2n4d: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 2n4d is ON HOLD
+==EC-NMR Structure of Agrobacterium tumefaciens Atu1203 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target AtT10==
+<StructureSection load='2n4d' size='340' side='right'caption='[[2n4d]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2n4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_fabrum_str._C58 Agrobacterium fabrum str. C58]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N4D 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=2n4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n4d OCA], [https://pdbe.org/2n4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n4d RCSB], [https://www.ebi.ac.uk/pdbsum/2n4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n4d ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A9CJD6_AGRFC A9CJD6_AGRFC]
+<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.
-Authors: Montelione, G.
+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>
-Description: EC-NMR Structure of Agrobacterium tumefaciens Atu1203 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target AtT10
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Montelione, G]]
+<div class="pdbe-citations 2n4d" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Agrobacterium fabrum str. C58]]
+[[Category: Large Structures]]
+[[Category: Hopf TA]]
+[[Category: Huang YJ]]
+[[Category: Marks D]]
+[[Category: Montelione GT]]
+[[Category: Sander C]]
+[[Category: Tang Y]]