2n47: Difference between revisions
New page: '''Unreleased structure''' The entry 2n47 is ON HOLD Authors: Tang, Y., Huang, Y.J., Hopf, T.A., Sander, C., Marks, D., Montelione, G.T. Description: EC-NMR Structure of Synechocystis ... |
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==EC-NMR Structure of Synechocystis sp. PCC 6803 Slr1183 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target SgR145== | |||
<StructureSection load='2n47' size='340' side='right'caption='[[2n47]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2n47]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N47 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n47 OCA], [https://pdbe.org/2n47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n47 RCSB], [https://www.ebi.ac.uk/pdbsum/2n47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n47 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P74712_SYNY3 P74712_SYNY3] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Accurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistical methods provide a rich complementary source of structural constraints. We have developed a hybrid approach (evolutionary coupling-NMR spectroscopy; EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings and demonstrate accurate structure determination for several proteins 6-41 kDa in size. | |||
Protein structure determination by combining sparse NMR data with evolutionary couplings.,Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT Nat Methods. 2015 Jun 29. doi: 10.1038/nmeth.3455. PMID:26121406<ref>PMID:26121406</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 2n47" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Huang | <references/> | ||
[[Category: Montelione | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] | |||
[[Category: Hopf TA]] | |||
[[Category: Huang YJ]] | |||
[[Category: Marks D]] | |||
[[Category: Montelione GT]] | |||
[[Category: Sander C]] | |||
[[Category: Tang Y]] |