2jtv
From Proteopedia
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<StructureSection load='2jtv' size='340' side='right' caption='[[2jtv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2jtv' size='340' side='right' caption='[[2jtv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[2jtv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTV OCA]. <br> | + | <table><tr><td colspan='2'>[[2jtv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTV OCA]. <br> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jtv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jtv RCSB], [http://www.ebi.ac.uk/pdbsum/2jtv PDBsum], [http://www.topsan.org/Proteins/NESGC/2jtv TOPSAN]</span>< | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jtv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jtv RCSB], [http://www.ebi.ac.uk/pdbsum/2jtv PDBsum], [http://www.topsan.org/Proteins/NESGC/2jtv TOPSAN]</span></td></tr> |
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:50, 1 May 2014
Solution Structure of protein RPA3401, Northeast Structural Genomics Consortium Target RpT7, Ontario Center for Structural Proteomics Target RP3384
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Categories: Rhodopseudomonas palustris | Arrowsmith, C. | Gutmanas, A. | Ignatchenko, A. | Karra, M. | Lemak, A. | NESG, Northeast Structural Genomics Consortium. | Srisailam, S. | Yee, A. | Nesg | Northeast structural genomics consortium | Protein structure initiative | Protein with unknown function rpa3401 | Psi-2 | Structural genomic
