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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 Differences in the electrostatic surfaces of the type III secretion needle proteins.

BMRB ID: 15206

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Graph for Differences in the electrostatic surfaces of the type III secretion needle proteins

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_0014_322_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0014_322_0001.pdb 0.1471
S_0001_124_0001.pdb 0.2058
S_0030_63_0001.pdb 0.1371
S_0006_235_0001.pdb 0.1767
S_0030_308_0001.pdb 0.2802
S_0025_308_0001.pdb 0.1926
S_0007_217_0001.pdb 0.2606
S_0005_207_0001.pdb 0.2089
S_0008_247_0001.pdb 0.4613
S_0007_293_0001.pdb 0.1461
Averaged Ca-rmsd 0.222 +/- 0.097

RMSD against lowest energy structure for residues 1-39

Structure Score
S_0014_322_0001.pdb 0.1439
S_0001_124_0001.pdb 0.2029
S_0030_63_0001.pdb 0.1384
S_0006_235_0001.pdb 0.1764
S_0030_308_0001.pdb 0.2792
S_0025_308_0001.pdb 0.1942
S_0007_217_0001.pdb 0.2634
S_0005_207_0001.pdb 0.2090
S_0008_247_0001.pdb 0.4648
S_0007_293_0001.pdb 0.1473
Averaged Ca-rmsd 0.222 +/- 0.098

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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