2n47: Difference between revisions

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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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2n47' size='340' side='right'caption='[[2n47]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2n47]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N47 FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kw5|2kw5]], [[2n42|2n42]], [[2n44|2n44]], [[2n45|2n45]], [[2n46|2n46]], [[2n48|2n48]], [[2n49|2n49]], [[2n4a|2n4a]], [[2n4b|2n4b]], [[2n4c|2n4c]], [[2n4d|2n4d]], [[2n4f|2n4f]]</td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2n47 RCSB], [http://www.ebi.ac.uk/pdbsum/2n47 PDBsum]</span></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 ==
-We have developed an approach for determining NMR structures of proteins over 20 kDa that utilizes sparse distance restraints obtained using transverse relaxation optimized spectroscopy experiments on perdeuterated samples to guide RASREC Rosetta NMR structure calculations. The method was tested on 11 proteins ranging from 15 to 40 kDa, seven of which were previously unsolved. The RASREC Rosetta models were in good agreement with models obtained using traditional NMR methods with larger restraint sets. In five cases X-ray structures were determined or were available, allowing comparison of the accuracy of the Rosetta models and conventional NMR models. In all five cases, the Rosetta models were more similar to the X-ray structures over both the backbone and side-chain conformations than the "best effort" structures determined by conventional methods. The incorporation of sparse distance restraints into RASREC Rosetta allows routine determination of high-quality solution NMR structures for proteins up to 40 kDa, and should be broadly useful in structural biology.
+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.
-Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples.,Lange OF, Rossi P, Sgourakis NG, Song Y, Lee HW, Aramini JM, Ertekin A, Xiao R, Acton TB, Montelione GT, Baker D Proc Natl Acad Sci U S A. 2012 Jul 3;109(27):10873-8. Epub 2012 Jun 25. PMID:22733734<ref>PMID:22733734</ref>
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2n47" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Hopf, T A]]
+[[Category: Large Structures]]
-[[Category: Huang, Y J]]
+[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
-[[Category: Marks, D]]
+[[Category: Hopf TA]]
-[[Category: Montelione, G T]]
+[[Category: Huang YJ]]
-[[Category: Structural genomic]]
+[[Category: Marks D]]
-[[Category: Sander, C]]
+[[Category: Montelione GT]]
-[[Category: Tang, Y]]
+[[Category: Sander C]]
-[[Category: Ec-nmr]]
+[[Category: Tang Y]]
-[[Category: Nesg]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: Psi-biology]]
-[[Category: Unknown function]]

2n47: Difference between revisions

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