Published September 9, 2021 | Version v1

Dataset of "Unveiling the gating mechanism of CRAC channel: a computational study"

  • 1. Dipartimento di Ingegneria meccanica e Aerospaziale, Sapienza Università di Roma, 00184, Rome, Italy
  • 2. Dipartimento di Ingegneria Meccanica e Aerospaziale, Sapienza Università di Roma, 00184, Rome, Italy

Description

Molecular Dynamics simulation trajectories of CRAC ion channel. All of the trajectories can be visualized using the topology file CRAC_topol.prmtop. Three trajectories refer to equilibrium simulations of the closed state of the channel PDB: 4HKR (4HKR_equil_100ns.dcd) and of the two putative open states PDB: 6BBF (6BBF_equil_100ns.dcd) and PDB ID: 6AKI (6AKI_equil_100ns.dcd). The remaining two trajectories refer to Targeted Molecular Dynamics simulations steering the molecular system from the closed to the open state (TMD_C_to_O_100ns.dcd) and from the open to the closed state (TMD_O_to_C_500ns.dcd).

All simulations have been performed with the NAMD 2.11b2 suite of programs using the Amber ff15ipq force field for the protein, the Lipid17 force field for the phospholipids and the SPC/E water model. 

 

 

Files

Files (8.5 GB)

Name Size
md5:cd2fd60cd42a61d7a68e6a132d8fb293
1.7 GB Download
md5:c8856eed091610ed05d310a73a5edb76
1.7 GB Download
md5:85b01ce6b5c33382389948631cc9d176
1.7 GB Download
md5:402592737092ffb6b17add439e00ae5e
66.3 MB Download
md5:dc19eb344db1234a648214675300d2da
1.7 GB Download
md5:491b3d4d3bf5209d4a11982fe6ae14e1
1.7 GB Download

Additional details

Related works

Is cited by
Journal article: 10.3389/fmolb.2021.773388 (DOI)

Funding

European Commission
HyGate - Hydrophobic Gating in nanochannels: understanding single channel mechanisms for designing better nanoscale sensors 803213

References

  • Unveiling the gating mechanism of CRAC channel: a computational study (2021), Frontiers in Molecular Biosciences