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==Solution structure of protein af2351 from Archaeoglobus fulgidus. Northeast Structural Genomics Consortium target AtT9/Ontario Center for Structural Proteomics Target af2351==
==Solution structure of protein af2351 from Archaeoglobus fulgidus. Northeast Structural Genomics Consortium target AtT9/Ontario Center for Structural Proteomics Target af2351==
<StructureSection load='2kku' size='340' side='right'caption='[[2kku]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2kku' size='340' side='right'caption='[[2kku]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kku]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KKU FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kku]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KKU FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF_2351 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</td></tr>
</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=2kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kku OCA], [https://pdbe.org/2kku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kku RCSB], [https://www.ebi.ac.uk/pdbsum/2kku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kku ProSAT], [https://www.topsan.org/Proteins/NESGC/2kku TOPSAN]</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=2kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kku OCA], [https://pdbe.org/2kku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kku RCSB], [https://www.ebi.ac.uk/pdbsum/2kku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kku ProSAT], [https://www.topsan.org/Proteins/NESGC/2kku TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O30319_ARCFU O30319_ARCFU]
== 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=2kku 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=2kku 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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kku" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arcfl]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Fares, C]]
[[Category: Fares C]]
[[Category: Lemak, A]]
[[Category: Lemak A]]
[[Category: Montelione, G T]]
[[Category: Montelione GT]]
[[Category: Structural genomic]]
[[Category: Rumpel S]]
[[Category: OCSP, Ontario Centre for Structural Proteomics]]
[[Category: Semest A]]
[[Category: Rumpel, S]]
[[Category: Wu B]]
[[Category: Semest, A]]
[[Category: Yee A]]
[[Category: Wu, B]]
[[Category: Yee, A]]
[[Category: Alpha/beta protein]]
[[Category: Nesg]]
[[Category: Ocsp]]
[[Category: Ontario centre for structural proteomic]]
[[Category: PSI, Protein structure initiative]]
[[Category: Unknown function]]
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