View source for 6qf8


==Solution NMR ensemble for human ubiquitin at 298K compiled using the CoMAND method==
<StructureSection load='6qf8' size='340' side='right'caption='[[6qf8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QF8 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6qf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qf8 OCA], [http://pdbe.org/6qf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qf8 RCSB], [http://www.ebi.ac.uk/pdbsum/6qf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qf8 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The ability of proteins to adopt multiple conformational states is essential to their function, and elucidating the details of such diversity under physiological conditions has been a major challenge. Here we present a generalized method for mapping protein population landscapes by NMR spectroscopy. Experimental NOESY spectra are directly compared with a set of expectation spectra back-calculated across an arbitrary conformational space. Signal decomposition of the experimental spectrum then directly yields the relative populations of local conformational microstates. In this way, averaged descriptions of conformation can be eliminated. As the method quantitatively compares experimental and expectation spectra, it inherently delivers an R factor expressing how well structural models explain the input data. We demonstrate that our method extracts sufficient information from a single 3D NOESY experiment to perform initial model building, refinement, and validation, thus offering a complete de novo structure determination protocol.

Mapping Local Conformational Landscapes of Proteins in Solution.,ElGamacy M, Riss M, Zhu H, Truffault V, Coles M Structure. 2019 Mar 26. pii: S0969-2126(19)30083-8. doi:, 10.1016/j.str.2019.03.005. PMID:30930065<ref>PMID:30930065</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6qf8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Coles, M]]
[[Category: ElGamacy, M]]
[[Category: Truffault, V]]
[[Category: Zhu, H]]
[[Category: Comand method]]
[[Category: R-factor refinement]]
[[Category: Signaling protein]]