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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 1H, 13C, and 15N NMR resonance assignments of Sec95Cys MsrB1 protein.

BMRB ID: 15193

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Graph for 1H, 13C, and 15N NMR resonance assignments of Sec95Cys MsrB1 protein

It appears this run did not converge (based on the residues marked non-flexible). While the best predicted structure is displayed, the lack of convergence means that this structure is unlikely to resemble the actual structure. Furthermore, it is not necessarily representative of the ensemble of structures formed.

Lowest energy structure: S_0019_108_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0019_108_0001.pdb 5.0414
S_0012_364_0001.pdb 5.2798
S_0013_206_0001.pdb 8.2735
S_0003_188_0001.pdb 6.2127
S_0017_345_0001.pdb 9.4314
S_0014_61_0001.pdb 7.4723
S_0023_255_0001.pdb 7.2775
S_0001_70_0001.pdb 11.4825
S_0001_53_0001.pdb 7.7034
S_0004_15_0001.pdb 6.2340
Averaged Ca-rmsd 7.441 +/- 1.957

RMSD against lowest energy structure for residues 42-42, 44-88

Structure Score
S_0019_108_0001.pdb 2.0600
S_0012_364_0001.pdb 2.1476
S_0013_206_0001.pdb 2.4164
S_0003_188_0001.pdb 2.0481
S_0017_345_0001.pdb 3.0898
S_0014_61_0001.pdb 1.9562
S_0023_255_0001.pdb 4.4198
S_0001_70_0001.pdb 2.7871
S_0001_53_0001.pdb 3.3515
S_0004_15_0001.pdb 2.3234
Averaged Ca-rmsd 2.660 +/- 0.778

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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