BMRB

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 Main chain NMR assignments of SBT70 in its prodomain-bound state.

BMRB ID: 15248

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Graph for Main chain NMR assignments of SBT70 in its prodomain-bound state

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_03578

RMSD against lowest energy structure for all residues

Structure Score
S_03578.pdb 12.3829
S_02718.pdb 10.7388
S_03356.pdb 14.3195
S_07242.pdb 13.0526
S_02303.pdb 15.4671
S_00928.pdb 12.7278
S_09765.pdb 13.4524
S_05646.pdb 13.7826
S_09293.pdb 14.2467
S_08143.pdb 12.6420
Averaged Ca-rmsd 13.281 +/- 1.296

RMSD against lowest energy structure for residues 79-94, 97-98, 114-117

Structure Score
S_03578.pdb 2.9911
S_02718.pdb 3.0070
S_03356.pdb 3.2573
S_07242.pdb 3.0370
S_02303.pdb 6.2649
S_00928.pdb 3.0545
S_09765.pdb 4.9430
S_05646.pdb 3.1256
S_09293.pdb 3.1701
S_08143.pdb 2.6696
Averaged Ca-rmsd 3.552 +/- 1.136

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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