View source for 2n49


==EC-NMR Structure of Erwinia carotovora ECA1580 N-terminal Domain Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target EwR156A==
<StructureSection load='2n49' size='340' side='right'caption='[[2n49]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2n49]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_atrosepticum_SCRI1043 Pectobacterium atrosepticum SCRI1043]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N49 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=2n49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n49 OCA], [https://pdbe.org/2n49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n49 RCSB], [https://www.ebi.ac.uk/pdbsum/2n49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n49 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6D6V0_PECAS Q6D6V0_PECAS] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2n49" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pectobacterium atrosepticum SCRI1043]]
[[Category: Hopf TA]]
[[Category: Huang YJ]]
[[Category: Marks D]]
[[Category: Montelione GT]]
[[Category: Sander C]]
[[Category: Tang Y]]