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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 Solution structure of NusB from Aquifex Aeolicus.

BMRB ID: 15312

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Graph for Solution structure of NusB from Aquifex Aeolicus

This run appears to have converged (based on the residues marked non-flexible). That means that the results may be a meaningful prediction of the real structure. Please validate the structure against your experimental data.

Lowest energy structure: S_0022_81_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0022_81_0001.pdb 0.7296
S_0013_296_0001.pdb 0.7300
S_0014_318_0001.pdb 1.0903
S_0010_244_0001.pdb 1.8182
S_0003_311_0001.pdb 0.8312
S_0020_228_0001.pdb 1.2782
S_0008_391_0001.pdb 1.3041
S_0004_44_0001.pdb 1.1774
S_0005_266_0001.pdb 1.2426
S_0002_90_0001.pdb 0.9673
Averaged Ca-rmsd 1.117 +/- 0.329

RMSD against lowest energy structure for residues 1-132

Structure Score
S_0022_81_0001.pdb 0.7284
S_0013_296_0001.pdb 0.7299
S_0014_318_0001.pdb 1.0918
S_0010_244_0001.pdb 1.8222
S_0003_311_0001.pdb 0.8284
S_0020_228_0001.pdb 1.2761
S_0008_391_0001.pdb 1.2946
S_0004_44_0001.pdb 1.1699
S_0005_266_0001.pdb 1.1763
S_0002_90_0001.pdb 0.9612
Averaged Ca-rmsd 1.108 +/- 0.328

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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