2q4e: Difference between revisions
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==Ensemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At4g09670== | ==Ensemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At4g09670== | ||
<StructureSection load='2q4e' size='340' side='right' caption='[[2q4e]], [[Resolution|resolution]] 2.49Å' scene=''> | <StructureSection load='2q4e' size='340' side='right' caption='[[2q4e]], [[Resolution|resolution]] 2.49Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ydw|1ydw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ydw|1ydw]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At4g09670, F17A8.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At4g09670, F17A8.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q4e OCA], [http://pdbe.org/2q4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q4e RCSB], [http://www.ebi.ac.uk/pdbsum/2q4e PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q4e OCA], [http://pdbe.org/2q4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q4e RCSB], [http://www.ebi.ac.uk/pdbsum/2q4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q4e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
{{Large structure}} | {{Large structure}} | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q4/2q4e_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q4/2q4e_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 11:21, 29 August 2018
Ensemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At4g09670Ensemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At4g09670
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedX-ray crystallography typically uses a single set of coordinates and B factors to describe macromolecular conformations. Refinement of multiple copies of the entire structure has been previously used in specific cases as an alternative means of representing structural flexibility. Here, we systematically validate this method by using simulated diffraction data, and we find that ensemble refinement produces better representations of the distributions of atomic positions in the simulated structures than single-conformer refinements. Comparison of principal components calculated from the refined ensembles and simulations shows that concerted motions are captured locally, but that correlations dissipate over long distances. Ensemble refinement is also used on 50 experimental structures of varying resolution and leads to decreases in R(free) values, implying that improvements in the representation of flexibility observed for the simulated structures may apply to real structures. These gains are essentially independent of resolution or data-to-parameter ratio, suggesting that even structures at moderate resolution can benefit from ensemble refinement. Ensemble refinement of protein crystal structures: validation and application.,Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr Structure. 2007 Sep;15(9):1040-52. PMID:17850744[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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