2n4a: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2n4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_metallidurans_CH34 Cupriavidus metallidurans CH34]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N4A FirstGlance]. <br> | <table><tr><td colspan='2'>[[2n4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_metallidurans_CH34 Cupriavidus metallidurans CH34]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N4A FirstGlance]. <br> | ||
</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=2n4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n4a OCA], [https://pdbe.org/2n4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n4a RCSB], [https://www.ebi.ac.uk/pdbsum/2n4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n4a ProSAT]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=2n4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n4a OCA], [https://pdbe.org/2n4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n4a RCSB], [https://www.ebi.ac.uk/pdbsum/2n4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n4a ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
Latest revision as of 09:14, 15 May 2024
EC-NMR Structure of Ralstonia metallidurans Rmet_5065 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target CrR115EC-NMR Structure of Ralstonia metallidurans Rmet_5065 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target CrR115
Structural highlights
FunctionPublication Abstract from PubMedAccurate 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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