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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 sturcture of human MEKK3 PB1 domain cis isomer.

BMRB ID: 15332

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Graph for Solution sturcture of human MEKK3 PB1 domain cis isomer

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_0029_135_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0029_135_0001.pdb 1.3071
S_0007_20_0001.pdb 1.0289
S_0009_147_0001.pdb 0.6716
S_0006_178_0001.pdb 1.0741
S_0021_45_0001.pdb 0.7569
S_0019_253_0001.pdb 1.0323
S_0022_135_0001.pdb 0.7111
S_0001_337_0001.pdb 1.8812
S_0029_334_0001.pdb 1.9857
S_0015_239_0001.pdb 1.2160
Averaged Ca-rmsd 1.166 +/- 0.456

RMSD against lowest energy structure for residues 1-78

Structure Score
S_0029_135_0001.pdb 1.3107
S_0007_20_0001.pdb 1.0349
S_0009_147_0001.pdb 0.6708
S_0006_178_0001.pdb 1.0703
S_0021_45_0001.pdb 0.7569
S_0019_253_0001.pdb 1.0333
S_0022_135_0001.pdb 0.7085
S_0001_337_0001.pdb 1.8595
S_0029_334_0001.pdb 1.9914
S_0015_239_0001.pdb 1.2178
Averaged Ca-rmsd 1.165 +/- 0.454

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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