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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 Backbone Chemical Shift Assignments of Cholera Toxin Enzymatic Domain (1-167).

BMRB ID: 15162

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Graph for Backbone Chemical Shift Assignments of Cholera Toxin Enzymatic Domain (1-167)

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_245_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0019_245_0001.pdb 9.2673
S_0012_421_0001.pdb 12.3508
S_0006_343_0001.pdb 12.9625
S_0004_444_0001.pdb 14.0906
S_0019_274_0001.pdb 11.4291
S_0004_375_0001.pdb 12.2979
S_0019_256_0001.pdb 11.7639
S_0010_491_0001.pdb 11.7229
S_0002_482_0001.pdb 11.6914
S_0007_285_0001.pdb 10.5444
Averaged Ca-rmsd 11.812 +/- 1.304

RMSD against lowest energy structure for residues 11-11, 13-21

Structure Score
S_0019_245_0001.pdb 2.6322
S_0012_421_0001.pdb 2.6328
S_0006_343_0001.pdb 2.6684
S_0004_444_0001.pdb 2.5530
S_0019_274_0001.pdb 2.7110
S_0004_375_0001.pdb 2.6139
S_0019_256_0001.pdb 2.5871
S_0010_491_0001.pdb 2.5927
S_0002_482_0001.pdb 2.5820
S_0007_285_0001.pdb 2.5131
Averaged Ca-rmsd 2.609 +/- 0.057

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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