2k7i: Difference between revisions
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[[2k7i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrt5 Agrt5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7I OCA]. <br> | [[2k7i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrt5 Agrt5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7I 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><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><br> | ||
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k7i RCSB], [http://www.ebi.ac.uk/pdbsum/2k7i PDBsum], [http://www.topsan.org/Proteins/NESGC/2k7i TOPSAN]</span><br> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|right]] | [[Image:Consurf_key_small.gif|right]] | ||
Revision as of 13:28, 30 April 2014
Solution NMR structure of protein ATU0232 from AGROBACTERIUM TUMEFACIENS. Northeast Structural Genomics Consortium (NESG) target AtT3. Ontario Center for Structural Proteomics target ATC0223.Solution NMR structure of protein ATU0232 from AGROBACTERIUM TUMEFACIENS. Northeast Structural Genomics Consortium (NESG) target AtT3. Ontario Center for Structural Proteomics target ATC0223.
Structural highlights2k7i is a 2 chain structure with sequence from Agrt5. Full experimental information is available from OCA. Activity: Glucokinase, with EC number 2.7.1.2 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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