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 NMR Structure of Bordetella bronchiseptica protein BB2007: Northeast Structural Genomics Consortium Target BoR54.

BMRB ID: 15353

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Graph for Solution NMR Structure of Bordetella bronchiseptica protein BB2007: Northeast Structural Genomics Consortium Target BoR54

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_0032_25_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0032_25_0001.pdb 1.7599
S_0025_191_0001.pdb 3.4696
S_0015_278_0001.pdb 2.9521
S_0018_310_0001.pdb 2.4549
S_0013_66_0001.pdb 3.1559
S_0025_254_0001.pdb 2.2519
S_0018_294_0001.pdb 3.0271
S_0028_104_0001.pdb 2.1985
S_0001_236_0001.pdb 2.2182
S_0013_207_0001.pdb 2.0424
Averaged Ca-rmsd 2.553 +/- 0.559

RMSD against lowest energy structure for residues 1-48

Structure Score
S_0032_25_0001.pdb 1.7259
S_0025_191_0001.pdb 3.4368
S_0015_278_0001.pdb 2.9072
S_0018_310_0001.pdb 2.4267
S_0013_66_0001.pdb 3.0699
S_0025_254_0001.pdb 2.2201
S_0018_294_0001.pdb 2.3431
S_0028_104_0001.pdb 2.1486
S_0001_236_0001.pdb 2.2103
S_0013_207_0001.pdb 1.8816
Averaged Ca-rmsd 2.437 +/- 0.540

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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