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Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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Results for submission Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin.

BMRB ID: 15129

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Graph for Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin

This run appears to have converged (based on the residues marked non-flexible). That means that the results may be a meaningful prediction of the real structure. Please validate the structure against your experimental data.

Lowest energy structure: S_0030_152_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0030_152_0001.pdb 0.4180
S_0016_300_0001.pdb 0.4823
S_0030_238_0001.pdb 0.7523
S_0018_185_0001.pdb 1.0511
S_0004_86_0001.pdb 0.5862
S_0014_73_0001.pdb 0.4277
S_0007_283_0001.pdb 0.4567
S_0007_200_0001.pdb 0.8097
S_0030_311_0001.pdb 0.4889
S_0030_137_0001.pdb 0.5341
Averaged Ca-rmsd 0.601 +/- 0.207

RMSD against lowest energy structure for residues 1-58

Structure Score
S_0030_152_0001.pdb 0.4154
S_0016_300_0001.pdb 0.4154
S_0030_238_0001.pdb 0.6998
S_0018_185_0001.pdb 1.0189
S_0004_86_0001.pdb 0.5282
S_0014_73_0001.pdb 0.4211
S_0007_283_0001.pdb 0.4540
S_0007_200_0001.pdb 0.8038
S_0030_311_0001.pdb 0.4830
S_0030_137_0001.pdb 0.5286
Averaged Ca-rmsd 0.577 +/- 0.202

This entry was calculated with Rosetta version 3.5 and version 3.2 of the CS-Rosetta Toolbox.

The flexible tails of this protein were automatically trimmed by the server. This means that the results you see might not have the same residue sequence as the data you submitted.

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Citation information:

"Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples" Oliver F. Lange; Paolo Rossi; Nikolaos G. Sgourakis; Yifan Song; Hsiau-Wei Lee; James M. Aramini; Asli Ertekin; Rong Xiao; Thomas B. Acton; Gaetano T. Montelione; David Baker; Proceedings of the National Academy of Sciences 109(27) 10873-10878 (2012) doi: 10.1073/pnas.1203013109

"De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds," Yang Shen; Philip N. Bryan; Yanan He; John Orban; David Baker; Ad Bax; Protein Science 19, 349-356 (2010) doi: 10.1002/pro.303

"De novo protein structure generation from incomplete chemical shift assignments," Yang Shen; Robert Vernon; David Baker; Ad Bax; J. Biomol. NMR 43, 63-78 (2009) doi: 10.1007/s10858-008-9288-5

"Consistent blind protein structure generation from NMR chemical shift data," Yang Shen; Oliver Lange; Frank Delaglio; Paolo Rossi; James M. Aramini; Gaohua Liu; Alexander Eletsky; Yibing Wu; Kiran K. Singarapu; Alexander Lemak; Alexandr Ignatchenko; Cheryl H. Arrowsmith; Thomas Szyperski; Gaetano T. Montelione; David Baker; Ad Bax; Proceedings of the National Academy of Sciences 105(12) 4685-4690 (2008) doi: 10.1073/pnas.0800256105

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