.43719 2.42927 0.41582  -0.64511 -0.45776 96  GLN E O   
8330 C CB  . GLN E 116 ? 2.83161 2.65262 2.53108 0.41669  -0.67602 -0.53842 96  GLN E CB  
8331 C CG  . GLN E 116 ? 2.83498 2.63838 2.49086 0.44543  -0.69317 -0.49509 96  GLN E CG  
8332 C CD  . GLN E 116 ? 2.79757 2.60000 2.46204 0.46767  -0.71343 -0.46816 96  GLN E CD  
8333 O OE1 . GLN E 116 ? 2.76762 2.58653 2.47020 0.46413  -0.71633 -0.48368 96  GLN E OE1 
8334 N NE2 . GLN E 116 ? 2.79935 2.58208 2.42863 0.49085  -0.72710 -0.42769 96  GLN E NE2 
8335 N N   . TYR E 117 ? 2.74375 2.50872 2.49978 0.39762  -0.64549 -0.52020 97  TYR E N   
8336 C CA  . TYR E 117 ? 2.72564 2.47348 2.49280 0.41121  -0.65198 -0.49740 97  TYR E CA  
8337 C C   . TYR E 117 ? 2.72263 2.53107 2.52924 0.42114  -0.67229 -0.52515 97  TYR E C   
8338 O O   . TYR E 117 ? 2.70896 2.51908 2.54525 0.41636  -0.66442 -0.53370 97  TYR E O   
8339 C CB  . TYR E 117 ? 2.71241 2.40516 2.48331 0.39097  -0.62114 -0.48911 97  TYR E CB  
8340 C CG  . TYR E 117 ? 2.71491 2.41685 2.51292 0.35886  -0.59373 -0.52769 97  TYR E CG  
8341 C CD1 . TYR E 117 ? 2.72925 2.41704 2.51517 0.33604  -0.57423 -0.54240 97  TYR E CD1 
8342 C CD2 . TYR E 117 ? 2.71176 2.43410 2.54731 0.35111  -0.58610 -0.54857 97  TYR E CD2 
8343 C CE1 . TYR E 117 ? 2.76620 2.45871 2.57725 0.30532  -0.54909 -0.57632 97  TYR E CE1 
8344 C CE2 . TYR E 117 ? 2.74989 2.47933 2.61123 0.32005  -0.55856 -0.58201 97  TYR E CE2 
8345 C CZ  . TYR E 117 ? 2.77696 2.49019 2.62605 0.29662  -0.54052 -0.59525 97  TYR E CZ  
8346 O OH  . TYR E 117 ? 2.82079 2.53797 2.69599 0.26439  -0.51316 -0.62751 97  TYR E OH  
8347 N N   . TYR E 118 ? 2.81733 2.67643 2.62320 0.43677  -0.69946 -0.54003 98  TYR E N   
8348 C CA  . TYR E 118 ? 2.81851 2.74012 2.66209 0.44932  -0.72371 -0.56882 98  TYR E CA  
8349 C C   . TYR E 118 ? 2.78367 2.70497 2.61951 0.48273  -0.75376 -0.54000 98  TYR E C   
8350 O O   . TYR E 118 ? 2.76499 2.71684 2.63644 0.49156  -0.76537 -0.55491 98  TYR E O   
8351 C CB  . TYR E 118 ? 2.86191 2.83637 2.70712 0.45160  -0.74179 -0.60119 98  TYR E CB  
8352 C CG  . TYR E 118 ? 2.86700 2.91107 2.76161 0.45725  -0.76240 -0.64251 98  TYR E CG  
8353 C CD1 . TYR E 118 ? 2.86522 2.93485 2.81258 0.43148  -0.74130 -0.67944 98  TYR E CD1 
8354 C CD2 . TYR E 118 ? 2.87897 2.96315 2.76805 0.48832  -0.80278 -0.64512 98  TYR E CD2 
8355 C CE1 . TYR E 118 ? 2.86797 3.00501 2.86657 0.43615  -0.75928 -0.71888 98  TYR E CE1 
8356 C CE2 . TYR E 118 ? 2.88003 3.02948 2.81744 0.49483  -0.82366 -0.68505 98  TYR E CE2 
8357 C CZ  . TYR E 118 ? 2.87045 3.04813 2.86526 0.46844  -0.80150 -0.72247 98  TYR E CZ  
8358 O OH  . TYR E 118 ? 2.86680 3.11305 2.91579 0.47448  -0.82141 -0.76365 98  TYR E OH  
8359 N N   . SER E 119 ? 2.85626 2.74347 2.64733 0.50134  -0.76613 -0.49918 99  SER E N   
8360 C CA  . SER E 119 ? 2.81793 2.69603 2.59790 0.53213  -0.79440 -0.46708 99  SER E CA  
8361 C C   . SER E 119 ? 2.79604 2.61469 2.53114 0.53889  -0.78957 -0.41732 99  SER E C   
8362 O O   . SER E 119 ? 2.82436 2.62280 2.53302 0.52605  -0.77188 -0.41087 99  SER E O   
8363 C CB  . SER E 119 ? 2.84812 2.78003 2.62782 0.55797  -0.83308 -0.48105 99  SER E CB  
8364 O OG  . SER E 119 ? 2.86015 2.84938 2.68893 0.55404  -0.84015 -0.52694 99  SER E OG  
8365 N N   . TYR E 120 ? 2.86065 2.65217 2.59008 0.55936  -0.80574 -0.38315 100 TYR E N   
8366 C CA  . TYR E 120 ? 2.83566 2.57201 2.52959 0.56644  -0.80289 -0.33460 100 TYR E CA  
8367 C C   . TYR E 120 ? 2.88137 2.63053 2.53735 0.58308  -0.82091 -0.31822 100 TYR E C   
8368 O O   . TYR E 120 ? 2.90944 2.69868 2.56398 0.60339  -0.85067 -0.32850 100 TYR E O   
8369 C CB  . TYR E 120 ? 2.76553 2.47011 2.46673 0.58440  -0.81839 -0.30401 100 TYR E CB  
8370 C CG  . TYR E 120 ? 2.72217 2.39272 2.44596 0.56892  -0.79601 -0.30728 100 TYR E CG  
8371 C CD1 . TYR E 120 ? 2.73821 2.37148 2.45466 0.54369  -0.76233 -0.30611 100 TYR E CD1 
8372 C CD2 . TYR E 120 ? 2.67601 2.34999 2.42563 0.58099  -0.80913 -0.31212 100 TYR E CD2 
8373 C CE1 . TYR E 120 ? 2.71092 2.30885 2.44217 0.53089  -0.74261 -0.30856 100 TYR E CE1 
8374 C CE2 . TYR E 120 ? 2.65176 2.29229 2.41639 0.56850  -0.78825 -0.31505 100 TYR E CE2 
8375 C CZ  . TYR E 120 ? 2.66973 2.27116 2.42359 0.54342  -0.75512 -0.31275 100 TYR E CZ  
8376 O OH  . TYR E 120 ? 2.64350 2.20746 2.40665 0.53221  -0.73500 -0.31510 100 TYR E OH  
8377 N N   . PRO E 121 ? 2.75529 2.47054 2.37857 0.57612  -0.80350 -0.29284 101 PRO E N   
8378 C CA  . PRO E 121 ? 2.73496 2.40216 2.35803 0.55371  -0.77026 -0.28130 101 PRO E CA  
8379 C C   . PRO E 121 ? 2.78051 2.46119 2.40691 0.52739  -0.74395 -0.31741 101 PRO E C   
8380 O O   . PRO E 121 ? 2.83455 2.55805 2.45382 0.52815  -0.75134 -0.34425 101 PRO E O   
8381 C CB  . PRO E 121 ? 2.74666 2.37777 2.33392 0.56424  -0.76984 -0.23522 101 PRO E CB  
8382 C CG  . PRO E 121 ? 2.81450 2.48445 2.37345 0.58091  -0.78941 -0.23885 101 PRO E CG  
8383 C CD  . PRO E 121 ? 2.80903 2.52684 2.39025 0.59382  -0.81755 -0.26823 101 PRO E CD  
8384 N N   . PRO E 122 ? 2.71806 2.36022 2.35413 0.50508  -0.71519 -0.31856 102 PRO E N   
8385 C CA  . PRO E 122 ? 2.76342 2.41039 2.40086 0.47897  -0.68936 -0.35033 102 PRO E CA  
8386 C C   . PRO E 122 ? 2.80272 2.42933 2.40381 0.47735  -0.67756 -0.33298 102 PRO E C   
8387 O O   . PRO E 122 ? 2.77522 2.35572 2.36110 0.48027  -0.66877 -0.29674 102 PRO E O   
8388 C CB  . PRO E 122 ? 2.72121 2.32756 2.37920 0.45909  -0.66549 -0.35327 102 PRO E CB  
8389 C CG  . PRO E 122 ? 2.65933 2.22154 2.31106 0.47501  -0.67379 -0.31022 102 PRO E CG  
8390 C CD  . PRO E 122 ? 2.65114 2.24357 2.29896 0.50339  -0.70740 -0.29458 102 PRO E CD  
8391 N N   . THR E 123 ? 2.77181 2.43379 2.36046 0.47340  -0.67782 -0.36017 103 THR E N   
8392 C CA  . THR E 123 ? 2.82010 2.46926 2.37244 0.47327  -0.66656 -0.34917 103 THR E CA  
8393 C C   . THR E 123 ? 2.84545 2.49001 2.40235 0.44651  -0.64156 -0.38293 103 THR E C   
8394 O O   . THR E 123 ? 2.83969 2.50826 2.42504 0.43047  -0.63880 -0.42117 103 THR E O   
8395 C CB  . THR E 123 ? 2.87587 2.56567 2.39938 0.49533  -0.68996 -0.34999 103 THR E CB  
8396 O OG1 . THR E 123 ? 2.90156 2.64301 2.44269 0.49160  -0.70302 -0.39621 103 THR E OG1 
8397 C CG2 . THR E 123 ? 2.85368 2.54232 2.36882 0.52202  -0.71497 -0.31352 103 THR E CG2 
8398 N N   . PHE E 124 ? 2.91328 2.52661 2.44355 0.44172  -0.62309 -0.36855 104 PHE E N   
8399 C CA  . PHE E 124 ? 2.93129 2.53265 2.46076 0.41808  -0.59975 -0.39676 104 PHE E CA  
8400 C C   . PHE E 124 ? 2.99279 2.62759 2.49424 0.42395  -0.60517 -0.41720 104 PHE E C   
8401 O O   . PHE E 124 ? 3.03012 2.69618 2.51055 0.44646  -0.62637 -0.40910 104 PHE E O   
8402 C CB  . PHE E 124 ? 2.90296 2.44417 2.42356 0.40905  -0.57568 -0.37051 104 PHE E CB  
8403 C CG  . PHE E 124 ? 2.80861 2.31178 2.35577 0.39751  -0.56666 -0.36222 104 PHE E CG  
8404 C CD1 . PHE E 124 ? 2.76743 2.26080 2.32483 0.41291  -0.58094 -0.33244 104 PHE E CD1 
8405 C CD2 . PHE E 124 ? 2.77475 2.24865 2.33358 0.37209  -0.54438 -0.38396 104 PHE E CD2 
8406 C CE1 . PHE E 124 ? 2.69557 2.15212 2.27340 0.40437  -0.57353 -0.32583 104 PHE E CE1 
8407 C CE2 . PHE E 124 ? 2.72337 2.15894 2.30042 0.36296  -0.53569 -0.37595 104 PHE E CE2 
8408 C CZ  . PHE E 124 ? 2.69047 2.11793 2.27647 0.37975  -0.55043 -0.34739 104 PHE E CZ  
8409 N N   . GLY E 125 ? 3.00708 2.63229 2.50559 0.40422  -0.58649 -0.44445 105 GLY E N   
8410 C CA  . GLY E 125 ? 3.06776 2.71921 2.53875 0.40850  -0.58996 -0.46719 105 GLY E CA  
8411 C C   . GLY E 125 ? 3.10662 2.72592 2.54012 0.41463  -0.57328 -0.44299 105 GLY E C   
8412 O O   . GLY E 125 ? 3.08919 2.66689 2.52082 0.41541  -0.55966 -0.40796 105 GLY E O   
8413 N N   . GLY E 126 ? 3.15327 2.79409 2.55751 0.41999  -0.57527 -0.46410 106 GLY E N   
8414 C CA  . GLY E 126 ? 3.20410 2.82043 2.57189 0.42679  -0.55845 -0.44629 106 GLY E CA  
8415 C C   . GLY E 126 ? 3.17600 2.75101 2.55252 0.40389  -0.53229 -0.45831 106 GLY E C   
8416 O O   . GLY E 126 ? 3.19533 2.73968 2.55199 0.40837  -0.51529 -0.43510 106 GLY E O   
8417 N N   . GLY E 127 ? 3.17111 2.74402 2.57749 0.37969  -0.52848 -0.49364 107 GLY E N   
8418 C CA  . GLY E 127 ? 3.12669 2.65692 2.53964 0.35711  -0.50511 -0.50699 107 GLY E CA  
8419 C C   . GLY E 127 ? 3.18529 2.72840 2.58080 0.35062  -0.50273 -0.54617 107 GLY E C   
8420 O O   . GLY E 127 ? 3.25352 2.82623 2.61715 0.36945  -0.51309 -0.55102 107 GLY E O   
8421 N N   . THR E 128 ? 3.23607 2.75428 2.65067 0.32395  -0.48932 -0.57486 108 THR E N   
8422 C CA  . THR E 128 ? 3.28968 2.81246 2.69244 0.31404  -0.48654 -0.61481 108 THR E CA  
8423 C C   . THR E 128 ? 3.25271 2.71654 2.65027 0.29899  -0.46212 -0.61175 108 THR E C   
8424 O O   . THR E 128 ? 3.21917 2.65141 2.64232 0.27376  -0.45066 -0.62372 108 THR E O   
8425 C CB  . THR E 128 ? 3.29493 2.84829 2.73053 0.29403  -0.49710 -0.65941 108 THR E CB  
8426 O OG1 . THR E 128 ? 3.27600 2.80160 2.74867 0.26937  -0.48431 -0.65882 108 THR E OG1 
8427 C CG2 . THR E 128 ? 3.31994 2.93357 2.76038 0.31171  -0.52428 -0.66555 108 THR E CG2 
8428 N N   . LYS E 129 ? 3.26536 2.71369 2.62916 0.31517  -0.45383 -0.59530 109 LYS E N   
8429 C CA  . LYS E 129 ? 3.25274 2.64697 2.61023 0.30418  -0.43287 -0.59456 109 LYS E CA  
8430 C C   . LYS E 129 ? 3.26324 2.64802 2.62709 0.28115  -0.42992 -0.64162 109 LYS E C   
8431 O O   . LYS E 129 ? 3.31612 2.73968 2.67338 0.28291  -0.44339 -0.67445 109 LYS E O   
8432 C CB  . LYS E 129 ? 3.28465 2.67437 2.60611 0.32752  -0.42539 -0.57417 109 LYS E CB  
8433 C CG  . LYS E 129 ? 3.28925 2.69211 2.60198 0.35129  -0.42823 -0.52785 109 LYS E CG  
8434 C CD  . LYS E 129 ? 3.36477 2.76317 2.64408 0.37146  -0.41643 -0.51109 109 LYS E CD  
8435 C CE  . LYS E 129 ? 3.39954 2.81790 2.66689 0.39559  -0.41964 -0.46703 109 LYS E CE  
8436 N NZ  . LYS E 129 ? 3.49393 2.91228 2.72897 0.41470  -0.40532 -0.45212 109 LYS E NZ  
8437 N N   . LEU E 130 ? 3.28998 2.62062 2.66600 0.25983  -0.41346 -0.64512 110 LEU E N   
8438 C CA  . LEU E 130 ? 3.31189 2.62324 2.69366 0.23595  -0.40852 -0.68676 110 LEU E CA  
8439 C C   . LEU E 130 ? 3.32502 2.59497 2.67953 0.24062  -0.39572 -0.68842 110 LEU E C   
8440 O O   . LEU E 130 ? 3.29963 2.51235 2.65810 0.22614  -0.38102 -0.68460 110 LEU E O   
8441 C CB  . LEU E 130 ? 3.28125 2.56027 2.69602 0.20597  -0.39937 -0.69332 110 LEU E CB  
8442 C CG  . LEU E 130 ? 3.31238 2.57488 2.73834 0.17767  -0.39492 -0.73744 110 LEU E CG  
8443 C CD1 . LEU E 130 ? 3.34382 2.66693 2.77639 0.17897  -0.41366 -0.77436 110 LEU E CD1 
8444 C CD2 . LEU E 130 ? 3.32347 2.55286 2.77938 0.14814  -0.38265 -0.74000 110 LEU E CD2 
8445 N N   . GLU E 131 ? 3.29716 2.59592 2.62165 0.26293  -0.40176 -0.69399 111 GLU E N   
8446 C CA  . GLU E 131 ? 3.31925 2.58823 2.61896 0.26636  -0.39217 -0.70883 111 GLU E CA  
8447 C C   . GLU E 131 ? 3.34140 2.59602 2.65101 0.24092  -0.39466 -0.75626 111 GLU E C   
8448 O O   . GLU E 131 ? 3.36406 2.65120 2.69341 0.22784  -0.40735 -0.78185 111 GLU E O   
8449 C CB  . GLU E 131 ? 3.38798 2.69550 2.65103 0.29703  -0.39771 -0.70595 111 GLU E CB  
8450 C CG  . GLU E 131 ? 3.38965 2.71190 2.64351 0.32119  -0.39419 -0.65768 111 GLU E CG  
8451 C CD  . GLU E 131 ? 3.47359 2.83565 2.68811 0.35105  -0.39814 -0.65365 111 GLU E CD  
8452 O OE1 . GLU E 131 ? 3.51805 2.90637 2.71276 0.35486  -0.40932 -0.68971 111 GLU E OE1 
8453 O OE2 . GLU E 131 ? 3.50028 2.86628 2.70317 0.37083  -0.38996 -0.61434 111 GLU E OE2 
8454 N N   . ILE E 132 ? 3.34672 2.55093 2.64574 0.23306  -0.38287 -0.76831 112 ILE E N   
8455 C CA  . ILE E 132 ? 3.37853 2.55715 2.68886 0.20573  -0.38336 -0.80995 112 ILE E CA  
8456 C C   . ILE E 132 ? 3.41164 2.57809 2.69217 0.21569  -0.38391 -0.83690 112 ILE E C   
8457 O O   . ILE E 132 ? 3.40307 2.55350 2.65860 0.23686  -0.37516 -0.81846 112 ILE E O   
8458 C CB  . ILE E 132 ? 3.34673 2.46110 2.67727 0.17883  -0.36835 -0.80133 112 ILE E CB  
8459 C CG1 . ILE E 132 ? 3.30152 2.36267 2.61351 0.19089  -0.35432 -0.77384 112 ILE E CG1 
8460 C CG2 . ILE E 132 ? 3.31654 2.44493 2.67675 0.16777  -0.36829 -0.78068 112 ILE E CG2 
8461 C CD1 . ILE E 132 ? 3.24345 2.23532 2.56780 0.16728  -0.34146 -0.76637 112 ILE E CD1 
8462 N N   . LYS E 133 ? 3.34584 2.52113 2.63132 0.20065  -0.39457 -0.88175 113 LYS E N   
8463 C CA  . LYS E 133 ? 3.37818 2.53450 2.63803 0.20613  -0.39645 -0.91333 113 LYS E CA  
8464 C C   . LYS E 133 ? 3.37190 2.45249 2.63621 0.18558  -0.38166 -0.91644 113 LYS E C   
8465 O O   . LYS E 133 ? 3.36003 2.41071 2.65165 0.15427  -0.37792 -0.92588 113 LYS E O   
8466 C CB  . LYS E 133 ? 3.40434 2.59602 2.67012 0.19742  -0.41608 -0.96134 113 LYS E CB  
8467 C CG  . LYS E 133 ? 3.41985 2.68249 2.66964 0.22393  -0.43403 -0.96357 113 LYS E CG  
8468 C CD  . LYS E 133 ? 3.44831 2.74110 2.70238 0.21729  -0.45609 -1.01522 113 LYS E CD  
8469 C CE  . LYS E 133 ? 3.46760 2.82688 2.69894 0.24699  -0.47609 -1.01820 113 LYS E CE  
8470 N NZ  . LYS E 133 ? 3.49644 2.88488 2.73191 0.24264  -0.50089 -1.07074 113 LYS E NZ  
8471 N N   . ARG E 134 ? 3.39396 2.44326 2.63092 0.20374  -0.37290 -0.90839 114 ARG E N   
8472 C CA  . ARG E 134 ? 3.36732 2.34202 2.60342 0.19063  -0.36003 -0.90686 114 ARG E CA  
8473 C C   . ARG E 134 ? 3.40184 2.35462 2.61450 0.19553  -0.36441 -0.94458 114 ARG E C   
8474 O O   . ARG E 134 ? 3.44096 2.43518 2.63030 0.21903  -0.37301 -0.96013 114 ARG E O   
8475 C CB  . ARG E 134 ? 3.30497 2.25782 2.53446 0.20937  -0.34626 -0.86150 114 ARG E CB  
8476 C CG  . ARG E 134 ? 3.28049 2.15809 2.50314 0.20484  -0.33519 -0.85860 114 ARG E CG  
8477 C CD  . ARG E 134 ? 3.23157 2.05467 2.47502 0.17619  -0.32839 -0.84674 114 ARG E CD  
8478 N NE  . ARG E 134 ? 3.23714 1.98587 2.47020 0.17549  -0.31979 -0.84118 114 ARG E NE  
8479 C CZ  . ARG E 134 ? 3.28162 1.97941 2.50405 0.16208  -0.32062 -0.87217 114 ARG E CZ  
8480 N NH1 . ARG E 134 ? 3.31378 2.02568 2.53673 0.14660  -0.32918 -0.91148 114 ARG E NH1 
8481 N NH2 . ARG E 134 ? 3.29631 1.92605 2.50817 0.16477  -0.31433 -0.86424 114 ARG E NH2 
8482 N N   . ALA E 135 ? 3.30944 2.19500 2.52593 0.17378  -0.35919 -0.96011 115 ALA E N   
8483 C CA  . ALA E 135 ? 3.35946 2.21434 2.55256 0.18056  -0.36278 -0.99261 115 ALA E CA  
8484 C C   . ALA E 135 ? 3.35808 2.21266 2.52482 0.21569  -0.35451 -0.97181 115 ALA E C   
8485 O O   . ALA E 135 ? 3.32885 2.15718 2.50031 0.22153  -0.34204 -0.93557 115 ALA E O   
8486 C CB  . ALA E 135 ? 3.38551 2.16097 2.58681 0.15060  -0.35807 -1.00779 115 ALA E CB  
8487 N N   . ASP E 136 ? 3.30234 2.18740 2.44232 0.23960  -0.36150 -0.99545 116 ASP E N   
8488 C CA  . ASP E 136 ? 3.30228 2.20211 2.41796 0.27531  -0.35199 -0.97619 116 ASP E CA  
8489 C C   . ASP E 136 ? 3.30433 2.13800 2.42064 0.27688  -0.33944 -0.96318 116 ASP E C   
8490 O O   . ASP E 136 ? 3.33696 2.11283 2.45223 0.26095  -0.34255 -0.98921 116 ASP E O   
8491 C CB  . ASP E 136 ? 3.34990 2.28295 2.43292 0.29837  -0.36130 -1.01118 116 ASP E CB  
8492 C CG  . ASP E 136 ? 3.34802 2.35244 2.42382 0.30663  -0.37402 -1.01760 116 ASP E CG  
8493 O OD1 . ASP E 136 ? 3.30544 2.34476 2.39372 0.30869  -0.37065 -0.98322 116 ASP E OD1 
8494 O OD2 . ASP E 136 ? 3.39159 2.41564 2.44839 0.31222  -0.38911 -1.05776 116 ASP E OD2 
8495 N N   . ALA E 137 ? 3.20738 2.04849 2.32658 0.29624  -0.32637 -0.92281 117 ALA E N   
8496 C CA  . ALA E 137 ? 3.20454 1.98853 2.32826 0.30133  -0.31567 -0.90655 117 ALA E CA  
8497 C C   . ALA E 137 ? 3.20342 2.01808 2.31426 0.33757  -0.30444 -0.88928 117 ALA E C   
8498 O O   . ALA E 137 ? 3.19806 2.07658 2.29687 0.35690  -0.30251 -0.88071 117 ALA E O   
8499 C CB  . ALA E 137 ? 3.16069 1.91241 2.31114 0.28356  -0.31051 -0.87054 117 ALA E CB  
8500 N N   . ALA E 138 ? 3.27230 2.03896 2.38610 0.34709  -0.29647 -0.88368 118 ALA E N   
8501 C CA  . ALA E 138 ? 3.27666 2.06561 2.38311 0.38026  -0.28384 -0.87147 118 ALA E CA  
8502 C C   . ALA E 138 ? 3.22814 2.01941 2.36120 0.38775  -0.27238 -0.82272 118 ALA E C   
8503 O O   . ALA E 138 ? 3.20213 1.94942 2.35659 0.36904  -0.27513 -0.80487 118 ALA E O   
8504 C CB  . ALA E 138 ? 3.32007 2.05794 2.41585 0.38878  -0.28394 -0.90075 118 ALA E CB  
8505 N N   . PRO E 139 ? 3.27374 2.11476 2.40554 0.41511  -0.25932 -0.80049 119 PRO E N   
8506 C CA  . PRO E 139 ? 3.24958 2.09401 2.41076 0.42275  -0.24886 -0.75441 119 PRO E CA  
8507 C C   . PRO E 139 ? 3.21820 2.01417 2.39625 0.43305  -0.24258 -0.75194 119 PRO E C   
8508 O O   . PRO E 139 ? 3.25378 2.04170 2.41795 0.44875  -0.23860 -0.77834 119 PRO E O   
8509 C CB  . PRO E 139 ? 3.32594 2.24477 2.47663 0.44717  -0.23655 -0.73468 119 PRO E CB  
8510 C CG  . PRO E 139 ? 3.38411 2.32308 2.49887 0.46252  -0.23558 -0.77363 119 PRO E CG  
8511 C CD  . PRO E 139 ? 3.35101 2.25111 2.45327 0.43917  -0.25376 -0.81477 119 PRO E CD  
8512 N N   . THR E 140 ? 3.39277 2.15621 2.60130 0.42552  -0.24309 -0.72075 120 THR E N   
8513 C CA  . THR E 140 ? 3.39426 2.10871 2.62389 0.43501  -0.24032 -0.71508 120 THR E CA  
8514 C C   . THR E 140 ? 3.36960 2.12566 2.62719 0.45690  -0.22580 -0.67702 120 THR E C   
8515 O O   . THR E 140 ? 3.33803 2.08908 2.62314 0.45161  -0.22720 -0.64180 120 THR E O   
8516 C CB  . THR E 140 ? 3.38182 2.02377 2.62375 0.41206  -0.25303 -0.70936 120 THR E CB  
8517 O OG1 . THR E 140 ? 3.33860 1.99807 2.59474 0.39880  -0.25556 -0.67707 120 THR E OG1 
8518 C CG2 . THR E 140 ? 3.42047 2.01566 2.63596 0.39073  -0.26454 -0.74863 120 THR E CG2 
8519 N N   . VAL E 141 ? 3.34770 2.14468 2.59847 0.48175  -0.21129 -0.68470 121 VAL E N   
8520 C CA  . VAL E 141 ? 3.32557 2.16822 2.60262 0.50276  -0.19370 -0.65015 121 VAL E CA  
8521 C C   . VAL E 141 ? 3.31594 2.11582 2.63182 0.51114  -0.19253 -0.64028 121 VAL E C   
8522 O O   . VAL E 141 ? 3.34248 2.08863 2.65500 0.51095  -0.20072 -0.66864 121 VAL E O   
8523 C CB  . VAL E 141 ? 3.38143 2.28462 2.63293 0.52642  -0.17627 -0.66304 121 VAL E CB  
8524 C CG1 . VAL E 141 ? 3.40593 2.28220 2.64193 0.53867  -0.17563 -0.70501 121 VAL E CG1 
8525 C CG2 . VAL E 141 ? 3.44849 2.40275 2.72614 0.54609  -0.15478 -0.62442 121 VAL E CG2 
8526 N N   . SER E 142 ? 3.48665 2.30833 2.84089 0.51855  -0.18411 -0.60000 122 SER E N   
8527 C CA  . SER E 142 ? 3.44160 2.22751 2.83945 0.52756  -0.18463 -0.58803 122 SER E CA  
8528 C C   . SER E 142 ? 3.50440 2.34392 2.94077 0.54288  -0.16678 -0.54852 122 SER E C   
8529 O O   . SER E 142 ? 3.51807 2.37959 2.96560 0.53416  -0.16799 -0.51486 122 SER E O   
8530 C CB  . SER E 142 ? 3.34783 2.06502 2.75844 0.50758  -0.20628 -0.57991 122 SER E CB  
8531 O OG  . SER E 142 ? 3.30385 1.97262 2.67781 0.49005  -0.22066 -0.61315 122 SER E OG  
8532 N N   . ILE E 143 ? 3.47225 2.33200 2.93093 0.56538  -0.15014 -0.55258 123 ILE E N   
8533 C CA  . ILE E 143 ? 3.55791 2.47091 3.05649 0.58035  -0.12925 -0.51681 123 ILE E CA  
8534 C C   . ILE E 143 ? 3.49916 2.37535 3.05740 0.58151  -0.13792 -0.49654 123 ILE E C   
8535 O O   . ILE E 143 ? 3.41265 2.22954 2.98041 0.58158  -0.15334 -0.51852 123 ILE E O   
8536 C CB  . ILE E 143 ? 3.63163 2.59413 3.12147 0.60479  -0.10295 -0.53272 123 ILE E CB  
8537 C CG1 . ILE E 143 ? 3.68704 2.70620 3.21977 0.61892  -0.07756 -0.49398 123 ILE E CG1 
8538 C CG2 . ILE E 143 ? 3.58615 2.50726 3.08211 0.61638  -0.10756 -0.57080 123 ILE E CG2 
8539 C CD1 . ILE E 143 ? 3.76624 2.84173 3.28439 0.64256  -0.04728 -0.50521 123 ILE E CD1 
8540 N N   . PHE E 144 ? 3.70097 2.61024 3.29942 0.58284  -0.12956 -0.45428 124 PHE E N   
8541 C CA  . PHE E 144 ? 3.65091 2.52996 3.31026 0.58411  -0.13946 -0.43200 124 PHE E CA  
8542 C C   . PHE E 144 ? 3.70999 2.64651 3.42108 0.59953  -0.11496 -0.40129 124 PHE E C   
8543 O O   . PHE E 144 ? 3.79076 2.78370 3.49288 0.59936  -0.09730 -0.37549 124 PHE E O   
8544 C CB  . PHE E 144 ? 3.60490 2.44947 3.26659 0.56405  -0.16243 -0.40849 124 PHE E CB  
8545 C CG  . PHE E 144 ? 3.47199 2.24558 3.09983 0.54903  -0.18749 -0.43566 124 PHE E CG  
8546 C CD1 . PHE E 144 ? 3.46337 2.23660 3.03497 0.53496  -0.19125 -0.45488 124 PHE E CD1 
8547 C CD2 . PHE E 144 ? 3.37196 2.07808 3.02436 0.54909  -0.20733 -0.44206 124 PHE E CD2 
8548 C CE1 . PHE E 144 ? 3.37016 2.07816 2.91280 0.51934  -0.21170 -0.47876 124 PHE E CE1 
8549 C CE2 . PHE E 144 ? 3.27798 1.91547 2.89548 0.53489  -0.22835 -0.46517 124 PHE E CE2 
8550 C CZ  . PHE E 144 ? 3.28276 1.92177 2.84635 0.51905  -0.22920 -0.48293 124 PHE E CZ  
8551 N N   . PRO E 145 ? 3.51497 2.43830 3.28114 0.61265  -0.11352 -0.40269 125 PRO E N   
8552 C CA  . PRO E 145 ? 3.57787 2.55714 3.40054 0.62632  -0.08822 -0.37439 125 PRO E CA  
8553 C C   . PRO E 145 ? 3.57121 2.54861 3.44225 0.61644  -0.09811 -0.33079 125 PRO E C   
8554 O O   . PRO E 145 ? 3.49958 2.42279 3.36894 0.60287  -0.12742 -0.32691 125 PRO E O   
8555 C CB  . PRO E 145 ? 3.53483 2.49414 3.39866 0.64395  -0.08741 -0.40001 125 PRO E CB  
8556 C CG  . PRO E 145 ? 3.43098 2.30662 3.28204 0.63492  -0.12318 -0.42271 125 PRO E CG  
8557 C CD  . PRO E 145 ? 3.42949 2.28598 3.20797 0.61661  -0.13454 -0.43281 125 PRO E CD  
8558 N N   . PRO E 146 ? 3.44675 2.48099 3.36075 0.62289  -0.07405 -0.29713 126 PRO E N   
8559 C CA  . PRO E 146 ? 3.44091 2.47265 3.40664 0.61412  -0.08440 -0.25551 126 PRO E CA  
8560 C C   . PRO E 146 ? 3.35485 2.33583 3.38307 0.61763  -0.10769 -0.25950 126 PRO E C   
8561 O O   . PRO E 146 ? 3.32425 2.29035 3.37403 0.63114  -0.10666 -0.28738 126 PRO E O   
8562 C CB  . PRO E 146 ? 3.53141 2.63729 3.52932 0.62223  -0.04834 -0.22347 126 PRO E CB  
8563 C CG  . PRO E 146 ? 3.59774 2.74526 3.53621 0.63155  -0.02138 -0.24467 126 PRO E CG  
8564 C CD  . PRO E 146 ? 3.53418 2.63819 3.44513 0.63748  -0.03526 -0.29398 126 PRO E CD  
8565 N N   . SER E 147 ? 3.51169 2.46498 3.56823 0.60670  -0.13051 -0.23199 127 SER E N   
8566 C CA  . SER E 147 ? 3.42591 2.32650 3.53869 0.61013  -0.15732 -0.23362 127 SER E CA  
8567 C C   . SER E 147 ? 3.44868 2.38869 3.64927 0.62117  -0.14186 -0.21096 127 SER E C   
8568 O O   . SER E 147 ? 3.52576 2.52840 3.74578 0.62064  -0.11408 -0.18154 127 SER E O   
8569 C CB  . SER E 147 ? 3.37523 2.22701 3.47924 0.59518  -0.18971 -0.21538 127 SER E CB  
8570 O OG  . SER E 147 ? 3.42343 2.22200 3.57910 0.60028  -0.21746 -0.21652 127 SER E OG  
8571 N N   . SER E 148 ? 3.32660 2.22803 3.58109 0.63128  -0.16046 -0.22512 128 SER E N   
8572 C CA  . SER E 148 ? 3.34685 2.28268 3.69432 0.64143  -0.14907 -0.20650 128 SER E CA  
8573 C C   . SER E 148 ? 3.35935 2.30246 3.75135 0.63037  -0.15891 -0.16208 128 SER E C   
8574 O O   . SER E 148 ? 3.39402 2.39484 3.84042 0.63126  -0.13382 -0.13260 128 SER E O   
8575 C CB  . SER E 148 ? 3.31431 2.20251 3.70783 0.65595  -0.17183 -0.23529 128 SER E CB  
8576 O OG  . SER E 148 ? 3.30369 2.19197 3.66477 0.66842  -0.15967 -0.27531 128 SER E OG  
8577 N N   . GLU E 149 ? 3.33909 2.22324 3.70847 0.61996  -0.19476 -0.15659 129 GLU E N   
8578 C CA  . GLU E 149 ? 3.34660 2.23505 3.74894 0.60944  -0.20624 -0.11560 129 GLU E CA  
8579 C C   . GLU E 149 ? 3.36032 2.30736 3.72786 0.59903  -0.17834 -0.08698 129 GLU E C   
8580 O O   . GLU E 149 ? 3.34187 2.31603 3.75033 0.59304  -0.17439 -0.04852 129 GLU E O   
8581 C CB  . GLU E 149 ? 3.30512 2.11736 3.67794 0.60186  -0.24911 -0.11927 129 GLU E CB  
8582 C CG  . GLU E 149 ? 3.26309 2.00539 3.62858 0.61141  -0.27641 -0.15686 129 GLU E CG  
8583 C CD  . GLU E 149 ? 3.26741 2.00331 3.72141 0.62676  -0.28568 -0.16074 129 GLU E CD  
8584 O OE1 . GLU E 149 ? 3.28592 2.05333 3.81239 0.62663  -0.28305 -0.13006 129 GLU E OE1 
8585 O OE2 . GLU E 149 ? 3.24951 1.94801 3.70216 0.63903  -0.29661 -0.19508 129 GLU E OE2 
8586 N N   . GLN E 150 ? 3.21821 2.18310 3.50992 0.59732  -0.16046 -0.10567 130 GLN E N   
8587 C CA  . GLN E 150 ? 3.25949 2.28092 3.51286 0.59047  -0.13353 -0.08200 130 GLN E CA  
8588 C C   . GLN E 150 ? 3.29854 2.38990 3.59752 0.59910  -0.09317 -0.06370 130 GLN E C   
8589 O O   . GLN E 150 ? 3.31315 2.44775 3.61896 0.59338  -0.07502 -0.02686 130 GLN E O   
8590 C CB  . GLN E 150 ? 3.31371 2.33149 3.47511 0.58771  -0.12893 -0.11144 130 GLN E CB  
8591 C CG  . GLN E 150 ? 3.37321 2.44704 3.48543 0.58348  -0.10301 -0.09352 130 GLN E CG  
8592 C CD  . GLN E 150 ? 3.41524 2.47759 3.44023 0.57941  -0.10654 -0.12469 130 GLN E CD  
8593 O OE1 . GLN E 150 ? 3.40100 2.41420 3.40325 0.57885  -0.12554 -0.15940 130 GLN E OE1 
8594 N NE2 . GLN E 150 ? 3.46774 2.57372 3.44366 0.57653  -0.08916 -0.11254 130 GLN E NE2 
8595 N N   . LEU E 151 ? 3.25777 2.36020 3.58818 0.61326  -0.07815 -0.08874 131 LEU E N   
8596 C CA  . LEU E 151 ? 3.29723 2.46698 3.67527 0.62233  -0.03714 -0.07326 131 LEU E CA  
8597 C C   . LEU E 151 ? 3.24956 2.43418 3.72052 0.61837  -0.03773 -0.03440 131 LEU E C   
8598 O O   . LEU E 151 ? 3.28177 2.52564 3.78398 0.61851  -0.00274 -0.00496 131 LEU E O   
8599 C CB  . LEU E 151 ? 3.32088 2.49531 3.71618 0.63970  -0.02440 -0.11232 131 LEU E CB  
8600 C CG  . LEU E 151 ? 3.36536 2.52209 3.67593 0.64530  -0.02473 -0.15522 131 LEU E CG  
8601 C CD1 . LEU E 151 ? 3.34583 2.49093 3.68579 0.66294  -0.02320 -0.19456 131 LEU E CD1 
8602 C CD2 . LEU E 151 ? 3.44298 2.65607 3.68969 0.64596  0.01069  -0.14846 131 LEU E CD2 
8603 N N   . THR E 152 ? 3.28329 2.41352 3.79838 0.61499  -0.07699 -0.03377 132 THR E N   
8604 C CA  . THR E 152 ? 3.24533 2.38500 3.85385 0.61153  -0.08240 0.00024  132 THR E CA  
8605 C C   . THR E 152 ? 3.23889 2.40835 3.83828 0.59762  -0.07189 0.04671  132 THR E C   
8606 O O   . THR E 152 ? 3.23535 2.44413 3.90356 0.59482  -0.05303 0.08042  132 THR E O   
8607 C CB  . THR E 152 ? 3.22172 2.28976 3.86530 0.61177  -0.13173 -0.01068 132 THR E CB  
8608 O OG1 . THR E 152 ? 3.23585 2.26335 3.85805 0.62362  -0.14625 -0.05670 132 THR E OG1 
8609 C CG2 . THR E 152 ? 3.20474 2.28413 3.96074 0.61364  -0.13689 0.01220  132 THR E CG2 
8610 N N   . SER E 153 ? 3.21822 2.36910 3.73459 0.58868  -0.08408 0.04893  133 SER E N   
8611 C CA  . SER E 153 ? 3.22404 2.39958 3.72509 0.57689  -0.07719 0.09123  133 SER E CA  
8612 C C   . SER E 153 ? 3.29840 2.54551 3.78717 0.57910  -0.02769 0.11136  133 SER E C   
8613 O O   . SER E 153 ? 3.30061 2.57716 3.81042 0.57149  -0.01427 0.15354  133 SER E O   
8614 C CB  . SER E 153 ? 3.22313 2.36363 3.63767 0.56858  -0.10215 0.08406  133 SER E CB  
8615 O OG  . SER E 153 ? 3.17842 2.25149 3.60089 0.56629  -0.14601 0.06865  133 SER E OG  
8616 N N   . GLY E 154 ? 3.14453 2.41795 3.59743 0.59007  -0.00045 0.08227  134 GLY E N   
8617 C CA  . GLY E 154 ? 3.22252 2.56135 3.65178 0.59476  0.04749  0.09732  134 GLY E CA  
8618 C C   . GLY E 154 ? 3.28925 2.63799 3.61153 0.59777  0.05730  0.07769  134 GLY E C   
8619 O O   . GLY E 154 ? 3.35898 2.75924 3.64899 0.60286  0.09545  0.09067  134 GLY E O   
8620 N N   . GLY E 155 ? 3.31753 2.61876 3.58278 0.59497  0.02474  0.04681  135 GLY E N   
8621 C CA  . GLY E 155 ? 3.37780 2.68610 3.54644 0.59703  0.03019  0.02480  135 GLY E CA  
8622 C C   . GLY E 155 ? 3.39091 2.67342 3.53187 0.60613  0.02299  -0.02755 135 GLY E C   
8623 O O   . GLY E 155 ? 3.34571 2.59467 3.53643 0.60984  0.00699  -0.04716 135 GLY E O   
8624 N N   . ALA E 156 ? 3.32030 2.61706 3.37999 0.61035  0.03348  -0.05057 136 ALA E N   
8625 C CA  . ALA E 156 ? 3.33850 2.61124 3.36256 0.61849  0.02717  -0.10105 136 ALA E CA  
8626 C C   . ALA E 156 ? 3.38688 2.66037 3.31719 0.61512  0.02255  -0.11912 136 ALA E C   
8627 O O   . ALA E 156 ? 3.45128 2.77246 3.33898 0.62107  0.04908  -0.10902 136 ALA E O   
8628 C CB  . ALA E 156 ? 3.38004 2.69090 3.42927 0.63660  0.06166  -0.11694 136 ALA E CB  
8629 N N   . SER E 157 ? 3.32980 2.55040 3.22809 0.60588  -0.01081 -0.14579 137 SER E N   
8630 C CA  . SER E 157 ? 3.36719 2.58528 3.18405 0.60007  -0.01964 -0.16392 137 SER E CA  
8631 C C   . SER E 157 ? 3.35621 2.52824 3.14246 0.59969  -0.03811 -0.21320 137 SER E C   
8632 O O   . SER E 157 ? 3.27069 2.39018 3.08932 0.59476  -0.06149 -0.22450 137 SER E O   
8633 C CB  . SER E 157 ? 3.33654 2.53890 3.14150 0.58374  -0.04350 -0.13748 137 SER E CB  
8634 O OG  . SER E 157 ? 3.34510 2.58890 3.17115 0.58413  -0.02690 -0.09185 137 SER E OG  
8635 N N   . VAL E 158 ? 3.42997 2.61950 3.15229 0.60529  -0.02845 -0.24230 138 VAL E N   
8636 C CA  . VAL E 158 ? 3.36506 2.51407 3.05171 0.60462  -0.04390 -0.29037 138 VAL E CA  
8637 C C   . VAL E 158 ? 3.35949 2.49381 2.98575 0.58963  -0.06400 -0.30127 138 VAL E C   
8638 O O   . VAL E 158 ? 3.43015 2.60451 3.02193 0.58877  -0.05568 -0.28452 138 VAL E O   
8639 C CB  . VAL E 158 ? 3.39598 2.57516 3.06019 0.62404  -0.01837 -0.32018 138 VAL E CB  
8640 C CG1 . VAL E 158 ? 3.33131 2.46555 2.95773 0.62294  -0.03609 -0.37058 138 VAL E CG1 
8641 C CG2 . VAL E 158 ? 3.40281 2.60159 3.13275 0.63910  0.00339  -0.30917 138 VAL E CG2 
8642 N N   . VAL E 159 ? 3.45761 2.53400 3.07152 0.57795  -0.09040 -0.32925 139 VAL E N   
8643 C CA  . VAL E 159 ? 3.44033 2.49838 3.00623 0.56121  -0.11074 -0.34093 139 VAL E CA  
8644 C C   . VAL E 159 ? 3.38188 2.40472 2.90910 0.55883  -0.12029 -0.39014 139 VAL E C   
8645 O O   . VAL E 159 ? 3.31226 2.28809 2.86011 0.56020  -0.12880 -0.40973 139 VAL E O   
8646 C CB  . VAL E 159 ? 3.38765 2.40487 2.97938 0.54416  -0.13576 -0.31876 139 VAL E CB  
8647 C CG1 . VAL E 159 ? 3.34172 2.33524 2.88715 0.52644  -0.15602 -0.33744 139 VAL E CG1 
8648 C CG2 . VAL E 159 ? 3.45726 2.51097 3.08032 0.54529  -0.12872 -0.27065 139 VAL E CG2 
8649 N N   . CYS E 160 ? 3.39486 2.43862 2.86644 0.55556  -0.12045 -0.41039 140 CYS E N   
8650 C CA  . CYS E 160 ? 3.34998 2.36182 2.78209 0.55049  -0.13139 -0.45714 140 CYS E CA  
8651 C C   . CYS E 160 ? 3.26787 2.25217 2.67643 0.52713  -0.15475 -0.46294 140 CYS E C   
8652 O O   . CYS E 160 ? 3.29775 2.31856 2.68258 0.52226  -0.15566 -0.45117 140 CYS E O   
8653 C CB  . CYS E 160 ? 3.41528 2.47226 2.80325 0.56621  -0.11416 -0.48130 140 CYS E CB  
8654 S SG  . CYS E 160 ? 3.45943 2.54508 2.87182 0.59461  -0.08465 -0.48351 140 CYS E SG  
8655 N N   . PHE E 161 ? 3.49946 2.41918 2.91418 0.51333  -0.17317 -0.48116 141 PHE E N   
8656 C CA  . PHE E 161 ? 3.42952 2.31740 2.82843 0.48981  -0.19356 -0.48529 141 PHE E CA  
8657 C C   . PHE E 161 ? 3.42621 2.30783 2.77863 0.48117  -0.19932 -0.52789 141 PHE E C   
8658 O O   . PHE E 161 ? 3.37658 2.21416 2.71986 0.47961  -0.20408 -0.56000 141 PHE E O   
8659 C CB  . PHE E 161 ? 3.32864 2.14677 2.75537 0.47919  -0.20937 -0.48052 141 PHE E CB  
8660 C CG  . PHE E 161 ? 3.31515 2.13534 2.78356 0.48010  -0.21236 -0.43743 141 PHE E CG  
8661 C CD1 . PHE E 161 ? 3.34113 2.20717 2.81050 0.47725  -0.21049 -0.40782 141 PHE E CD1 
8662 C CD2 . PHE E 161 ? 3.26804 2.04245 2.77471 0.48472  -0.21915 -0.42750 141 PHE E CD2 
8663 C CE1 . PHE E 161 ? 3.32823 2.19390 2.83660 0.47816  -0.21485 -0.36881 141 PHE E CE1 
8664 C CE2 . PHE E 161 ? 3.26314 2.03814 2.80981 0.48597  -0.22414 -0.38938 141 PHE E CE2 
8665 C CZ  . PHE E 161 ? 3.29499 2.11542 2.84287 0.48226  -0.22174 -0.35984 141 PHE E CZ  
8666 N N   . LEU E 162 ? 3.28501 2.20911 2.60929 0.47580  -0.20054 -0.52871 142 LEU E N   
8667 C CA  . LEU E 162 ? 3.28943 2.20878 2.57479 0.46369  -0.21017 -0.56715 142 LEU E CA  
8668 C C   . LEU E 162 ? 3.17826 2.07130 2.46603 0.43795  -0.22742 -0.56330 142 LEU E C   
8669 O O   . LEU E 162 ? 3.11727 2.03567 2.41728 0.43453  -0.22991 -0.53232 142 LEU E O   
8670 C CB  . LEU E 162 ? 3.38972 2.37475 2.64121 0.47627  -0.20210 -0.57435 142 LEU E CB  
8671 C CG  . LEU E 162 ? 3.47953 2.49687 2.71246 0.50177  -0.18430 -0.58838 142 LEU E CG  
8672 C CD1 . LEU E 162 ? 3.52497 2.56594 2.78869 0.52073  -0.16454 -0.55189 142 LEU E CD1 
8673 C CD2 . LEU E 162 ? 3.56107 2.63133 2.75027 0.50886  -0.18379 -0.60191 142 LEU E CD2 
8674 N N   . ASN E 163 ? 3.40873 2.25078 2.68489 0.41999  -0.23864 -0.59442 143 ASN E N   
8675 C CA  . ASN E 163 ? 3.32782 2.14372 2.60749 0.39492  -0.25205 -0.59092 143 ASN E CA  
8676 C C   . ASN E 163 ? 3.32894 2.10955 2.58538 0.37530  -0.26090 -0.63284 143 ASN E C   
8677 O O   . ASN E 163 ? 3.37036 2.12342 2.61359 0.37972  -0.25949 -0.66186 143 ASN E O   
8678 C CB  . ASN E 163 ? 3.24504 2.01053 2.55496 0.38976  -0.25636 -0.56336 143 ASN E CB  
8679 C CG  . ASN E 163 ? 3.30456 2.00746 2.61963 0.39361  -0.25676 -0.57806 143 ASN E CG  
8680 O OD1 . ASN E 163 ? 3.33600 2.03958 2.63737 0.40452  -0.25120 -0.60416 143 ASN E OD1 
8681 N ND2 . ASN E 163 ? 3.27013 1.91699 2.60348 0.38628  -0.26462 -0.56196 143 ASN E ND2 
8682 N N   . ASN E 164 ? 3.35558 2.13801 2.60938 0.35349  -0.27001 -0.63565 144 ASN E N   
8683 C CA  . ASN E 164 ? 3.38661 2.13563 2.62520 0.32943  -0.27824 -0.67149 144 ASN E CA  
8684 C C   . ASN E 164 ? 3.44344 2.21920 2.65576 0.33572  -0.27863 -0.71020 144 ASN E C   
8685 O O   . ASN E 164 ? 3.46646 2.20327 2.66632 0.33572  -0.27909 -0.73886 144 ASN E O   
8686 C CB  . ASN E 164 ? 3.32475 1.98992 2.56766 0.31679  -0.28068 -0.67713 144 ASN E CB  
8687 C CG  . ASN E 164 ? 3.26707 1.90153 2.52935 0.30530  -0.28371 -0.64566 144 ASN E CG  
8688 O OD1 . ASN E 164 ? 3.21757 1.79942 2.48954 0.30952  -0.28414 -0.63122 144 ASN E OD1 
8689 N ND2 . ASN E 164 ? 3.25526 1.92291 2.52300 0.29238  -0.28705 -0.63582 144 ASN E ND2 
8690 N N   . PHE E 165 ? 3.16057 2.00262 2.36322 0.34207  -0.28024 -0.71080 145 PHE E N   
8691 C CA  . PHE E 165 ? 3.22188 2.09662 2.39724 0.34873  -0.28366 -0.74711 145 PHE E CA  
8692 C C   . PHE E 165 ? 3.25729 2.18037 2.42897 0.33807  -0.29401 -0.75334 145 PHE E C   
8693 O O   . PHE E 165 ? 3.23928 2.17793 2.42891 0.33017  -0.29632 -0.72616 145 PHE E O   
8694 C CB  . PHE E 165 ? 3.30719 2.22117 2.46685 0.38134  -0.27241 -0.74139 145 PHE E CB  
8695 C CG  . PHE E 165 ? 3.30390 2.26166 2.47559 0.39770  -0.26340 -0.69653 145 PHE E CG  
8696 C CD1 . PHE E 165 ? 3.35886 2.37783 2.51739 0.40475  -0.26648 -0.68747 145 PHE E CD1 
8697 C CD2 . PHE E 165 ? 3.24010 2.17604 2.43686 0.40633  -0.25320 -0.66381 145 PHE E CD2 
8698 C CE1 . PHE E 165 ? 3.33213 2.38751 2.50044 0.41918  -0.25846 -0.64510 145 PHE E CE1 
8699 C CE2 . PHE E 165 ? 3.21480 2.18925 2.42557 0.41997  -0.24521 -0.62232 145 PHE E CE2 
8700 C CZ  . PHE E 165 ? 3.27290 2.30609 2.46846 0.42597  -0.24727 -0.61220 145 PHE E CZ  
8701 N N   . TYR E 166 ? 3.31090 2.25766 2.45976 0.33907  -0.30191 -0.79121 146 TYR E N   
8702 C CA  . TYR E 166 ? 3.34652 2.34302 2.49112 0.33245  -0.31416 -0.80231 146 TYR E CA  
8703 C C   . TYR E 166 ? 3.42612 2.46338 2.53637 0.35340  -0.31863 -0.83149 146 TYR E C   
8704 O O   . TYR E 166 ? 3.43875 2.44877 2.53352 0.35552  -0.31931 -0.86429 146 TYR E O   
8705 C CB  . TYR E 166 ? 3.30943 2.27864 2.47096 0.29837  -0.32521 -0.82711 146 TYR E CB  
8706 C CG  . TYR E 166 ? 3.32760 2.35153 2.49236 0.29164  -0.33884 -0.83774 146 TYR E CG  
8707 C CD1 . TYR E 166 ? 3.28946 2.34329 2.47253 0.28972  -0.34015 -0.80562 146 TYR E CD1 
8708 C CD2 . TYR E 166 ? 3.37791 2.42374 2.52839 0.28870  -0.35232 -0.88111 146 TYR E CD2 
8709 C CE1 . TYR E 166 ? 3.31466 2.41929 2.50223 0.28531  -0.35424 -0.81647 146 TYR E CE1 
8710 C CE2 . TYR E 166 ? 3.40141 2.49841 2.55745 0.28395  -0.36711 -0.89255 146 TYR E CE2 
8711 C CZ  . TYR E 166 ? 3.37138 2.49799 2.54619 0.28246  -0.36786 -0.86018 146 TYR E CZ  
8712 O OH  . TYR E 166 ? 3.40611 2.58404 2.58783 0.27921  -0.38420 -0.87316 146 TYR E OH  
8713 N N   . PRO E 167 ? 3.42146 2.52091 2.51643 0.37009  -0.32289 -0.82146 147 PRO E N   
8714 C CA  . PRO E 167 ? 3.41506 2.54830 2.52595 0.36889  -0.32498 -0.78553 147 PRO E CA  
8715 C C   . PRO E 167 ? 3.43350 2.57922 2.54635 0.39032  -0.30902 -0.73773 147 PRO E C   
8716 O O   . PRO E 167 ? 3.43589 2.55861 2.54590 0.40289  -0.29447 -0.72991 147 PRO E O   
8717 C CB  . PRO E 167 ? 3.47672 2.66746 2.56379 0.37857  -0.34040 -0.80585 147 PRO E CB  
8718 C CG  . PRO E 167 ? 3.54195 2.74125 2.59042 0.40183  -0.33689 -0.83071 147 PRO E CG  
8719 C CD  . PRO E 167 ? 3.49651 2.63575 2.55318 0.39118  -0.32940 -0.85038 147 PRO E CD  
8720 N N   . LYS E 168 ? 3.40198 2.58471 2.52195 0.39434  -0.31255 -0.70674 148 LYS E N   
8721 C CA  . LYS E 168 ? 3.43649 2.63232 2.56188 0.41256  -0.29864 -0.65941 148 LYS E CA  
8722 C C   . LYS E 168 ? 3.54731 2.78203 2.63605 0.44330  -0.28819 -0.65558 148 LYS E C   
8723 O O   . LYS E 168 ? 3.56396 2.80006 2.65671 0.45926  -0.27063 -0.62367 148 LYS E O   
8724 C CB  . LYS E 168 ? 3.39382 2.61427 2.53710 0.40711  -0.30745 -0.62859 148 LYS E CB  
8725 C CG  . LYS E 168 ? 3.40187 2.62075 2.56377 0.41779  -0.29530 -0.57777 148 LYS E CG  
8726 C CD  . LYS E 168 ? 3.40423 2.64795 2.58075 0.41364  -0.30689 -0.55076 148 LYS E CD  
8727 C CE  . LYS E 168 ? 3.29867 2.52228 2.50574 0.41517  -0.29863 -0.50483 148 LYS E CE  
8728 N NZ  . LYS E 168 ? 3.38556 2.63431 2.60469 0.41451  -0.31044 -0.47702 148 LYS E NZ  
8729 N N   . ASP E 169 ? 3.44112 2.70739 2.49439 0.45220  -0.29844 -0.68792 149 ASP E N   
8730 C CA  . ASP E 169 ? 3.54100 2.84524 2.55138 0.48285  -0.28911 -0.68633 149 ASP E CA  
8731 C C   . ASP E 169 ? 3.54268 2.82313 2.54659 0.49573  -0.26910 -0.69240 149 ASP E C   
8732 O O   . ASP E 169 ? 3.50826 2.76158 2.50571 0.49003  -0.27318 -0.73213 149 ASP E O   
8733 C CB  . ASP E 169 ? 3.58034 2.91545 2.55337 0.48875  -0.30809 -0.72675 149 ASP E CB  
8734 C CG  . ASP E 169 ? 3.68401 3.06593 2.60754 0.52137  -0.30232 -0.71643 149 ASP E CG  
8735 O OD1 . ASP E 169 ? 3.73249 3.14165 2.65361 0.53072  -0.29912 -0.67696 149 ASP E OD1 
8736 O OD2 . ASP E 169 ? 3.71693 3.10648 2.60172 0.53818  -0.30126 -0.74775 149 ASP E OD2 
8737 N N   . ILE E 170 ? 3.48428 2.77470 2.49231 0.51300  -0.24771 -0.65366 150 ILE E N   
8738 C CA  . ILE E 170 ? 3.48090 2.75332 2.48913 0.52691  -0.22688 -0.65608 150 ILE E CA  
8739 C C   . ILE E 170 ? 3.55887 2.86602 2.56036 0.55061  -0.20404 -0.61341 150 ILE E C   
8740 O O   . ILE E 170 ? 3.58244 2.91252 2.59130 0.55050  -0.20486 -0.57656 150 ILE E O   
8741 C CB  . ILE E 170 ? 3.36483 2.57932 2.41873 0.50709  -0.22556 -0.65510 150 ILE E CB  
8742 C CG1 . ILE E 170 ? 3.36442 2.55411 2.41283 0.51901  -0.21274 -0.67885 150 ILE E CG1 
8743 C CG2 . ILE E 170 ? 3.34340 2.55268 2.43688 0.50373  -0.21646 -0.60468 150 ILE E CG2 
8744 C CD1 . ILE E 170 ? 3.26765 2.39485 2.35302 0.50058  -0.21567 -0.68535 150 ILE E CD1 
8745 N N   . ASN E 171 ? 3.37638 2.68754 2.36434 0.57115  -0.18298 -0.61856 151 ASN E N   
8746 C CA  . ASN E 171 ? 3.38316 2.72708 2.36671 0.59339  -0.15677 -0.57938 151 ASN E CA  
8747 C C   . ASN E 171 ? 3.37854 2.69901 2.39359 0.59963  -0.13554 -0.57561 151 ASN E C   
8748 O O   . ASN E 171 ? 3.40685 2.70655 2.41231 0.60393  -0.13509 -0.61373 151 ASN E O   
8749 C CB  . ASN E 171 ? 3.44320 2.83266 2.36411 0.61994  -0.14927 -0.58976 151 ASN E CB  
8750 C CG  . ASN E 171 ? 3.49454 2.92343 2.40454 0.63621  -0.13003 -0.54062 151 ASN E CG  
8751 O OD1 . ASN E 171 ? 3.49157 2.92073 2.43234 0.62443  -0.13367 -0.50251 151 ASN E OD1 
8752 N ND2 . ASN E 171 ? 3.55612 3.01692 2.42066 0.66374  -0.10905 -0.54106 151 ASN E ND2 
8753 N N   . VAL E 172 ? 3.45684 2.78014 2.51132 0.60049  -0.11958 -0.53088 152 VAL E N   
8754 C CA  . VAL E 172 ? 3.43311 2.73612 2.52724 0.60605  -0.10071 -0.52331 152 VAL E CA  
8755 C C   . VAL E 172 ? 3.50534 2.85319 2.58887 0.63170  -0.06875 -0.49681 152 VAL E C   
8756 O O   . VAL E 172 ? 3.55699 2.93474 2.64214 0.63490  -0.05993 -0.45536 152 VAL E O   
8757 C CB  . VAL E 172 ? 3.37752 2.64470 2.53232 0.58632  -0.10831 -0.49476 152 VAL E CB  
8758 C CG1 . VAL E 172 ? 3.36540 2.61862 2.56362 0.59552  -0.08858 -0.48299 152 VAL E CG1 
8759 C CG2 . VAL E 172 ? 3.29551 2.51385 2.45826 0.56164  -0.13595 -0.52308 152 VAL E CG2 
8760 N N   . LYS E 173 ? 3.58171 2.93339 2.65438 0.64999  -0.05078 -0.52047 153 LYS E N   
8761 C CA  . LYS E 173 ? 3.64633 3.03952 2.71114 0.67497  -0.01622 -0.49898 153 LYS E CA  
8762 C C   . LYS E 173 ? 3.61794 2.99465 2.74516 0.67667  0.00133  -0.48607 153 LYS E C   
8763 O O   . LYS E 173 ? 3.55221 2.88738 2.70392 0.66995  -0.01002 -0.51514 153 LYS E O   
8764 C CB  . LYS E 173 ? 3.68161 3.09778 2.68422 0.69874  -0.00655 -0.53666 153 LYS E CB  
8765 C CG  . LYS E 173 ? 3.69688 3.12042 2.63923 0.69704  -0.03083 -0.56330 153 LYS E CG  
8766 C CD  . LYS E 173 ? 3.72392 3.16178 2.60855 0.72102  -0.02461 -0.60656 153 LYS E CD  
8767 C CE  . LYS E 173 ? 3.75901 3.21178 2.58143 0.72353  -0.04751 -0.62966 153 LYS E CE  
8768 N NZ  . LYS E 173 ? 3.79968 3.26889 2.56150 0.75056  -0.04082 -0.66947 153 LYS E NZ  
8769 N N   . TRP E 174 ? 3.69277 3.10105 2.84644 0.68573  0.02831  -0.44267 154 TRP E N   
8770 C CA  . TRP E 174 ? 3.67089 3.07007 2.89127 0.68773  0.04555  -0.42592 154 TRP E CA  
8771 C C   . TRP E 174 ? 3.72552 3.16385 2.93480 0.71499  0.08260  -0.43005 154 TRP E C   
8772 O O   . TRP E 174 ? 3.80916 3.29341 2.98955 0.72851  0.10727  -0.40406 154 TRP E O   
8773 C CB  . TRP E 174 ? 3.68633 3.08987 2.95760 0.67504  0.04779  -0.37238 154 TRP E CB  
8774 C CG  . TRP E 174 ? 3.61231 2.96747 2.91719 0.64974  0.01445  -0.36996 154 TRP E CG  
8775 C CD1 . TRP E 174 ? 3.60794 2.95310 2.89086 0.63334  -0.01078 -0.36406 154 TRP E CD1 
8776 C CD2 . TRP E 174 ? 3.53371 2.84330 2.89866 0.63934  0.00295  -0.37391 154 TRP E CD2 
8777 N NE1 . TRP E 174 ? 3.53246 2.82929 2.85700 0.61307  -0.03514 -0.36352 154 TRP E NE1 
8778 C CE2 . TRP E 174 ? 3.48460 2.75693 2.85750 0.61662  -0.02796 -0.36917 154 TRP E CE2 
8779 C CE3 . TRP E 174 ? 3.49820 2.79457 2.91042 0.64827  0.01514  -0.38183 154 TRP E CE3 
8780 C CZ2 . TRP E 174 ? 3.40168 2.62167 2.82281 0.60305  -0.04640 -0.37107 154 TRP E CZ2 
8781 C CZ3 . TRP E 174 ? 3.41487 2.65899 2.87688 0.63503  -0.00556 -0.38440 154 TRP E CZ3 
8782 C CH2 . TRP E 174 ? 3.36674 2.57195 2.83038 0.61282  -0.03576 -0.37851 154 TRP E CH2 
8783 N N   . LYS E 175 ? 3.64294 3.06201 2.87405 0.72361  0.08684  -0.46232 155 LYS E N   
8784 C CA  . LYS E 175 ? 3.68627 3.14002 2.91293 0.75036  0.12177  -0.47163 155 LYS E CA  
8785 C C   . LYS E 175 ? 3.66840 3.12159 2.97737 0.75134  0.13957  -0.44916 155 LYS E C   
8786 O O   . LYS E 175 ? 3.59130 2.99895 2.95025 0.73774  0.11788  -0.45758 155 LYS E O   
8787 C CB  . LYS E 175 ? 3.65701 3.09233 2.84405 0.76331  0.11292  -0.53014 155 LYS E CB  
8788 C CG  . LYS E 175 ? 3.67936 3.11875 2.78593 0.76509  0.09580  -0.55680 155 LYS E CG  
8789 C CD  . LYS E 175 ? 3.65953 3.08072 2.72978 0.77915  0.08759  -0.61507 155 LYS E CD  
8790 C CE  . LYS E 175 ? 3.56704 2.92520 2.67378 0.76083  0.05737  -0.64398 155 LYS E CE  
8791 N NZ  . LYS E 175 ? 3.55411 2.89037 2.62308 0.77306  0.04631  -0.70127 155 LYS E NZ  
8792 N N   . ILE E 176 ? 3.60551 3.10857 2.92831 0.76756  0.17889  -0.42075 156 ILE E N   
8793 C CA  . ILE E 176 ? 3.59706 3.10958 3.00205 0.77030  0.20012  -0.39819 156 ILE E CA  
8794 C C   . ILE E 176 ? 3.64038 3.19289 3.03722 0.79890  0.23816  -0.41636 156 ILE E C   
8795 O O   . ILE E 176 ? 3.72243 3.32406 3.07968 0.81370  0.27065  -0.39845 156 ILE E O   
8796 C CB  . ILE E 176 ? 3.64326 3.18023 3.08774 0.75889  0.21388  -0.33828 156 ILE E CB  
8797 C CG1 . ILE E 176 ? 3.60245 3.09992 3.05335 0.73230  0.17538  -0.32186 156 ILE E CG1 
8798 C CG2 . ILE E 176 ? 3.63295 3.18248 3.16731 0.76220  0.23613  -0.31771 156 ILE E CG2 
8799 C CD1 . ILE E 176 ? 3.64811 3.16574 3.13292 0.72105  0.18458  -0.26420 156 ILE E CD1 
8800 N N   . ASP E 177 ? 3.62668 3.15725 3.05926 0.80768  0.23442  -0.45161 157 ASP E N   
8801 C CA  . ASP E 177 ? 3.65931 3.22362 3.08681 0.83638  0.26730  -0.47656 157 ASP E CA  
8802 C C   . ASP E 177 ? 3.71571 3.30364 3.04631 0.85454  0.27693  -0.50160 157 ASP E C   
8803 O O   . ASP E 177 ? 3.79291 3.43223 3.09756 0.87637  0.31642  -0.49325 157 ASP E O   
8804 C CB  . ASP E 177 ? 3.71190 3.32764 3.20005 0.84520  0.31109  -0.43677 157 ASP E CB  
8805 C CG  . ASP E 177 ? 3.65190 3.25124 3.23564 0.84480  0.30918  -0.44193 157 ASP E CG  
8806 O OD1 . ASP E 177 ? 3.57097 3.11308 3.17498 0.83376  0.27050  -0.46730 157 ASP E OD1 
8807 O OD2 . ASP E 177 ? 3.68615 3.32934 3.32484 0.85585  0.34640  -0.42092 157 ASP E OD2 
8808 N N   . GLY E 178 ? 3.65969 3.20877 2.93622 0.84541  0.24010  -0.53294 158 GLY E N   
8809 C CA  . GLY E 178 ? 3.72089 3.28548 2.90606 0.86163  0.24124  -0.56182 158 GLY E CA  
8810 C C   . GLY E 178 ? 3.75912 3.34898 2.88997 0.85564  0.24316  -0.52938 158 GLY E C   
8811 O O   . GLY E 178 ? 3.74577 3.31495 2.82224 0.84710  0.21300  -0.54805 158 GLY E O   
8812 N N   . SER E 179 ? 3.73828 3.37224 2.88490 0.85994  0.27799  -0.48086 159 SER E N   
8813 C CA  . SER E 179 ? 3.80584 3.46446 2.89845 0.85714  0.28231  -0.44712 159 SER E CA  
8814 C C   . SER E 179 ? 3.76194 3.38641 2.87274 0.82653  0.24438  -0.42668 159 SER E C   
8815 O O   . SER E 179 ? 3.69727 3.28999 2.87875 0.80679  0.22746  -0.41808 159 SER E O   
8816 C CB  . SER E 179 ? 3.88819 3.59756 2.99958 0.86719  0.33004  -0.39713 159 SER E CB  
8817 O OG  . SER E 179 ? 3.85470 3.55912 3.06319 0.85182  0.33728  -0.36623 159 SER E OG  
8818 N N   . GLU E 180 ? 3.95723 3.58830 3.00200 0.82421  0.23042  -0.42005 160 GLU E N   
8819 C CA  . GLU E 180 ? 3.92548 3.53051 2.97969 0.79778  0.19614  -0.40072 160 GLU E CA  
8820 C C   . GLU E 180 ? 3.98407 3.61423 3.06305 0.79062  0.21459  -0.33858 160 GLU E C   
8821 O O   . GLU E 180 ? 4.06054 3.73121 3.13059 0.80695  0.25394  -0.31100 160 GLU E O   
8822 C CB  . GLU E 180 ? 3.93071 3.52935 2.90516 0.79879  0.16774  -0.42877 160 GLU E CB  
8823 C CG  . GLU E 180 ? 3.87416 3.44382 2.82390 0.80275  0.14502  -0.49076 160 GLU E CG  
8824 C CD  . GLU E 180 ? 3.88432 3.45234 2.75827 0.80458  0.11780  -0.51862 160 GLU E CD  
8825 O OE1 . GLU E 180 ? 3.93238 3.52178 2.77186 0.80396  0.11576  -0.48996 160 GLU E OE1 
8826 O OE2 . GLU E 180 ? 3.84583 3.39033 2.69594 0.80689  0.09723  -0.56974 160 GLU E OE2 
8827 N N   . ARG E 181 ? 3.76526 3.36964 2.87523 0.76580  0.18599  -0.31663 161 ARG E N   
8828 C CA  . ARG E 181 ? 3.80987 3.43084 2.94616 0.75654  0.19680  -0.25862 161 ARG E CA  
8829 C C   . ARG E 181 ? 3.77193 3.36498 2.90434 0.73437  0.15636  -0.25019 161 ARG E C   
8830 O O   . ARG E 181 ? 3.70683 3.26134 2.85259 0.71991  0.12346  -0.28144 161 ARG E O   
8831 C CB  . ARG E 181 ? 3.77174 3.39258 3.00003 0.74986  0.21669  -0.22994 161 ARG E CB  
8832 C CG  . ARG E 181 ? 3.77989 3.42131 3.03841 0.74219  0.23314  -0.16868 161 ARG E CG  
8833 C CD  . ARG E 181 ? 3.73884 3.38229 3.09259 0.73658  0.25275  -0.14421 161 ARG E CD  
8834 N NE  . ARG E 181 ? 3.78336 3.46419 3.14431 0.75755  0.29704  -0.14846 161 ARG E NE  
8835 C CZ  . ARG E 181 ? 3.75931 3.45270 3.20103 0.75733  0.32138  -0.13043 161 ARG E CZ  
8836 N NH1 . ARG E 181 ? 3.68824 3.35785 3.21025 0.73790  0.30447  -0.10711 161 ARG E NH1 
8837 N NH2 . ARG E 181 ? 3.80597 3.53737 3.24896 0.77790  0.36331  -0.13705 161 ARG E NH2 
8838 N N   . GLN E 182 ? 3.65649 3.26875 2.76952 0.73224  0.15986  -0.20766 162 GLN E N   
8839 C CA  . GLN E 182 ? 3.62904 3.22167 2.73442 0.71425  0.12393  -0.19607 162 GLN E CA  
8840 C C   . GLN E 182 ? 3.61571 3.21326 2.76707 0.70312  0.13037  -0.13790 162 GLN E C   
8841 O O   . GLN E 182 ? 3.63419 3.23746 2.75575 0.69946  0.11735  -0.11289 162 GLN E O   
8842 C CB  . GLN E 182 ? 3.68203 3.29084 2.69818 0.72552  0.11166  -0.21118 162 GLN E CB  
8843 C CG  . GLN E 182 ? 3.66389 3.25307 2.64382 0.72519  0.08382  -0.26998 162 GLN E CG  
8844 C CD  . GLN E 182 ? 3.69281 3.29467 2.59646 0.73203  0.06304  -0.28182 162 GLN E CD  
8845 O OE1 . GLN E 182 ? 3.76672 3.39947 2.61851 0.74953  0.08016  -0.25887 162 GLN E OE1 
8846 N NE2 . GLN E 182 ? 3.62944 3.20672 2.52644 0.71825  0.02578  -0.31744 162 GLN E NE2 
8847 N N   . ASN E 183 ? 3.60020 3.19476 2.82644 0.69804  0.14879  -0.11632 163 ASN E N   
8848 C CA  . ASN E 183 ? 3.58027 3.18071 2.85687 0.68832  0.15803  -0.06058 163 ASN E CA  
8849 C C   . ASN E 183 ? 3.48516 3.04401 2.83486 0.66615  0.12775  -0.05787 163 ASN E C   
8850 O O   . ASN E 183 ? 3.43964 2.98297 2.85056 0.66297  0.13225  -0.06839 163 ASN E O   
8851 C CB  . ASN E 183 ? 3.61060 3.24403 2.91972 0.70023  0.20483  -0.03416 163 ASN E CB  
8852 C CG  . ASN E 183 ? 3.70114 3.37191 2.93713 0.72492  0.23715  -0.04709 163 ASN E CG  
8853 O OD1 . ASN E 183 ? 3.74413 3.41856 2.90010 0.73382  0.22408  -0.06731 163 ASN E OD1 
8854 N ND2 . ASN E 183 ? 3.72746 3.42679 2.99135 0.73697  0.27949  -0.03628 163 ASN E ND2 
8855 N N   . GLY E 184 ? 3.53479 3.07520 2.87652 0.65235  0.09640  -0.04425 164 GLY E N   
8856 C CA  . GLY E 184 ? 3.44583 2.94686 2.85049 0.63249  0.06765  -0.03710 164 GLY E CA  
8857 C C   . GLY E 184 ? 3.40266 2.86482 2.81719 0.62444  0.04278  -0.08498 164 GLY E C   
8858 O O   . GLY E 184 ? 3.35872 2.80083 2.82817 0.62211  0.04626  -0.09477 164 GLY E O   
8859 N N   . VAL E 185 ? 3.42500 2.87503 2.78792 0.61992  0.01697  -0.11483 165 VAL E N   
8860 C CA  . VAL E 185 ? 3.38776 2.79942 2.75180 0.61075  -0.00660 -0.16094 165 VAL E CA  
8861 C C   . VAL E 185 ? 3.35077 2.73699 2.70707 0.59329  -0.04247 -0.16275 165 VAL E C   
8862 O O   . VAL E 185 ? 3.38601 2.79272 2.69619 0.59478  -0.05120 -0.15697 165 VAL E O   
8863 C CB  . VAL E 185 ? 3.43959 2.86412 2.74552 0.62406  0.00137  -0.20650 165 VAL E CB  
8864 C CG1 . VAL E 185 ? 3.50795 2.97005 2.74246 0.63551  0.00540  -0.20275 165 VAL E CG1 
8865 C CG2 . VAL E 185 ? 3.39940 2.78185 2.70053 0.61149  -0.02671 -0.25234 165 VAL E CG2 
8866 N N   . LEU E 186 ? 3.37788 2.71939 2.77848 0.57791  -0.06313 -0.17096 166 LEU E N   
8867 C CA  . LEU E 186 ? 3.33784 2.65274 2.73680 0.56086  -0.09533 -0.17291 166 LEU E CA  
8868 C C   . LEU E 186 ? 3.34415 2.64188 2.70233 0.55429  -0.11230 -0.22233 166 LEU E C   
8869 O O   . LEU E 186 ? 3.35614 2.64574 2.70257 0.55963  -0.10400 -0.25648 166 LEU E O   
8870 C CB  . LEU E 186 ? 3.25918 2.53157 2.72190 0.54814  -0.10939 -0.15666 166 LEU E CB  
8871 C CG  . LEU E 186 ? 3.23437 2.51757 2.75035 0.55273  -0.09498 -0.11037 166 LEU E CG  
8872 C CD1 . LEU E 186 ? 3.15093 2.38811 2.72392 0.54013  -0.11628 -0.09804 166 LEU E CD1 
8873 C CD2 . LEU E 186 ? 3.26822 2.59075 2.76333 0.55777  -0.08814 -0.07268 166 LEU E CD2 
8874 N N   . ASN E 187 ? 3.43932 2.73227 2.77758 0.54268  -0.13634 -0.22653 167 ASN E N   
8875 C CA  . ASN E 187 ? 3.43997 2.71948 2.74302 0.53405  -0.15318 -0.27213 167 ASN E CA  
8876 C C   . ASN E 187 ? 3.36267 2.61422 2.68111 0.51435  -0.18054 -0.27125 167 ASN E C   
8877 O O   . ASN E 187 ? 3.39216 2.66313 2.70568 0.51307  -0.19064 -0.24725 167 ASN E O   
8878 C CB  . ASN E 187 ? 3.50205 2.82488 2.74302 0.54654  -0.14957 -0.28896 167 ASN E CB  
8879 C CG  . ASN E 187 ? 3.47234 2.83358 2.69456 0.55465  -0.14971 -0.25154 167 ASN E CG  
8880 O OD1 . ASN E 187 ? 3.50700 2.90470 2.69681 0.57297  -0.13065 -0.23913 167 ASN E OD1 
8881 N ND2 . ASN E 187 ? 3.40548 2.75590 2.64819 0.54194  -0.17029 -0.23202 167 ASN E ND2 
8882 N N   . SER E 188 ? 3.35252 2.55737 2.68840 0.49970  -0.19220 -0.29667 168 SER E N   
8883 C CA  . SER E 188 ? 3.25179 2.42688 2.60209 0.48082  -0.21545 -0.29700 168 SER E CA  
8884 C C   . SER E 188 ? 3.16914 2.32710 2.49222 0.46743  -0.22756 -0.34329 168 SER E C   
8885 O O   . SER E 188 ? 3.17467 2.30284 2.49603 0.46463  -0.22337 -0.37224 168 SER E O   
8886 C CB  . SER E 188 ? 3.16710 2.29510 2.56685 0.47393  -0.21939 -0.27836 168 SER E CB  
8887 O OG  . SER E 188 ? 3.23113 2.37609 2.66130 0.48417  -0.21106 -0.23450 168 SER E OG  
8888 N N   . TRP E 189 ? 3.23037 2.40707 2.53418 0.45921  -0.24300 -0.35068 169 TRP E N   
8889 C CA  . TRP E 189 ? 3.16115 2.32572 2.44442 0.44417  -0.25535 -0.39340 169 TRP E CA  
8890 C C   . TRP E 189 ? 2.99960 2.13056 2.30640 0.42333  -0.27191 -0.39154 169 TRP E C   
8891 O O   . TRP E 189 ? 2.99952 2.14149 2.32173 0.42292  -0.28015 -0.36203 169 TRP E O   
8892 C CB  . TRP E 189 ? 3.26592 2.48047 2.50924 0.45090  -0.26106 -0.41018 169 TRP E CB  
8893 C CG  . TRP E 189 ? 3.35901 2.59440 2.56769 0.46641  -0.24831 -0.43397 169 TRP E CG  
8894 C CD1 . TRP E 189 ? 3.35248 2.57344 2.54186 0.46118  -0.25015 -0.47877 169 TRP E CD1 
8895 C CD2 . TRP E 189 ? 3.53090 2.80438 2.71841 0.49031  -0.23143 -0.41435 169 TRP E CD2 
8896 N NE1 . TRP E 189 ? 3.47625 2.72436 2.63315 0.48187  -0.23664 -0.48954 169 TRP E NE1 
8897 C CE2 . TRP E 189 ? 3.56295 2.84411 2.71702 0.50005  -0.22368 -0.45012 169 TRP E CE2 
8898 C CE3 . TRP E 189 ? 3.63167 2.93207 2.82465 0.50424  -0.22140 -0.36956 169 TRP E CE3 
8899 C CZ2 . TRP E 189 ? 3.68161 2.99749 2.80546 0.52427  -0.20506 -0.44273 169 TRP E CZ2 
8900 C CZ3 . TRP E 189 ? 3.76326 3.09748 2.92730 0.52648  -0.20179 -0.36077 169 TRP E CZ3 
8901 C CH2 . TRP E 189 ? 3.77398 3.11626 2.90280 0.53685  -0.19313 -0.39726 169 TRP E CH2 
8902 N N   . THR E 190 ? 3.25294 2.34181 2.56061 0.40644  -0.27637 -0.42319 170 THR E N   
8903 C CA  . THR E 190 ? 3.15622 2.20577 2.48379 0.38633  -0.28834 -0.42290 170 THR E CA  
8904 C C   . THR E 190 ? 3.15075 2.21856 2.46351 0.37076  -0.30059 -0.45062 170 THR E C   
8905 O O   . THR E 190 ? 3.22000 2.33234 2.50854 0.37690  -0.30276 -0.46799 170 THR E O   
8906 C CB  . THR E 190 ? 3.08362 2.06853 2.42200 0.37684  -0.28473 -0.43678 170 THR E CB  
8907 O OG1 . THR E 190 ? 3.06090 2.03356 2.37637 0.36625  -0.28455 -0.48008 170 THR E OG1 
8908 C CG2 . THR E 190 ? 3.10175 2.07645 2.45381 0.39464  -0.27219 -0.41857 170 THR E CG2 
8909 N N   . ASP E 191 ? 3.20038 2.23343 2.52825 0.35090  -0.30871 -0.45541 171 ASP E N   
8910 C CA  . ASP E 191 ? 3.26153 2.30682 2.58420 0.33264  -0.31883 -0.48230 171 ASP E CA  
8911 C C   . ASP E 191 ? 3.24735 2.24610 2.56431 0.31279  -0.31580 -0.51868 171 ASP E C   
8912 O O   . ASP E 191 ? 3.18536 2.13598 2.50297 0.31308  -0.30805 -0.51972 171 ASP E O   
8913 C CB  . ASP E 191 ? 3.24111 2.28396 2.58539 0.32421  -0.32844 -0.46065 171 ASP E CB  
8914 C CG  . ASP E 191 ? 3.26717 2.33570 2.62237 0.34353  -0.33108 -0.41788 171 ASP E CG  
8915 O OD1 . ASP E 191 ? 3.33280 2.44844 2.67360 0.36058  -0.33018 -0.41016 171 ASP E OD1 
8916 O OD2 . ASP E 191 ? 3.22688 2.26611 2.60358 0.34195  -0.33429 -0.39181 171 ASP E OD2 
8917 N N   . GLN E 192 ? 3.27287 2.28560 2.58575 0.29532  -0.32274 -0.54898 172 GLN E N   
8918 C CA  . GLN E 192 ? 3.25815 2.22750 2.56638 0.27371  -0.32007 -0.58413 172 GLN E CA  
8919 C C   . GLN E 192 ? 3.19018 2.09430 2.51267 0.25792  -0.31639 -0.57217 172 GLN E C   
8920 O O   . GLN E 192 ? 3.14623 2.04815 2.48479 0.25733  -0.31951 -0.54518 172 GLN E O   
8921 C CB  . GLN E 192 ? 3.28072 2.28309 2.58818 0.25700  -0.32862 -0.61781 172 GLN E CB  
8922 C CG  . GLN E 192 ? 3.36021 2.41740 2.64740 0.27148  -0.33439 -0.63878 172 GLN E CG  
8923 C CD  . GLN E 192 ? 3.35995 2.45105 2.65165 0.25541  -0.34602 -0.67292 172 GLN E CD  
8924 O OE1 . GLN E 192 ? 3.41510 2.53628 2.68935 0.26126  -0.35238 -0.70198 172 GLN E OE1 
8925 N NE2 . GLN E 192 ? 3.29959 2.38669 2.61589 0.23574  -0.34919 -0.67065 172 GLN E NE2 
8926 N N   . ASP E 193 ? 3.17783 2.02596 2.49149 0.24628  -0.31064 -0.59294 173 ASP E N   
8927 C CA  . ASP E 193 ? 3.12785 1.90617 2.44717 0.23120  -0.30720 -0.58530 173 ASP E CA  
8928 C C   . ASP E 193 ? 3.13332 1.90015 2.45659 0.20203  -0.30744 -0.60700 173 ASP E C   
8929 O O   . ASP E 193 ? 3.17747 1.98170 2.50006 0.19138  -0.31034 -0.63563 173 ASP E O   
8930 C CB  . ASP E 193 ? 3.11264 1.83090 2.41861 0.23366  -0.30164 -0.59612 173 ASP E CB  
8931 C CG  . ASP E 193 ? 3.08429 1.78046 2.39794 0.25541  -0.30024 -0.56366 173 ASP E CG  
8932 O OD1 . ASP E 193 ? 3.10150 1.84720 2.42350 0.27624  -0.30060 -0.54245 173 ASP E OD1 
8933 O OD2 . ASP E 193 ? 3.07214 1.70033 2.38376 0.25169  -0.29914 -0.55953 173 ASP E OD2 
8934 N N   . SER E 194 ? 3.25148 1.96561 2.57949 0.18946  -0.30420 -0.59326 174 SER E N   
8935 C CA  . SER E 194 ? 3.27976 1.97795 2.61248 0.16091  -0.30060 -0.61026 174 SER E CA  
8936 C C   . SER E 194 ? 3.31423 1.95143 2.63139 0.13963  -0.29334 -0.63901 174 SER E C   
8937 O O   . SER E 194 ? 3.35788 1.99448 2.67995 0.11382  -0.28927 -0.66260 174 SER E O   
8938 C CB  . SER E 194 ? 3.25358 1.92396 2.59489 0.15797  -0.29936 -0.58153 174 SER E CB  
8939 O OG  . SER E 194 ? 3.23550 1.95872 2.59198 0.17741  -0.30757 -0.55453 174 SER E OG  
8940 N N   . LYS E 195 ? 3.37362 1.95970 2.67406 0.14966  -0.29188 -0.63802 175 LYS E N   
8941 C CA  . LYS E 195 ? 3.39854 1.91899 2.68115 0.13157  -0.28662 -0.66367 175 LYS E CA  
8942 C C   . LYS E 195 ? 3.42533 1.96336 2.69816 0.13719  -0.28962 -0.69417 175 LYS E C   
8943 O O   . LYS E 195 ? 3.49049 2.01075 2.75726 0.11573  -0.28783 -0.72633 175 LYS E O   
8944 C CB  . LYS E 195 ? 3.35378 1.79277 2.62169 0.13837  -0.28485 -0.64414 175 LYS E CB  
8945 C CG  . LYS E 195 ? 3.37642 1.73429 2.62511 0.11258  -0.27792 -0.66021 175 LYS E CG  
8946 C CD  . LYS E 195 ? 3.34840 1.62442 2.57906 0.12319  -0.27929 -0.64065 175 LYS E CD  
8947 C CE  . LYS E 195 ? 3.27628 1.55312 2.51645 0.13552  -0.28197 -0.60372 175 LYS E CE  
8948 N NZ  . LYS E 195 ? 3.29152 1.56669 2.53391 0.11313  -0.27444 -0.59944 175 LYS E NZ  
8949 N N   . ASP E 196 ? 3.30520 1.87738 2.57651 0.16558  -0.29366 -0.68516 176 ASP E N   
8950 C CA  . ASP E 196 ? 3.34169 1.93524 2.60109 0.17470  -0.29622 -0.71384 176 ASP E CA  
8951 C C   . ASP E 196 ? 3.37787 2.05766 2.64321 0.18270  -0.30169 -0.72399 176 ASP E C   
8952 O O   . ASP E 196 ? 3.41951 2.11859 2.67354 0.18420  -0.30525 -0.75548 176 ASP E O   
8953 C CB  . ASP E 196 ? 3.32107 1.89514 2.57197 0.20204  -0.29520 -0.70162 176 ASP E CB  
8954 C CG  . ASP E 196 ? 3.29081 1.88880 2.55664 0.22349  -0.29472 -0.66014 176 ASP E CG  
8955 O OD1 . ASP E 196 ? 3.24990 1.81007 2.52379 0.21760  -0.29455 -0.63626 176 ASP E OD1 
8956 O OD2 . ASP E 196 ? 3.31412 1.96755 2.58269 0.24626  -0.29448 -0.65131 176 ASP E OD2 
8957 N N   . SER E 197 ? 3.15140 1.88070 2.43207 0.18923  -0.30401 -0.69882 177 SER E N   
8958 C CA  . SER E 197 ? 3.17923 1.98822 2.46404 0.19676  -0.31131 -0.70684 177 SER E CA  
8959 C C   . SER E 197 ? 3.21039 2.05484 2.47742 0.22377  -0.31271 -0.71275 177 SER E C   
8960 O O   . SER E 197 ? 3.25626 2.13528 2.51215 0.22483  -0.31865 -0.74332 177 SER E O   
8961 C CB  . SER E 197 ? 3.22013 2.04303 2.51163 0.17043  -0.31596 -0.74318 177 SER E CB  
8962 O OG  . SER E 197 ? 3.20794 2.00814 2.51763 0.14662  -0.31216 -0.73531 177 SER E OG  
8963 N N   . THR E 198 ? 3.23601 2.07206 2.50096 0.24630  -0.30703 -0.68346 178 THR E N   
8964 C CA  . THR E 198 ? 3.27175 2.13693 2.52044 0.27305  -0.30403 -0.68501 178 THR E CA  
8965 C C   . THR E 198 ? 3.22280 2.12763 2.47977 0.29598  -0.30099 -0.64376 178 THR E C   
8966 O O   . THR E 198 ? 3.14522 2.04592 2.42117 0.29191  -0.30246 -0.61412 178 THR E O   
8967 C CB  . THR E 198 ? 3.25044 2.05882 2.48978 0.27834  -0.29749 -0.69543 178 THR E CB  
8968 O OG1 . THR E 198 ? 3.19436 1.95372 2.44911 0.27822  -0.29339 -0.66554 178 THR E OG1 
8969 C CG2 . THR E 198 ? 3.25997 2.02654 2.48865 0.25604  -0.30125 -0.73683 178 THR E CG2 
8970 N N   . TYR E 199 ? 3.19518 2.13735 2.43688 0.32048  -0.29624 -0.64205 179 TYR E N   
8971 C CA  . TYR E 199 ? 3.18652 2.16525 2.43417 0.34328  -0.29057 -0.60318 179 TYR E CA  
8972 C C   . TYR E 199 ? 3.17729 2.12671 2.43071 0.35932  -0.27841 -0.58878 179 TYR E C   
8973 O O   . TYR E 199 ? 3.18212 2.08639 2.43083 0.35551  -0.27571 -0.61131 179 TYR E O   
8974 C CB  . TYR E 199 ? 3.28304 2.32999 2.50756 0.36060  -0.29225 -0.60832 179 TYR E CB  
8975 C CG  . TYR E 199 ? 3.34857 2.43143 2.57023 0.34851  -0.30667 -0.62168 179 TYR E CG  
8976 C CD1 . TYR E 199 ? 3.41119 2.49698 2.61984 0.33540  -0.31557 -0.66558 179 TYR E CD1 
8977 C CD2 . TYR E 199 ? 3.33379 2.44819 2.56816 0.35084  -0.31264 -0.59152 179 TYR E CD2 
8978 C CE1 . TYR E 199 ? 3.42000 2.54143 2.63140 0.32469  -0.32970 -0.67967 179 TYR E CE1 
8979 C CE2 . TYR E 199 ? 3.40928 2.55846 2.64373 0.34138  -0.32695 -0.60529 179 TYR E CE2 
8980 C CZ  . TYR E 199 ? 3.41679 2.57068 2.64112 0.32830  -0.33527 -0.64969 179 TYR E CZ  
8981 O OH  . TYR E 199 ? 3.42018 2.61109 2.64990 0.31901  -0.35045 -0.66521 179 TYR E OH  
8982 N N   . SER E 200 ? 3.14467 2.12043 2.41042 0.37753  -0.27157 -0.55099 180 SER E N   
8983 C CA  . SER E 200 ? 3.14319 2.09991 2.42221 0.39401  -0.25946 -0.53399 180 SER E CA  
8984 C C   . SER E 200 ? 3.20997 2.22182 2.49112 0.41646  -0.24943 -0.50174 180 SER E C   
8985 O O   . SER E 200 ? 3.22225 2.27587 2.49807 0.41765  -0.25437 -0.48569 180 SER E O   
8986 C CB  . SER E 200 ? 3.04586 1.94439 2.35478 0.38450  -0.26306 -0.51433 180 SER E CB  
8987 O OG  . SER E 200 ? 3.03700 1.88072 2.33956 0.36324  -0.27079 -0.54199 180 SER E OG  
8988 N N   . MET E 201 ? 3.09097 2.10203 2.38062 0.43443  -0.23490 -0.49218 181 MET E N   
8989 C CA  . MET E 201 ? 3.11920 2.18050 2.41156 0.45531  -0.22137 -0.46066 181 MET E CA  
8990 C C   . MET E 201 ? 3.12255 2.16728 2.44406 0.46907  -0.20671 -0.44403 181 MET E C   
8991 O O   . MET E 201 ? 3.10431 2.11587 2.42653 0.47093  -0.20337 -0.46916 181 MET E O   
8992 C CB  . MET E 201 ? 3.22921 2.34169 2.47954 0.46937  -0.21438 -0.47962 181 MET E CB  
8993 C CG  . MET E 201 ? 3.33586 2.49975 2.58238 0.49048  -0.19872 -0.44513 181 MET E CG  
8994 S SD  . MET E 201 ? 3.55788 2.76732 2.75524 0.51445  -0.18232 -0.46843 181 MET E SD  
8995 C CE  . MET E 201 ? 3.70708 2.94969 2.92360 0.53608  -0.15562 -0.41993 181 MET E CE  
8996 N N   . SER E 202 ? 3.16292 2.23116 2.51028 0.47882  -0.19873 -0.40223 182 SER E N   
8997 C CA  . SER E 202 ? 3.19846 2.26226 2.57959 0.49310  -0.18322 -0.38311 182 SER E CA  
8998 C C   . SER E 202 ? 3.41857 2.54281 2.79318 0.51209  -0.16278 -0.35773 182 SER E C   
8999 O O   . SER E 202 ? 3.47976 2.64296 2.82716 0.51350  -0.16416 -0.34731 182 SER E O   
9000 C CB  . SER E 202 ? 3.12118 2.14691 2.55001 0.48541  -0.19312 -0.35387 182 SER E CB  
9001 O OG  . SER E 202 ? 3.15213 2.20168 2.58935 0.48172  -0.19956 -0.31949 182 SER E OG  
9002 N N   . SER E 203 ? 3.21310 2.34423 2.61296 0.52716  -0.14340 -0.34780 183 SER E N   
9003 C CA  . SER E 203 ? 3.32522 2.51127 2.72093 0.54536  -0.11918 -0.32256 183 SER E CA  
9004 C C   . SER E 203 ? 3.32558 2.50687 2.77724 0.55411  -0.10378 -0.29788 183 SER E C   
9005 O O   . SER E 203 ? 3.25945 2.40224 2.73818 0.55364  -0.10698 -0.31585 183 SER E O   
9006 C CB  . SER E 203 ? 3.36269 2.58006 2.70824 0.56012  -0.10447 -0.35367 183 SER E CB  
9007 O OG  . SER E 203 ? 3.45603 2.72762 2.78505 0.57667  -0.08208 -0.32755 183 SER E OG  
9008 N N   . THR E 204 ? 3.32689 2.54674 2.79673 0.56217  -0.08764 -0.25687 184 THR E N   
9009 C CA  . THR E 204 ? 3.31090 2.53075 2.84225 0.56844  -0.07365 -0.22853 184 THR E CA  
9010 C C   . THR E 204 ? 3.36855 2.64328 2.89402 0.58714  -0.03894 -0.21304 184 THR E C   
9011 O O   . THR E 204 ? 3.41038 2.72432 2.90523 0.59122  -0.02910 -0.19016 184 THR E O   
9012 C CB  . THR E 204 ? 3.25960 2.46705 2.83164 0.55727  -0.08830 -0.18779 184 THR E CB  
9013 O OG1 . THR E 204 ? 3.21223 2.36985 2.78265 0.54077  -0.11905 -0.20292 184 THR E OG1 
9014 C CG2 . THR E 204 ? 3.22023 2.42311 2.86222 0.56253  -0.07752 -0.16232 184 THR E CG2 
9015 N N   . LEU E 205 ? 3.34744 2.62407 2.90112 0.59923  -0.02017 -0.22556 185 LEU E N   
9016 C CA  . LEU E 205 ? 3.40107 2.72936 2.95498 0.61775  0.01677  -0.21184 185 LEU E CA  
9017 C C   . LEU E 205 ? 3.36798 2.70709 2.99406 0.61726  0.02970  -0.16775 185 LEU E C   
9018 O O   . LEU E 205 ? 3.34104 2.67222 3.02288 0.62282  0.03885  -0.17083 185 LEU E O   
9019 C CB  . LEU E 205 ? 3.41801 2.74618 2.96191 0.63254  0.03079  -0.25299 185 LEU E CB  
9020 C CG  . LEU E 205 ? 3.49098 2.87398 3.02157 0.65415  0.07087  -0.24786 185 LEU E CG  
9021 C CD1 . LEU E 205 ? 3.55802 2.97521 3.00820 0.66147  0.07842  -0.25208 185 LEU E CD1 
9022 C CD2 . LEU E 205 ? 3.45639 2.83149 2.99995 0.66846  0.08180  -0.28632 185 LEU E CD2 
9023 N N   . THR E 206 ? 3.36415 2.72140 2.99060 0.61067  0.02906  -0.12665 186 THR E N   
9024 C CA  . THR E 206 ? 3.32729 2.69388 3.02221 0.60795  0.03889  -0.08201 186 THR E CA  
9025 C C   . THR E 206 ? 3.37420 2.78885 3.08843 0.62389  0.08158  -0.06800 186 THR E C   
9026 O O   . THR E 206 ? 3.44733 2.90187 3.10683 0.63537  0.10592  -0.06702 186 THR E O   
9027 C CB  . THR E 206 ? 3.31830 2.69205 3.00198 0.59787  0.02744  -0.04251 186 THR E CB  
9028 O OG1 . THR E 206 ? 3.39575 2.81330 3.01627 0.60734  0.04789  -0.03290 186 THR E OG1 
9029 C CG2 . THR E 206 ? 3.27588 2.60580 2.93976 0.58295  -0.01277 -0.05804 186 THR E CG2 
9030 N N   . LEU E 207 ? 3.40140 2.81238 3.19378 0.62524  0.09073  -0.05755 187 LEU E N   
9031 C CA  . LEU E 207 ? 3.44134 2.89791 3.26334 0.63978  0.13267  -0.04689 187 LEU E CA  
9032 C C   . LEU E 207 ? 3.38301 2.83828 3.30255 0.63423  0.13673  -0.01483 187 LEU E C   
9033 O O   . LEU E 207 ? 3.30846 2.71940 3.27403 0.62335  0.10459  -0.01580 187 LEU E O   
9034 C CB  . LEU E 207 ? 3.47007 2.92768 3.27786 0.65512  0.14405  -0.09476 187 LEU E CB  
9035 C CG  . LEU E 207 ? 3.55355 3.04108 3.27427 0.66924  0.16287  -0.11851 187 LEU E CG  
9036 C CD1 . LEU E 207 ? 3.56126 3.03255 3.26793 0.68122  0.16055  -0.17210 187 LEU E CD1 
9037 C CD2 . LEU E 207 ? 3.61768 3.16509 3.33205 0.68193  0.20878  -0.08712 187 LEU E CD2 
9038 N N   . THR E 208 ? 3.37854 2.88253 3.32891 0.64209  0.17682  0.01329  188 THR E N   
9039 C CA  . THR E 208 ? 3.32969 2.83990 3.37945 0.63786  0.18549  0.04184  188 THR E CA  
9040 C C   . THR E 208 ? 3.30519 2.80400 3.41049 0.64750  0.18593  0.00654  188 THR E C   
9041 O O   . THR E 208 ? 3.34076 2.83852 3.40526 0.66010  0.19059  -0.03554 188 THR E O   
9042 C CB  . THR E 208 ? 3.38077 2.94855 3.44587 0.64190  0.23149  0.08428  188 THR E CB  
9043 O OG1 . THR E 208 ? 3.43500 3.04187 3.50512 0.65956  0.27073  0.06432  188 THR E OG1 
9044 C CG2 . THR E 208 ? 3.43780 3.02262 3.41671 0.64047  0.23810  0.10630  188 THR E CG2 
9045 N N   . LYS E 209 ? 3.36848 2.85749 3.56919 0.64225  0.17917  0.02328  189 LYS E N   
9046 C CA  . LYS E 209 ? 3.34112 2.81790 3.60199 0.65235  0.17651  -0.00895 189 LYS E CA  
9047 C C   . LYS E 209 ? 3.40659 2.94056 3.67886 0.67012  0.22503  -0.01783 189 LYS E C   
9048 O O   . LYS E 209 ? 3.42065 2.94908 3.68790 0.68448  0.22678  -0.06055 189 LYS E O   
9049 C CB  . LYS E 209 ? 3.25960 2.71351 3.62203 0.64345  0.15577  0.01168  189 LYS E CB  
9050 C CG  . LYS E 209 ? 3.22674 2.66370 3.65510 0.65480  0.14769  -0.02200 189 LYS E CG  
9051 C CD  . LYS E 209 ? 3.14590 2.55925 3.67445 0.64694  0.12396  -0.00193 189 LYS E CD  
9052 C CE  . LYS E 209 ? 3.11723 2.51438 3.71184 0.66044  0.11462  -0.03675 189 LYS E CE  
9053 N NZ  . LYS E 209 ? 3.03962 2.41336 3.73397 0.65450  0.08902  -0.01935 189 LYS E NZ  
9054 N N   . ASP E 210 ? 3.28074 2.86882 3.56689 0.66988  0.26536  0.02211  190 ASP E N   
9055 C CA  . ASP E 210 ? 3.34761 2.99338 3.64203 0.68712  0.31591  0.01631  190 ASP E CA  
9056 C C   . ASP E 210 ? 3.42048 3.07654 3.61109 0.70225  0.32812  -0.01832 190 ASP E C   
9057 O O   . ASP E 210 ? 3.45672 3.13642 3.64773 0.72073  0.35187  -0.04962 190 ASP E O   
9058 C CB  . ASP E 210 ? 3.38038 3.07805 3.70494 0.68162  0.35728  0.07040  190 ASP E CB  
9059 C CG  . ASP E 210 ? 3.42857 3.13380 3.66224 0.67554  0.36281  0.09842  190 ASP E CG  
9060 O OD1 . ASP E 210 ? 3.50983 3.24627 3.66631 0.68929  0.39242  0.08886  190 ASP E OD1 
9061 O OD2 . ASP E 210 ? 3.38517 3.06396 3.62327 0.65844  0.33597  0.12870  190 ASP E OD2 
9062 N N   . GLU E 211 ? 3.46601 3.10476 3.56868 0.69555  0.31083  -0.01474 191 GLU E N   
9063 C CA  . GLU E 211 ? 3.53181 3.17638 3.53515 0.70921  0.31672  -0.04953 191 GLU E CA  
9064 C C   . GLU E 211 ? 3.50157 3.10088 3.49281 0.71455  0.28440  -0.10510 191 GLU E C   
9065 O O   . GLU E 211 ? 3.54856 3.15935 3.49111 0.73170  0.29736  -0.14271 191 GLU E O   
9066 C CB  . GLU E 211 ? 3.55827 3.19546 3.47805 0.69991  0.30297  -0.03102 191 GLU E CB  
9067 C CG  . GLU E 211 ? 3.65375 3.33792 3.49428 0.71414  0.34074  -0.02293 191 GLU E CG  
9068 C CD  . GLU E 211 ? 3.67618 3.35242 3.44283 0.70501  0.32426  -0.00095 191 GLU E CD  
9069 O OE1 . GLU E 211 ? 3.62046 3.27075 3.41713 0.68645  0.29741  0.02709  191 GLU E OE1 
9070 O OE2 . GLU E 211 ? 3.74791 3.44320 3.42639 0.71763  0.33657  -0.01314 191 GLU E OE2 
9071 N N   . TYR E 212 ? 3.65512 3.20065 3.68768 0.70069  0.24217  -0.11079 192 TYR E N   
9072 C CA  . TYR E 212 ? 3.62445 3.11917 3.64213 0.70375  0.20931  -0.16066 192 TYR E CA  
9073 C C   . TYR E 212 ? 3.62320 3.12697 3.69447 0.72141  0.22414  -0.19058 192 TYR E C   
9074 O O   . TYR E 212 ? 3.63312 3.11280 3.67015 0.73201  0.21263  -0.23707 192 TYR E O   
9075 C CB  . TYR E 212 ? 3.54281 2.97655 3.58892 0.68482  0.16236  -0.15475 192 TYR E CB  
9076 C CG  . TYR E 212 ? 3.50728 2.88097 3.53986 0.68569  0.12708  -0.20176 192 TYR E CG  
9077 C CD1 . TYR E 212 ? 3.52809 2.88244 3.47620 0.68715  0.11552  -0.23694 192 TYR E CD1 
9078 C CD2 . TYR E 212 ? 3.44089 2.77448 3.54465 0.68477  0.10394  -0.21051 192 TYR E CD2 
9079 C CE1 . TYR E 212 ? 3.44433 2.74067 3.37931 0.68637  0.08425  -0.27816 192 TYR E CE1 
9080 C CE2 . TYR E 212 ? 3.36500 2.63881 3.45175 0.68573  0.07171  -0.25167 192 TYR E CE2 
9081 C CZ  . TYR E 212 ? 3.36416 2.61917 3.36638 0.68575  0.06300  -0.28454 192 TYR E CZ  
9082 O OH  . TYR E 212 ? 3.28189 2.47468 3.26656 0.68529  0.03207  -0.32400 192 TYR E OH  
9083 N N   . GLU E 213 ? 3.51684 3.05530 3.67370 0.72493  0.24925  -0.16552 193 GLU E N   
9084 C CA  . GLU E 213 ? 3.50963 3.05918 3.73087 0.74178  0.26210  -0.19224 193 GLU E CA  
9085 C C   . GLU E 213 ? 3.58848 3.20040 3.78682 0.76313  0.31226  -0.20294 193 GLU E C   
9086 O O   . GLU E 213 ? 3.59130 3.23512 3.85946 0.77650  0.33725  -0.20900 193 GLU E O   
9087 C CB  . GLU E 213 ? 3.45116 3.00453 3.78597 0.73456  0.26004  -0.16328 193 GLU E CB  
9088 C CG  . GLU E 213 ? 3.37024 2.85826 3.72937 0.71664  0.20866  -0.15619 193 GLU E CG  
9089 C CD  . GLU E 213 ? 3.30537 2.78932 3.77965 0.71377  0.19997  -0.13945 193 GLU E CD  
9090 O OE1 . GLU E 213 ? 3.30683 2.83561 3.83722 0.70807  0.22689  -0.09829 193 GLU E OE1 
9091 O OE2 . GLU E 213 ? 3.25360 2.68782 3.76211 0.71743  0.16542  -0.16784 193 GLU E OE2 
9092 N N   . ARG E 214 ? 3.48098 3.11145 3.58330 0.76778  0.32724  -0.20650 194 ARG E N   
9093 C CA  . ARG E 214 ? 3.55834 3.24111 3.62177 0.79062  0.37131  -0.22271 194 ARG E CA  
9094 C C   . ARG E 214 ? 3.57122 3.22625 3.56121 0.80485  0.35398  -0.27917 194 ARG E C   
9095 O O   . ARG E 214 ? 3.56150 3.22888 3.56769 0.82538  0.36810  -0.31448 194 ARG E O   
9096 C CB  . ARG E 214 ? 3.62347 3.35168 3.62962 0.78873  0.40495  -0.18325 194 ARG E CB  
9097 C CG  . ARG E 214 ? 3.61379 3.37488 3.68967 0.77609  0.42928  -0.12573 194 ARG E CG  
9098 C CD  . ARG E 214 ? 3.68217 3.47951 3.68892 0.77464  0.45893  -0.08785 194 ARG E CD  
9099 N NE  . ARG E 214 ? 3.67489 3.50145 3.74629 0.76158  0.48327  -0.03106 194 ARG E NE  
9100 C CZ  . ARG E 214 ? 3.72589 3.57985 3.75276 0.75705  0.50819  0.01167  194 ARG E CZ  
9101 N NH1 . ARG E 214 ? 3.78971 3.64724 3.70640 0.76559  0.51142  0.00442  194 ARG E NH1 
9102 N NH2 . ARG E 214 ? 3.71243 3.58891 3.80702 0.74389  0.52903  0.06264  194 ARG E NH2 
9103 N N   . HIS E 215 ? 3.57112 3.18888 3.48276 0.79432  0.32301  -0.28920 195 HIS E N   
9104 C CA  . HIS E 215 ? 3.53992 3.12637 3.38241 0.80434  0.30263  -0.34192 195 HIS E CA  
9105 C C   . HIS E 215 ? 3.43384 2.95516 3.31558 0.79793  0.25992  -0.37326 195 HIS E C   
9106 O O   . HIS E 215 ? 3.38461 2.87886 3.33326 0.78321  0.23962  -0.35239 195 HIS E O   
9107 C CB  . HIS E 215 ? 3.56865 3.14303 3.31630 0.79453  0.28646  -0.34008 195 HIS E CB  
9108 C CG  . HIS E 215 ? 3.66815 3.29681 3.37661 0.79745  0.32138  -0.30150 195 HIS E CG  
9109 N ND1 . HIS E 215 ? 3.74016 3.41589 3.39545 0.82040  0.35900  -0.31228 195 HIS E ND1 
9110 C CD2 . HIS E 215 ? 3.69316 3.33364 3.40474 0.78131  0.32377  -0.25204 195 HIS E CD2 
9111 C CE1 . HIS E 215 ? 3.81379 3.52666 3.43891 0.81807  0.38357  -0.27012 195 HIS E CE1 
9112 N NE2 . HIS E 215 ? 3.76885 3.46109 3.42825 0.79424  0.36244  -0.23298 195 HIS E NE2 
9113 N N   . ASN E 216 ? 3.65979 3.15328 3.49663 0.80997  0.24548  -0.42428 196 ASN E N   
9114 C CA  . ASN E 216 ? 3.56276 2.98906 3.42394 0.80554  0.20507  -0.45747 196 ASN E CA  
9115 C C   . ASN E 216 ? 3.52198 2.89530 3.30440 0.79662  0.17029  -0.49072 196 ASN E C   
9116 O O   . ASN E 216 ? 3.44232 2.75159 3.23901 0.78548  0.13291  -0.50751 196 ASN E O   
9117 C CB  . ASN E 216 ? 3.54459 2.97812 3.44960 0.82995  0.21752  -0.49244 196 ASN E CB  
9118 C CG  . ASN E 216 ? 3.52367 2.96805 3.53605 0.83062  0.22405  -0.46995 196 ASN E CG  
9119 O OD1 . ASN E 216 ? 3.44568 2.83916 3.50456 0.82849  0.19272  -0.48649 196 ASN E OD1 
9120 N ND2 . ASN E 216 ? 3.59319 3.10246 3.64538 0.83345  0.26416  -0.43180 196 ASN E ND2 
9121 N N   . SER E 217 ? 3.57289 2.96901 3.27381 0.80097  0.18067  -0.50082 197 SER E N   
9122 C CA  . SER E 217 ? 3.53883 2.88968 3.16746 0.79115  0.14873  -0.53195 197 SER E CA  
9123 C C   . SER E 217 ? 3.56933 2.92760 3.15717 0.77117  0.14094  -0.49980 197 SER E C   
9124 O O   . SER E 217 ? 3.64981 3.06218 3.21265 0.77707  0.16911  -0.47350 197 SER E O   
9125 C CB  . SER E 217 ? 3.57193 2.93860 3.13735 0.81343  0.16088  -0.57640 197 SER E CB  
9126 O OG  . SER E 217 ? 3.66565 3.10133 3.20350 0.82975  0.20147  -0.55893 197 SER E OG  
9127 N N   . TYR E 218 ? 3.54145 2.84461 3.12167 0.74835  0.10309  -0.50199 198 TYR E N   
9128 C CA  . TYR E 218 ? 3.56209 2.86666 3.10915 0.72841  0.09064  -0.47433 198 TYR E CA  
9129 C C   . TYR E 218 ? 3.51662 2.77408 3.00614 0.71571  0.05759  -0.50976 198 TYR E C   
9130 O O   . TYR E 218 ? 3.43945 2.63779 2.94592 0.70598  0.03039  -0.53174 198 TYR E O   
9131 C CB  . TYR E 218 ? 3.53383 2.82189 3.14353 0.71027  0.07889  -0.43193 198 TYR E CB  
9132 C CG  . TYR E 218 ? 3.58350 2.91874 3.25553 0.71950  0.11065  -0.39366 198 TYR E CG  
9133 C CD1 . TYR E 218 ? 3.66591 3.05130 3.32720 0.71811  0.13380  -0.35224 198 TYR E CD1 
9134 C CD2 . TYR E 218 ? 3.54864 2.87749 3.29172 0.72943  0.11705  -0.39905 198 TYR E CD2 
9135 C CE1 . TYR E 218 ? 3.71204 3.13965 3.43229 0.72454  0.16442  -0.31592 198 TYR E CE1 
9136 C CE2 . TYR E 218 ? 3.59261 2.96681 3.39901 0.73642  0.14683  -0.36463 198 TYR E CE2 
9137 C CZ  . TYR E 218 ? 3.67418 3.09754 3.46922 0.73302  0.17141  -0.32248 198 TYR E CZ  
9138 O OH  . TYR E 218 ? 3.71702 3.18461 3.57689 0.73806  0.20261  -0.28690 198 TYR E OH  
9139 N N   . THR E 219 ? 3.60717 2.88961 3.02932 0.71568  0.05963  -0.51498 199 THR E N   
9140 C CA  . THR E 219 ? 3.57531 2.82207 2.94144 0.70552  0.03181  -0.55246 199 THR E CA  
9141 C C   . THR E 219 ? 3.60214 2.86126 2.93171 0.68895  0.01996  -0.53117 199 THR E C   
9142 O O   . THR E 219 ? 3.66917 2.97617 2.99121 0.69386  0.03917  -0.49624 199 THR E O   
9143 C CB  . THR E 219 ? 3.60670 2.87067 2.91990 0.72744  0.04284  -0.59602 199 THR E CB  
9144 O OG1 . THR E 219 ? 3.60002 2.86846 2.95002 0.74785  0.06150  -0.60952 199 THR E OG1 
9145 C CG2 . THR E 219 ? 3.56051 2.77492 2.83209 0.71595  0.01079  -0.64102 199 THR E CG2 
9146 N N   . CYS E 220 ? 3.68971 2.90429 2.99740 0.66923  -0.01177 -0.55255 200 CYS E N   
9147 C CA  . CYS E 220 ? 3.71045 2.93414 2.98053 0.65386  -0.02692 -0.54257 200 CYS E CA  
9148 C C   . CYS E 220 ? 3.68966 2.89181 2.90619 0.64968  -0.04668 -0.59102 200 CYS E C   
9149 O O   . CYS E 220 ? 3.62531 2.77528 2.85009 0.64083  -0.06442 -0.62211 200 CYS E O   
9150 C CB  . CYS E 220 ? 3.66364 2.85472 2.97257 0.62915  -0.04734 -0.51334 200 CYS E CB  
9151 S SG  . CYS E 220 ? 3.54959 2.65866 2.89162 0.61179  -0.07479 -0.53833 200 CYS E SG  
9152 N N   . GLU E 221 ? 3.53562 2.77599 2.69725 0.65639  -0.04449 -0.59771 201 GLU E N   
9153 C CA  . GLU E 221 ? 3.52977 2.75656 2.64026 0.65390  -0.06337 -0.64430 201 GLU E CA  
9154 C C   . GLU E 221 ? 3.53546 2.76893 2.62222 0.63539  -0.08415 -0.63688 201 GLU E C   
9155 O O   . GLU E 221 ? 3.58826 2.86398 2.66244 0.64015  -0.07542 -0.60449 201 GLU E O   
9156 C CB  . GLU E 221 ? 3.59268 2.85830 2.65386 0.68276  -0.04497 -0.66888 201 GLU E CB  
9157 C CG  . GLU E 221 ? 3.67497 3.00214 2.71741 0.70167  -0.01729 -0.63296 201 GLU E CG  
9158 C CD  . GLU E 221 ? 3.73721 3.09957 2.72234 0.73108  -0.00003 -0.65975 201 GLU E CD  
9159 O OE1 . GLU E 221 ? 3.71853 3.05766 2.68084 0.73698  -0.01139 -0.70784 201 GLU E OE1 
9160 O OE2 . GLU E 221 ? 3.80842 3.21970 2.76931 0.74876  0.02482  -0.63259 201 GLU E OE2 
9161 N N   . ALA E 222 ? 3.46609 2.65747 2.54767 0.61444  -0.11128 -0.66694 202 ALA E N   
9162 C CA  . ALA E 222 ? 3.45331 2.64929 2.51588 0.59579  -0.13285 -0.66760 202 ALA E CA  
9163 C C   . ALA E 222 ? 3.50274 2.70131 2.51536 0.59853  -0.14743 -0.71652 202 ALA E C   
9164 O O   . ALA E 222 ? 3.53573 2.70763 2.53872 0.60403  -0.14958 -0.75458 202 ALA E O   
9165 C CB  . ALA E 222 ? 3.40499 2.55117 2.50697 0.56597  -0.15231 -0.65992 202 ALA E CB  
9166 N N   . THR E 223 ? 3.46417 2.69409 2.44623 0.59527  -0.15931 -0.71621 203 THR E N   
9167 C CA  . THR E 223 ? 3.49175 2.73197 2.42563 0.59969  -0.17512 -0.76085 203 THR E CA  
9168 C C   . THR E 223 ? 3.43499 2.65208 2.37954 0.56940  -0.20371 -0.77641 203 THR E C   
9169 O O   . THR E 223 ? 3.44058 2.68433 2.38231 0.56202  -0.21297 -0.75739 203 THR E O   
9170 C CB  . THR E 223 ? 3.61157 2.91064 2.49639 0.62502  -0.16583 -0.75131 203 THR E CB  
9171 O OG1 . THR E 223 ? 3.62727 2.95160 2.52131 0.61709  -0.16875 -0.71076 203 THR E OG1 
9172 C CG2 . THR E 223 ? 3.65018 2.97238 2.52437 0.65454  -0.13382 -0.73683 203 THR E CG2 
9173 N N   . HIS E 224 ? 3.72454 2.89177 2.68163 0.55208  -0.21718 -0.81122 204 HIS E N   
9174 C CA  . HIS E 224 ? 3.67035 2.81132 2.64067 0.52130  -0.24149 -0.82912 204 HIS E CA  
9175 C C   . HIS E 224 ? 3.70257 2.84068 2.63936 0.52088  -0.25934 -0.88310 204 HIS E C   
9176 O O   . HIS E 224 ? 3.72411 2.85682 2.63597 0.53967  -0.25436 -0.91128 204 HIS E O   
9177 C CB  . HIS E 224 ? 3.57021 2.64880 2.58370 0.49733  -0.24354 -0.82356 204 HIS E CB  
9178 C CG  . HIS E 224 ? 3.51524 2.57245 2.54956 0.46475  -0.26184 -0.82508 204 HIS E CG  
9179 N ND1 . HIS E 224 ? 3.49337 2.52668 2.52024 0.44513  -0.28035 -0.86695 204 HIS E ND1 
9180 C CD2 . HIS E 224 ? 3.48242 2.53912 2.54609 0.44846  -0.26365 -0.79031 204 HIS E CD2 
9181 C CE1 . HIS E 224 ? 3.44956 2.47057 2.50116 0.41769  -0.29074 -0.85739 204 HIS E CE1 
9182 N NE2 . HIS E 224 ? 3.43970 2.47428 2.51236 0.42004  -0.28128 -0.81159 204 HIS E NE2 
9183 N N   . LYS E 225 ? 3.69521 2.83725 2.63411 0.49940  -0.28090 -0.89849 205 LYS E N   
9184 C CA  . LYS E 225 ? 3.71720 2.86204 2.62804 0.49773  -0.30102 -0.94948 205 LYS E CA  
9185 C C   . LYS E 225 ? 3.67795 2.76405 2.59632 0.48488  -0.30753 -0.98820 205 LYS E C   
9186 O O   . LYS E 225 ? 3.71627 2.80183 2.60644 0.49199  -0.32026 -1.03248 205 LYS E O   
9187 C CB  . LYS E 225 ? 3.69842 2.86167 2.62009 0.47523  -0.32240 -0.95520 205 LYS E CB  
9188 C CG  . LYS E 225 ? 3.73837 2.95760 2.65025 0.48803  -0.32030 -0.91984 205 LYS E CG  
9189 C CD  . LYS E 225 ? 3.70692 2.93886 2.64110 0.46315  -0.34065 -0.92201 205 LYS E CD  
9190 C CE  . LYS E 225 ? 3.74228 3.02376 2.66984 0.47594  -0.33878 -0.88256 205 LYS E CE  
9191 N NZ  . LYS E 225 ? 3.70500 3.00282 2.65560 0.45416  -0.35943 -0.88595 205 LYS E NZ  
9192 N N   . THR E 226 ? 3.69211 2.72637 2.64582 0.46708  -0.30064 -0.97311 206 THR E N   
9193 C CA  . THR E 226 ? 3.65739 2.62915 2.61745 0.45268  -0.30851 -1.00824 206 THR E CA  
9194 C C   . THR E 226 ? 3.70131 2.66868 2.63166 0.48184  -0.30188 -1.03456 206 THR E C   
9195 O O   . THR E 226 ? 3.72090 2.66562 2.63326 0.47996  -0.31622 -1.08027 206 THR E O   
9196 C CB  . THR E 226 ? 3.58214 2.49816 2.58072 0.43204  -0.30166 -0.98242 206 THR E CB  
9197 O OG1 . THR E 226 ? 3.58114 2.51062 2.59021 0.45248  -0.28124 -0.94197 206 THR E OG1 
9198 C CG2 . THR E 226 ? 3.53681 2.44818 2.56240 0.40010  -0.31058 -0.96632 206 THR E CG2 
9199 N N   . SER E 227 ? 3.81201 2.80092 2.73879 0.50895  -0.28005 -1.00698 207 SER E N   
9200 C CA  . SER E 227 ? 3.85297 2.84075 2.75522 0.53878  -0.26985 -1.02858 207 SER E CA  
9201 C C   . SER E 227 ? 3.93723 2.99294 2.80052 0.57175  -0.25810 -1.02256 207 SER E C   
9202 O O   . SER E 227 ? 3.96191 3.06239 2.82407 0.57416  -0.25192 -0.98867 207 SER E O   
9203 C CB  . SER E 227 ? 3.81316 2.76827 2.74520 0.54534  -0.25195 -1.00489 207 SER E CB  
9204 O OG  . SER E 227 ? 3.81018 2.76101 2.72226 0.57329  -0.24320 -1.03030 207 SER E OG  
9205 N N   . THR E 228 ? 3.81611 2.87687 2.64450 0.59821  -0.25524 -1.05627 208 THR E N   
9206 C CA  . THR E 228 ? 3.90395 3.02427 2.68894 0.63319  -0.24086 -1.05217 208 THR E CA  
9207 C C   . THR E 228 ? 3.93410 3.07311 2.72916 0.65746  -0.20817 -1.01803 208 THR E C   
9208 O O   . THR E 228 ? 4.02455 3.21670 2.79191 0.68197  -0.19014 -0.99709 208 THR E O   
9209 C CB  . THR E 228 ? 3.95684 3.07716 2.69439 0.65257  -0.25387 -1.10714 208 THR E CB  
9210 O OG1 . THR E 228 ? 4.06385 3.24156 2.75309 0.68792  -0.23912 -1.10186 208 THR E OG1 
9211 C CG2 . THR E 228 ? 3.92565 2.99834 2.67196 0.65996  -0.25036 -1.13466 208 THR E CG2 
9212 N N   . SER E 229 ? 3.84828 2.94448 2.68254 0.65135  -0.20027 -1.01194 209 SER E N   
9213 C CA  . SER E 229 ? 3.87557 2.98991 2.73017 0.67188  -0.17002 -0.97874 209 SER E CA  
9214 C C   . SER E 229 ? 3.84406 2.96941 2.73958 0.65550  -0.16098 -0.92352 209 SER E C   
9215 O O   . SER E 229 ? 3.75910 2.85107 2.68233 0.62507  -0.17827 -0.91542 209 SER E O   
9216 C CB  . SER E 229 ? 3.82450 2.88842 2.70507 0.67538  -0.16767 -0.99819 209 SER E CB  
9217 O OG  . SER E 229 ? 3.72697 2.73104 2.64539 0.64301  -0.18573 -0.99617 209 SER E OG  
9218 N N   . PRO E 230 ? 3.72819 2.89931 2.62781 0.67495  -0.13385 -0.88517 210 PRO E N   
9219 C CA  . PRO E 230 ? 3.70185 2.87928 2.64539 0.66049  -0.12543 -0.83245 210 PRO E CA  
9220 C C   . PRO E 230 ? 3.61865 2.74199 2.61681 0.64592  -0.12765 -0.82552 210 PRO E C   
9221 O O   . PRO E 230 ? 3.61631 2.73162 2.63189 0.66302  -0.11218 -0.82970 210 PRO E O   
9222 C CB  . PRO E 230 ? 3.76020 2.99525 2.69424 0.68820  -0.09323 -0.79959 210 PRO E CB  
9223 C CG  . PRO E 230 ? 3.79488 3.03947 2.69699 0.71738  -0.08015 -0.83523 210 PRO E CG  
9224 C CD  . PRO E 230 ? 3.79145 3.00899 2.65631 0.71106  -0.10855 -0.88808 210 PRO E CD  
9225 N N   . ILE E 231 ? 3.70354 2.78879 2.72754 0.61542  -0.14746 -0.81656 211 ILE E N   
9226 C CA  . ILE E 231 ? 3.61404 2.64028 2.68295 0.60091  -0.15338 -0.81226 211 ILE E CA  
9227 C C   . ILE E 231 ? 3.63494 2.67846 2.74594 0.61331  -0.13108 -0.76981 211 ILE E C   
9228 O O   . ILE E 231 ? 3.65090 2.72265 2.77954 0.60793  -0.12451 -0.72794 211 ILE E O   
9229 C CB  . ILE E 231 ? 3.53458 2.51984 2.61775 0.56625  -0.17682 -0.80832 211 ILE E CB  
9230 C CG1 . ILE E 231 ? 3.45197 2.36944 2.57358 0.55282  -0.18399 -0.80587 211 ILE E CG1 
9231 C CG2 . ILE E 231 ? 3.54520 2.56922 2.63578 0.55652  -0.17568 -0.76791 211 ILE E CG2 
9232 C CD1 . ILE E 231 ? 3.47759 2.34522 2.58634 0.55618  -0.19307 -0.85142 211 ILE E CD1 
9233 N N   . VAL E 232 ? 3.57631 2.60384 2.70560 0.63062  -0.11994 -0.78141 212 VAL E N   
9234 C CA  . VAL E 232 ? 3.60119 2.65674 2.76903 0.64837  -0.09489 -0.74800 212 VAL E CA  
9235 C C   . VAL E 232 ? 3.51716 2.51663 2.73693 0.64031  -0.10290 -0.74216 212 VAL E C   
9236 O O   . VAL E 232 ? 3.46703 2.41030 2.68331 0.63495  -0.11981 -0.77615 212 VAL E O   
9237 C CB  . VAL E 232 ? 3.66114 2.75878 2.80697 0.68140  -0.07051 -0.76601 212 VAL E CB  
9238 C CG1 . VAL E 232 ? 3.63397 2.71673 2.82573 0.69722  -0.05703 -0.76627 212 VAL E CG1 
9239 C CG2 . VAL E 232 ? 3.73638 2.90518 2.86263 0.69524  -0.04650 -0.73461 212 VAL E CG2 
9240 N N   . LYS E 233 ? 3.66732 2.67968 2.93423 0.63953  -0.09236 -0.69887 213 LYS E N   
9241 C CA  . LYS E 233 ? 3.59780 2.56636 2.91827 0.63850  -0.09696 -0.68986 213 LYS E CA  
9242 C C   . LYS E 233 ? 3.63809 2.65449 3.00375 0.65471  -0.07099 -0.65158 213 LYS E C   
9243 O O   . LYS E 233 ? 3.67869 2.73780 3.04770 0.65068  -0.06046 -0.61476 213 LYS E O   
9244 C CB  . LYS E 233 ? 3.52300 2.43577 2.86001 0.61011  -0.12236 -0.67602 213 LYS E CB  
9245 C CG  . LYS E 233 ? 3.42974 2.27857 2.73627 0.59337  -0.14734 -0.71508 213 LYS E CG  
9246 C CD  . LYS E 233 ? 3.32540 2.11002 2.65676 0.57072  -0.16820 -0.70072 213 LYS E CD  
9247 C CE  . LYS E 233 ? 3.35234 2.06567 2.65695 0.55517  -0.19016 -0.73878 213 LYS E CE  
9248 N NZ  . LYS E 233 ? 3.36237 2.08163 2.62570 0.53492  -0.19949 -0.75399 213 LYS E NZ  
9249 N N   . SER E 234 ? 3.67805 2.68739 3.07991 0.67294  -0.06094 -0.66064 214 SER E N   
9250 C CA  . SER E 234 ? 3.71734 2.77746 3.16480 0.69053  -0.03248 -0.62992 214 SER E CA  
9251 C C   . SER E 234 ? 3.66013 2.68201 3.17274 0.69406  -0.03946 -0.62602 214 SER E C   
9252 O O   . SER E 234 ? 3.59201 2.54734 3.10660 0.68642  -0.06517 -0.65024 214 SER E O   
9253 C CB  . SER E 234 ? 3.78565 2.90027 3.20703 0.71795  -0.00336 -0.64862 214 SER E CB  
9254 O OG  . SER E 234 ? 3.82873 2.99248 3.29803 0.73414  0.02715  -0.61912 214 SER E OG  
9255 N N   . PHE E 235 ? 3.64772 2.71148 3.21435 0.70589  -0.01657 -0.59488 215 PHE E N   
9256 C CA  . PHE E 235 ? 3.60107 2.63935 3.23619 0.71368  -0.02057 -0.59194 215 PHE E CA  
9257 C C   . PHE E 235 ? 3.66132 2.76393 3.33675 0.73798  0.01580  -0.58172 215 PHE E C   
9258 O O   . PHE E 235 ? 3.73747 2.90345 3.39884 0.74300  0.04427  -0.55880 215 PHE E O   
9259 C CB  . PHE E 235 ? 3.55450 2.56168 3.23467 0.69441  -0.03975 -0.55536 215 PHE E CB  
9260 C CG  . PHE E 235 ? 3.61618 2.68072 3.33360 0.69284  -0.01810 -0.50607 215 PHE E CG  
9261 C CD1 . PHE E 235 ? 3.62881 2.72180 3.41801 0.70616  -0.00032 -0.48665 215 PHE E CD1 
9262 C CD2 . PHE E 235 ? 3.65533 2.74318 3.33892 0.67751  -0.01698 -0.47921 215 PHE E CD2 
9263 C CE1 . PHE E 235 ? 3.68170 2.82457 3.50683 0.70305  0.01967  -0.44048 215 PHE E CE1 
9264 C CE2 . PHE E 235 ? 3.70906 2.84483 3.42521 0.67584  0.00154  -0.43317 215 PHE E CE2 
9265 C CZ  . PHE E 235 ? 3.72238 2.88478 3.50908 0.68788  0.02034  -0.41315 215 PHE E CZ  
9266 N N   . ASN E 236 ? 3.61619 2.70113 3.34183 0.75338  0.01482  -0.59898 216 ASN E N   
9267 C CA  . ASN E 236 ? 3.66193 2.80466 3.43736 0.77682  0.04881  -0.59270 216 ASN E CA  
9268 C C   . ASN E 236 ? 3.61815 2.74481 3.48220 0.77617  0.04064  -0.57159 216 ASN E C   
9269 O O   . ASN E 236 ? 3.54191 2.60394 3.42581 0.77451  0.00974  -0.59167 216 ASN E O   
9270 C CB  . ASN E 236 ? 3.67148 2.81621 3.42531 0.80175  0.05742  -0.64144 216 ASN E CB  
9271 C CG  . ASN E 236 ? 3.59246 2.80754 3.38865 0.82717  0.09875  -0.63604 216 ASN E CG  
9272 O OD1 . ASN E 236 ? 3.56092 2.83624 3.37237 0.82631  0.12899  -0.59800 216 ASN E OD1 
9273 N ND2 . ASN E 236 ? 3.56543 2.77257 3.38079 0.85012  0.10086  -0.67414 216 ASN E ND2 
9274 N N   . ARG E 237 ? 3.38254 2.56571 3.29876 0.77757  0.06732  -0.53124 217 ARG E N   
9275 C CA  . ARG E 237 ? 3.34975 2.52536 3.35704 0.77730  0.06102  -0.50923 217 ARG E CA  
9276 C C   . ARG E 237 ? 3.32632 2.49633 3.38350 0.80112  0.06325  -0.54251 217 ARG E C   
9277 O O   . ARG E 237 ? 3.24972 2.37063 3.35708 0.80133  0.03539  -0.54945 217 ARG E O   
9278 C CB  . ARG E 237 ? 3.41800 2.66103 3.47035 0.77389  0.09314  -0.45968 217 ARG E CB  
9279 C CG  . ARG E 237 ? 3.41598 2.64675 3.45793 0.74857  0.07808  -0.41875 217 ARG E CG  
9280 C CD  . ARG E 237 ? 3.51776 2.81368 3.52498 0.74558  0.11202  -0.38699 217 ARG E CD  
9281 N NE  . ARG E 237 ? 3.58325 2.94826 3.63172 0.76343  0.15644  -0.37575 217 ARG E NE  
9282 C CZ  . ARG E 237 ? 3.61139 3.01390 3.73210 0.76053  0.17613  -0.33532 217 ARG E CZ  
9283 N NH1 . ARG E 237 ? 3.58019 2.95792 3.74087 0.74170  0.15376  -0.30210 217 ARG E NH1 
9284 N NH2 . ARG E 237 ? 3.67147 3.13783 3.82566 0.77694  0.21985  -0.32826 217 ARG E NH2 
9285 C C1  . NAG F .   ? 2.94527 2.56341 3.46232 -0.12446 -0.04684 -0.59922 1   NAG F C1  
9286 C C2  . NAG F .   ? 2.98928 2.61007 3.53326 -0.14546 -0.03862 -0.60810 1   NAG F C2  
9287 C C3  . NAG F .   ? 2.99784 2.62721 3.57975 -0.17890 -0.01508 -0.66785 1   NAG F C3  
9288 C C4  . NAG F .   ? 2.96321 2.54261 3.59280 -0.16152 0.00428  -0.68743 1   NAG F C4  
9289 C C5  . NAG F .   ? 2.91753 2.48762 3.51889 -0.13203 -0.00667 -0.66626 1   NAG F C5  
9290 C C6  . NAG F .   ? 2.88456 2.39802 3.53675 -0.10565 0.00886  -0.66842 1   NAG F C6  
9291 C C7  . NAG F .   ? 3.04705 2.77374 3.51340 -0.18393 -0.07002 -0.59944 1   NAG F C7  
9292 C C8  . NAG F .   ? 3.08827 2.85613 3.52684 -0.19358 -0.08955 -0.57200 1   NAG F C8  
9293 N N2  . NAG F .   ? 3.02620 2.69361 3.53207 -0.15967 -0.05736 -0.58857 1   NAG F N2  
9294 O O3  . NAG F .   ? 3.03260 2.66026 3.64317 -0.19792 -0.00599 -0.67599 1   NAG F O3  
9295 O O4  . NAG F .   ? 2.96409 2.56318 3.62209 -0.19386 0.02481  -0.74989 1   NAG F O4  
9296 O O5  . NAG F .   ? 2.91041 2.48001 3.46953 -0.10586 -0.02987 -0.61037 1   NAG F O5  
9297 O O6  . NAG F .   ? 2.88430 2.35165 3.56526 -0.08093 0.00860  -0.62749 1   NAG F O6  
9298 O O7  . NAG F .   ? 3.03322 2.78220 3.48857 -0.19823 -0.06628 -0.62907 1   NAG F O7  
9299 C C1  . NAG F .   ? 3.02814 2.61592 3.73793 -0.21726 0.04481  -0.78042 2   NAG F C1  
9300 C C2  . NAG F .   ? 3.00707 2.55155 3.78717 -0.21342 0.07149  -0.81998 2   NAG F C2  
9301 C C3  . NAG F .   ? 3.03318 2.57140 3.87384 -0.24486 0.09638  -0.86619 2   NAG F C3  
9302 C C4  . NAG F .   ? 3.07068 2.67112 3.88012 -0.28732 0.09333  -0.88764 2   NAG F C4  
9303 C C5  . NAG F .   ? 3.08330 2.72663 3.81480 -0.28317 0.06254  -0.84005 2   NAG F C5  
9304 C C6  . NAG F .   ? 3.11327 2.83437 3.80901 -0.32843 0.05809  -0.86796 2   NAG F C6  
9305 C C7  . NAG F .   ? 2.95659 2.39294 3.82392 -0.15401 0.08698  -0.79368 2   NAG F C7  
9306 C C8  . NAG F .   ? 2.93266 2.31240 3.82144 -0.11055 0.08049  -0.73829 2   NAG F C8  
9307 N N2  . NAG F .   ? 2.98384 2.46417 3.79215 -0.16988 0.06966  -0.77658 2   NAG F N2  
9308 O O3  . NAG F .   ? 3.01647 2.54920 3.90700 -0.25706 0.12053  -0.92510 2   NAG F O3  
9309 O O4  . NAG F .   ? 3.09936 2.66997 3.95362 -0.29447 0.10465  -0.88538 2   NAG F O4  
9310 O O5  . NAG F .   ? 3.05342 2.70380 3.74188 -0.25997 0.04616  -0.81725 2   NAG F O5  
9311 O O6  . NAG F .   ? 3.12400 2.88792 3.75037 -0.32256 0.02846  -0.82602 2   NAG F O6  
9312 O O7  . NAG F .   ? 2.95008 2.39572 3.85361 -0.17456 0.10698  -0.85151 2   NAG F O7  
9313 C C1  . BMA F .   ? 2.98174 2.55349 3.89737 -0.33024 0.13352  -0.94713 3   BMA F C1  
9314 C C2  . BMA F .   ? 2.96050 2.51405 3.93413 -0.33416 0.15908  -1.00454 3   BMA F C2  
9315 C C3  . BMA F .   ? 2.99423 2.53367 4.04362 -0.36492 0.18922  -1.05848 3   BMA F C3  
9316 C C4  . BMA F .   ? 3.02656 2.64035 4.04240 -0.41541 0.19054  -1.09289 3   BMA F C4  
9317 C C5  . BMA F .   ? 3.04622 2.68863 3.98778 -0.40923 0.15963  -1.03105 3   BMA F C5  
9318 C C6  . BMA F .   ? 3.07354 2.80027 3.97389 -0.45751 0.15643  -1.05995 3   BMA F C6  
9319 O O2  . BMA F .   ? 2.95146 2.57117 3.88456 -0.35957 0.15800  -1.04502 3   BMA F O2  
9320 O O3  . BMA F .   ? 2.99030 2.51270 4.10537 -0.37097 0.21587  -1.11727 3   BMA F O3  
9321 O O4  . BMA F .   ? 3.05167 2.64540 4.13829 -0.44104 0.21738  -1.13458 3   BMA F O4  
9322 O O5  . BMA F .   ? 3.02140 2.66893 3.90224 -0.37657 0.13294  -0.98204 3   BMA F O5  
9323 O O6  . BMA F .   ? 3.09721 2.81852 4.05745 -0.49000 0.18327  -1.10794 3   BMA F O6  
9324 C C1  . MAN F .   ? 3.03866 2.48093 4.24430 -0.35016 0.23375  -1.11147 4   MAN F C1  
9325 C C2  . MAN F .   ? 3.07951 2.51638 4.36721 -0.37113 0.26806  -1.19266 4   MAN F C2  
9326 C C3  . MAN F .   ? 3.09453 2.44989 4.46506 -0.33110 0.27882  -1.17695 4   MAN F C3  
9327 C C4  . MAN F .   ? 3.09152 2.38297 4.48204 -0.30044 0.26700  -1.10421 4   MAN F C4  
9328 C C5  . MAN F .   ? 3.04126 2.34885 4.33502 -0.27324 0.23116  -1.02889 4   MAN F C5  
9329 C C6  . MAN F .   ? 3.03443 2.31081 4.32084 -0.25976 0.21711  -0.96457 4   MAN F C6  
9330 O O2  . MAN F .   ? 3.11810 2.56155 4.45811 -0.41023 0.29214  -1.24282 4   MAN F O2  
9331 O O3  . MAN F .   ? 3.14045 2.47789 4.60874 -0.35083 0.31366  -1.24955 4   MAN F O3  
9332 O O4  . MAN F .   ? 3.11194 2.33101 4.58966 -0.26783 0.27842  -1.09101 4   MAN F O4  
9333 O O5  . MAN F .   ? 3.01568 2.40344 4.21919 -0.29954 0.21733  -1.04602 4   MAN F O5  
9334 O O6  . MAN F .   ? 3.05653 2.35668 4.35186 -0.29948 0.22837  -0.99626 4   MAN F O6  
9335 C C1  . NAG G .   ? 2.71368 2.34773 3.15112 -0.04271 -0.12445 -0.38718 1   NAG G C1  
9336 C C2  . NAG G .   ? 3.08780 2.75542 3.52899 -0.08047 -0.12013 -0.41985 1   NAG G C2  
9337 C C3  . NAG G .   ? 3.26884 2.90481 3.75131 -0.09377 -0.09575 -0.45325 1   NAG G C3  
9338 C C4  . NAG G .   ? 3.31228 2.90082 3.82972 -0.07324 -0.08605 -0.43052 1   NAG G C4  
9339 C C5  . NAG G .   ? 3.02803 2.59927 3.53021 -0.03649 -0.09764 -0.38716 1   NAG G C5  
9340 C C6  . NAG G .   ? 3.08246 2.62793 3.61010 -0.02264 -0.09352 -0.35777 1   NAG G C6  
9341 C C7  . NAG G .   ? 2.87468 2.58417 3.27085 -0.09677 -0.12952 -0.45024 1   NAG G C7  
9342 C C8  . NAG G .   ? 2.93875 2.70343 3.30079 -0.12051 -0.14347 -0.46059 1   NAG G C8  
9343 N N2  . NAG G .   ? 3.07484 2.78640 3.48401 -0.09840 -0.13123 -0.43472 1   NAG G N2  
9344 O O3  . NAG G .   ? 3.45699 3.12454 3.94817 -0.13099 -0.08884 -0.48586 1   NAG G O3  
9345 O O4  . NAG G .   ? 3.38715 2.93639 3.94560 -0.07483 -0.06529 -0.45519 1   NAG G O4  
9346 O O5  . NAG G .   ? 2.78209 2.39079 3.24418 -0.03089 -0.11851 -0.36740 1   NAG G O5  
9347 O O6  . NAG G .   ? 3.34103 2.90369 3.88001 -0.04436 -0.09186 -0.36199 1   NAG G O6  
9348 O O7  . NAG G .   ? 2.72052 2.38870 3.13243 -0.07789 -0.11797 -0.45407 1   NAG G O7  
9349 C C1  . NAG G .   ? 3.20357 2.72952 3.80296 -0.08267 -0.05302 -0.45284 2   NAG G C1  
9350 C C2  . NAG G .   ? 3.21895 2.69317 3.87228 -0.07588 -0.03252 -0.46576 2   NAG G C2  
9351 C C3  . NAG G .   ? 3.26845 2.71799 3.96672 -0.08537 -0.02080 -0.45955 2   NAG G C3  
9352 C C4  . NAG G .   ? 3.33581 2.82019 4.03236 -0.12240 -0.01675 -0.49099 2   NAG G C4  
9353 C C5  . NAG G .   ? 3.33961 2.88045 3.97786 -0.12868 -0.03794 -0.48053 2   NAG G C5  
9354 C C6  . NAG G .   ? 3.40251 2.98689 4.03627 -0.16759 -0.03484 -0.51430 2   NAG G C6  
9355 C C7  . NAG G .   ? 3.01633 2.45187 3.65954 -0.01669 -0.04676 -0.38981 2   NAG G C7  
9356 C C8  . NAG G .   ? 2.84503 2.25609 3.48901 0.01417  -0.04858 -0.36739 2   NAG G C8  
9357 N N2  . NAG G .   ? 3.13014 2.57515 3.78288 -0.04156 -0.03642 -0.43644 2   NAG G N2  
9358 O O3  . NAG G .   ? 3.27022 2.67125 4.02657 -0.08041 -0.00183 -0.47177 2   NAG G O3  
9359 O O4  . NAG G .   ? 3.37087 2.83688 4.10096 -0.12988 -0.00940 -0.47795 2   NAG G O4  
9360 O O5  . NAG G .   ? 3.29368 2.85289 3.89503 -0.11838 -0.04872 -0.48353 2   NAG G O5  
9361 O O6  . NAG G .   ? 3.43851 3.03347 4.07546 -0.17468 -0.03891 -0.49448 2   NAG G O6  
9362 O O7  . NAG G .   ? 3.03031 2.48037 3.66489 -0.02008 -0.05394 -0.36800 2   NAG G O7  
9363 C C1  . BMA G .   ? 3.18896 2.61997 3.97956 -0.14565 0.01409  -0.51071 3   BMA G C1  
9364 C C2  . BMA G .   ? 3.25155 2.70521 4.05532 -0.18198 0.02253  -0.53671 3   BMA G C2  
9365 C C3  . BMA G .   ? 3.27826 2.68799 4.15550 -0.19736 0.04834  -0.56549 3   BMA G C3  
9366 C C4  . BMA G .   ? 3.25745 2.60618 4.18052 -0.16778 0.05263  -0.52644 3   BMA G C4  
9367 C C5  . BMA G .   ? 3.19459 2.53223 4.09693 -0.13405 0.04273  -0.50566 3   BMA G C5  
9368 C C6  . BMA G .   ? 3.17234 2.45911 4.11527 -0.10486 0.04414  -0.46173 3   BMA G C6  
9369 O O2  . BMA G .   ? 3.27003 2.73498 4.05726 -0.17792 0.01051  -0.49749 3   BMA G O2  
9370 O O3  . BMA G .   ? 3.32617 2.75176 4.21730 -0.22774 0.05544  -0.57977 3   BMA G O3  
9371 O O4  . BMA G .   ? 3.27407 2.57999 4.27228 -0.18069 0.07675  -0.55611 3   BMA G O4  
9372 O O5  . BMA G .   ? 3.17053 2.54970 4.00333 -0.12264 0.01988  -0.47857 3   BMA G O5  
9373 O O6  . BMA G .   ? 3.11425 2.41577 4.00694 -0.07611 0.02382  -0.41737 3   BMA G O6  
9374 C C1  . MAN G .   ? 3.19046 2.61960 4.11958 -0.26100 0.07778  -0.64163 4   MAN G C1  
9375 C C2  . MAN G .   ? 3.22480 2.62485 4.21081 -0.28014 0.09452  -0.64660 4   MAN G C2  
9376 C C3  . MAN G .   ? 3.25760 2.70135 4.20499 -0.29698 0.08212  -0.62950 4   MAN G C3  
9377 C C4  . MAN G .   ? 3.27592 2.79218 4.17182 -0.32427 0.07484  -0.66417 4   MAN G C4  
9378 C C5  . MAN G .   ? 3.24073 2.77905 4.08664 -0.30262 0.05791  -0.65483 4   MAN G C5  
9379 C C6  . MAN G .   ? 3.25570 2.86659 4.05583 -0.33136 0.05062  -0.68771 4   MAN G C6  
9380 O O2  . MAN G .   ? 3.24565 2.64481 4.27911 -0.31362 0.11967  -0.71022 4   MAN G O2  
9381 O O3  . MAN G .   ? 3.29167 2.71353 4.28846 -0.31863 0.09788  -0.63718 4   MAN G O3  
9382 O O4  . MAN G .   ? 3.30471 2.86283 4.16535 -0.33525 0.06066  -0.64233 4   MAN G O4  
9383 O O5  . MAN G .   ? 3.20934 2.70469 4.09157 -0.28857 0.07158  -0.67358 4   MAN G O5  
9384 O O6  . MAN G .   ? 3.22696 2.86542 3.96838 -0.30775 0.02469  -0.65160 4   MAN G O6  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -1  ?   ?   ?   A . n 
A 1 2   MET 2   0   ?   ?   ?   A . n 
A 1 3   LEU 3   1   ?   ?   ?   A . n 
A 1 4   TYR 4   2   ?   ?   ?   A . n 
A 1 5   ILE 5   3   ?   ?   ?   A . n 
A 1 6   SER 6   4   ?   ?   ?   A . n 
A 1 7   ALA 7   5   ?   ?   ?   A . n 
A 1 8   LYS 8   6   ?   ?   ?   A . n 
A 1 9   LYS 9   7   ?   ?   ?   A . n 
A 1 10  ALA 10  8   ?   ?   ?   A . n 
A 1 11  GLN 11  9   ?   ?   ?   A . n 
A 1 12  VAL 12  10  ?   ?   ?   A . n 
A 1 13  ALA 13  11  ?   ?   ?   A . n 
A 1 14  PHE 14  12  ?   ?   ?   A . n 
A 1 15  ILE 15  13  ?   ?   ?   A . n 
A 1 16  LEU 16  14  ?   ?   ?   A . n 
A 1 17  TYR 17  15  ?   ?   ?   A . n 
A 1 18  ILE 18  16  ?   ?   ?   A . n 
A 1 19  VAL 19  17  ?   ?   ?   A . n 
A 1 20  LEU 20  18  ?   ?   ?   A . n 
A 1 21  VAL 21  19  ?   ?   ?   A . n 
A 1 22  LEU 22  20  ?   ?   ?   A . n 
A 1 23  ARG 23  21  ?   ?   ?   A . n 
A 1 24  ILE 24  22  ?   ?   ?   A . n 
A 1 25  ILE 25  23  ?   ?   ?   A . n 
A 1 26  SER 26  24  ?   ?   ?   A . n 
A 1 27  GLY 27  25  ?   ?   ?   A . n 
A 1 28  ASN 28  26  ?   ?   ?   A . n 
A 1 29  ASN 29  27  ?   ?   ?   A . n 
A 1 30  ASP 30  28  ?   ?   ?   A . n 
A 1 31  PHE 31  29  ?   ?   ?   A . n 
A 1 32  CYS 32  30  ?   ?   ?   A . n 
A 1 33  LYS 33  31  ?   ?   ?   A . n 
A 1 34  PRO 34  32  ?   ?   ?   A . n 
A 1 35  SER 35  33  ?   ?   ?   A . n 
A 1 36  SER 36  34  ?   ?   ?   A . n 
A 1 37  LEU 37  35  ?   ?   ?   A . n 
A 1 38  ASN 38  36  ?   ?   ?   A . n 
A 1 39  SER 39  37  ?   ?   ?   A . n 
A 1 40  GLU 40  38  ?   ?   ?   A . n 
A 1 41  ILE 41  39  ?   ?   ?   A . n 
A 1 42  SER 42  40  ?   ?   ?   A . n 
A 1 43  GLY 43  41  ?   ?   ?   A . n 
A 1 44  PHE 44  42  ?   ?   ?   A . n 
A 1 45  ILE 45  43  43  ILE ILE A . n 
A 1 46  GLY 46  44  44  GLY GLY A . n 
A 1 47  TYR 47  45  45  TYR TYR A . n 
A 1 48  LYS 48  46  46  LYS LYS A . n 
A 1 49  CYS 49  47  47  CYS CYS A . n 
A 1 50  ASN 50  48  48  ASN ASN A . n 
A 1 51  PHE 51  49  49  PHE PHE A . n 
A 1 52  SER 52  50  50  SER SER A . n 
A 1 53  ASN 53  51  51  ASN ASN A . n 
A 1 54  GLU 54  56  ?   ?   ?   A . n 
A 1 55  GLY 55  57  ?   ?   ?   A . n 
A 1 56  VAL 56  58  ?   ?   ?   A . n 
A 1 57  HIS 57  59  ?   ?   ?   A . n 
A 1 58  ASN 58  60  ?   ?   ?   A . n 
A 1 59  LEU 59  61  ?   ?   ?   A . n 
A 1 60  LYS 60  62  ?   ?   ?   A . n 
A 1 61  PRO 61  63  ?   ?   ?   A . n 
A 1 62  ASP 62  64  ?   ?   ?   A . n 
A 1 63  MET 63  65  ?   ?   ?   A . n 
A 1 64  ARG 64  66  ?   ?   ?   A . n 
A 1 65  GLU 65  67  ?   ?   ?   A . n 
A 1 66  ARG 66  68  ?   ?   ?   A . n 
A 1 67  ARG 67  69  ?   ?   ?   A . n 
A 1 68  SER 68  70  ?   ?   ?   A . n 
A 1 69  ILE 69  71  71  ILE ILE A . n 
A 1 70  PHE 70  72  72  PHE PHE A . n 
A 1 71  CYS 71  73  73  CYS CYS A . n 
A 1 72  THR 72  74  74  THR THR A . n 
A 1 73  ILE 73  75  75  ILE ILE A . n 
A 1 74  HIS 74  76  76  HIS HIS A . n 
A 1 75  SER 75  77  77  SER SER A . n 
A 1 76  TYR 76  78  78  TYR TYR A . n 
A 1 77  PHE 77  79  79  PHE PHE A . n 
A 1 78  ILE 78  80  80  ILE ILE A . n 
A 1 79  TYR 79  81  81  TYR TYR A . n 
A 1 80  ASP 80  82  82  ASP ASP A . n 
A 1 81  LYS 81  83  83  LYS LYS A . n 
A 1 82  ILE 82  84  84  ILE ILE A . n 
A 1 83  ARG 83  85  85  ARG ARG A . n 
A 1 84  LEU 84  86  86  LEU LEU A . n 
A 1 85  ILE 85  87  87  ILE ILE A . n 
A 1 86  ILE 86  88  88  ILE ILE A . n 
A 1 87  PRO 87  89  ?   ?   ?   A . n 
A 1 88  LYS 88  90  ?   ?   ?   A . n 
A 1 89  LYS 89  91  ?   ?   ?   A . n 
A 1 90  SER 90  92  ?   ?   ?   A . n 
A 1 91  SER 91  93  ?   ?   ?   A . n 
A 1 92  SER 92  94  ?   ?   ?   A . n 
A 1 93  PRO 93  95  ?   ?   ?   A . n 
A 1 94  GLU 94  96  ?   ?   ?   A . n 
A 1 95  PHE 95  97  ?   ?   ?   A . n 
A 1 96  LYS 96  98  ?   ?   ?   A . n 
A 1 97  ILE 97  99  99  ILE ILE A . n 
A 1 98  LEU 98  100 100 LEU LEU A . n 
A 1 99  PRO 99  101 101 PRO PRO A . n 
A 1 100 GLU 100 102 102 GLU GLU A . n 
A 1 101 LYS 101 103 103 LYS LYS A . n 
A 1 102 CYS 102 104 104 CYS CYS A . n 
A 1 103 PHE 103 105 105 PHE PHE A . n 
A 1 104 GLN 104 106 106 GLN GLN A . n 
A 1 105 LYS 105 107 107 LYS LYS A . n 
A 1 106 VAL 106 108 108 VAL VAL A . n 
A 1 107 TYR 107 109 109 TYR TYR A . n 
A 1 108 THR 108 110 110 THR THR A . n 
A 1 109 ASP 109 111 111 ASP ASP A . n 
A 1 110 TYR 110 112 112 TYR TYR A . n 
A 1 111 GLU 111 113 113 GLU GLU A . n 
A 1 112 ASN 112 114 114 ASN ASN A . n 
A 1 113 ARG 113 115 115 ARG ARG A . n 
A 1 114 VAL 114 116 116 VAL VAL A . n 
A 1 115 GLU 115 117 117 GLU GLU A . n 
A 1 116 THR 116 118 118 THR THR A . n 
A 1 117 ASP 117 119 119 ASP ASP A . n 
A 1 118 ILE 118 120 120 ILE ILE A . n 
A 1 119 SER 119 121 121 SER SER A . n 
A 1 120 GLU 120 122 122 GLU GLU A . n 
A 1 121 LEU 121 123 123 LEU LEU A . n 
A 1 122 GLY 122 124 124 GLY GLY A . n 
A 1 123 LEU 123 125 125 LEU LEU A . n 
A 1 124 ILE 124 126 126 ILE ILE A . n 
A 1 125 GLU 125 127 127 GLU GLU A . n 
A 1 126 TYR 126 128 128 TYR TYR A . n 
A 1 127 GLU 127 129 129 GLU GLU A . n 
A 1 128 ILE 128 130 130 ILE ILE A . n 
A 1 129 GLU 129 131 131 GLU GLU A . n 
A 1 130 GLU 130 132 132 GLU GLU A . n 
A 1 131 ASN 131 133 133 ASN ASN A . n 
A 1 132 ASP 132 134 134 ASP ASP A . n 
A 1 133 THR 133 135 135 THR THR A . n 
A 1 134 ASN 134 136 136 ASN ASN A . n 
A 1 135 PRO 135 137 137 PRO PRO A . n 
A 1 136 ASN 136 138 138 ASN ASN A . n 
A 1 137 TYR 137 139 139 TYR TYR A . n 
A 1 138 ASN 138 140 140 ASN ASN A . n 
A 1 139 GLU 139 141 141 GLU GLU A . n 
A 1 140 ARG 140 142 142 ARG ARG A . n 
A 1 141 THR 141 143 143 THR THR A . n 
A 1 142 ILE 142 144 144 ILE ILE A . n 
A 1 143 THR 143 145 145 THR THR A . n 
A 1 144 ILE 144 146 146 ILE ILE A . n 
A 1 145 SER 145 147 147 SER SER A . n 
A 1 146 PRO 146 148 148 PRO PRO A . n 
A 1 147 PHE 147 149 149 PHE PHE A . n 
A 1 148 SER 148 150 150 SER SER A . n 
A 1 149 PRO 149 151 151 PRO PRO A . n 
A 1 150 LYS 150 152 152 LYS LYS A . n 
A 1 151 ASP 151 153 153 ASP ASP A . n 
A 1 152 ILE 152 154 154 ILE ILE A . n 
A 1 153 GLU 153 155 155 GLU GLU A . n 
A 1 154 PHE 154 156 156 PHE PHE A . n 
A 1 155 PHE 155 157 157 PHE PHE A . n 
A 1 156 CYS 156 158 158 CYS CYS A . n 
A 1 157 PHE 157 159 159 PHE PHE A . n 
A 1 158 CYS 158 160 160 CYS CYS A . n 
A 1 159 ASP 159 160 ?   ?   ?   A A n 
A 1 160 ASN 160 160 ?   ?   ?   A B n 
A 1 161 THR 161 160 ?   ?   ?   A C n 
A 1 162 GLU 162 160 ?   ?   ?   A D n 
A 1 163 LYS 163 160 ?   ?   ?   A E n 
A 1 164 VAL 164 160 ?   ?   ?   A F n 
A 1 165 ILE 165 160 ?   ?   ?   A G n 
A 1 166 SER 166 160 ?   ?   ?   A H n 
A 1 167 SER 167 160 ?   ?   ?   A I n 
A 1 168 ILE 168 160 ?   ?   ?   A J n 
A 1 169 GLU 169 160 ?   ?   ?   A K n 
A 1 170 GLY 170 160 ?   ?   ?   A L n 
A 1 171 ARG 171 160 ?   ?   ?   A M n 
A 1 172 SER 172 160 ?   ?   ?   A N n 
A 1 173 ALA 173 160 ?   ?   ?   A O n 
A 1 174 MET 174 174 174 MET MET A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 HIS 176 176 176 HIS HIS A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 ARG 178 178 178 ARG ARG A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 LYS 181 181 181 LYS LYS A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 PRO 183 183 183 PRO PRO A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 PHE 188 188 188 PHE PHE A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 ASP 194 194 194 ASP ASP A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 PHE 196 196 196 PHE PHE A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 CYS 227 227 227 CYS CYS A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 CYS 234 234 234 CYS CYS A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 GLN 236 236 236 GLN GLN A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 LYS 239 239 239 LYS LYS A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 TYR 244 244 244 TYR TYR A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 ASN 247 247 247 ASN ASN A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 HIS 252 252 252 HIS HIS A . n 
A 1 253 LYS 253 253 253 LYS LYS A . n 
A 1 254 ASN 254 254 254 ASN ASN A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 THR 256 256 256 THR THR A . n 
A 1 257 ILE 257 257 257 ILE ILE A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 LYS 267 267 267 LYS LYS A . n 
A 1 268 ASP 268 268 268 ASP ASP A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 ASN 270 270 270 ASN ASN A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 GLU 272 272 272 GLU GLU A . n 
A 1 273 CYS 273 273 273 CYS CYS A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 CYS 275 275 275 CYS CYS A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 PHE 277 277 277 PHE PHE A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 ASN 279 279 279 ASN ASN A . n 
A 1 280 ASN 280 280 280 ASN ASN A . n 
A 1 281 ASN 281 281 281 ASN ASN A . n 
A 1 282 TYR 282 282 282 TYR TYR A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 LYS 292 292 292 LYS LYS A . n 
A 1 293 LYS 293 293 293 LYS LYS A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 HIS 296 296 296 HIS HIS A . n 
A 1 297 GLY 297 297 297 GLY GLY A . n 
A 1 298 CYS 298 298 298 CYS CYS A . n 
A 1 299 ASN 299 299 299 ASN ASN A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 ASN 303 303 303 ASN ASN A . n 
A 1 304 VAL 304 304 304 VAL VAL A . n 
A 1 305 SER 305 305 305 SER SER A . n 
A 1 306 SER 306 306 306 SER SER A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 HIS 308 308 308 HIS HIS A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 PHE 310 310 310 PHE PHE A . n 
A 1 311 THR 311 311 311 THR THR A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 HIS 324 324 324 HIS HIS A . n 
A 1 325 ILE 325 325 325 ILE ILE A . n 
A 1 326 SER 326 326 326 SER SER A . n 
A 1 327 CYS 327 327 327 CYS CYS A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 VAL 329 329 329 VAL VAL A . n 
A 1 330 HIS 330 330 330 HIS HIS A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 SER 332 332 332 SER SER A . n 
A 1 333 GLU 333 333 333 GLU GLU A . n 
A 1 334 PRO 334 334 334 PRO PRO A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 TYR 336 336 336 TYR TYR A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 ASN 343 343 343 ASN ASN A . n 
A 1 344 CYS 344 344 344 CYS CYS A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 ILE 348 348 348 ILE ILE A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 PRO 350 350 350 PRO PRO A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 CYS 352 352 352 CYS CYS A . n 
A 1 353 PHE 353 353 353 PHE PHE A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 GLN 355 355 355 GLN GLN A . n 
A 1 356 VAL 356 356 356 VAL VAL A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 GLN 358 358 358 GLN GLN A . n 
A 1 359 PRO 359 359 359 PRO PRO A . n 
A 1 360 GLU 360 360 ?   ?   ?   A . n 
A 1 361 SER 361 361 ?   ?   ?   A . n 
A 1 362 GLU 362 362 ?   ?   ?   A . n 
A 1 363 GLU 363 363 ?   ?   ?   A . n 
A 1 364 LEU 364 364 ?   ?   ?   A . n 
A 1 365 GLU 365 365 ?   ?   ?   A . n 
A 1 366 PRO 366 366 ?   ?   ?   A . n 
A 1 367 SER 367 367 367 SER SER A . n 
A 1 368 ASN 368 368 368 ASN ASN A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 TYR 371 371 371 TYR TYR A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 ASP 373 373 373 ASP ASP A . n 
A 1 374 SER 374 374 374 SER SER A . n 
A 1 375 GLN 375 375 375 GLN GLN A . n 
A 1 376 ILE 376 376 376 ILE ILE A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 ILE 378 378 378 ILE ILE A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 ASP 380 380 380 ASP ASP A . n 
A 1 381 ILE 381 381 381 ILE ILE A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 TYR 383 383 383 TYR TYR A . n 
A 1 384 TYR 384 384 384 TYR TYR A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 ASP 386 386 386 ASP ASP A . n 
A 1 387 ALA 387 387 387 ALA ALA A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 ASP 390 390 390 ASP ASP A . n 
A 1 391 ASP 391 391 391 ASP ASP A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 ILE 393 393 393 ILE ILE A . n 
A 1 394 LYS 394 394 394 LYS LYS A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 PHE 396 396 396 PHE PHE A . n 
A 1 397 GLY 397 397 397 GLY GLY A . n 
A 1 398 ILE 398 398 398 ILE ILE A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 GLY 400 400 400 GLY GLY A . n 
A 1 401 SER 401 401 401 SER SER A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 PRO 403 403 403 PRO PRO A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 THR 405 405 405 THR THR A . n 
A 1 406 THR 406 406 406 THR THR A . n 
A 1 407 SER 407 407 407 SER SER A . n 
A 1 408 PHE 408 408 408 PHE PHE A . n 
A 1 409 THR 409 409 409 THR THR A . n 
A 1 410 CYS 410 410 410 CYS CYS A . n 
A 1 411 ILE 411 411 411 ILE ILE A . n 
A 1 412 CYS 412 412 412 CYS CYS A . n 
A 1 413 LYS 413 413 413 LYS LYS A . n 
A 1 414 LYS 414 414 414 LYS LYS A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 LYS 416 416 416 LYS LYS A . n 
A 1 417 LYS 417 417 417 LYS LYS A . n 
A 1 418 SER 418 418 418 SER SER A . n 
A 1 419 ALA 419 419 419 ALA ALA A . n 
A 1 420 TYR 420 420 420 TYR TYR A . n 
A 1 421 MET 421 421 421 MET MET A . n 
A 1 422 THR 422 422 422 THR THR A . n 
A 1 423 VAL 423 423 423 VAL VAL A . n 
A 1 424 THR 424 424 424 THR THR A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 ASP 426 426 426 ASP ASP A . n 
A 1 427 SER 427 427 427 SER SER A . n 
A 1 428 ALA 428 428 428 ALA ALA A . n 
A 1 429 TYR 429 429 ?   ?   ?   A . n 
A 1 430 TYR 430 430 ?   ?   ?   A . n 
A 1 431 GLY 431 431 ?   ?   ?   A . n 
A 1 432 PHE 432 432 ?   ?   ?   A . n 
A 1 433 LEU 433 433 ?   ?   ?   A . n 
A 1 434 ALA 434 434 ?   ?   ?   A . n 
A 1 435 LYS 435 435 ?   ?   ?   A . n 
A 1 436 THR 436 436 ?   ?   ?   A . n 
A 1 437 PHE 437 437 ?   ?   ?   A . n 
A 1 438 ILE 438 438 ?   ?   ?   A . n 
A 1 439 PHE 439 439 ?   ?   ?   A . n 
A 1 440 LEU 440 440 ?   ?   ?   A . n 
A 1 441 ILE 441 441 ?   ?   ?   A . n 
A 1 442 VAL 442 442 ?   ?   ?   A . n 
A 1 443 ALA 443 443 ?   ?   ?   A . n 
A 1 444 ILE 444 444 ?   ?   ?   A . n 
A 1 445 LEU 445 445 ?   ?   ?   A . n 
A 1 446 LEU 446 446 ?   ?   ?   A . n 
A 1 447 TYR 447 447 ?   ?   ?   A . n 
A 1 448 ILE 448 448 ?   ?   ?   A . n 
B 2 1   GLU 1   1   ?   ?   ?   B . n 
B 2 2   VAL 2   2   2   VAL VAL B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   GLU 6   6   6   GLU GLU B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   GLY 9   9   9   GLY GLY B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  LEU 11  11  11  LEU LEU B . n 
B 2 12  LEU 12  12  12  LEU LEU B . n 
B 2 13  GLN 13  13  13  GLN GLN B . n 
B 2 14  PRO 14  14  14  PRO PRO B . n 
B 2 15  GLY 15  15  15  GLY GLY B . n 
B 2 16  ARG 16  16  16  ARG ARG B . n 
B 2 17  SER 17  17  17  SER SER B . n 
B 2 18  LEU 18  18  18  LEU LEU B . n 
B 2 19  LYS 19  19  19  LYS LYS B . n 
B 2 20  LEU 20  20  20  LEU LEU B . n 
B 2 21  SER 21  21  21  SER SER B . n 
B 2 22  CYS 22  22  22  CYS CYS B . n 
B 2 23  VAL 23  23  23  VAL VAL B . n 
B 2 24  ALA 24  24  24  ALA ALA B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  GLY 26  26  26  GLY GLY B . n 
B 2 27  PHE 27  27  27  PHE PHE B . n 
B 2 28  THR 28  28  28  THR THR B . n 
B 2 29  PHE 29  29  29  PHE PHE B . n 
B 2 30  ASN 30  30  30  ASN ASN B . n 
B 2 31  ASN 31  31  31  ASN ASN B . n 
B 2 32  TYR 32  32  32  TYR TYR B . n 
B 2 33  TRP 33  33  33  TRP TRP B . n 
B 2 34  MET 34  34  34  MET MET B . n 
B 2 35  SER 35  35  35  SER SER B . n 
B 2 36  TRP 36  36  36  TRP TRP B . n 
B 2 37  ILE 37  37  37  ILE ILE B . n 
B 2 38  ARG 38  38  38  ARG ARG B . n 
B 2 39  GLN 39  39  39  GLN GLN B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  PRO 41  41  41  PRO PRO B . n 
B 2 42  GLY 42  42  42  GLY GLY B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  TRP 47  47  47  TRP TRP B . n 
B 2 48  ILE 48  48  48  ILE ILE B . n 
B 2 49  ALA 49  49  49  ALA ALA B . n 
B 2 50  SER 50  50  50  SER SER B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  SER 52  52  52  SER SER B . n 
B 2 53  ASN 53  53  53  ASN ASN B . n 
B 2 54  ILE 54  54  54  ILE ILE B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  THR 57  57  57  THR THR B . n 
B 2 58  ILE 58  58  58  ILE ILE B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  TYR 60  60  60  TYR TYR B . n 
B 2 61  PRO 61  61  61  PRO PRO B . n 
B 2 62  ASP 62  62  62  ASP ASP B . n 
B 2 63  SER 63  63  63  SER SER B . n 
B 2 64  VAL 64  64  64  VAL VAL B . n 
B 2 65  LYS 65  65  65  LYS LYS B . n 
B 2 66  GLY 66  66  66  GLY GLY B . n 
B 2 67  ARG 67  67  67  ARG ARG B . n 
B 2 68  PHE 68  68  68  PHE PHE B . n 
B 2 69  THR 69  69  69  THR THR B . n 
B 2 70  ILE 70  70  70  ILE ILE B . n 
B 2 71  SER 71  71  71  SER SER B . n 
B 2 72  ARG 72  72  72  ARG ARG B . n 
B 2 73  ASP 73  73  73  ASP ASP B . n 
B 2 74  SER 74  74  74  SER SER B . n 
B 2 75  ALA 75  75  75  ALA ALA B . n 
B 2 76  GLN 76  76  76  GLN GLN B . n 
B 2 77  ASN 77  77  77  ASN ASN B . n 
B 2 78  THR 78  78  78  THR THR B . n 
B 2 79  LEU 79  79  79  LEU LEU B . n 
B 2 80  TYR 80  80  80  TYR TYR B . n 
B 2 81  LEU 81  81  81  LEU LEU B . n 
B 2 82  GLN 82  82  82  GLN GLN B . n 
B 2 83  MET 83  83  83  MET MET B . n 
B 2 84  ASN 84  84  84  ASN ASN B . n 
B 2 85  SER 85  85  85  SER SER B . n 
B 2 86  LEU 86  86  86  LEU LEU B . n 
B 2 87  ARG 87  87  87  ARG ARG B . n 
B 2 88  SER 88  88  88  SER SER B . n 
B 2 89  GLU 89  89  89  GLU GLU B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  THR 91  91  91  THR THR B . n 
B 2 92  ALA 92  92  92  ALA ALA B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  TYR 95  95  95  TYR TYR B . n 
B 2 96  CYS 96  96  96  CYS CYS B . n 
B 2 97  THR 97  97  97  THR THR B . n 
B 2 98  ARG 98  98  98  ARG ARG B . n 
B 2 99  ASP 99  99  99  ASP ASP B . n 
B 2 100 LEU 100 100 100 LEU LEU B . n 
B 2 101 ARG 101 101 101 ARG ARG B . n 
B 2 102 MET 102 102 102 MET MET B . n 
B 2 103 SER 103 103 103 SER SER B . n 
B 2 104 ASP 104 104 104 ASP ASP B . n 
B 2 105 TYR 105 105 105 TYR TYR B . n 
B 2 106 PHE 106 106 106 PHE PHE B . n 
B 2 107 ASP 107 107 107 ASP ASP B . n 
B 2 108 TYR 108 108 108 TYR TYR B . n 
B 2 109 TRP 109 109 109 TRP TRP B . n 
B 2 110 GLY 110 110 110 GLY GLY B . n 
B 2 111 GLN 111 111 111 GLN GLN B . n 
B 2 112 GLY 112 112 112 GLY GLY B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 MET 114 114 114 MET MET B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 THR 116 116 116 THR THR B . n 
B 2 117 VAL 117 117 117 VAL VAL B . n 
B 2 118 SER 118 118 118 SER SER B . n 
B 2 119 SER 119 119 119 SER SER B . n 
B 2 120 ALA 120 120 120 ALA ALA B . n 
B 2 121 GLU 121 121 121 GLU GLU B . n 
B 2 122 THR 122 122 122 THR THR B . n 
B 2 123 THR 123 123 123 THR THR B . n 
B 2 124 ALA 124 124 124 ALA ALA B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 VAL 127 127 127 VAL VAL B . n 
B 2 128 TYR 128 128 128 TYR TYR B . n 
B 2 129 PRO 129 129 129 PRO PRO B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 ALA 131 131 131 ALA ALA B . n 
B 2 132 PRO 132 132 ?   ?   ?   B . n 
B 2 133 GLY 133 133 ?   ?   ?   B . n 
B 2 134 THR 134 134 ?   ?   ?   B . n 
B 2 135 ALA 135 135 ?   ?   ?   B . n 
B 2 136 LEU 136 136 ?   ?   ?   B . n 
B 2 137 LYS 137 137 ?   ?   ?   B . n 
B 2 138 SER 138 138 ?   ?   ?   B . n 
B 2 139 ASN 139 139 ?   ?   ?   B . n 
B 2 140 SER 140 140 ?   ?   ?   B . n 
B 2 141 MET 141 141 ?   ?   ?   B . n 
B 2 142 VAL 142 142 ?   ?   ?   B . n 
B 2 143 THR 143 143 143 THR THR B . n 
B 2 144 LEU 144 144 144 LEU LEU B . n 
B 2 145 GLY 145 145 145 GLY GLY B . n 
B 2 146 CYS 146 146 146 CYS CYS B . n 
B 2 147 LEU 147 147 147 LEU LEU B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 LYS 149 149 149 LYS LYS B . n 
B 2 150 GLY 150 150 150 GLY GLY B . n 
B 2 151 TYR 151 151 151 TYR TYR B . n 
B 2 152 PHE 152 152 152 PHE PHE B . n 
B 2 153 PRO 153 153 153 PRO PRO B . n 
B 2 154 GLU 154 154 154 GLU GLU B . n 
B 2 155 PRO 155 155 155 PRO PRO B . n 
B 2 156 VAL 156 156 156 VAL VAL B . n 
B 2 157 THR 157 157 157 THR THR B . n 
B 2 158 VAL 158 158 158 VAL VAL B . n 
B 2 159 THR 159 159 159 THR THR B . n 
B 2 160 TRP 160 160 160 TRP TRP B . n 
B 2 161 ASN 161 161 161 ASN ASN B . n 
B 2 162 SER 162 162 162 SER SER B . n 
B 2 163 GLY 163 163 163 GLY GLY B . n 
B 2 164 ALA 164 164 164 ALA ALA B . n 
B 2 165 LEU 165 165 165 LEU LEU B . n 
B 2 166 SER 166 166 166 SER SER B . n 
B 2 167 SER 167 167 167 SER SER B . n 
B 2 168 GLY 168 168 168 GLY GLY B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 HIS 170 170 170 HIS HIS B . n 
B 2 171 THR 171 171 171 THR THR B . n 
B 2 172 PHE 172 172 172 PHE PHE B . n 
B 2 173 PRO 173 173 173 PRO PRO B . n 
B 2 174 ALA 174 174 174 ALA ALA B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 GLN 177 177 177 GLN GLN B . n 
B 2 178 SER 178 178 178 SER SER B . n 
B 2 179 GLY 179 179 179 GLY GLY B . n 
B 2 180 LEU 180 180 180 LEU LEU B . n 
B 2 181 TYR 181 181 181 TYR TYR B . n 
B 2 182 THR 182 182 182 THR THR B . n 
B 2 183 LEU 183 183 183 LEU LEU B . n 
B 2 184 THR 184 184 184 THR THR B . n 
B 2 185 SER 185 185 185 SER SER B . n 
B 2 186 SER 186 186 186 SER SER B . n 
B 2 187 VAL 187 187 187 VAL VAL B . n 
B 2 188 THR 188 188 188 THR THR B . n 
B 2 189 VAL 189 189 189 VAL VAL B . n 
B 2 190 PRO 190 190 190 PRO PRO B . n 
B 2 191 SER 191 191 191 SER SER B . n 
B 2 192 SER 192 192 192 SER SER B . n 
B 2 193 THR 193 193 193 THR THR B . n 
B 2 194 TRP 194 194 194 TRP TRP B . n 
B 2 195 PRO 195 195 195 PRO PRO B . n 
B 2 196 SER 196 196 196 SER SER B . n 
B 2 197 GLN 197 197 197 GLN GLN B . n 
B 2 198 THR 198 198 198 THR THR B . n 
B 2 199 VAL 199 199 199 VAL VAL B . n 
B 2 200 THR 200 200 200 THR THR B . n 
B 2 201 CYS 201 201 201 CYS CYS B . n 
B 2 202 ASN 202 202 202 ASN ASN B . n 
B 2 203 VAL 203 203 203 VAL VAL B . n 
B 2 204 ALA 204 204 204 ALA ALA B . n 
B 2 205 HIS 205 205 205 HIS HIS B . n 
B 2 206 PRO 206 206 206 PRO PRO B . n 
B 2 207 ALA 207 207 207 ALA ALA B . n 
B 2 208 SER 208 208 208 SER SER B . n 
B 2 209 SER 209 209 209 SER SER B . n 
B 2 210 THR 210 210 210 THR THR B . n 
B 2 211 LYS 211 211 211 LYS LYS B . n 
B 2 212 VAL 212 212 212 VAL VAL B . n 
B 2 213 ASP 213 213 213 ASP ASP B . n 
B 2 214 LYS 214 214 214 LYS LYS B . n 
B 2 215 LYS 215 215 215 LYS LYS B . n 
B 2 216 ILE 216 216 216 ILE ILE B . n 
B 2 217 VAL 217 217 217 VAL VAL B . n 
B 2 218 PRO 218 218 218 PRO PRO B . n 
B 2 219 ARG 219 219 ?   ?   ?   B . n 
B 2 220 ASN 220 220 ?   ?   ?   B . n 
B 2 221 CYS 221 221 ?   ?   ?   B . n 
B 2 222 GLY 222 222 ?   ?   ?   B . n 
B 2 223 GLY 223 223 ?   ?   ?   B . n 
B 2 224 ASP 224 224 ?   ?   ?   B . n 
B 2 225 CYS 225 225 ?   ?   ?   B . n 
B 2 226 LYS 226 226 ?   ?   ?   B . n 
B 2 227 PRO 227 227 ?   ?   ?   B . n 
B 2 228 CYS 228 228 ?   ?   ?   B . n 
B 2 229 ILE 229 229 ?   ?   ?   B . n 
B 2 230 CYS 230 230 ?   ?   ?   B . n 
B 2 231 THR 231 231 ?   ?   ?   B . n 
B 2 232 GLY 232 232 ?   ?   ?   B . n 
B 2 233 SER 233 233 ?   ?   ?   B . n 
B 2 234 GLU 234 234 ?   ?   ?   B . n 
B 2 235 VAL 235 235 ?   ?   ?   B . n 
B 2 236 SER 236 236 ?   ?   ?   B . n 
B 2 237 SER 237 237 ?   ?   ?   B . n 
B 2 238 VAL 238 238 ?   ?   ?   B . n 
B 2 239 PHE 239 239 ?   ?   ?   B . n 
B 2 240 ILE 240 240 ?   ?   ?   B . n 
B 2 241 PHE 241 241 ?   ?   ?   B . n 
B 2 242 PRO 242 242 ?   ?   ?   B . n 
B 2 243 PRO 243 243 ?   ?   ?   B . n 
B 2 244 LYS 244 244 ?   ?   ?   B . n 
B 2 245 PRO 245 245 ?   ?   ?   B . n 
B 2 246 LYS 246 246 ?   ?   ?   B . n 
B 2 247 ASP 247 247 ?   ?   ?   B . n 
B 2 248 VAL 248 248 ?   ?   ?   B . n 
B 2 249 LEU 249 249 ?   ?   ?   B . n 
B 2 250 THR 250 250 ?   ?   ?   B . n 
B 2 251 ILE 251 251 ?   ?   ?   B . n 
B 2 252 THR 252 252 ?   ?   ?   B . n 
B 2 253 LEU 253 253 ?   ?   ?   B . n 
B 2 254 THR 254 254 ?   ?   ?   B . n 
B 2 255 PRO 255 255 ?   ?   ?   B . n 
B 2 256 LYS 256 256 ?   ?   ?   B . n 
B 2 257 VAL 257 257 ?   ?   ?   B . n 
B 2 258 THR 258 258 ?   ?   ?   B . n 
B 2 259 CYS 259 259 ?   ?   ?   B . n 
B 2 260 VAL 260 260 ?   ?   ?   B . n 
B 2 261 VAL 261 261 ?   ?   ?   B . n 
B 2 262 VAL 262 262 ?   ?   ?   B . n 
B 2 263 ASP 263 263 ?   ?   ?   B . n 
B 2 264 ILE 264 264 ?   ?   ?   B . n 
B 2 265 SER 265 265 ?   ?   ?   B . n 
B 2 266 GLN 266 266 ?   ?   ?   B . n 
B 2 267 ASP 267 267 ?   ?   ?   B . n 
B 2 268 ASP 268 268 ?   ?   ?   B . n 
B 2 269 PRO 269 269 ?   ?   ?   B . n 
B 2 270 GLU 270 270 ?   ?   ?   B . n 
B 2 271 VAL 271 271 ?   ?   ?   B . n 
B 2 272 HIS 272 272 ?   ?   ?   B . n 
B 2 273 PHE 273 273 ?   ?   ?   B . n 
B 2 274 SER 274 274 ?   ?   ?   B . n 
B 2 275 TRP 275 275 ?   ?   ?   B . n 
B 2 276 PHE 276 276 ?   ?   ?   B . n 
B 2 277 VAL 277 277 ?   ?   ?   B . n 
B 2 278 ASP 278 278 ?   ?   ?   B . n 
B 2 279 ASP 279 279 ?   ?   ?   B . n 
B 2 280 VAL 280 280 ?   ?   ?   B . n 
B 2 281 GLU 281 281 ?   ?   ?   B . n 
B 2 282 VAL 282 282 ?   ?   ?   B . n 
B 2 283 HIS 283 283 ?   ?   ?   B . n 
B 2 284 THR 284 284 ?   ?   ?   B . n 
B 2 285 ALA 285 285 ?   ?   ?   B . n 
B 2 286 GLN 286 286 ?   ?   ?   B . n 
B 2 287 THR 287 287 ?   ?   ?   B . n 
B 2 288 ARG 288 288 ?   ?   ?   B . n 
B 2 289 PRO 289 289 ?   ?   ?   B . n 
B 2 290 PRO 290 290 ?   ?   ?   B . n 
B 2 291 GLU 291 291 ?   ?   ?   B . n 
B 2 292 GLU 292 292 ?   ?   ?   B . n 
B 2 293 GLN 293 293 ?   ?   ?   B . n 
B 2 294 PHE 294 294 ?   ?   ?   B . n 
B 2 295 ASN 295 295 ?   ?   ?   B . n 
B 2 296 SER 296 296 ?   ?   ?   B . n 
B 2 297 THR 297 297 ?   ?   ?   B . n 
B 2 298 PHE 298 298 ?   ?   ?   B . n 
B 2 299 ARG 299 299 ?   ?   ?   B . n 
B 2 300 SER 300 300 ?   ?   ?   B . n 
B 2 301 VAL 301 301 ?   ?   ?   B . n 
B 2 302 SER 302 302 ?   ?   ?   B . n 
B 2 303 GLU 303 303 ?   ?   ?   B . n 
B 2 304 LEU 304 304 ?   ?   ?   B . n 
B 2 305 PRO 305 305 ?   ?   ?   B . n 
B 2 306 ILE 306 306 ?   ?   ?   B . n 
B 2 307 LEU 307 307 ?   ?   ?   B . n 
B 2 308 HIS 308 308 ?   ?   ?   B . n 
B 2 309 GLN 309 309 ?   ?   ?   B . n 
B 2 310 ASP 310 310 ?   ?   ?   B . n 
B 2 311 TRP 311 311 ?   ?   ?   B . n 
B 2 312 LEU 312 312 ?   ?   ?   B . n 
B 2 313 ASN 313 313 ?   ?   ?   B . n 
B 2 314 GLY 314 314 ?   ?   ?   B . n 
B 2 315 ARG 315 315 ?   ?   ?   B . n 
B 2 316 THR 316 316 ?   ?   ?   B . n 
B 2 317 PHE 317 317 ?   ?   ?   B . n 
B 2 318 ARG 318 318 ?   ?   ?   B . n 
B 2 319 CYS 319 319 ?   ?   ?   B . n 
B 2 320 LYS 320 320 ?   ?   ?   B . n 
B 2 321 VAL 321 321 ?   ?   ?   B . n 
B 2 322 THR 322 322 ?   ?   ?   B . n 
B 2 323 SER 323 323 ?   ?   ?   B . n 
B 2 324 ALA 324 324 ?   ?   ?   B . n 
B 2 325 ALA 325 325 ?   ?   ?   B . n 
B 2 326 PHE 326 326 ?   ?   ?   B . n 
B 2 327 PRO 327 327 ?   ?   ?   B . n 
B 2 328 SER 328 328 ?   ?   ?   B . n 
B 2 329 PRO 329 329 ?   ?   ?   B . n 
B 2 330 ILE 330 330 ?   ?   ?   B . n 
B 2 331 GLU 331 331 ?   ?   ?   B . n 
B 2 332 LYS 332 332 ?   ?   ?   B . n 
B 2 333 THR 333 333 ?   ?   ?   B . n 
B 2 334 ILE 334 334 ?   ?   ?   B . n 
B 2 335 SER 335 335 ?   ?   ?   B . n 
B 2 336 LYS 336 336 ?   ?   ?   B . n 
B 2 337 PRO 337 337 ?   ?   ?   B . n 
B 2 338 GLU 338 338 ?   ?   ?   B . n 
B 2 339 GLY 339 339 ?   ?   ?   B . n 
B 2 340 ARG 340 340 ?   ?   ?   B . n 
B 2 341 THR 341 341 ?   ?   ?   B . n 
B 2 342 GLN 342 342 ?   ?   ?   B . n 
B 2 343 VAL 343 343 ?   ?   ?   B . n 
B 2 344 PRO 344 344 ?   ?   ?   B . n 
B 2 345 HIS 345 345 ?   ?   ?   B . n 
B 2 346 VAL 346 346 ?   ?   ?   B . n 
B 2 347 TYR 347 347 ?   ?   ?   B . n 
B 2 348 THR 348 348 ?   ?   ?   B . n 
B 2 349 MET 349 349 ?   ?   ?   B . n 
B 2 350 SER 350 350 ?   ?   ?   B . n 
B 2 351 PRO 351 351 ?   ?   ?   B . n 
B 2 352 THR 352 352 ?   ?   ?   B . n 
B 2 353 LYS 353 353 ?   ?   ?   B . n 
B 2 354 GLU 354 354 ?   ?   ?   B . n 
B 2 355 GLU 355 355 ?   ?   ?   B . n 
B 2 356 MET 356 356 ?   ?   ?   B . n 
B 2 357 THR 357 357 ?   ?   ?   B . n 
B 2 358 GLN 358 358 ?   ?   ?   B . n 
B 2 359 ASN 359 359 ?   ?   ?   B . n 
B 2 360 GLU 360 360 ?   ?   ?   B . n 
B 2 361 VAL 361 361 ?   ?   ?   B . n 
B 2 362 SER 362 362 ?   ?   ?   B . n 
B 2 363 ILE 363 363 ?   ?   ?   B . n 
B 2 364 THR 364 364 ?   ?   ?   B . n 
B 2 365 CYS 365 365 ?   ?   ?   B . n 
B 2 366 MET 366 366 ?   ?   ?   B . n 
B 2 367 VAL 367 367 ?   ?   ?   B . n 
B 2 368 LYS 368 368 ?   ?   ?   B . n 
B 2 369 GLY 369 369 ?   ?   ?   B . n 
B 2 370 PHE 370 370 ?   ?   ?   B . n 
B 2 371 TYR 371 371 ?   ?   ?   B . n 
B 2 372 PRO 372 372 ?   ?   ?   B . n 
B 2 373 PRO 373 373 ?   ?   ?   B . n 
B 2 374 ASP 374 374 ?   ?   ?   B . n 
B 2 375 ILE 375 375 ?   ?   ?   B . n 
B 2 376 TYR 376 376 ?   ?   ?   B . n 
B 2 377 VAL 377 377 ?   ?   ?   B . n 
B 2 378 GLU 378 378 ?   ?   ?   B . n 
B 2 379 TRP 379 379 ?   ?   ?   B . n 
B 2 380 GLN 380 380 ?   ?   ?   B . n 
B 2 381 MET 381 381 ?   ?   ?   B . n 
B 2 382 ASN 382 382 ?   ?   ?   B . n 
B 2 383 GLY 383 383 ?   ?   ?   B . n 
B 2 384 GLN 384 384 ?   ?   ?   B . n 
B 2 385 PRO 385 385 ?   ?   ?   B . n 
B 2 386 GLN 386 386 ?   ?   ?   B . n 
B 2 387 GLU 387 387 ?   ?   ?   B . n 
B 2 388 ASN 388 388 ?   ?   ?   B . n 
B 2 389 TYR 389 389 ?   ?   ?   B . n 
B 2 390 LYS 390 390 ?   ?   ?   B . n 
B 2 391 ASN 391 391 ?   ?   ?   B . n 
B 2 392 THR 392 392 ?   ?   ?   B . n 
B 2 393 PRO 393 393 ?   ?   ?   B . n 
B 2 394 PRO 394 394 ?   ?   ?   B . n 
B 2 395 THR 395 395 ?   ?   ?   B . n 
B 2 396 MET 396 396 ?   ?   ?   B . n 
B 2 397 ASP 397 397 ?   ?   ?   B . n 
B 2 398 THR 398 398 ?   ?   ?   B . n 
B 2 399 ASP 399 399 ?   ?   ?   B . n 
B 2 400 GLY 400 400 ?   ?   ?   B . n 
B 2 401 SER 401 401 ?   ?   ?   B . n 
B 2 402 TYR 402 402 ?   ?   ?   B . n 
B 2 403 PHE 403 403 ?   ?   ?   B . n 
B 2 404 LEU 404 404 ?   ?   ?   B . n 
B 2 405 TYR 405 405 ?   ?   ?   B . n 
B 2 406 SER 406 406 ?   ?   ?   B . n 
B 2 407 LYS 407 407 ?   ?   ?   B . n 
B 2 408 LEU 408 408 ?   ?   ?   B . n 
B 2 409 ASN 409 409 ?   ?   ?   B . n 
B 2 410 VAL 410 410 ?   ?   ?   B . n 
B 2 411 LYS 411 411 ?   ?   ?   B . n 
B 2 412 LYS 412 412 ?   ?   ?   B . n 
B 2 413 GLU 413 413 ?   ?   ?   B . n 
B 2 414 LYS 414 414 ?   ?   ?   B . n 
B 2 415 TRP 415 415 ?   ?   ?   B . n 
B 2 416 GLN 416 416 ?   ?   ?   B . n 
B 2 417 GLN 417 417 ?   ?   ?   B . n 
B 2 418 GLY 418 418 ?   ?   ?   B . n 
B 2 419 ASN 419 419 ?   ?   ?   B . n 
B 2 420 THR 420 420 ?   ?   ?   B . n 
B 2 421 PHE 421 421 ?   ?   ?   B . n 
B 2 422 THR 422 422 ?   ?   ?   B . n 
B 2 423 CYS 423 423 ?   ?   ?   B . n 
B 2 424 SER 424 424 ?   ?   ?   B . n 
B 2 425 VAL 425 425 ?   ?   ?   B . n 
B 2 426 LEU 426 426 ?   ?   ?   B . n 
B 2 427 HIS 427 427 ?   ?   ?   B . n 
B 2 428 GLU 428 428 ?   ?   ?   B . n 
B 2 429 GLY 429 429 ?   ?   ?   B . n 
B 2 430 LEU 430 430 ?   ?   ?   B . n 
B 2 431 HIS 431 431 ?   ?   ?   B . n 
B 2 432 ASN 432 432 ?   ?   ?   B . n 
B 2 433 HIS 433 433 ?   ?   ?   B . n 
B 2 434 HIS 434 434 ?   ?   ?   B . n 
B 2 435 THR 435 435 ?   ?   ?   B . n 
B 2 436 GLU 436 436 ?   ?   ?   B . n 
B 2 437 LYS 437 437 ?   ?   ?   B . n 
B 2 438 SER 438 438 ?   ?   ?   B . n 
B 2 439 LEU 439 439 ?   ?   ?   B . n 
B 2 440 SER 440 440 ?   ?   ?   B . n 
B 2 441 HIS 441 441 ?   ?   ?   B . n 
B 2 442 SER 442 442 ?   ?   ?   B . n 
B 2 443 PRO 443 443 ?   ?   ?   B . n 
B 2 444 GLY 444 444 ?   ?   ?   B . n 
B 2 445 LYS 445 445 ?   ?   ?   B . n 
C 3 1   GLN 1   1   1   GLN GLN C . n 
C 3 2   PHE 2   2   2   PHE PHE C . n 
C 3 3   VAL 3   3   3   VAL VAL C . n 
C 3 4   LEU 4   4   4   LEU LEU C . n 
C 3 5   SER 5   5   5   SER SER C . n 
C 3 6   GLN 6   6   6   GLN GLN C . n 
C 3 7   PRO 7   7   7   PRO PRO C . n 
C 3 8   ASN 8   8   8   ASN ASN C . n 
C 3 9   SER 9   9   9   SER SER C . n 
C 3 10  VAL 10  10  10  VAL VAL C . n 
C 3 11  SER 11  11  11  SER SER C . n 
C 3 12  THR 12  12  12  THR THR C . n 
C 3 13  ASN 13  13  13  ASN ASN C . n 
C 3 14  LEU 14  14  14  LEU LEU C . n 
C 3 15  GLY 15  15  15  GLY GLY C . n 
C 3 16  SER 16  16  16  SER SER C . n 
C 3 17  THR 17  17  17  THR THR C . n 
C 3 18  VAL 18  18  18  VAL VAL C . n 
C 3 19  LYS 19  19  19  LYS LYS C . n 
C 3 20  LEU 20  20  20  LEU LEU C . n 
C 3 21  SER 21  21  21  SER SER C . n 
C 3 22  CYS 22  22  22  CYS CYS C . n 
C 3 23  LYS 23  23  23  LYS LYS C . n 
C 3 24  ARG 24  24  24  ARG ARG C . n 
C 3 25  SER 25  25  25  SER SER C . n 
C 3 26  THR 26  26  26  THR THR C . n 
C 3 27  GLY 27  27  27  GLY GLY C . n 
C 3 28  ASN 28  28  28  ASN ASN C . n 
C 3 29  ILE 29  29  29  ILE ILE C . n 
C 3 30  GLY 30  30  30  GLY GLY C . n 
C 3 31  SER 31  31  31  SER SER C . n 
C 3 32  ASN 32  32  32  ASN ASN C . n 
C 3 33  TYR 33  33  33  TYR TYR C . n 
C 3 34  VAL 34  34  34  VAL VAL C . n 
C 3 35  SER 35  35  35  SER SER C . n 
C 3 36  TRP 36  36  36  TRP TRP C . n 
C 3 37  TYR 37  37  37  TYR TYR C . n 
C 3 38  GLN 38  38  38  GLN GLN C . n 
C 3 39  HIS 39  39  39  HIS HIS C . n 
C 3 40  HIS 40  40  40  HIS HIS C . n 
C 3 41  GLU 41  41  41  GLU GLU C . n 
C 3 42  GLY 42  42  42  GLY GLY C . n 
C 3 43  ARG 43  43  43  ARG ARG C . n 
C 3 44  SER 44  44  44  SER SER C . n 
C 3 45  PRO 45  45  45  PRO PRO C . n 
C 3 46  THR 46  46  46  THR THR C . n 
C 3 47  THR 47  47  47  THR THR C . n 
C 3 48  MET 48  48  48  MET MET C . n 
C 3 49  ILE 49  49  49  ILE ILE C . n 
C 3 50  TYR 50  50  50  TYR TYR C . n 
C 3 51  ARG 51  51  51  ARG ARG C . n 
C 3 52  ASP 52  52  52  ASP ASP C . n 
C 3 53  ASP 53  53  53  ASP ASP C . n 
C 3 54  GLN 54  54  54  GLN GLN C . n 
C 3 55  ARG 55  55  55  ARG ARG C . n 
C 3 56  PRO 56  56  56  PRO PRO C . n 
C 3 57  ASP 57  57  57  ASP ASP C . n 
C 3 58  GLY 58  58  58  GLY GLY C . n 
C 3 59  VAL 59  59  59  VAL VAL C . n 
C 3 60  PRO 60  60  60  PRO PRO C . n 
C 3 61  ASP 61  61  61  ASP ASP C . n 
C 3 62  ARG 62  62  62  ARG ARG C . n 
C 3 63  PHE 63  63  63  PHE PHE C . n 
C 3 64  SER 64  64  64  SER SER C . n 
C 3 65  GLY 65  65  65  GLY GLY C . n 
C 3 66  SER 66  66  66  SER SER C . n 
C 3 67  ILE 67  67  67  ILE ILE C . n 
C 3 68  ASP 68  68  68  ASP ASP C . n 
C 3 69  ARG 69  69  69  ARG ARG C . n 
C 3 70  SER 70  70  70  SER SER C . n 
C 3 71  SER 71  71  71  SER SER C . n 
C 3 72  ASN 72  72  72  ASN ASN C . n 
C 3 73  SER 73  73  73  SER SER C . n 
C 3 74  ALA 74  74  74  ALA ALA C . n 
C 3 75  LEU 75  75  75  LEU LEU C . n 
C 3 76  LEU 76  76  76  LEU LEU C . n 
C 3 77  THR 77  77  77  THR THR C . n 
C 3 78  ILE 78  78  78  ILE ILE C . n 
C 3 79  ASP 79  79  79  ASP ASP C . n 
C 3 80  ASN 80  80  80  ASN ASN C . n 
C 3 81  VAL 81  81  81  VAL VAL C . n 
C 3 82  GLN 82  82  82  GLN GLN C . n 
C 3 83  THR 83  83  83  THR THR C . n 
C 3 84  GLU 84  84  84  GLU GLU C . n 
C 3 85  ASP 85  85  85  ASP ASP C . n 
C 3 86  GLU 86  86  86  GLU GLU C . n 
C 3 87  ALA 87  87  87  ALA ALA C . n 
C 3 88  ALA 88  88  88  ALA ALA C . n 
C 3 89  TYR 89  89  89  TYR TYR C . n 
C 3 90  PHE 90  90  90  PHE PHE C . n 
C 3 91  CYS 91  91  91  CYS CYS C . n 
C 3 92  HIS 92  92  92  HIS HIS C . n 
C 3 93  SER 93  93  93  SER SER C . n 
C 3 94  TYR 94  94  94  TYR TYR C . n 
C 3 95  SER 95  95  95  SER SER C . n 
C 3 96  THR 96  96  96  THR THR C . n 
C 3 97  GLY 97  97  97  GLY GLY C . n 
C 3 98  MET 98  98  98  MET MET C . n 
C 3 99  TYR 99  99  99  TYR TYR C . n 
C 3 100 ILE 100 100 100 ILE ILE C . n 
C 3 101 PHE 101 101 101 PHE PHE C . n 
C 3 102 GLY 102 102 102 GLY GLY C . n 
C 3 103 GLY 103 103 103 GLY GLY C . n 
C 3 104 GLY 104 104 104 GLY GLY C . n 
C 3 105 THR 105 105 105 THR THR C . n 
C 3 106 LYS 106 106 106 LYS LYS C . n 
C 3 107 LEU 107 107 107 LEU LEU C . n 
C 3 108 THR 108 108 108 THR THR C . n 
C 3 109 VAL 109 109 109 VAL VAL C . n 
C 3 110 LEU 110 110 110 LEU LEU C . n 
C 3 111 GLY 111 111 111 GLY GLY C . n 
C 3 112 GLN 112 112 112 GLN GLN C . n 
C 3 113 PRO 113 113 113 PRO PRO C . n 
C 3 114 LYS 114 114 114 LYS LYS C . n 
C 3 115 SER 115 115 115 SER SER C . n 
C 3 116 THR 116 116 116 THR THR C . n 
C 3 117 PRO 117 117 117 PRO PRO C . n 
C 3 118 THR 118 118 118 THR THR C . n 
C 3 119 LEU 119 119 119 LEU LEU C . n 
C 3 120 THR 120 120 120 THR THR C . n 
C 3 121 MET 121 121 121 MET MET C . n 
C 3 122 PHE 122 122 122 PHE PHE C . n 
C 3 123 PRO 123 123 123 PRO PRO C . n 
C 3 124 PRO 124 124 124 PRO PRO C . n 
C 3 125 SER 125 125 125 SER SER C . n 
C 3 126 PRO 126 126 126 PRO PRO C . n 
C 3 127 GLU 127 127 127 GLU GLU C . n 
C 3 128 GLU 128 128 128 GLU GLU C . n 
C 3 129 LEU 129 129 129 LEU LEU C . n 
C 3 130 GLN 130 130 130 GLN GLN C . n 
C 3 131 GLU 131 131 131 GLU GLU C . n 
C 3 132 ASN 132 132 132 ASN ASN C . n 
C 3 133 LYS 133 133 133 LYS LYS C . n 
C 3 134 ALA 134 134 134 ALA ALA C . n 
C 3 135 THR 135 135 135 THR THR C . n 
C 3 136 LEU 136 136 136 LEU LEU C . n 
C 3 137 VAL 137 137 137 VAL VAL C . n 
C 3 138 CYS 138 138 138 CYS CYS C . n 
C 3 139 LEU 139 139 139 LEU LEU C . n 
C 3 140 ILE 140 140 140 ILE ILE C . n 
C 3 141 SER 141 141 141 SER SER C . n 
C 3 142 ASN 142 142 142 ASN ASN C . n 
C 3 143 PHE 143 143 143 PHE PHE C . n 
C 3 144 SER 144 144 144 SER SER C . n 
C 3 145 PRO 145 145 145 PRO PRO C . n 
C 3 146 SER 146 146 146 SER SER C . n 
C 3 147 GLY 147 147 147 GLY GLY C . n 
C 3 148 VAL 148 148 148 VAL VAL C . n 
C 3 149 THR 149 149 149 THR THR C . n 
C 3 150 VAL 150 150 150 VAL VAL C . n 
C 3 151 ALA 151 151 151 ALA ALA C . n 
C 3 152 TRP 152 152 152 TRP TRP C . n 
C 3 153 LYS 153 153 153 LYS LYS C . n 
C 3 154 ALA 154 154 154 ALA ALA C . n 
C 3 155 ASN 155 155 155 ASN ASN C . n 
C 3 156 GLY 156 156 156 GLY GLY C . n 
C 3 157 THR 157 157 157 THR THR C . n 
C 3 158 PRO 158 158 158 PRO PRO C . n 
C 3 159 ILE 159 159 159 ILE ILE C . n 
C 3 160 THR 160 160 160 THR THR C . n 
C 3 161 GLN 161 161 161 GLN GLN C . n 
C 3 162 GLY 162 162 162 GLY GLY C . n 
C 3 163 VAL 163 163 163 VAL VAL C . n 
C 3 164 ASP 164 164 164 ASP ASP C . n 
C 3 165 THR 165 165 165 THR THR C . n 
C 3 166 SER 166 166 166 SER SER C . n 
C 3 167 ASN 167 167 167 ASN ASN C . n 
C 3 168 PRO 168 168 168 PRO PRO C . n 
C 3 169 THR 169 169 169 THR THR C . n 
C 3 170 LYS 170 170 170 LYS LYS C . n 
C 3 171 GLU 171 171 171 GLU GLU C . n 
C 3 172 ASP 172 172 172 ASP ASP C . n 
C 3 173 ASN 173 173 173 ASN ASN C . n 
C 3 174 LYS 174 174 174 LYS LYS C . n 
C 3 175 TYR 175 175 175 TYR TYR C . n 
C 3 176 MET 176 176 176 MET MET C . n 
C 3 177 ALA 177 177 177 ALA ALA C . n 
C 3 178 SER 178 178 178 SER SER C . n 
C 3 179 SER 179 179 179 SER SER C . n 
C 3 180 PHE 180 180 180 PHE PHE C . n 
C 3 181 LEU 181 181 181 LEU LEU C . n 
C 3 182 HIS 182 182 182 HIS HIS C . n 
C 3 183 LEU 183 183 183 LEU LEU C . n 
C 3 184 THR 184 184 184 THR THR C . n 
C 3 185 SER 185 185 185 SER SER C . n 
C 3 186 ASP 186 186 186 ASP ASP C . n 
C 3 187 GLN 187 187 187 GLN GLN C . n 
C 3 188 TRP 188 188 188 TRP TRP C . n 
C 3 189 ARG 189 189 189 ARG ARG C . n 
C 3 190 SER 190 190 190 SER SER C . n 
C 3 191 HIS 191 191 191 HIS HIS C . n 
C 3 192 ASN 192 192 192 ASN ASN C . n 
C 3 193 SER 193 193 193 SER SER C . n 
C 3 194 PHE 194 194 194 PHE PHE C . n 
C 3 195 THR 195 195 195 THR THR C . n 
C 3 196 CYS 196 196 196 CYS CYS C . n 
C 3 197 GLN 197 197 197 GLN GLN C . n 
C 3 198 VAL 198 198 198 VAL VAL C . n 
C 3 199 THR 199 199 199 THR THR C . n 
C 3 200 HIS 200 200 200 HIS HIS C . n 
C 3 201 GLU 201 201 201 GLU GLU C . n 
C 3 202 GLY 202 202 202 GLY GLY C . n 
C 3 203 ASN 203 203 203 ASN ASN C . n 
C 3 204 THR 204 204 204 THR THR C . n 
C 3 205 VAL 205 205 205 VAL VAL C . n 
C 3 206 GLU 206 206 206 GLU GLU C . n 
C 3 207 LYS 207 207 207 LYS LYS C . n 
C 3 208 THR 208 208 208 THR THR C . n 
C 3 209 VAL 209 209 209 VAL VAL C . n 
C 3 210 SER 210 210 210 SER SER C . n 
C 3 211 PRO 211 211 211 PRO PRO C . n 
C 3 212 THR 212 212 212 THR THR C . n 
C 3 213 GLU 213 213 213 GLU GLU C . n 
C 3 214 CYS 214 214 214 CYS CYS C . n 
C 3 215 VAL 215 215 215 VAL VAL C . n 
C 3 216 ALA 216 216 216 ALA ALA C . n 
D 4 1   MET 1   -18 ?   ?   ?   D . n 
D 4 2   ASN 2   -17 ?   ?   ?   D . n 
D 4 3   PHE 3   -16 ?   ?   ?   D . n 
D 4 4   GLY 4   -15 ?   ?   ?   D . n 
D 4 5   LEU 5   -14 ?   ?   ?   D . n 
D 4 6   SER 6   -13 ?   ?   ?   D . n 
D 4 7   LEU 7   -12 ?   ?   ?   D . n 
D 4 8   ILE 8   -11 ?   ?   ?   D . n 
D 4 9   PHE 9   -10 ?   ?   ?   D . n 
D 4 10  LEU 10  -9  ?   ?   ?   D . n 
D 4 11  VAL 11  -8  ?   ?   ?   D . n 
D 4 12  LEU 12  -7  ?   ?   ?   D . n 
D 4 13  VAL 13  -6  ?   ?   ?   D . n 
D 4 14  LEU 14  -5  ?   ?   ?   D . n 
D 4 15  LYS 15  -4  ?   ?   ?   D . n 
D 4 16  GLY 16  -3  ?   ?   ?   D . n 
D 4 17  VAL 17  -2  ?   ?   ?   D . n 
D 4 18  GLN 18  -1  ?   ?   ?   D . n 
D 4 19  CYS 19  0   ?   ?   ?   D . n 
D 4 20  GLU 20  1   1   GLU GLU D . n 
D 4 21  VAL 21  2   2   VAL VAL D . n 
D 4 22  MET 22  3   3   MET MET D . n 
D 4 23  LEU 23  4   4   LEU LEU D . n 
D 4 24  VAL 24  5   5   VAL VAL D . n 
D 4 25  GLU 25  6   6   GLU GLU D . n 
D 4 26  SER 26  7   7   SER SER D . n 
D 4 27  GLY 27  8   8   GLY GLY D . n 
D 4 28  GLY 28  9   9   GLY GLY D . n 
D 4 29  ASP 29  10  10  ASP ASP D . n 
D 4 30  LEU 30  11  11  LEU LEU D . n 
D 4 31  VAL 31  12  12  VAL VAL D . n 
D 4 32  LYS 32  13  13  LYS LYS D . n 
D 4 33  PRO 33  14  14  PRO PRO D . n 
D 4 34  GLY 34  15  15  GLY GLY D . n 
D 4 35  GLY 35  16  16  GLY GLY D . n 
D 4 36  SER 36  17  17  SER SER D . n 
D 4 37  LEU 37  18  18  LEU LEU D . n 
D 4 38  LYS 38  19  19  LYS LYS D . n 
D 4 39  VAL 39  20  20  VAL VAL D . n 
D 4 40  SER 40  21  21  SER SER D . n 
D 4 41  CYS 41  22  22  CYS CYS D . n 
D 4 42  ALA 42  23  23  ALA ALA D . n 
D 4 43  ALA 43  24  24  ALA ALA D . n 
D 4 44  SER 44  25  25  SER SER D . n 
D 4 45  GLY 45  26  26  GLY GLY D . n 
D 4 46  PHE 46  27  27  PHE PHE D . n 
D 4 47  THR 47  28  28  THR THR D . n 
D 4 48  PHE 48  29  29  PHE PHE D . n 
D 4 49  SER 49  30  30  SER SER D . n 
D 4 50  ASN 50  31  31  ASN ASN D . n 
D 4 51  TYR 51  32  32  TYR TYR D . n 
D 4 52  ALA 52  33  33  ALA ALA D . n 
D 4 53  MET 53  34  34  MET MET D . n 
D 4 54  SER 54  35  35  SER SER D . n 
D 4 55  TRP 55  36  36  TRP TRP D . n 
D 4 56  VAL 56  37  37  VAL VAL D . n 
D 4 57  ARG 57  38  38  ARG ARG D . n 
D 4 58  GLN 58  39  39  GLN GLN D . n 
D 4 59  THR 59  40  40  THR THR D . n 
D 4 60  PRO 60  41  41  PRO PRO D . n 
D 4 61  GLU 61  42  42  GLU GLU D . n 
D 4 62  LYS 62  43  43  LYS LYS D . n 
D 4 63  ARG 63  44  44  ARG ARG D . n 
D 4 64  LEU 64  45  45  LEU LEU D . n 
D 4 65  GLU 65  46  46  GLU GLU D . n 
D 4 66  TRP 66  47  47  TRP TRP D . n 
D 4 67  VAL 67  48  48  VAL VAL D . n 
D 4 68  ALA 68  49  49  ALA ALA D . n 
D 4 69  THR 69  50  50  THR THR D . n 
D 4 70  ILE 70  51  51  ILE ILE D . n 
D 4 71  SER 71  52  52  SER SER D . n 
D 4 72  SER 72  53  53  SER SER D . n 
D 4 73  GLY 73  54  54  GLY GLY D . n 
D 4 74  ALA 74  55  55  ALA ALA D . n 
D 4 75  SER 75  56  56  SER SER D . n 
D 4 76  TYR 76  57  57  TYR TYR D . n 
D 4 77  THR 77  58  58  THR THR D . n 
D 4 78  HIS 78  59  59  HIS HIS D . n 
D 4 79  TYR 79  60  60  TYR TYR D . n 
D 4 80  PRO 80  61  61  PRO PRO D . n 
D 4 81  ASP 81  62  62  ASP ASP D . n 
D 4 82  SER 82  63  63  SER SER D . n 
D 4 83  VAL 83  64  64  VAL VAL D . n 
D 4 84  LYS 84  65  65  LYS LYS D . n 
D 4 85  GLY 85  66  66  GLY GLY D . n 
D 4 86  ARG 86  67  67  ARG ARG D . n 
D 4 87  PHE 87  68  68  PHE PHE D . n 
D 4 88  THR 88  69  69  THR THR D . n 
D 4 89  ILE 89  70  70  ILE ILE D . n 
D 4 90  SER 90  71  71  SER SER D . n 
D 4 91  ARG 91  72  72  ARG ARG D . n 
D 4 92  ASP 92  73  73  ASP ASP D . n 
D 4 93  ASN 93  74  74  ASN ASN D . n 
D 4 94  ALA 94  75  75  ALA ALA D . n 
D 4 95  LYS 95  76  76  LYS LYS D . n 
D 4 96  ASN 96  77  77  ASN ASN D . n 
D 4 97  THR 97  78  78  THR THR D . n 
D 4 98  LEU 98  79  79  LEU LEU D . n 
D 4 99  TYR 99  80  80  TYR TYR D . n 
D 4 100 LEU 100 81  81  LEU LEU D . n 
D 4 101 GLN 101 82  82  GLN GLN D . n 
D 4 102 MET 102 83  83  MET MET D . n 
D 4 103 SER 103 84  84  SER SER D . n 
D 4 104 SER 104 85  85  SER SER D . n 
D 4 105 LEU 105 86  86  LEU LEU D . n 
D 4 106 ARG 106 87  87  ARG ARG D . n 
D 4 107 SER 107 88  88  SER SER D . n 
D 4 108 GLU 108 89  89  GLU GLU D . n 
D 4 109 ASP 109 90  90  ASP ASP D . n 
D 4 110 THR 110 91  91  THR THR D . n 
D 4 111 ALA 111 92  92  ALA ALA D . n 
D 4 112 MET 112 93  93  MET MET D . n 
D 4 113 TYR 113 94  94  TYR TYR D . n 
D 4 114 TYR 114 95  95  TYR TYR D . n 
D 4 115 CYS 115 96  96  CYS CYS D . n 
D 4 116 GLY 116 97  97  GLY GLY D . n 
D 4 117 ARG 117 98  98  ARG ARG D . n 
D 4 118 GLN 118 99  99  GLN GLN D . n 
D 4 119 VAL 119 100 100 VAL VAL D . n 
D 4 120 ASN 120 101 101 ASN ASN D . n 
D 4 121 ARG 121 102 102 ARG ARG D . n 
D 4 122 HIS 122 103 103 HIS HIS D . n 
D 4 123 ASP 123 104 104 ASP ASP D . n 
D 4 124 ARG 124 105 105 ARG ARG D . n 
D 4 125 ALA 125 106 106 ALA ALA D . n 
D 4 126 LEU 126 107 107 LEU LEU D . n 
D 4 127 ASP 127 108 108 ASP ASP D . n 
D 4 128 ALA 128 109 109 ALA ALA D . n 
D 4 129 MET 129 110 110 MET MET D . n 
D 4 130 ASP 130 111 111 ASP ASP D . n 
D 4 131 TYR 131 112 112 TYR TYR D . n 
D 4 132 TRP 132 113 113 TRP TRP D . n 
D 4 133 GLY 133 114 114 GLY GLY D . n 
D 4 134 GLN 134 115 115 GLN GLN D . n 
D 4 135 GLY 135 116 116 GLY GLY D . n 
D 4 136 THR 136 117 117 THR THR D . n 
D 4 137 SER 137 118 118 SER SER D . n 
D 4 138 VAL 138 119 119 VAL VAL D . n 
D 4 139 THR 139 120 120 THR THR D . n 
D 4 140 VAL 140 121 121 VAL VAL D . n 
D 4 141 SER 141 122 122 SER SER D . n 
D 4 142 PRO 142 123 123 PRO PRO D . n 
D 4 143 ALA 143 124 124 ALA ALA D . n 
D 4 144 LYS 144 125 125 LYS LYS D . n 
D 4 145 THR 145 126 126 THR THR D . n 
D 4 146 THR 146 127 127 THR THR D . n 
D 4 147 PRO 147 128 128 PRO PRO D . n 
D 4 148 PRO 148 129 129 PRO PRO D . n 
D 4 149 SER 149 130 130 SER SER D . n 
D 4 150 VAL 150 131 131 VAL VAL D . n 
D 4 151 TYR 151 132 132 TYR TYR D . n 
D 4 152 PRO 152 133 133 PRO PRO D . n 
D 4 153 LEU 153 134 134 LEU LEU D . n 
D 4 154 ALA 154 135 135 ALA ALA D . n 
D 4 155 PRO 155 136 136 PRO PRO D . n 
D 4 156 GLY 156 137 ?   ?   ?   D . n 
D 4 157 SER 157 138 ?   ?   ?   D . n 
D 4 158 ALA 158 139 ?   ?   ?   D . n 
D 4 159 ALA 159 140 ?   ?   ?   D . n 
D 4 160 GLN 160 141 ?   ?   ?   D . n 
D 4 161 THR 161 142 ?   ?   ?   D . n 
D 4 162 ASN 162 143 143 ASN ASN D . n 
D 4 163 SER 163 144 144 SER SER D . n 
D 4 164 MET 164 145 145 MET MET D . n 
D 4 165 VAL 165 146 146 VAL VAL D . n 
D 4 166 THR 166 147 147 THR THR D . n 
D 4 167 LEU 167 148 148 LEU LEU D . n 
D 4 168 GLY 168 149 149 GLY GLY D . n 
D 4 169 CYS 169 150 150 CYS CYS D . n 
D 4 170 LEU 170 151 151 LEU LEU D . n 
D 4 171 VAL 171 152 152 VAL VAL D . n 
D 4 172 LYS 172 153 153 LYS LYS D . n 
D 4 173 GLY 173 154 154 GLY GLY D . n 
D 4 174 TYR 174 155 155 TYR TYR D . n 
D 4 175 PHE 175 156 156 PHE PHE D . n 
D 4 176 PRO 176 157 157 PRO PRO D . n 
D 4 177 GLU 177 158 158 GLU GLU D . n 
D 4 178 PRO 178 159 159 PRO PRO D . n 
D 4 179 VAL 179 160 160 VAL VAL D . n 
D 4 180 THR 180 161 161 THR THR D . n 
D 4 181 VAL 181 162 162 VAL VAL D . n 
D 4 182 THR 182 163 163 THR THR D . n 
D 4 183 TRP 183 164 164 TRP TRP D . n 
D 4 184 ASN 184 165 165 ASN ASN D . n 
D 4 185 SER 185 166 166 SER SER D . n 
D 4 186 GLY 186 167 167 GLY GLY D . n 
D 4 187 SER 187 168 168 SER SER D . n 
D 4 188 LEU 188 169 169 LEU LEU D . n 
D 4 189 SER 189 170 170 SER SER D . n 
D 4 190 SER 190 171 171 SER SER D . n 
D 4 191 GLY 191 172 172 GLY GLY D . n 
D 4 192 VAL 192 173 173 VAL VAL D . n 
D 4 193 HIS 193 174 174 HIS HIS D . n 
D 4 194 THR 194 175 175 THR THR D . n 
D 4 195 PHE 195 176 176 PHE PHE D . n 
D 4 196 PRO 196 177 177 PRO PRO D . n 
D 4 197 ALA 197 178 178 ALA ALA D . n 
D 4 198 VAL 198 179 179 VAL VAL D . n 
D 4 199 LEU 199 180 180 LEU LEU D . n 
D 4 200 GLN 200 181 181 GLN GLN D . n 
D 4 201 SER 201 182 182 SER SER D . n 
D 4 202 ASP 202 183 183 ASP ASP D . n 
D 4 203 LEU 203 184 184 LEU LEU D . n 
D 4 204 TYR 204 185 185 TYR TYR D . n 
D 4 205 THR 205 186 186 THR THR D . n 
D 4 206 LEU 206 187 187 LEU LEU D . n 
D 4 207 SER 207 188 188 SER SER D . n 
D 4 208 SER 208 189 189 SER SER D . n 
D 4 209 SER 209 190 190 SER SER D . n 
D 4 210 VAL 210 191 191 VAL VAL D . n 
D 4 211 THR 211 192 192 THR THR D . n 
D 4 212 VAL 212 193 193 VAL VAL D . n 
D 4 213 PRO 213 194 194 PRO PRO D . n 
D 4 214 SER 214 195 195 SER SER D . n 
D 4 215 SER 215 196 196 SER SER D . n 
D 4 216 THR 216 197 197 THR THR D . n 
D 4 217 TRP 217 198 198 TRP TRP D . n 
D 4 218 PRO 218 199 199 PRO PRO D . n 
D 4 219 SER 219 200 200 SER SER D . n 
D 4 220 GLU 220 201 201 GLU GLU D . n 
D 4 221 THR 221 202 202 THR THR D . n 
D 4 222 VAL 222 203 203 VAL VAL D . n 
D 4 223 THR 223 204 204 THR THR D . n 
D 4 224 CYS 224 205 205 CYS CYS D . n 
D 4 225 ASN 225 206 206 ASN ASN D . n 
D 4 226 VAL 226 207 207 VAL VAL D . n 
D 4 227 ALA 227 208 208 ALA ALA D . n 
D 4 228 HIS 228 209 209 HIS HIS D . n 
D 4 229 PRO 229 210 210 PRO PRO D . n 
D 4 230 ALA 230 211 211 ALA ALA D . n 
D 4 231 SER 231 212 212 SER SER D . n 
D 4 232 SER 232 213 213 SER SER D . n 
D 4 233 THR 233 214 214 THR THR D . n 
D 4 234 LYS 234 215 215 LYS LYS D . n 
D 4 235 VAL 235 216 216 VAL VAL D . n 
D 4 236 ASP 236 217 217 ASP ASP D . n 
D 4 237 LYS 237 218 218 LYS LYS D . n 
D 4 238 LYS 238 219 219 LYS LYS D . n 
D 4 239 ILE 239 220 220 ILE ILE D . n 
D 4 240 VAL 240 221 ?   ?   ?   D . n 
D 4 241 PRO 241 222 ?   ?   ?   D . n 
D 4 242 ARG 242 223 ?   ?   ?   D . n 
D 4 243 ASP 243 224 ?   ?   ?   D . n 
D 4 244 CYS 244 225 ?   ?   ?   D . n 
D 4 245 GLY 245 226 ?   ?   ?   D . n 
D 4 246 CYS 246 227 ?   ?   ?   D . n 
D 4 247 LYS 247 228 ?   ?   ?   D . n 
D 4 248 PRO 248 229 ?   ?   ?   D . n 
D 4 249 CYS 249 230 ?   ?   ?   D . n 
D 4 250 ILE 250 231 ?   ?   ?   D . n 
D 4 251 CYS 251 232 ?   ?   ?   D . n 
D 4 252 THR 252 233 ?   ?   ?   D . n 
D 4 253 VAL 253 234 ?   ?   ?   D . n 
D 4 254 PRO 254 235 ?   ?   ?   D . n 
D 4 255 GLU 255 236 ?   ?   ?   D . n 
D 4 256 VAL 256 237 ?   ?   ?   D . n 
D 4 257 SER 257 238 ?   ?   ?   D . n 
D 4 258 SER 258 239 ?   ?   ?   D . n 
D 4 259 VAL 259 240 ?   ?   ?   D . n 
D 4 260 PHE 260 241 ?   ?   ?   D . n 
D 4 261 ILE 261 242 ?   ?   ?   D . n 
D 4 262 PHE 262 243 ?   ?   ?   D . n 
D 4 263 PRO 263 244 ?   ?   ?   D . n 
D 4 264 PRO 264 245 ?   ?   ?   D . n 
D 4 265 LYS 265 246 ?   ?   ?   D . n 
D 4 266 PRO 266 247 ?   ?   ?   D . n 
D 4 267 LYS 267 248 ?   ?   ?   D . n 
D 4 268 ASP 268 249 ?   ?   ?   D . n 
D 4 269 VAL 269 250 ?   ?   ?   D . n 
D 4 270 LEU 270 251 ?   ?   ?   D . n 
D 4 271 THR 271 252 ?   ?   ?   D . n 
D 4 272 ILE 272 253 ?   ?   ?   D . n 
D 4 273 THR 273 254 ?   ?   ?   D . n 
D 4 274 LEU 274 255 ?   ?   ?   D . n 
D 4 275 THR 275 256 ?   ?   ?   D . n 
D 4 276 PRO 276 257 ?   ?   ?   D . n 
D 4 277 LYS 277 258 ?   ?   ?   D . n 
D 4 278 VAL 278 259 ?   ?   ?   D . n 
D 4 279 THR 279 260 ?   ?   ?   D . n 
D 4 280 CYS 280 261 ?   ?   ?   D . n 
D 4 281 VAL 281 262 ?   ?   ?   D . n 
D 4 282 VAL 282 263 ?   ?   ?   D . n 
D 4 283 VAL 283 264 ?   ?   ?   D . n 
D 4 284 ASP 284 265 ?   ?   ?   D . n 
D 4 285 ILE 285 266 ?   ?   ?   D . n 
D 4 286 SER 286 267 ?   ?   ?   D . n 
D 4 287 LYS 287 268 ?   ?   ?   D . n 
D 4 288 ASP 288 269 ?   ?   ?   D . n 
D 4 289 ASP 289 270 ?   ?   ?   D . n 
D 4 290 PRO 290 271 ?   ?   ?   D . n 
D 4 291 GLU 291 272 ?   ?   ?   D . n 
D 4 292 VAL 292 273 ?   ?   ?   D . n 
D 4 293 GLN 293 274 ?   ?   ?   D . n 
D 4 294 PHE 294 275 ?   ?   ?   D . n 
D 4 295 SER 295 276 ?   ?   ?   D . n 
D 4 296 TRP 296 277 ?   ?   ?   D . n 
D 4 297 PHE 297 278 ?   ?   ?   D . n 
D 4 298 VAL 298 279 ?   ?   ?   D . n 
D 4 299 ASP 299 280 ?   ?   ?   D . n 
D 4 300 ASP 300 281 ?   ?   ?   D . n 
D 4 301 VAL 301 282 ?   ?   ?   D . n 
D 4 302 GLU 302 283 ?   ?   ?   D . n 
D 4 303 VAL 303 284 ?   ?   ?   D . n 
D 4 304 HIS 304 285 ?   ?   ?   D . n 
D 4 305 THR 305 286 ?   ?   ?   D . n 
D 4 306 ALA 306 287 ?   ?   ?   D . n 
D 4 307 GLN 307 288 ?   ?   ?   D . n 
D 4 308 THR 308 289 ?   ?   ?   D . n 
D 4 309 GLN 309 290 ?   ?   ?   D . n 
D 4 310 PRO 310 291 ?   ?   ?   D . n 
D 4 311 ARG 311 292 ?   ?   ?   D . n 
D 4 312 GLU 312 293 ?   ?   ?   D . n 
D 4 313 GLU 313 294 ?   ?   ?   D . n 
D 4 314 GLN 314 295 ?   ?   ?   D . n 
D 4 315 PHE 315 296 ?   ?   ?   D . n 
D 4 316 ASN 316 297 ?   ?   ?   D . n 
D 4 317 SER 317 298 ?   ?   ?   D . n 
D 4 318 THR 318 299 ?   ?   ?   D . n 
D 4 319 PHE 319 300 ?   ?   ?   D . n 
D 4 320 ARG 320 301 ?   ?   ?   D . n 
D 4 321 SER 321 302 ?   ?   ?   D . n 
D 4 322 VAL 322 303 ?   ?   ?   D . n 
D 4 323 SER 323 304 ?   ?   ?   D . n 
D 4 324 GLU 324 305 ?   ?   ?   D . n 
D 4 325 LEU 325 306 ?   ?   ?   D . n 
D 4 326 PRO 326 307 ?   ?   ?   D . n 
D 4 327 ILE 327 308 ?   ?   ?   D . n 
D 4 328 MET 328 309 ?   ?   ?   D . n 
D 4 329 HIS 329 310 ?   ?   ?   D . n 
D 4 330 GLN 330 311 ?   ?   ?   D . n 
D 4 331 ASP 331 312 ?   ?   ?   D . n 
D 4 332 TRP 332 313 ?   ?   ?   D . n 
D 4 333 LEU 333 314 ?   ?   ?   D . n 
D 4 334 ASN 334 315 ?   ?   ?   D . n 
D 4 335 GLY 335 316 ?   ?   ?   D . n 
D 4 336 LYS 336 317 ?   ?   ?   D . n 
D 4 337 GLU 337 318 ?   ?   ?   D . n 
D 4 338 PHE 338 319 ?   ?   ?   D . n 
D 4 339 LYS 339 320 ?   ?   ?   D . n 
D 4 340 CYS 340 321 ?   ?   ?   D . n 
D 4 341 ARG 341 322 ?   ?   ?   D . n 
D 4 342 VAL 342 323 ?   ?   ?   D . n 
D 4 343 ASN 343 324 ?   ?   ?   D . n 
D 4 344 SER 344 325 ?   ?   ?   D . n 
D 4 345 ALA 345 326 ?   ?   ?   D . n 
D 4 346 ALA 346 327 ?   ?   ?   D . n 
D 4 347 PHE 347 328 ?   ?   ?   D . n 
D 4 348 PRO 348 329 ?   ?   ?   D . n 
D 4 349 ALA 349 330 ?   ?   ?   D . n 
D 4 350 PRO 350 331 ?   ?   ?   D . n 
D 4 351 ILE 351 332 ?   ?   ?   D . n 
D 4 352 GLU 352 333 ?   ?   ?   D . n 
D 4 353 LYS 353 334 ?   ?   ?   D . n 
D 4 354 THR 354 335 ?   ?   ?   D . n 
D 4 355 ILE 355 336 ?   ?   ?   D . n 
D 4 356 SER 356 337 ?   ?   ?   D . n 
D 4 357 LYS 357 338 ?   ?   ?   D . n 
D 4 358 THR 358 339 ?   ?   ?   D . n 
D 4 359 LYS 359 340 ?   ?   ?   D . n 
D 4 360 GLY 360 341 ?   ?   ?   D . n 
D 4 361 ARG 361 342 ?   ?   ?   D . n 
D 4 362 PRO 362 343 ?   ?   ?   D . n 
D 4 363 LYS 363 344 ?   ?   ?   D . n 
D 4 364 ALA 364 345 ?   ?   ?   D . n 
D 4 365 PRO 365 346 ?   ?   ?   D . n 
D 4 366 GLN 366 347 ?   ?   ?   D . n 
D 4 367 VAL 367 348 ?   ?   ?   D . n 
D 4 368 TYR 368 349 ?   ?   ?   D . n 
D 4 369 THR 369 350 ?   ?   ?   D . n 
D 4 370 ILE 370 351 ?   ?   ?   D . n 
D 4 371 PRO 371 352 ?   ?   ?   D . n 
D 4 372 PRO 372 353 ?   ?   ?   D . n 
D 4 373 PRO 373 354 ?   ?   ?   D . n 
D 4 374 LYS 374 355 ?   ?   ?   D . n 
D 4 375 GLU 375 356 ?   ?   ?   D . n 
D 4 376 GLN 376 357 ?   ?   ?   D . n 
D 4 377 MET 377 358 ?   ?   ?   D . n 
D 4 378 ALA 378 359 ?   ?   ?   D . n 
D 4 379 LYS 379 360 ?   ?   ?   D . n 
D 4 380 ASP 380 361 ?   ?   ?   D . n 
D 4 381 LYS 381 362 ?   ?   ?   D . n 
D 4 382 VAL 382 363 ?   ?   ?   D . n 
D 4 383 SER 383 364 ?   ?   ?   D . n 
D 4 384 LEU 384 365 ?   ?   ?   D . n 
D 4 385 THR 385 366 ?   ?   ?   D . n 
D 4 386 CYS 386 367 ?   ?   ?   D . n 
D 4 387 MET 387 368 ?   ?   ?   D . n 
D 4 388 ILE 388 369 ?   ?   ?   D . n 
D 4 389 THR 389 370 ?   ?   ?   D . n 
D 4 390 ASP 390 371 ?   ?   ?   D . n 
D 4 391 PHE 391 372 ?   ?   ?   D . n 
D 4 392 PHE 392 373 ?   ?   ?   D . n 
D 4 393 PRO 393 374 ?   ?   ?   D . n 
D 4 394 GLU 394 375 ?   ?   ?   D . n 
D 4 395 ASP 395 376 ?   ?   ?   D . n 
D 4 396 ILE 396 377 ?   ?   ?   D . n 
D 4 397 THR 397 378 ?   ?   ?   D . n 
D 4 398 VAL 398 379 ?   ?   ?   D . n 
D 4 399 GLU 399 380 ?   ?   ?   D . n 
D 4 400 TRP 400 381 ?   ?   ?   D . n 
D 4 401 GLN 401 382 ?   ?   ?   D . n 
D 4 402 TRP 402 383 ?   ?   ?   D . n 
D 4 403 ASN 403 384 ?   ?   ?   D . n 
D 4 404 GLY 404 385 ?   ?   ?   D . n 
D 4 405 GLN 405 386 ?   ?   ?   D . n 
D 4 406 PRO 406 387 ?   ?   ?   D . n 
D 4 407 ALA 407 388 ?   ?   ?   D . n 
D 4 408 GLU 408 389 ?   ?   ?   D . n 
D 4 409 ASN 409 390 ?   ?   ?   D . n 
D 4 410 TYR 410 391 ?   ?   ?   D . n 
D 4 411 LYS 411 392 ?   ?   ?   D . n 
D 4 412 ASN 412 393 ?   ?   ?   D . n 
D 4 413 THR 413 394 ?   ?   ?   D . n 
D 4 414 GLN 414 395 ?   ?   ?   D . n 
D 4 415 PRO 415 396 ?   ?   ?   D . n 
D 4 416 ILE 416 397 ?   ?   ?   D . n 
D 4 417 MET 417 398 ?   ?   ?   D . n 
D 4 418 ASP 418 399 ?   ?   ?   D . n 
D 4 419 THR 419 400 ?   ?   ?   D . n 
D 4 420 ASP 420 401 ?   ?   ?   D . n 
D 4 421 GLY 421 402 ?   ?   ?   D . n 
D 4 422 SER 422 403 ?   ?   ?   D . n 
D 4 423 TYR 423 404 ?   ?   ?   D . n 
D 4 424 PHE 424 405 ?   ?   ?   D . n 
D 4 425 VAL 425 406 ?   ?   ?   D . n 
D 4 426 TYR 426 407 ?   ?   ?   D . n 
D 4 427 SER 427 408 ?   ?   ?   D . n 
D 4 428 LYS 428 409 ?   ?   ?   D . n 
D 4 429 LEU 429 410 ?   ?   ?   D . n 
D 4 430 ASN 430 411 ?   ?   ?   D . n 
D 4 431 VAL 431 412 ?   ?   ?   D . n 
D 4 432 GLN 432 413 ?   ?   ?   D . n 
D 4 433 LYS 433 414 ?   ?   ?   D . n 
D 4 434 SER 434 415 ?   ?   ?   D . n 
D 4 435 ASN 435 416 ?   ?   ?   D . n 
D 4 436 TRP 436 417 ?   ?   ?   D . n 
D 4 437 GLU 437 418 ?   ?   ?   D . n 
D 4 438 ALA 438 419 ?   ?   ?   D . n 
D 4 439 GLY 439 420 ?   ?   ?   D . n 
D 4 440 ASN 440 421 ?   ?   ?   D . n 
D 4 441 THR 441 422 ?   ?   ?   D . n 
D 4 442 PHE 442 423 ?   ?   ?   D . n 
D 4 443 THR 443 424 ?   ?   ?   D . n 
D 4 444 CYS 444 425 ?   ?   ?   D . n 
D 4 445 SER 445 426 ?   ?   ?   D . n 
D 4 446 VAL 446 427 ?   ?   ?   D . n 
D 4 447 LEU 447 428 ?   ?   ?   D . n 
D 4 448 HIS 448 429 ?   ?   ?   D . n 
D 4 449 GLU 449 430 ?   ?   ?   D . n 
D 4 450 GLY 450 431 ?   ?   ?   D . n 
D 4 451 LEU 451 432 ?   ?   ?   D . n 
D 4 452 HIS 452 433 ?   ?   ?   D . n 
D 4 453 ASN 453 434 ?   ?   ?   D . n 
D 4 454 HIS 454 435 ?   ?   ?   D . n 
D 4 455 HIS 455 436 ?   ?   ?   D . n 
D 4 456 THR 456 437 ?   ?   ?   D . n 
D 4 457 GLU 457 438 ?   ?   ?   D . n 
D 4 458 LYS 458 439 ?   ?   ?   D . n 
D 4 459 SER 459 440 ?   ?   ?   D . n 
D 4 460 LEU 460 441 ?   ?   ?   D . n 
D 4 461 SER 461 442 ?   ?   ?   D . n 
D 4 462 HIS 462 443 ?   ?   ?   D . n 
D 4 463 SER 463 444 ?   ?   ?   D . n 
D 4 464 PRO 464 445 ?   ?   ?   D . n 
D 4 465 GLY 465 446 ?   ?   ?   D . n 
D 4 466 LYS 466 447 ?   ?   ?   D . n 
E 5 1   MET 1   -19 ?   ?   ?   E . n 
E 5 2   ASP 2   -18 ?   ?   ?   E . n 
E 5 3   SER 3   -17 ?   ?   ?   E . n 
E 5 4   GLN 4   -16 ?   ?   ?   E . n 
E 5 5   ALA 5   -15 ?   ?   ?   E . n 
E 5 6   GLN 6   -14 ?   ?   ?   E . n 
E 5 7   VAL 7   -13 ?   ?   ?   E . n 
E 5 8   LEU 8   -12 ?   ?   ?   E . n 
E 5 9   MET 9   -11 ?   ?   ?   E . n 
E 5 10  LEU 10  -10 ?   ?   ?   E . n 
E 5 11  LEU 11  -9  ?   ?   ?   E . n 
E 5 12  LEU 12  -8  ?   ?   ?   E . n 
E 5 13  LEU 13  -7  ?   ?   ?   E . n 
E 5 14  TRP 14  -6  ?   ?   ?   E . n 
E 5 15  VAL 15  -5  ?   ?   ?   E . n 
E 5 16  SER 16  -4  ?   ?   ?   E . n 
E 5 17  GLY 17  -3  ?   ?   ?   E . n 
E 5 18  THR 18  -2  ?   ?   ?   E . n 
E 5 19  CYS 19  -1  ?   ?   ?   E . n 
E 5 20  GLY 20  0   ?   ?   ?   E . n 
E 5 21  ASP 21  1   1   ASP ASP E . n 
E 5 22  ILE 22  2   2   ILE ILE E . n 
E 5 23  VAL 23  3   3   VAL VAL E . n 
E 5 24  MET 24  4   4   MET MET E . n 
E 5 25  SER 25  5   5   SER SER E . n 
E 5 26  GLN 26  6   6   GLN GLN E . n 
E 5 27  SER 27  7   7   SER SER E . n 
E 5 28  PRO 28  8   8   PRO PRO E . n 
E 5 29  SER 29  9   9   SER SER E . n 
E 5 30  SER 30  10  10  SER SER E . n 
E 5 31  LEU 31  11  11  LEU LEU E . n 
E 5 32  ALA 32  12  12  ALA ALA E . n 
E 5 33  VAL 33  13  13  VAL VAL E . n 
E 5 34  SER 34  14  14  SER SER E . n 
E 5 35  VAL 35  15  15  VAL VAL E . n 
E 5 36  GLY 36  16  16  GLY GLY E . n 
E 5 37  GLU 37  17  17  GLU GLU E . n 
E 5 38  LYS 38  18  18  LYS LYS E . n 
E 5 39  VAL 39  19  19  VAL VAL E . n 
E 5 40  THR 40  20  20  THR THR E . n 
E 5 41  MET 41  21  21  MET MET E . n 
E 5 42  SER 42  22  22  SER SER E . n 
E 5 43  CYS 43  23  23  CYS CYS E . n 
E 5 44  LYS 44  24  24  LYS LYS E . n 
E 5 45  SER 45  25  25  SER SER E . n 
E 5 46  SER 46  26  26  SER SER E . n 
E 5 47  GLN 47  27  27  GLN GLN E . n 
E 5 48  SER 48  28  28  SER SER E . n 
E 5 49  LEU 49  29  29  LEU LEU E . n 
E 5 50  PHE 50  30  30  PHE PHE E . n 
E 5 51  TYR 51  31  31  TYR TYR E . n 
E 5 52  SER 52  32  32  SER SER E . n 
E 5 53  SER 53  33  33  SER SER E . n 
E 5 54  ASN 54  34  34  ASN ASN E . n 
E 5 55  GLN 55  35  35  GLN GLN E . n 
E 5 56  LYS 56  36  36  LYS LYS E . n 
E 5 57  ASN 57  37  37  ASN ASN E . n 
E 5 58  TYR 58  38  38  TYR TYR E . n 
E 5 59  LEU 59  39  39  LEU LEU E . n 
E 5 60  ALA 60  40  40  ALA ALA E . n 
E 5 61  TRP 61  41  41  TRP TRP E . n 
E 5 62  TYR 62  42  42  TYR TYR E . n 
E 5 63  GLN 63  43  43  GLN GLN E . n 
E 5 64  GLN 64  44  44  GLN GLN E . n 
E 5 65  LYS 65  45  45  LYS LYS E . n 
E 5 66  PRO 66  46  46  PRO PRO E . n 
E 5 67  GLY 67  47  47  GLY GLY E . n 
E 5 68  GLN 68  48  48  GLN GLN E . n 
E 5 69  SER 69  49  49  SER SER E . n 
E 5 70  PRO 70  50  50  PRO PRO E . n 
E 5 71  LYS 71  51  51  LYS LYS E . n 
E 5 72  LEU 72  52  52  LEU LEU E . n 
E 5 73  LEU 73  53  53  LEU LEU E . n 
E 5 74  ILE 74  54  54  ILE ILE E . n 
E 5 75  TYR 75  55  55  TYR TYR E . n 
E 5 76  TRP 76  56  56  TRP TRP E . n 
E 5 77  ALA 77  57  57  ALA ALA E . n 
E 5 78  SER 78  58  58  SER SER E . n 
E 5 79  THR 79  59  59  THR THR E . n 
E 5 80  ARG 80  60  60  ARG ARG E . n 
E 5 81  GLU 81  61  61  GLU GLU E . n 
E 5 82  SER 82  62  62  SER SER E . n 
E 5 83  GLY 83  63  63  GLY GLY E . n 
E 5 84  VAL 84  64  64  VAL VAL E . n 
E 5 85  PRO 85  65  65  PRO PRO E . n 
E 5 86  ASP 86  66  66  ASP ASP E . n 
E 5 87  ARG 87  67  67  ARG ARG E . n 
E 5 88  PHE 88  68  68  PHE PHE E . n 
E 5 89  THR 89  69  69  THR THR E . n 
E 5 90  GLY 90  70  70  GLY GLY E . n 
E 5 91  SER 91  71  71  SER SER E . n 
E 5 92  GLY 92  72  72  GLY GLY E . n 
E 5 93  SER 93  73  73  SER SER E . n 
E 5 94  GLY 94  74  74  GLY GLY E . n 
E 5 95  THR 95  75  75  THR THR E . n 
E 5 96  ASP 96  76  76  ASP ASP E . n 
E 5 97  PHE 97  77  77  PHE PHE E . n 
E 5 98  THR 98  78  78  THR THR E . n 
E 5 99  LEU 99  79  79  LEU LEU E . n 
E 5 100 THR 100 80  80  THR THR E . n 
E 5 101 ILE 101 81  81  ILE ILE E . n 
E 5 102 SER 102 82  82  SER SER E . n 
E 5 103 SER 103 83  83  SER SER E . n 
E 5 104 VAL 104 84  84  VAL VAL E . n 
E 5 105 LYS 105 85  85  LYS LYS E . n 
E 5 106 ALA 106 86  86  ALA ALA E . n 
E 5 107 GLU 107 87  87  GLU GLU E . n 
E 5 108 ASP 108 88  88  ASP ASP E . n 
E 5 109 LEU 109 89  89  LEU LEU E . n 
E 5 110 ALA 110 90  90  ALA ALA E . n 
E 5 111 VAL 111 91  91  VAL VAL E . n 
E 5 112 TYR 112 92  92  TYR TYR E . n 
E 5 113 TYR 113 93  93  TYR TYR E . n 
E 5 114 CYS 114 94  94  CYS CYS E . n 
E 5 115 GLN 115 95  95  GLN GLN E . n 
E 5 116 GLN 116 96  96  GLN GLN E . n 
E 5 117 TYR 117 97  97  TYR TYR E . n 
E 5 118 TYR 118 98  98  TYR TYR E . n 
E 5 119 SER 119 99  99  SER SER E . n 
E 5 120 TYR 120 100 100 TYR TYR E . n 
E 5 121 PRO 121 101 101 PRO PRO E . n 
E 5 122 PRO 122 102 102 PRO PRO E . n 
E 5 123 THR 123 103 103 THR THR E . n 
E 5 124 PHE 124 104 104 PHE PHE E . n 
E 5 125 GLY 125 105 105 GLY GLY E . n 
E 5 126 GLY 126 106 106 GLY GLY E . n 
E 5 127 GLY 127 107 107 GLY GLY E . n 
E 5 128 THR 128 108 108 THR THR E . n 
E 5 129 LYS 129 109 109 LYS LYS E . n 
E 5 130 LEU 130 110 110 LEU LEU E . n 
E 5 131 GLU 131 111 111 GLU GLU E . n 
E 5 132 ILE 132 112 112 ILE ILE E . n 
E 5 133 LYS 133 113 113 LYS LYS E . n 
E 5 134 ARG 134 114 114 ARG ARG E . n 
E 5 135 ALA 135 115 115 ALA ALA E . n 
E 5 136 ASP 136 116 116 ASP ASP E . n 
E 5 137 ALA 137 117 117 ALA ALA E . n 
E 5 138 ALA 138 118 118 ALA ALA E . n 
E 5 139 PRO 139 119 119 PRO PRO E . n 
E 5 140 THR 140 120 120 THR THR E . n 
E 5 141 VAL 141 121 121 VAL VAL E . n 
E 5 142 SER 142 122 122 SER SER E . n 
E 5 143 ILE 143 123 123 ILE ILE E . n 
E 5 144 PHE 144 124 124 PHE PHE E . n 
E 5 145 PRO 145 125 125 PRO PRO E . n 
E 5 146 PRO 146 126 126 PRO PRO E . n 
E 5 147 SER 147 127 127 SER SER E . n 
E 5 148 SER 148 128 128 SER SER E . n 
E 5 149 GLU 149 129 129 GLU GLU E . n 
E 5 150 GLN 150 130 130 GLN GLN E . n 
E 5 151 LEU 151 131 131 LEU LEU E . n 
E 5 152 THR 152 132 132 THR THR E . n 
E 5 153 SER 153 133 133 SER SER E . n 
E 5 154 GLY 154 134 134 GLY GLY E . n 
E 5 155 GLY 155 135 135 GLY GLY E . n 
E 5 156 ALA 156 136 136 ALA ALA E . n 
E 5 157 SER 157 137 137 SER SER E . n 
E 5 158 VAL 158 138 138 VAL VAL E . n 
E 5 159 VAL 159 139 139 VAL VAL E . n 
E 5 160 CYS 160 140 140 CYS CYS E . n 
E 5 161 PHE 161 141 141 PHE PHE E . n 
E 5 162 LEU 162 142 142 LEU LEU E . n 
E 5 163 ASN 163 143 143 ASN ASN E . n 
E 5 164 ASN 164 144 144 ASN ASN E . n 
E 5 165 PHE 165 145 145 PHE PHE E . n 
E 5 166 TYR 166 146 146 TYR TYR E . n 
E 5 167 PRO 167 147 147 PRO PRO E . n 
E 5 168 LYS 168 148 148 LYS LYS E . n 
E 5 169 ASP 169 149 149 ASP ASP E . n 
E 5 170 ILE 170 150 150 ILE ILE E . n 
E 5 171 ASN 171 151 151 ASN ASN E . n 
E 5 172 VAL 172 152 152 VAL VAL E . n 
E 5 173 LYS 173 153 153 LYS LYS E . n 
E 5 174 TRP 174 154 154 TRP TRP E . n 
E 5 175 LYS 175 155 155 LYS LYS E . n 
E 5 176 ILE 176 156 156 ILE ILE E . n 
E 5 177 ASP 177 157 157 ASP ASP E . n 
E 5 178 GLY 178 158 158 GLY GLY E . n 
E 5 179 SER 179 159 159 SER SER E . n 
E 5 180 GLU 180 160 160 GLU GLU E . n 
E 5 181 ARG 181 161 161 ARG ARG E . n 
E 5 182 GLN 182 162 162 GLN GLN E . n 
E 5 183 ASN 183 163 163 ASN ASN E . n 
E 5 184 GLY 184 164 164 GLY GLY E . n 
E 5 185 VAL 185 165 165 VAL VAL E . n 
E 5 186 LEU 186 166 166 LEU LEU E . n 
E 5 187 ASN 187 167 167 ASN ASN E . n 
E 5 188 SER 188 168 168 SER SER E . n 
E 5 189 TRP 189 169 169 TRP TRP E . n 
E 5 190 THR 190 170 170 THR THR E . n 
E 5 191 ASP 191 171 171 ASP ASP E . n 
E 5 192 GLN 192 172 172 GLN GLN E . n 
E 5 193 ASP 193 173 173 ASP ASP E . n 
E 5 194 SER 194 174 174 SER SER E . n 
E 5 195 LYS 195 175 175 LYS LYS E . n 
E 5 196 ASP 196 176 176 ASP ASP E . n 
E 5 197 SER 197 177 177 SER SER E . n 
E 5 198 THR 198 178 178 THR THR E . n 
E 5 199 TYR 199 179 179 TYR TYR E . n 
E 5 200 SER 200 180 180 SER SER E . n 
E 5 201 MET 201 181 181 MET MET E . n 
E 5 202 SER 202 182 182 SER SER E . n 
E 5 203 SER 203 183 183 SER SER E . n 
E 5 204 THR 204 184 184 THR THR E . n 
E 5 205 LEU 205 185 185 LEU LEU E . n 
E 5 206 THR 206 186 186 THR THR E . n 
E 5 207 LEU 207 187 187 LEU LEU E . n 
E 5 208 THR 208 188 188 THR THR E . n 
E 5 209 LYS 209 189 189 LYS LYS E . n 
E 5 210 ASP 210 190 190 ASP ASP E . n 
E 5 211 GLU 211 191 191 GLU GLU E . n 
E 5 212 TYR 212 192 192 TYR TYR E . n 
E 5 213 GLU 213 193 193 GLU GLU E . n 
E 5 214 ARG 214 194 194 ARG ARG E . n 
E 5 215 HIS 215 195 195 HIS HIS E . n 
E 5 216 ASN 216 196 196 ASN ASN E . n 
E 5 217 SER 217 197 197 SER SER E . n 
E 5 218 TYR 218 198 198 TYR TYR E . n 
E 5 219 THR 219 199 199 THR THR E . n 
E 5 220 CYS 220 200 200 CYS CYS E . n 
E 5 221 GLU 221 201 201 GLU GLU E . n 
E 5 222 ALA 222 202 202 ALA ALA E . n 
E 5 223 THR 223 203 203 THR THR E . n 
E 5 224 HIS 224 204 204 HIS HIS E . n 
E 5 225 LYS 225 205 205 LYS LYS E . n 
E 5 226 THR 226 206 206 THR THR E . n 
E 5 227 SER 227 207 207 SER SER E . n 
E 5 228 THR 228 208 208 THR THR E . n 
E 5 229 SER 229 209 209 SER SER E . n 
E 5 230 PRO 230 210 210 PRO PRO E . n 
E 5 231 ILE 231 211 211 ILE ILE E . n 
E 5 232 VAL 232 212 212 VAL VAL E . n 
E 5 233 LYS 233 213 213 LYS LYS E . n 
E 5 234 SER 234 214 214 SER SER E . n 
E 5 235 PHE 235 215 215 PHE PHE E . n 
E 5 236 ASN 236 216 216 ASN ASN E . n 
E 5 237 ARG 237 217 217 ARG ARG E . n 
E 5 238 ASN 238 218 ?   ?   ?   E . n 
E 5 239 GLU 239 219 ?   ?   ?   E . n 
E 5 240 CYS 240 220 ?   ?   ?   E . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              matthew.higgins@bioch.ox.ac.uk 
_pdbx_contact_author.name_first         Matthew 
_pdbx_contact_author.name_last          Higgins 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2870-1955 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2022-06-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/4  
3 y+1/2,-x+1/2,z+3/4  
4 x+1/2,-y+1/2,-z+3/4 
5 -x+1/2,y+1/2,-z+1/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -5.05536654639  29.4509628061  35.7111288642 2.06609103675 ? 0.133766917389   ? 0.0236878207021 ? 
1.47102212475 ? -0.464095748497 ? 1.95950896312 ? 5.01200235145  ? -1.1758339509   ? -0.349847017786 ? 0.665192723074 ? 
1.00415729627  ? 5.54582380696 ? -0.414120176049  ? 0.361238262232  ? 0.274790798342  ? 0.491772026372  ? -0.289061437958   ? 
-0.266612580064  ? -0.510780268947 ? -0.529955185282 ? 0.679370582088  ? 
2 'X-RAY DIFFRACTION' ? refined -0.350869343793 42.5387542231  47.8201401173 2.52896590415 ? 0.345460758886   ? -0.349683882236 ? 
1.72261818514 ? -0.483432436773 ? 1.83531453499 ? 1.54640512445  ? -0.927646710227 ? 0.709398296801  ? 3.00081515761  ? 
0.769952736916 ? 1.65476551118 ? -0.147972484464  ? -1.50182828131  ? 0.335396070581  ? 0.554409520333  ? 0.558599376807    ? 
-0.0538069690323 ? -0.51900727382  ? 0.524647101774  ? -0.470442831697 ? 
3 'X-RAY DIFFRACTION' ? refined 27.2323094494   4.09630767792  9.93827476635 1.77297758894 ? 0.319464761794   ? -0.164797084376 ? 
1.47398910391 ? -0.151375184825 ? 2.00797692457 ? 4.95902905188  ? 1.80158753395   ? -0.239192208234 ? 0.615769715288 ? 
0.244460070084 ? 1.35619316098 ? 0.11638781849    ? 0.460076148428  ? 0.233092850828  ? 0.156377039389  ? -0.0794542482052  ? 
-0.421819551581  ? -0.217887752821 ? 0.172785494915  ? 0.0268504182622 ? 
4 'X-RAY DIFFRACTION' ? refined 14.8930133351   -48.2721952886 16.2136976087 1.67046057097 ? -0.0535563305125 ? -0.303044984399 ? 
1.6672012835  ? -0.382725222487 ? 1.92307553237 ? 0.675677699856 ? -1.32044304408  ? -0.589943207406 ? 7.88739862244  ? 
-2.40082590218 ? 2.62095669524 ? -0.20195124878   ? -0.275393098996 ? -0.183394498254 ? 0.014964984501  ? -0.00126631090511 ? 
-0.739345717979  ? 0.643645441893  ? -0.191056001375 ? 0.229743576645  ? 
5 'X-RAY DIFFRACTION' ? refined -2.30948864869  -52.177386997  11.3480571072 1.79572159784 ? -0.40271063453   ? -0.363761770198 ? 
2.82818276344 ? -0.310659187221 ? 1.57318532377 ? 1.36562630509  ? -0.33734569848  ? 0.173261967482  ? 3.21652913105  ? 
-2.65527113673 ? 2.200599355   ? -0.0877570492244 ? -0.266666527088 ? -0.510029762604 ? -0.825831145463 ? 0.412764119506    ? 
0.554805253035   ? 0.818206113016  ? -1.19401499852  ? -0.324300431171 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? D 1  ? ? ? D 220 ? ? '{ D|1-220 }'  
2 'X-RAY DIFFRACTION' 2 ? ? E 1  ? ? ? E 217 ? ? '{ E|1-217 }'  
3 'X-RAY DIFFRACTION' 3 ? ? A 43 ? ? ? A 428 ? ? '{ A|43-428 }' 
4 'X-RAY DIFFRACTION' 4 ? ? B 2  ? ? ? B 218 ? ? '{ B|2-218 }'  
5 'X-RAY DIFFRACTION' 5 ? ? C 1  ? ? ? C 216 ? ? '{ C|1-216 }'  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? 1.19_4092 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.19_4092 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .         3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .         4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .         5 
# 
_pdbx_entry_details.entry_id                 7ZXF 
_pdbx_entry_details.has_ligand_of_interest   N 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 50  ? ? -140.56 -42.51  
2  1 GLU A 102 ? ? 43.95   -124.23 
3  1 PHE A 105 ? ? 70.83   -11.92  
4  1 THR A 110 ? ? -60.41  -72.84  
5  1 GLU A 122 ? ? -93.03  55.81   
6  1 CYS A 158 ? ? -166.06 118.27  
7  1 CYS A 227 ? ? -162.24 -169.34 
8  1 ASN A 231 ? ? 58.07   5.27    
9  1 LYS A 241 ? ? 54.07   18.15   
10 1 LYS A 248 ? ? -163.48 119.96  
11 1 LYS A 253 ? ? 60.67   -131.97 
12 1 TYR A 290 ? ? -56.22  101.75  
13 1 LYS A 292 ? ? -58.36  102.67  
14 1 VAL A 294 ? ? -114.53 77.40   
15 1 HIS A 296 ? ? -68.00  76.82   
16 1 SER A 302 ? ? -88.61  38.63   
17 1 LEU A 314 ? ? 176.62  163.51  
18 1 PRO A 350 ? ? -79.07  -155.45 
19 1 THR A 405 ? ? -67.20  98.45   
20 1 ASP A 415 ? ? 58.08   -137.40 
21 1 THR B 91  ? ? -68.43  95.43   
22 1 PRO B 195 ? ? -80.86  30.17   
23 1 LYS B 211 ? ? -160.43 96.95   
24 1 CYS C 22  ? ? -157.53 78.37   
25 1 ASP C 52  ? ? 76.28   -59.54  
26 1 SER C 66  ? ? -166.53 119.61  
27 1 ALA C 151 ? ? -163.48 112.58  
28 1 GLU C 171 ? ? -130.03 -30.58  
29 1 THR C 204 ? ? -101.27 77.76   
30 1 PRO D 14  ? ? -56.06  109.29  
31 1 LEU D 81  ? ? -165.36 111.93  
32 1 ASP D 90  ? ? -68.89  2.16    
33 1 SER D 170 ? ? -141.04 -26.34  
34 1 TYR E 38  ? ? -105.00 68.82   
35 1 LEU E 53  ? ? -113.98 -72.93  
36 1 ALA E 57  ? ? 59.52   10.48   
37 1 SER E 58  ? ? -153.03 -55.02  
38 1 ASP E 88  ? ? -114.01 57.25   
39 1 TYR E 97  ? ? -142.25 46.43   
40 1 LEU E 110 ? ? -108.37 72.98   
41 1 ASN E 144 ? ? 58.85   71.07   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 B SER 185 ? CA ? B SER 185 CA 
2 1 Y 0 B SER 185 ? C  ? B SER 185 C  
3 1 Y 0 B SER 185 ? O  ? B SER 185 O  
4 1 Y 0 B SER 185 ? CB ? B SER 185 CB 
5 1 Y 0 B SER 185 ? OG ? B SER 185 OG 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -1  ? A MET 1   
2   1 Y 1 A MET 0   ? A MET 2   
3   1 Y 1 A LEU 1   ? A LEU 3   
4   1 Y 1 A TYR 2   ? A TYR 4   
5   1 Y 1 A ILE 3   ? A ILE 5   
6   1 Y 1 A SER 4   ? A SER 6   
7   1 Y 1 A ALA 5   ? A ALA 7   
8   1 Y 1 A LYS 6   ? A LYS 8   
9   1 Y 1 A LYS 7   ? A LYS 9   
10  1 Y 1 A ALA 8   ? A ALA 10  
11  1 Y 1 A GLN 9   ? A GLN 11  
12  1 Y 1 A VAL 10  ? A VAL 12  
13  1 Y 1 A ALA 11  ? A ALA 13  
14  1 Y 1 A PHE 12  ? A PHE 14  
15  1 Y 1 A ILE 13  ? A ILE 15  
16  1 Y 1 A LEU 14  ? A LEU 16  
17  1 Y 1 A TYR 15  ? A TYR 17  
18  1 Y 1 A ILE 16  ? A ILE 18  
19  1 Y 1 A VAL 17  ? A VAL 19  
20  1 Y 1 A LEU 18  ? A LEU 20  
21  1 Y 1 A VAL 19  ? A VAL 21  
22  1 Y 1 A LEU 20  ? A LEU 22  
23  1 Y 1 A ARG 21  ? A ARG 23  
24  1 Y 1 A ILE 22  ? A ILE 24  
25  1 Y 1 A ILE 23  ? A ILE 25  
26  1 Y 1 A SER 24  ? A SER 26  
27  1 Y 1 A GLY 25  ? A GLY 27  
28  1 Y 1 A ASN 26  ? A ASN 28  
29  1 Y 1 A ASN 27  ? A ASN 29  
30  1 Y 1 A ASP 28  ? A ASP 30  
31  1 Y 1 A PHE 29  ? A PHE 31  
32  1 Y 1 A CYS 30  ? A CYS 32  
33  1 Y 1 A LYS 31  ? A LYS 33  
34  1 Y 1 A PRO 32  ? A PRO 34  
35  1 Y 1 A SER 33  ? A SER 35  
36  1 Y 1 A SER 34  ? A SER 36  
37  1 Y 1 A LEU 35  ? A LEU 37  
38  1 Y 1 A ASN 36  ? A ASN 38  
39  1 Y 1 A SER 37  ? A SER 39  
40  1 Y 1 A GLU 38  ? A GLU 40  
41  1 Y 1 A ILE 39  ? A ILE 41  
42  1 Y 1 A SER 40  ? A SER 42  
43  1 Y 1 A GLY 41  ? A GLY 43  
44  1 Y 1 A PHE 42  ? A PHE 44  
45  1 Y 1 A GLU 56  ? A GLU 54  
46  1 Y 1 A GLY 57  ? A GLY 55  
47  1 Y 1 A VAL 58  ? A VAL 56  
48  1 Y 1 A HIS 59  ? A HIS 57  
49  1 Y 1 A ASN 60  ? A ASN 58  
50  1 Y 1 A LEU 61  ? A LEU 59  
51  1 Y 1 A LYS 62  ? A LYS 60  
52  1 Y 1 A PRO 63  ? A PRO 61  
53  1 Y 1 A ASP 64  ? A ASP 62  
54  1 Y 1 A MET 65  ? A MET 63  
55  1 Y 1 A ARG 66  ? A ARG 64  
56  1 Y 1 A GLU 67  ? A GLU 65  
57  1 Y 1 A ARG 68  ? A ARG 66  
58  1 Y 1 A ARG 69  ? A ARG 67  
59  1 Y 1 A SER 70  ? A SER 68  
60  1 Y 1 A PRO 89  ? A PRO 87  
61  1 Y 1 A LYS 90  ? A LYS 88  
62  1 Y 1 A LYS 91  ? A LYS 89  
63  1 Y 1 A SER 92  ? A SER 90  
64  1 Y 1 A SER 93  ? A SER 91  
65  1 Y 1 A SER 94  ? A SER 92  
66  1 Y 1 A PRO 95  ? A PRO 93  
67  1 Y 1 A GLU 96  ? A GLU 94  
68  1 Y 1 A PHE 97  ? A PHE 95  
69  1 Y 1 A LYS 98  ? A LYS 96  
70  1 Y 1 A ASP 160 A A ASP 159 
71  1 Y 1 A ASN 160 B A ASN 160 
72  1 Y 1 A THR 160 C A THR 161 
73  1 Y 1 A GLU 160 D A GLU 162 
74  1 Y 1 A LYS 160 E A LYS 163 
75  1 Y 1 A VAL 160 F A VAL 164 
76  1 Y 1 A ILE 160 G A ILE 165 
77  1 Y 1 A SER 160 H A SER 166 
78  1 Y 1 A SER 160 I A SER 167 
79  1 Y 1 A ILE 160 J A ILE 168 
80  1 Y 1 A GLU 160 K A GLU 169 
81  1 Y 1 A GLY 160 L A GLY 170 
82  1 Y 1 A ARG 160 M A ARG 171 
83  1 Y 1 A SER 160 N A SER 172 
84  1 Y 1 A ALA 160 O A ALA 173 
85  1 Y 1 A GLU 360 ? A GLU 360 
86  1 Y 1 A SER 361 ? A SER 361 
87  1 Y 1 A GLU 362 ? A GLU 362 
88  1 Y 1 A GLU 363 ? A GLU 363 
89  1 Y 1 A LEU 364 ? A LEU 364 
90  1 Y 1 A GLU 365 ? A GLU 365 
91  1 Y 1 A PRO 366 ? A PRO 366 
92  1 Y 1 A TYR 429 ? A TYR 429 
93  1 Y 1 A TYR 430 ? A TYR 430 
94  1 Y 1 A GLY 431 ? A GLY 431 
95  1 Y 1 A PHE 432 ? A PHE 432 
96  1 Y 1 A LEU 433 ? A LEU 433 
97  1 Y 1 A ALA 434 ? A ALA 434 
98  1 Y 1 A LYS 435 ? A LYS 435 
99  1 Y 1 A THR 436 ? A THR 436 
100 1 Y 1 A PHE 437 ? A PHE 437 
101 1 Y 1 A ILE 438 ? A ILE 438 
102 1 Y 1 A PHE 439 ? A PHE 439 
103 1 Y 1 A LEU 440 ? A LEU 440 
104 1 Y 1 A ILE 441 ? A ILE 441 
105 1 Y 1 A VAL 442 ? A VAL 442 
106 1 Y 1 A ALA 443 ? A ALA 443 
107 1 Y 1 A ILE 444 ? A ILE 444 
108 1 Y 1 A LEU 445 ? A LEU 445 
109 1 Y 1 A LEU 446 ? A LEU 446 
110 1 Y 1 A TYR 447 ? A TYR 447 
111 1 Y 1 A ILE 448 ? A ILE 448 
112 1 Y 1 B GLU 1   ? B GLU 1   
113 1 Y 0 B LEU 130 ? B LEU 130 
114 1 Y 0 B ALA 131 ? B ALA 131 
115 1 Y 1 B PRO 132 ? B PRO 132 
116 1 Y 1 B GLY 133 ? B GLY 133 
117 1 Y 1 B THR 134 ? B THR 134 
118 1 Y 1 B ALA 135 ? B ALA 135 
119 1 Y 1 B LEU 136 ? B LEU 136 
120 1 Y 1 B LYS 137 ? B LYS 137 
121 1 Y 1 B SER 138 ? B SER 138 
122 1 Y 1 B ASN 139 ? B ASN 139 
123 1 Y 1 B SER 140 ? B SER 140 
124 1 Y 1 B MET 141 ? B MET 141 
125 1 Y 1 B VAL 142 ? B VAL 142 
126 1 Y 0 B THR 143 ? B THR 143 
127 1 Y 0 B LEU 144 ? B LEU 144 
128 1 Y 0 B GLY 145 ? B GLY 145 
129 1 Y 0 B SER 186 ? B SER 186 
130 1 Y 0 B VAL 187 ? B VAL 187 
131 1 Y 0 B THR 188 ? B THR 188 
132 1 Y 0 B VAL 189 ? B VAL 189 
133 1 Y 0 B PRO 190 ? B PRO 190 
134 1 Y 0 B VAL 217 ? B VAL 217 
135 1 Y 0 B PRO 218 ? B PRO 218 
136 1 Y 1 B ARG 219 ? B ARG 219 
137 1 Y 1 B ASN 220 ? B ASN 220 
138 1 Y 1 B CYS 221 ? B CYS 221 
139 1 Y 1 B GLY 222 ? B GLY 222 
140 1 Y 1 B GLY 223 ? B GLY 223 
141 1 Y 1 B ASP 224 ? B ASP 224 
142 1 Y 1 B CYS 225 ? B CYS 225 
143 1 Y 1 B LYS 226 ? B LYS 226 
144 1 Y 1 B PRO 227 ? B PRO 227 
145 1 Y 1 B CYS 228 ? B CYS 228 
146 1 Y 1 B ILE 229 ? B ILE 229 
147 1 Y 1 B CYS 230 ? B CYS 230 
148 1 Y 1 B THR 231 ? B THR 231 
149 1 Y 1 B GLY 232 ? B GLY 232 
150 1 Y 1 B SER 233 ? B SER 233 
151 1 Y 1 B GLU 234 ? B GLU 234 
152 1 Y 1 B VAL 235 ? B VAL 235 
153 1 Y 1 B SER 236 ? B SER 236 
154 1 Y 1 B SER 237 ? B SER 237 
155 1 Y 1 B VAL 238 ? B VAL 238 
156 1 Y 1 B PHE 239 ? B PHE 239 
157 1 Y 1 B ILE 240 ? B ILE 240 
158 1 Y 1 B PHE 241 ? B PHE 241 
159 1 Y 1 B PRO 242 ? B PRO 242 
160 1 Y 1 B PRO 243 ? B PRO 243 
161 1 Y 1 B LYS 244 ? B LYS 244 
162 1 Y 1 B PRO 245 ? B PRO 245 
163 1 Y 1 B LYS 246 ? B LYS 246 
164 1 Y 1 B ASP 247 ? B ASP 247 
165 1 Y 1 B VAL 248 ? B VAL 248 
166 1 Y 1 B LEU 249 ? B LEU 249 
167 1 Y 1 B THR 250 ? B THR 250 
168 1 Y 1 B ILE 251 ? B ILE 251 
169 1 Y 1 B THR 252 ? B THR 252 
170 1 Y 1 B LEU 253 ? B LEU 253 
171 1 Y 1 B THR 254 ? B THR 254 
172 1 Y 1 B PRO 255 ? B PRO 255 
173 1 Y 1 B LYS 256 ? B LYS 256 
174 1 Y 1 B VAL 257 ? B VAL 257 
175 1 Y 1 B THR 258 ? B THR 258 
176 1 Y 1 B CYS 259 ? B CYS 259 
177 1 Y 1 B VAL 260 ? B VAL 260 
178 1 Y 1 B VAL 261 ? B VAL 261 
179 1 Y 1 B VAL 262 ? B VAL 262 
180 1 Y 1 B ASP 263 ? B ASP 263 
181 1 Y 1 B ILE 264 ? B ILE 264 
182 1 Y 1 B SER 265 ? B SER 265 
183 1 Y 1 B GLN 266 ? B GLN 266 
184 1 Y 1 B ASP 267 ? B ASP 267 
185 1 Y 1 B ASP 268 ? B ASP 268 
186 1 Y 1 B PRO 269 ? B PRO 269 
187 1 Y 1 B GLU 270 ? B GLU 270 
188 1 Y 1 B VAL 271 ? B VAL 271 
189 1 Y 1 B HIS 272 ? B HIS 272 
190 1 Y 1 B PHE 273 ? B PHE 273 
191 1 Y 1 B SER 274 ? B SER 274 
192 1 Y 1 B TRP 275 ? B TRP 275 
193 1 Y 1 B PHE 276 ? B PHE 276 
194 1 Y 1 B VAL 277 ? B VAL 277 
195 1 Y 1 B ASP 278 ? B ASP 278 
196 1 Y 1 B ASP 279 ? B ASP 279 
197 1 Y 1 B VAL 280 ? B VAL 280 
198 1 Y 1 B GLU 281 ? B GLU 281 
199 1 Y 1 B VAL 282 ? B VAL 282 
200 1 Y 1 B HIS 283 ? B HIS 283 
201 1 Y 1 B THR 284 ? B THR 284 
202 1 Y 1 B ALA 285 ? B ALA 285 
203 1 Y 1 B GLN 286 ? B GLN 286 
204 1 Y 1 B THR 287 ? B THR 287 
205 1 Y 1 B ARG 288 ? B ARG 288 
206 1 Y 1 B PRO 289 ? B PRO 289 
207 1 Y 1 B PRO 290 ? B PRO 290 
208 1 Y 1 B GLU 291 ? B GLU 291 
209 1 Y 1 B GLU 292 ? B GLU 292 
210 1 Y 1 B GLN 293 ? B GLN 293 
211 1 Y 1 B PHE 294 ? B PHE 294 
212 1 Y 1 B ASN 295 ? B ASN 295 
213 1 Y 1 B SER 296 ? B SER 296 
214 1 Y 1 B THR 297 ? B THR 297 
215 1 Y 1 B PHE 298 ? B PHE 298 
216 1 Y 1 B ARG 299 ? B ARG 299 
217 1 Y 1 B SER 300 ? B SER 300 
218 1 Y 1 B VAL 301 ? B VAL 301 
219 1 Y 1 B SER 302 ? B SER 302 
220 1 Y 1 B GLU 303 ? B GLU 303 
221 1 Y 1 B LEU 304 ? B LEU 304 
222 1 Y 1 B PRO 305 ? B PRO 305 
223 1 Y 1 B ILE 306 ? B ILE 306 
224 1 Y 1 B LEU 307 ? B LEU 307 
225 1 Y 1 B HIS 308 ? B HIS 308 
226 1 Y 1 B GLN 309 ? B GLN 309 
227 1 Y 1 B ASP 310 ? B ASP 310 
228 1 Y 1 B TRP 311 ? B TRP 311 
229 1 Y 1 B LEU 312 ? B LEU 312 
230 1 Y 1 B ASN 313 ? B ASN 313 
231 1 Y 1 B GLY 314 ? B GLY 314 
232 1 Y 1 B ARG 315 ? B ARG 315 
233 1 Y 1 B THR 316 ? B THR 316 
234 1 Y 1 B PHE 317 ? B PHE 317 
235 1 Y 1 B ARG 318 ? B ARG 318 
236 1 Y 1 B CYS 319 ? B CYS 319 
237 1 Y 1 B LYS 320 ? B LYS 320 
238 1 Y 1 B VAL 321 ? B VAL 321 
239 1 Y 1 B THR 322 ? B THR 322 
240 1 Y 1 B SER 323 ? B SER 323 
241 1 Y 1 B ALA 324 ? B ALA 324 
242 1 Y 1 B ALA 325 ? B ALA 325 
243 1 Y 1 B PHE 326 ? B PHE 326 
244 1 Y 1 B PRO 327 ? B PRO 327 
245 1 Y 1 B SER 328 ? B SER 328 
246 1 Y 1 B PRO 329 ? B PRO 329 
247 1 Y 1 B ILE 330 ? B ILE 330 
248 1 Y 1 B GLU 331 ? B GLU 331 
249 1 Y 1 B LYS 332 ? B LYS 332 
250 1 Y 1 B THR 333 ? B THR 333 
251 1 Y 1 B ILE 334 ? B ILE 334 
252 1 Y 1 B SER 335 ? B SER 335 
253 1 Y 1 B LYS 336 ? B LYS 336 
254 1 Y 1 B PRO 337 ? B PRO 337 
255 1 Y 1 B GLU 338 ? B GLU 338 
256 1 Y 1 B GLY 339 ? B GLY 339 
257 1 Y 1 B ARG 340 ? B ARG 340 
258 1 Y 1 B THR 341 ? B THR 341 
259 1 Y 1 B GLN 342 ? B GLN 342 
260 1 Y 1 B VAL 343 ? B VAL 343 
261 1 Y 1 B PRO 344 ? B PRO 344 
262 1 Y 1 B HIS 345 ? B HIS 345 
263 1 Y 1 B VAL 346 ? B VAL 346 
264 1 Y 1 B TYR 347 ? B TYR 347 
265 1 Y 1 B THR 348 ? B THR 348 
266 1 Y 1 B MET 349 ? B MET 349 
267 1 Y 1 B SER 350 ? B SER 350 
268 1 Y 1 B PRO 351 ? B PRO 351 
269 1 Y 1 B THR 352 ? B THR 352 
270 1 Y 1 B LYS 353 ? B LYS 353 
271 1 Y 1 B GLU 354 ? B GLU 354 
272 1 Y 1 B GLU 355 ? B GLU 355 
273 1 Y 1 B MET 356 ? B MET 356 
274 1 Y 1 B THR 357 ? B THR 357 
275 1 Y 1 B GLN 358 ? B GLN 358 
276 1 Y 1 B ASN 359 ? B ASN 359 
277 1 Y 1 B GLU 360 ? B GLU 360 
278 1 Y 1 B VAL 361 ? B VAL 361 
279 1 Y 1 B SER 362 ? B SER 362 
280 1 Y 1 B ILE 363 ? B ILE 363 
281 1 Y 1 B THR 364 ? B THR 364 
282 1 Y 1 B CYS 365 ? B CYS 365 
283 1 Y 1 B MET 366 ? B MET 366 
284 1 Y 1 B VAL 367 ? B VAL 367 
285 1 Y 1 B LYS 368 ? B LYS 368 
286 1 Y 1 B GLY 369 ? B GLY 369 
287 1 Y 1 B PHE 370 ? B PHE 370 
288 1 Y 1 B TYR 371 ? B TYR 371 
289 1 Y 1 B PRO 372 ? B PRO 372 
290 1 Y 1 B PRO 373 ? B PRO 373 
291 1 Y 1 B ASP 374 ? B ASP 374 
292 1 Y 1 B ILE 375 ? B ILE 375 
293 1 Y 1 B TYR 376 ? B TYR 376 
294 1 Y 1 B VAL 377 ? B VAL 377 
295 1 Y 1 B GLU 378 ? B GLU 378 
296 1 Y 1 B TRP 379 ? B TRP 379 
297 1 Y 1 B GLN 380 ? B GLN 380 
298 1 Y 1 B MET 381 ? B MET 381 
299 1 Y 1 B ASN 382 ? B ASN 382 
300 1 Y 1 B GLY 383 ? B GLY 383 
301 1 Y 1 B GLN 384 ? B GLN 384 
302 1 Y 1 B PRO 385 ? B PRO 385 
303 1 Y 1 B GLN 386 ? B GLN 386 
304 1 Y 1 B GLU 387 ? B GLU 387 
305 1 Y 1 B ASN 388 ? B ASN 388 
306 1 Y 1 B TYR 389 ? B TYR 389 
307 1 Y 1 B LYS 390 ? B LYS 390 
308 1 Y 1 B ASN 391 ? B ASN 391 
309 1 Y 1 B THR 392 ? B THR 392 
310 1 Y 1 B PRO 393 ? B PRO 393 
311 1 Y 1 B PRO 394 ? B PRO 394 
312 1 Y 1 B THR 395 ? B THR 395 
313 1 Y 1 B MET 396 ? B MET 396 
314 1 Y 1 B ASP 397 ? B ASP 397 
315 1 Y 1 B THR 398 ? B THR 398 
316 1 Y 1 B ASP 399 ? B ASP 399 
317 1 Y 1 B GLY 400 ? B GLY 400 
318 1 Y 1 B SER 401 ? B SER 401 
319 1 Y 1 B TYR 402 ? B TYR 402 
320 1 Y 1 B PHE 403 ? B PHE 403 
321 1 Y 1 B LEU 404 ? B LEU 404 
322 1 Y 1 B TYR 405 ? B TYR 405 
323 1 Y 1 B SER 406 ? B SER 406 
324 1 Y 1 B LYS 407 ? B LYS 407 
325 1 Y 1 B LEU 408 ? B LEU 408 
326 1 Y 1 B ASN 409 ? B ASN 409 
327 1 Y 1 B VAL 410 ? B VAL 410 
328 1 Y 1 B LYS 411 ? B LYS 411 
329 1 Y 1 B LYS 412 ? B LYS 412 
330 1 Y 1 B GLU 413 ? B GLU 413 
331 1 Y 1 B LYS 414 ? B LYS 414 
332 1 Y 1 B TRP 415 ? B TRP 415 
333 1 Y 1 B GLN 416 ? B GLN 416 
334 1 Y 1 B GLN 417 ? B GLN 417 
335 1 Y 1 B GLY 418 ? B GLY 418 
336 1 Y 1 B ASN 419 ? B ASN 419 
337 1 Y 1 B THR 420 ? B THR 420 
338 1 Y 1 B PHE 421 ? B PHE 421 
339 1 Y 1 B THR 422 ? B THR 422 
340 1 Y 1 B CYS 423 ? B CYS 423 
341 1 Y 1 B SER 424 ? B SER 424 
342 1 Y 1 B VAL 425 ? B VAL 425 
343 1 Y 1 B LEU 426 ? B LEU 426 
344 1 Y 1 B HIS 427 ? B HIS 427 
345 1 Y 1 B GLU 428 ? B GLU 428 
346 1 Y 1 B GLY 429 ? B GLY 429 
347 1 Y 1 B LEU 430 ? B LEU 430 
348 1 Y 1 B HIS 431 ? B HIS 431 
349 1 Y 1 B ASN 432 ? B ASN 432 
350 1 Y 1 B HIS 433 ? B HIS 433 
351 1 Y 1 B HIS 434 ? B HIS 434 
352 1 Y 1 B THR 435 ? B THR 435 
353 1 Y 1 B GLU 436 ? B GLU 436 
354 1 Y 1 B LYS 437 ? B LYS 437 
355 1 Y 1 B SER 438 ? B SER 438 
356 1 Y 1 B LEU 439 ? B LEU 439 
357 1 Y 1 B SER 440 ? B SER 440 
358 1 Y 1 B HIS 441 ? B HIS 441 
359 1 Y 1 B SER 442 ? B SER 442 
360 1 Y 1 B PRO 443 ? B PRO 443 
361 1 Y 1 B GLY 444 ? B GLY 444 
362 1 Y 1 B LYS 445 ? B LYS 445 
363 1 Y 1 D MET -18 ? D MET 1   
364 1 Y 1 D ASN -17 ? D ASN 2   
365 1 Y 1 D PHE -16 ? D PHE 3   
366 1 Y 1 D GLY -15 ? D GLY 4   
367 1 Y 1 D LEU -14 ? D LEU 5   
368 1 Y 1 D SER -13 ? D SER 6   
369 1 Y 1 D LEU -12 ? D LEU 7   
370 1 Y 1 D ILE -11 ? D ILE 8   
371 1 Y 1 D PHE -10 ? D PHE 9   
372 1 Y 1 D LEU -9  ? D LEU 10  
373 1 Y 1 D VAL -8  ? D VAL 11  
374 1 Y 1 D LEU -7  ? D LEU 12  
375 1 Y 1 D VAL -6  ? D VAL 13  
376 1 Y 1 D LEU -5  ? D LEU 14  
377 1 Y 1 D LYS -4  ? D LYS 15  
378 1 Y 1 D GLY -3  ? D GLY 16  
379 1 Y 1 D VAL -2  ? D VAL 17  
380 1 Y 1 D GLN -1  ? D GLN 18  
381 1 Y 1 D CYS 0   ? D CYS 19  
382 1 Y 0 D ALA 135 ? D ALA 154 
383 1 Y 0 D PRO 136 ? D PRO 155 
384 1 Y 1 D GLY 137 ? D GLY 156 
385 1 Y 1 D SER 138 ? D SER 157 
386 1 Y 1 D ALA 139 ? D ALA 158 
387 1 Y 1 D ALA 140 ? D ALA 159 
388 1 Y 1 D GLN 141 ? D GLN 160 
389 1 Y 1 D THR 142 ? D THR 161 
390 1 Y 0 D ASN 143 ? D ASN 162 
391 1 Y 0 D SER 144 ? D SER 163 
392 1 Y 0 D MET 145 ? D MET 164 
393 1 Y 1 D VAL 221 ? D VAL 240 
394 1 Y 1 D PRO 222 ? D PRO 241 
395 1 Y 1 D ARG 223 ? D ARG 242 
396 1 Y 1 D ASP 224 ? D ASP 243 
397 1 Y 1 D CYS 225 ? D CYS 244 
398 1 Y 1 D GLY 226 ? D GLY 245 
399 1 Y 1 D CYS 227 ? D CYS 246 
400 1 Y 1 D LYS 228 ? D LYS 247 
401 1 Y 1 D PRO 229 ? D PRO 248 
402 1 Y 1 D CYS 230 ? D CYS 249 
403 1 Y 1 D ILE 231 ? D ILE 250 
404 1 Y 1 D CYS 232 ? D CYS 251 
405 1 Y 1 D THR 233 ? D THR 252 
406 1 Y 1 D VAL 234 ? D VAL 253 
407 1 Y 1 D PRO 235 ? D PRO 254 
408 1 Y 1 D GLU 236 ? D GLU 255 
409 1 Y 1 D VAL 237 ? D VAL 256 
410 1 Y 1 D SER 238 ? D SER 257 
411 1 Y 1 D SER 239 ? D SER 258 
412 1 Y 1 D VAL 240 ? D VAL 259 
413 1 Y 1 D PHE 241 ? D PHE 260 
414 1 Y 1 D ILE 242 ? D ILE 261 
415 1 Y 1 D PHE 243 ? D PHE 262 
416 1 Y 1 D PRO 244 ? D PRO 263 
417 1 Y 1 D PRO 245 ? D PRO 264 
418 1 Y 1 D LYS 246 ? D LYS 265 
419 1 Y 1 D PRO 247 ? D PRO 266 
420 1 Y 1 D LYS 248 ? D LYS 267 
421 1 Y 1 D ASP 249 ? D ASP 268 
422 1 Y 1 D VAL 250 ? D VAL 269 
423 1 Y 1 D LEU 251 ? D LEU 270 
424 1 Y 1 D THR 252 ? D THR 271 
425 1 Y 1 D ILE 253 ? D ILE 272 
426 1 Y 1 D THR 254 ? D THR 273 
427 1 Y 1 D LEU 255 ? D LEU 274 
428 1 Y 1 D THR 256 ? D THR 275 
429 1 Y 1 D PRO 257 ? D PRO 276 
430 1 Y 1 D LYS 258 ? D LYS 277 
431 1 Y 1 D VAL 259 ? D VAL 278 
432 1 Y 1 D THR 260 ? D THR 279 
433 1 Y 1 D CYS 261 ? D CYS 280 
434 1 Y 1 D VAL 262 ? D VAL 281 
435 1 Y 1 D VAL 263 ? D VAL 282 
436 1 Y 1 D VAL 264 ? D VAL 283 
437 1 Y 1 D ASP 265 ? D ASP 284 
438 1 Y 1 D ILE 266 ? D ILE 285 
439 1 Y 1 D SER 267 ? D SER 286 
440 1 Y 1 D LYS 268 ? D LYS 287 
441 1 Y 1 D ASP 269 ? D ASP 288 
442 1 Y 1 D ASP 270 ? D ASP 289 
443 1 Y 1 D PRO 271 ? D PRO 290 
444 1 Y 1 D GLU 272 ? D GLU 291 
445 1 Y 1 D VAL 273 ? D VAL 292 
446 1 Y 1 D GLN 274 ? D GLN 293 
447 1 Y 1 D PHE 275 ? D PHE 294 
448 1 Y 1 D SER 276 ? D SER 295 
449 1 Y 1 D TRP 277 ? D TRP 296 
450 1 Y 1 D PHE 278 ? D PHE 297 
451 1 Y 1 D VAL 279 ? D VAL 298 
452 1 Y 1 D ASP 280 ? D ASP 299 
453 1 Y 1 D ASP 281 ? D ASP 300 
454 1 Y 1 D VAL 282 ? D VAL 301 
455 1 Y 1 D GLU 283 ? D GLU 302 
456 1 Y 1 D VAL 284 ? D VAL 303 
457 1 Y 1 D HIS 285 ? D HIS 304 
458 1 Y 1 D THR 286 ? D THR 305 
459 1 Y 1 D ALA 287 ? D ALA 306 
460 1 Y 1 D GLN 288 ? D GLN 307 
461 1 Y 1 D THR 289 ? D THR 308 
462 1 Y 1 D GLN 290 ? D GLN 309 
463 1 Y 1 D PRO 291 ? D PRO 310 
464 1 Y 1 D ARG 292 ? D ARG 311 
465 1 Y 1 D GLU 293 ? D GLU 312 
466 1 Y 1 D GLU 294 ? D GLU 313 
467 1 Y 1 D GLN 295 ? D GLN 314 
468 1 Y 1 D PHE 296 ? D PHE 315 
469 1 Y 1 D ASN 297 ? D ASN 316 
470 1 Y 1 D SER 298 ? D SER 317 
471 1 Y 1 D THR 299 ? D THR 318 
472 1 Y 1 D PHE 300 ? D PHE 319 
473 1 Y 1 D ARG 301 ? D ARG 320 
474 1 Y 1 D SER 302 ? D SER 321 
475 1 Y 1 D VAL 303 ? D VAL 322 
476 1 Y 1 D SER 304 ? D SER 323 
477 1 Y 1 D GLU 305 ? D GLU 324 
478 1 Y 1 D LEU 306 ? D LEU 325 
479 1 Y 1 D PRO 307 ? D PRO 326 
480 1 Y 1 D ILE 308 ? D ILE 327 
481 1 Y 1 D MET 309 ? D MET 328 
482 1 Y 1 D HIS 310 ? D HIS 329 
483 1 Y 1 D GLN 311 ? D GLN 330 
484 1 Y 1 D ASP 312 ? D ASP 331 
485 1 Y 1 D TRP 313 ? D TRP 332 
486 1 Y 1 D LEU 314 ? D LEU 333 
487 1 Y 1 D ASN 315 ? D ASN 334 
488 1 Y 1 D GLY 316 ? D GLY 335 
489 1 Y 1 D LYS 317 ? D LYS 336 
490 1 Y 1 D GLU 318 ? D GLU 337 
491 1 Y 1 D PHE 319 ? D PHE 338 
492 1 Y 1 D LYS 320 ? D LYS 339 
493 1 Y 1 D CYS 321 ? D CYS 340 
494 1 Y 1 D ARG 322 ? D ARG 341 
495 1 Y 1 D VAL 323 ? D VAL 342 
496 1 Y 1 D ASN 324 ? D ASN 343 
497 1 Y 1 D SER 325 ? D SER 344 
498 1 Y 1 D ALA 326 ? D ALA 345 
499 1 Y 1 D ALA 327 ? D ALA 346 
500 1 Y 1 D PHE 328 ? D PHE 347 
501 1 Y 1 D PRO 329 ? D PRO 348 
502 1 Y 1 D ALA 330 ? D ALA 349 
503 1 Y 1 D PRO 331 ? D PRO 350 
504 1 Y 1 D ILE 332 ? D ILE 351 
505 1 Y 1 D GLU 333 ? D GLU 352 
506 1 Y 1 D LYS 334 ? D LYS 353 
507 1 Y 1 D THR 335 ? D THR 354 
508 1 Y 1 D ILE 336 ? D ILE 355 
509 1 Y 1 D SER 337 ? D SER 356 
510 1 Y 1 D LYS 338 ? D LYS 357 
511 1 Y 1 D THR 339 ? D THR 358 
512 1 Y 1 D LYS 340 ? D LYS 359 
513 1 Y 1 D GLY 341 ? D GLY 360 
514 1 Y 1 D ARG 342 ? D ARG 361 
515 1 Y 1 D PRO 343 ? D PRO 362 
516 1 Y 1 D LYS 344 ? D LYS 363 
517 1 Y 1 D ALA 345 ? D ALA 364 
518 1 Y 1 D PRO 346 ? D PRO 365 
519 1 Y 1 D GLN 347 ? D GLN 366 
520 1 Y 1 D VAL 348 ? D VAL 367 
521 1 Y 1 D TYR 349 ? D TYR 368 
522 1 Y 1 D THR 350 ? D THR 369 
523 1 Y 1 D ILE 351 ? D ILE 370 
524 1 Y 1 D PRO 352 ? D PRO 371 
525 1 Y 1 D PRO 353 ? D PRO 372 
526 1 Y 1 D PRO 354 ? D PRO 373 
527 1 Y 1 D LYS 355 ? D LYS 374 
528 1 Y 1 D GLU 356 ? D GLU 375 
529 1 Y 1 D GLN 357 ? D GLN 376 
530 1 Y 1 D MET 358 ? D MET 377 
531 1 Y 1 D ALA 359 ? D ALA 378 
532 1 Y 1 D LYS 360 ? D LYS 379 
533 1 Y 1 D ASP 361 ? D ASP 380 
534 1 Y 1 D LYS 362 ? D LYS 381 
535 1 Y 1 D VAL 363 ? D VAL 382 
536 1 Y 1 D SER 364 ? D SER 383 
537 1 Y 1 D LEU 365 ? D LEU 384 
538 1 Y 1 D THR 366 ? D THR 385 
539 1 Y 1 D CYS 367 ? D CYS 386 
540 1 Y 1 D MET 368 ? D MET 387 
541 1 Y 1 D ILE 369 ? D ILE 388 
542 1 Y 1 D THR 370 ? D THR 389 
543 1 Y 1 D ASP 371 ? D ASP 390 
544 1 Y 1 D PHE 372 ? D PHE 391 
545 1 Y 1 D PHE 373 ? D PHE 392 
546 1 Y 1 D PRO 374 ? D PRO 393 
547 1 Y 1 D GLU 375 ? D GLU 394 
548 1 Y 1 D ASP 376 ? D ASP 395 
549 1 Y 1 D ILE 377 ? D ILE 396 
550 1 Y 1 D THR 378 ? D THR 397 
551 1 Y 1 D VAL 379 ? D VAL 398 
552 1 Y 1 D GLU 380 ? D GLU 399 
553 1 Y 1 D TRP 381 ? D TRP 400 
554 1 Y 1 D GLN 382 ? D GLN 401 
555 1 Y 1 D TRP 383 ? D TRP 402 
556 1 Y 1 D ASN 384 ? D ASN 403 
557 1 Y 1 D GLY 385 ? D GLY 404 
558 1 Y 1 D GLN 386 ? D GLN 405 
559 1 Y 1 D PRO 387 ? D PRO 406 
560 1 Y 1 D ALA 388 ? D ALA 407 
561 1 Y 1 D GLU 389 ? D GLU 408 
562 1 Y 1 D ASN 390 ? D ASN 409 
563 1 Y 1 D TYR 391 ? D TYR 410 
564 1 Y 1 D LYS 392 ? D LYS 411 
565 1 Y 1 D ASN 393 ? D ASN 412 
566 1 Y 1 D THR 394 ? D THR 413 
567 1 Y 1 D GLN 395 ? D GLN 414 
568 1 Y 1 D PRO 396 ? D PRO 415 
569 1 Y 1 D ILE 397 ? D ILE 416 
570 1 Y 1 D MET 398 ? D MET 417 
571 1 Y 1 D ASP 399 ? D ASP 418 
572 1 Y 1 D THR 400 ? D THR 419 
573 1 Y 1 D ASP 401 ? D ASP 420 
574 1 Y 1 D GLY 402 ? D GLY 421 
575 1 Y 1 D SER 403 ? D SER 422 
576 1 Y 1 D TYR 404 ? D TYR 423 
577 1 Y 1 D PHE 405 ? D PHE 424 
578 1 Y 1 D VAL 406 ? D VAL 425 
579 1 Y 1 D TYR 407 ? D TYR 426 
580 1 Y 1 D SER 408 ? D SER 427 
581 1 Y 1 D LYS 409 ? D LYS 428 
582 1 Y 1 D LEU 410 ? D LEU 429 
583 1 Y 1 D ASN 411 ? D ASN 430 
584 1 Y 1 D VAL 412 ? D VAL 431 
585 1 Y 1 D GLN 413 ? D GLN 432 
586 1 Y 1 D LYS 414 ? D LYS 433 
587 1 Y 1 D SER 415 ? D SER 434 
588 1 Y 1 D ASN 416 ? D ASN 435 
589 1 Y 1 D TRP 417 ? D TRP 436 
590 1 Y 1 D GLU 418 ? D GLU 437 
591 1 Y 1 D ALA 419 ? D ALA 438 
592 1 Y 1 D GLY 420 ? D GLY 439 
593 1 Y 1 D ASN 421 ? D ASN 440 
594 1 Y 1 D THR 422 ? D THR 441 
595 1 Y 1 D PHE 423 ? D PHE 442 
596 1 Y 1 D THR 424 ? D THR 443 
597 1 Y 1 D CYS 425 ? D CYS 444 
598 1 Y 1 D SER 426 ? D SER 445 
599 1 Y 1 D VAL 427 ? D VAL 446 
600 1 Y 1 D LEU 428 ? D LEU 447 
601 1 Y 1 D HIS 429 ? D HIS 448 
602 1 Y 1 D GLU 430 ? D GLU 449 
603 1 Y 1 D GLY 431 ? D GLY 450 
604 1 Y 1 D LEU 432 ? D LEU 451 
605 1 Y 1 D HIS 433 ? D HIS 452 
606 1 Y 1 D ASN 434 ? D ASN 453 
607 1 Y 1 D HIS 435 ? D HIS 454 
608 1 Y 1 D HIS 436 ? D HIS 455 
609 1 Y 1 D THR 437 ? D THR 456 
610 1 Y 1 D GLU 438 ? D GLU 457 
611 1 Y 1 D LYS 439 ? D LYS 458 
612 1 Y 1 D SER 440 ? D SER 459 
613 1 Y 1 D LEU 441 ? D LEU 460 
614 1 Y 1 D SER 442 ? D SER 461 
615 1 Y 1 D HIS 443 ? D HIS 462 
616 1 Y 1 D SER 444 ? D SER 463 
617 1 Y 1 D PRO 445 ? D PRO 464 
618 1 Y 1 D GLY 446 ? D GLY 465 
619 1 Y 1 D LYS 447 ? D LYS 466 
620 1 Y 1 E MET -19 ? E MET 1   
621 1 Y 1 E ASP -18 ? E ASP 2   
622 1 Y 1 E SER -17 ? E SER 3   
623 1 Y 1 E GLN -16 ? E GLN 4   
624 1 Y 1 E ALA -15 ? E ALA 5   
625 1 Y 1 E GLN -14 ? E GLN 6   
626 1 Y 1 E VAL -13 ? E VAL 7   
627 1 Y 1 E LEU -12 ? E LEU 8   
628 1 Y 1 E MET -11 ? E MET 9   
629 1 Y 1 E LEU -10 ? E LEU 10  
630 1 Y 1 E LEU -9  ? E LEU 11  
631 1 Y 1 E LEU -8  ? E LEU 12  
632 1 Y 1 E LEU -7  ? E LEU 13  
633 1 Y 1 E TRP -6  ? E TRP 14  
634 1 Y 1 E VAL -5  ? E VAL 15  
635 1 Y 1 E SER -4  ? E SER 16  
636 1 Y 1 E GLY -3  ? E GLY 17  
637 1 Y 1 E THR -2  ? E THR 18  
638 1 Y 1 E CYS -1  ? E CYS 19  
639 1 Y 1 E GLY 0   ? E GLY 20  
640 1 Y 0 E GLU 111 ? E GLU 131 
641 1 Y 0 E ILE 112 ? E ILE 132 
642 1 Y 0 E LYS 113 ? E LYS 133 
643 1 Y 0 E ARG 114 ? E ARG 134 
644 1 Y 0 E ALA 115 ? E ALA 135 
645 1 Y 0 E ASP 116 ? E ASP 136 
646 1 Y 1 E ASN 218 ? E ASN 238 
647 1 Y 1 E GLU 219 ? E GLU 239 
648 1 Y 1 E CYS 220 ? E CYS 240 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Medical Research Council (MRC, United Kingdom)' 'United Kingdom' MR/R001138/1  1 
'Wellcome Trust'                                 'United Kingdom' 218482/Z/19/Z 2 
'Wellcome Trust'                                 'United Kingdom' 101020/Z/13/Z 3 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
F 6 NAG 1 F NAG 1 A NAG 601 n 
F 6 NAG 2 F NAG 2 A NAG 602 n 
F 6 BMA 3 F BMA 3 A BMA 603 n 
F 6 MAN 4 F MAN 4 A MAN 604 n 
G 6 NAG 1 G NAG 1 A NAG 606 n 
G 6 NAG 2 G NAG 2 A NAG 607 n 
G 6 BMA 3 G BMA 3 A BMA 608 n 
G 6 MAN 4 G MAN 4 A MAN 609 n 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
_pdbx_entity_branch.entity_id   6 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 6 DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                        
'Glycam Condensed Sequence' GMML       1.0   
2 6 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1' WURCS PDB2Glycan 1.1.0 
3 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}'               LINUCS PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 6 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 6 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 6 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
6 NAG 1 n 
6 NAG 2 n 
6 BMA 3 n 
6 MAN 4 n 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_space_group.name_H-M_alt     'P 41 21 2' 
_space_group.name_Hall        'P 4abw 2nw' 
_space_group.IT_number        92 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
