2kp6
From Proteopedia
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==Solution NMR structure of protein CV0237 from Chromobacterium violaceum. Northeast Structural Genomics Consortium (NESG) target CvT1== | ==Solution NMR structure of protein CV0237 from Chromobacterium violaceum. Northeast Structural Genomics Consortium (NESG) target CvT1== | ||
| - | <StructureSection load='2kp6' size='340' side='right'caption='[[2kp6 | + | <StructureSection load='2kp6' size='340' side='right'caption='[[2kp6]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2kp6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2kp6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KP6 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </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=2kp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kp6 OCA], [https://pdbe.org/2kp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kp6 RCSB], [https://www.ebi.ac.uk/pdbsum/2kp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kp6 ProSAT]</span></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=2kp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kp6 OCA], [https://pdbe.org/2kp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kp6 RCSB], [https://www.ebi.ac.uk/pdbsum/2kp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kp6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q7P1H6_CHRVO Q7P1H6_CHRVO] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2kp6 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2kp6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The quality of protein structures determined by nuclear magnetic resonance (NMR) spectroscopy is contingent on the number and quality of experimentally-derived resonance assignments, distance and angular restraints. Two key features of protein NMR data have posed challenges for the routine and automated structure determination of small to medium sized proteins; (1) spectral resolution - especially of crowded nuclear Overhauser effect spectroscopy (NOESY) spectra, and (2) the reliance on a continuous network of weak scalar couplings as part of most common assignment protocols. In order to facilitate NMR structure determination, we developed a semi-automated strategy that utilizes non-uniform sampling (NUS) and multidimensional decomposition (MDD) for optimal data collection and processing of selected, high resolution multidimensional NMR experiments, combined it with an ABACUS protocol for sequential and side chain resonance assignments, and streamlined this procedure to execute structure and refinement calculations in CYANA and CNS, respectively. Two graphical user interfaces (GUIs) were developed to facilitate efficient analysis and compilation of the data and to guide automated structure determination. This integrated method was implemented and refined on over 30 high quality structures of proteins ranging from 5.5 to 16.5 kDa in size. | ||
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| - | A novel strategy for NMR resonance assignment and protein structure determination.,Lemak A, Gutmanas A, Chitayat S, Karra M, Fares C, Sunnerhagen M, Arrowsmith CH J Biomol NMR. 2011 Jan;49(1):27-38. Epub 2010 Dec 14. PMID:21161328<ref>PMID:21161328</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2kp6" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Chromobacterium violaceum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Arrowsmith | + | [[Category: Arrowsmith CT]] |
| - | [[Category: Fares | + | [[Category: Fares C]] |
| - | [[Category: Garcia | + | [[Category: Garcia M]] |
| - | [[Category: Lemak | + | [[Category: Lemak A]] |
| - | [[Category: Montelione | + | [[Category: Montelione GT]] |
| - | + | [[Category: Yee A]] | |
| - | [[Category: Yee | + | |
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Current revision
Solution NMR structure of protein CV0237 from Chromobacterium violaceum. Northeast Structural Genomics Consortium (NESG) target CvT1
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