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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 H, C, N Chemical Shifts for Influenza A NS1 (1-73) Protein Bound to dsRNA.

BMRB ID: 15117

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Graph for Backbone H, C, N Chemical Shifts for Influenza A NS1 (1-73) Protein Bound to dsRNA

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_0006_244_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0006_244_0001.pdb 0.6537
S_0026_134_0001.pdb 0.4142
S_0001_236_0001.pdb 0.2512
S_0003_222_0001.pdb 0.3869
S_0009_119_0001.pdb 0.4320
S_0030_300_0001.pdb 0.3689
S_0031_119_0001.pdb 0.5193
S_0029_129_0001.pdb 0.2694
S_0008_267_0001.pdb 1.7225
S_0013_65_0001.pdb 1.2404
Averaged Ca-rmsd 0.626 +/- 0.479

RMSD against lowest energy structure for residues 1-70

Structure Score
S_0006_244_0001.pdb 0.4517
S_0026_134_0001.pdb 0.3912
S_0001_236_0001.pdb 0.2322
S_0003_222_0001.pdb 0.3793
S_0009_119_0001.pdb 0.4307
S_0030_300_0001.pdb 0.3411
S_0031_119_0001.pdb 0.5094
S_0029_129_0001.pdb 0.2365
S_0008_267_0001.pdb 1.6557
S_0013_65_0001.pdb 1.1749
Averaged Ca-rmsd 0.580 +/- 0.463

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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