2q4p

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|PDB= 2q4p |SIZE=350|CAPTION= <scene name='initialview01'>2q4p</scene>, resolution 2.320&Aring;
|PDB= 2q4p |SIZE=350|CAPTION= <scene name='initialview01'>2q4p</scene>, resolution 2.320&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= 2410015N17Rik, Tdrg-TL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
|GENE= 2410015N17Rik, Tdrg-TL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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|DOMAIN=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q4p OCA], [http://www.ebi.ac.uk/pdbsum/2q4p PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2q4p RCSB]</span>
}}
}}
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[[Category: unknown function]]
[[Category: unknown function]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:21:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:41:57 2008''

Revision as of 04:41, 26 March 2008

Image:2q4p.jpg


PDB ID 2q4p

Drag the structure with the mouse to rotate
, resolution 2.320Å
Ligands:
Gene: 2410015N17Rik, Tdrg-TL1 (Mus musculus)
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



Ensemble refinement of the crystal structure of protein from Mus musculus Mm.29898


Overview

X-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.

About this Structure

2Q4P is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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

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