Data molecular dynamic simulations of CTR in "Calcitonin receptor N-glycosylation enhances peptide hormone affinity by controlling receptor dynamics"

433 13 1745 3 8343 document 1745 5ii0-combined.eigenvector1.pdb text/plain a5ad9bcad709794cff5fa66934657886 MD5 3594977 2019-08-06 07:24:33 https://researchdata.aston.ac.uk/id/eprint/433/1/5ii0-combined.eigenvector1.pdb 433 1 1 text/plain text en public cc_by_4

5ii0-combined.eigenvector1.pdb

1746 3 8345 document 1746 RMSF plots.pzfx application/xml 1f10e762a28bd173b57c1eab9825c0dd MD5 13303 2019-08-06 07:25:10 https://researchdata.aston.ac.uk/id/eprint/433/2/RMSF%20plots.pzfx 433 2 2 application/xml other en public cc_by_4

RMSF plots.pzfx

archive 77 disk0/00/00/04/33 2019-08-09 10:54:48 2025-04-16 08:35:36 2019-08-09 10:54:48 data_collection show Simms John Poyner David 0000-0003-1590-112X Data molecular dynamic simulations of CTR in "Calcitonin receptor N-glycosylation enhances peptide hormone affinity by controlling receptor dynamics" D204 public Molecular dynamics G protein coupled receptors Glycosylation Dynamic allostery 2019-08-06 Aston University 10.17036/researchdata.aston.ac.uk.00000433 BBSRC Addressing the architecture, dynamics and activation mechanism of the CGRP receptor Collection These datasets show 100 snapshots for the trajectory of the non-glycosylated CTR (PDB 5II0) as a pdb file. The first eigenvectors for each snap shot have been used to calculate the RMSD of this structure and glycosylated CTR and the numerical values are tabulated and shown graphically in a pzsf file (openable with Graphpad Prism 6 or higher versions). Poyner David BBSRC BB/M007529/1 Aston University 2017-10-01 2017-11-16