2n45: 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 2n45 is ON HOLD
+==EC-NMR Structure of Escherichia coli Maltose-binding protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data with a second set of RDC data simulated for an alternative alignment tensor. Northeast Structural Genomics Consortium target ER690==
+<StructureSection load='2n45' size='340' side='right'caption='[[2n45]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2n45]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N45 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=2n45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n45 OCA], [https://pdbe.org/2n45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n45 RCSB], [https://www.ebi.ac.uk/pdbsum/2n45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n45 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
+<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: Tang, Y., Huang, Y.J., Hopf, T.A., Sander, C., Marks, D., Montelione, G.T.
+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 Escherichia coli Maltose-binding protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER690
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Sander, C]]
+<div class="pdbe-citations 2n45" style="background-color:#fffaf0;"></div>
-[[Category: Tang, Y]]
+== References ==
-[[Category: Huang, Y.J]]
+<references/>
-[[Category: Montelione, G.T]]
+__TOC__
-[[Category: Hopf, T.A]]
+</StructureSection>
-[[Category: Marks, D]]
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Hopf TA]]
+[[Category: Huang YJ]]
+[[Category: Marks D]]
+[[Category: Montelione GT]]
+[[Category: Sander C]]
+[[Category: Tang Y]]