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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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CS-Rosetta Results Access

Results for submission ErbB2TM.

BMRB ID: 15231

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Graph for ErbB2TM

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_0017_234_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0017_234_0001.pdb 0.1422
S_0034_177_0001.pdb 0.1637
S_0035_107_0001.pdb 0.1903
S_0034_130_0001.pdb 0.1915
S_0020_73_0001.pdb 0.3381
S_0015_211_0001.pdb 0.1764
S_0003_142_0001.pdb 0.1462
S_0029_114_0001.pdb 0.3470
S_0005_255_0001.pdb 0.1364
S_0023_149_0001.pdb 0.3483
Averaged Ca-rmsd 0.218 +/- 0.089

RMSD against lowest energy structure for residues 1-30

Structure Score
S_0017_234_0001.pdb 0.1311
S_0034_177_0001.pdb 0.1530
S_0035_107_0001.pdb 0.1816
S_0034_130_0001.pdb 0.1804
S_0020_73_0001.pdb 0.3109
S_0015_211_0001.pdb 0.1621
S_0003_142_0001.pdb 0.1339
S_0029_114_0001.pdb 0.3207
S_0005_255_0001.pdb 0.1269
S_0023_149_0001.pdb 0.3202
Averaged Ca-rmsd 0.202 +/- 0.082

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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