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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 first SH3 domain of adaptor Nck.

BMRB ID: 15351

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Graph for Solution structure of first SH3 domain of adaptor Nck

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_0021_233_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0021_233_0001.pdb 0.3777
S_0030_76_0001.pdb 0.5784
S_0015_148_0001.pdb 0.3488
S_0008_255_0001.pdb 0.3980
S_0004_224_0001.pdb 0.2770
S_0015_74_0001.pdb 0.5705
S_0031_88_0001.pdb 0.4014
S_0023_308_0001.pdb 0.3883
S_0021_167_0001.pdb 0.2938
S_0018_55_0001.pdb 0.2922
Averaged Ca-rmsd 0.393 +/- 0.106

RMSD against lowest energy structure for residues 1-53

Structure Score
S_0021_233_0001.pdb 0.3747
S_0030_76_0001.pdb 0.5653
S_0015_148_0001.pdb 0.3441
S_0008_255_0001.pdb 0.3894
S_0004_224_0001.pdb 0.2740
S_0015_74_0001.pdb 0.5739
S_0031_88_0001.pdb 0.4000
S_0023_308_0001.pdb 0.3911
S_0021_167_0001.pdb 0.2867
S_0018_55_0001.pdb 0.2944
Averaged Ca-rmsd 0.389 +/- 0.106

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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