2lnu: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[2lnu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloarcula_marismortui_ATCC_43049 Haloarcula marismortui ATCC 43049]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LNU 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=2lnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lnu OCA], [https://pdbe.org/2lnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lnu RCSB], [https://www.ebi.ac.uk/pdbsum/2lnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lnu 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=2lnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lnu OCA], [https://pdbe.org/2lnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lnu RCSB], [https://www.ebi.ac.uk/pdbsum/2lnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lnu ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/Q5V502_HALMA Q5V502_HALMA]
-<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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2lnu" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>