Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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CS-Rosetta Results Access

Results for submission Soution Structure of Af54 M-domain.

BMRB ID: 15275

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Graph for Soution Structure of Af54 M-domain

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_06208

RMSD against lowest energy structure for all residues

Structure Score
S_06208.pdb 5.7544
S_05395.pdb 6.9158
S_08118.pdb 7.9291
S_03241.pdb 6.6520
S_05147.pdb 7.6167
S_09737.pdb 7.0424
S_04525.pdb 10.4348
S_09550.pdb 11.8913
S_02960.pdb 10.8323
S_08150.pdb 7.0036
Averaged Ca-rmsd 8.207 +/- 2.075

RMSD against lowest energy structure for residues 45-111

Structure Score
S_06208.pdb 1.4419
S_05395.pdb 1.6219
S_08118.pdb 1.5204
S_03241.pdb 3.4456
S_05147.pdb 2.1881
S_09737.pdb 1.6509
S_04525.pdb 1.5627
S_09550.pdb 1.2540
S_02960.pdb 1.8256
S_08150.pdb 3.7283
Averaged Ca-rmsd 2.024 +/- 0.862

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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