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| | ==Sidechain chi1 distribution in B3 domain of protein G from extensive sets of residual dipolar couplings== | | ==Sidechain chi1 distribution in B3 domain of protein G from extensive sets of residual dipolar couplings== |
| - | <StructureSection load='2n7j' size='340' side='right'caption='[[2n7j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2n7j' size='340' side='right'caption='[[2n7j]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strsg Strsg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N7J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N7J FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2oed|2oed]]</div></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=2n7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n7j OCA], [https://pdbe.org/2n7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n7j RCSB], [https://www.ebi.ac.uk/pdbsum/2n7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n7j ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spg ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1320 STRSG])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n7j OCA], [https://pdbe.org/2n7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n7j RCSB], [https://www.ebi.ac.uk/pdbsum/2n7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n7j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG]] Binds to the constant Fc region of IgG with high affinity.
| + | [https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strsg]] | + | [[Category: Streptococcus sp. 'group G']] |
| - | [[Category: Bax, A]] | + | [[Category: Bax A]] |
| - | [[Category: Grishaev, A]] | + | [[Category: Grishaev A]] |
| - | [[Category: Li, F]] | + | [[Category: Li F]] |
| - | [[Category: Ying, J]] | + | [[Category: Ying J]] |
| - | [[Category: Signaling protein]]
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| Structural highlights
Function
SPG1_STRSG Binds to the constant Fc region of IgG with high affinity.
Publication Abstract from PubMed
Accurate quantitative measurement of structural dispersion in proteins remains a prime challenge to both X-ray crystallography and NMR spectroscopy. Here we use a model-free approach based on measurement of many residual dipolar couplings (RDCs) in differentially orienting aqueous liquid crystalline solutions to obtain the side chain chi1 distribution sampled by each residue in solution. Applied to the small well-ordered model protein GB3, our approach reveals that the RDC data are compatible with a single narrow distribution of side chain chi1 angles for only about 40% of the residues. For more than half of the residues, populations greater than 10% for a second rotamer are observed, and four residues require sampling of three rotameric states to fit the RDC data. In virtually all cases, sampled chi1 values are found to center closely around ideal g(-), g(+) and t rotameric angles, even though no rotamer restraint is used when deriving the sampled angles. The root-mean-square difference between experimental (3)JHalphaHbeta couplings and those predicted by the Haasnoot-parametrized, motion-adjusted Karplus equation reduces from 2.05 to 0.75 Hz when using the new rotamer analysis instead of the 1.1-A X-ray structure as input for the dihedral angles. A comparison between observed and predicted (3)JHalphaHbeta values suggests that the root-mean-square amplitude of chi1 angle fluctuations within a given rotamer well is ca. 20 degrees . The quantitatively defined side chain rotamer equilibria obtained from our study set new benchmarks for evaluating improved molecular dynamics force fields, and also will enable further development of quantitative relations between side chain chemical shift and structure.
Side Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar Couplings.,Li F, Grishaev A, Ying J, Bax A J Am Chem Soc. 2015 Nov 25;137(46):14798-811. doi: 10.1021/jacs.5b10072. Epub, 2015 Nov 17. PMID:26523828[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li F, Grishaev A, Ying J, Bax A. Side Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar Couplings. J Am Chem Soc. 2015 Nov 25;137(46):14798-811. doi: 10.1021/jacs.5b10072. Epub, 2015 Nov 17. PMID:26523828 doi:http://dx.doi.org/10.1021/jacs.5b10072
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