Characterizing Protein Dynamics with Integrative Use of Bulk and Single-Molecule Techniques

Lys63-linked diubiquitin dynamically interconverts among three conformational states. The ensemble structures of this multi-domain protein can be determined through conjoined refinement against single-molecule fluorescence resonance energy transfer (smFRET), cross-linking coupled with mass spectrometry (CXMS) and small-angle X-ray scattering (SAXS) restraints. The smFRET and CXMS restraints for ensemble structures modeling are uploaded here and the SAXS restrains are deposited to SASBDB with SASDCG7 accession code. The atomic coordinates for the conformation closest-to-mean in each state is deposited to PDB-Dev.