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| ==Solution Structure of Northeast Structural Genomics Target Protein BcR68 encoded in gene Q816V6 of B. cereus== | | ==Solution Structure of Northeast Structural Genomics Target Protein BcR68 encoded in gene Q816V6 of B. cereus== |
- | <StructureSection load='1xn6' size='340' side='right' caption='[[1xn6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1xn6' size='340' side='right'caption='[[1xn6]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1xn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XN6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xn6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XN6 FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xn6 OCA], [http://pdbe.org/1xn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xn6 RCSB], [http://www.ebi.ac.uk/pdbsum/1xn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xn6 ProSAT], [http://www.topsan.org/Proteins/NESGC/1xn6 TOPSAN]</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=1xn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xn6 OCA], [https://pdbe.org/1xn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xn6 RCSB], [https://www.ebi.ac.uk/pdbsum/1xn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xn6 ProSAT], [https://www.topsan.org/Proteins/NESGC/1xn6 TOPSAN]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q816V6_BACCR Q816V6_BACCR] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Atcc 14579]] | + | [[Category: Bacillus cereus]] |
- | [[Category: Acton, T]] | + | [[Category: Large Structures]] |
- | [[Category: Liu, G]] | + | [[Category: Acton T]] |
- | [[Category: Ma, L]] | + | [[Category: Liu G]] |
- | [[Category: Montelione, G T]] | + | [[Category: Ma L]] |
- | [[Category: Structural genomic]]
| + | [[Category: Montelione GT]] |
- | [[Category: Parish, D]] | + | [[Category: Parish D]] |
- | [[Category: Szyperski, T]] | + | [[Category: Szyperski T]] |
- | [[Category: Xiao, R]] | + | [[Category: Xiao R]] |
- | [[Category: Xu, D]] | + | [[Category: Xu D]] |
- | [[Category: Alpha + beta]]
| + | |
- | [[Category: Gft nmr]]
| + | |
- | [[Category: Nesg]]
| + | |
- | [[Category: Nesg target protein bcr68]]
| + | |
- | [[Category: PSI, Protein structure initiative]]
| + | |
- | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
Q816V6_BACCR
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 PubMed
A standardized protocol enabling rapid NMR data collection for high-quality protein structure determination is presented that allows one to capitalize on high spectrometer sensitivity: a set of five G-matrix Fourier transform NMR experiments for resonance assignment based on highly resolved 4D and 5D spectral information is acquired in conjunction with a single simultaneous 3D 15N,13C(aliphatic),13C(aromatic)-resolved [1H,1H]-NOESY spectrum providing 1H-1H upper distance limit constraints. The protocol was integrated with methodology for semiautomated data analysis and used to solve eight NMR protein structures of the Northeast Structural Genomics Consortium pipeline. The molecular masses of the hypothetical target proteins ranged from 9 to 20 kDa with an average of approximately 14 kDa. Between 1 and 9 days of instrument time were invested per structure, which is less than approximately 10-25% of the measurement time routinely required to date with conventional approaches. The protocol presented here effectively removes data collection as a bottleneck for high-throughput solution structure determination of proteins up to at least approximately 20 kDa, while concurrently providing spectra that are highly amenable to fast and robust analysis.
NMR data collection and analysis protocol for high-throughput protein structure determination.,Liu G, Shen Y, Atreya HS, Parish D, Shao Y, Sukumaran DK, Xiao R, Yee A, Lemak A, Bhattacharya A, Acton TA, Arrowsmith CH, Montelione GT, Szyperski T Proc Natl Acad Sci U S A. 2005 Jul 26;102(30):10487-92. Epub 2005 Jul 18. PMID:16027363[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu G, Shen Y, Atreya HS, Parish D, Shao Y, Sukumaran DK, Xiao R, Yee A, Lemak A, Bhattacharya A, Acton TA, Arrowsmith CH, Montelione GT, Szyperski T. NMR data collection and analysis protocol for high-throughput protein structure determination. Proc Natl Acad Sci U S A. 2005 Jul 26;102(30):10487-92. Epub 2005 Jul 18. PMID:16027363
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