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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 A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris.

BMRB ID: 15324

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Graph for A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris

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_0019_204_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0019_204_0001.pdb 0.8922
S_0027_136_0001.pdb 1.0091
S_0024_181_0001.pdb 0.9231
S_0021_187_0001.pdb 3.4689
S_0029_244_0001.pdb 1.9269
S_0031_151_0001.pdb 1.2261
S_0001_79_0001.pdb 2.3617
S_0002_272_0001.pdb 1.7162
S_0028_193_0001.pdb 0.9358
S_0009_198_0001.pdb 1.4407
Averaged Ca-rmsd 1.590 +/- 0.824

RMSD against lowest energy structure for residues 1-46

Structure Score
S_0019_204_0001.pdb 0.8919
S_0027_136_0001.pdb 1.0178
S_0024_181_0001.pdb 0.9283
S_0021_187_0001.pdb 3.5068
S_0029_244_0001.pdb 1.9340
S_0031_151_0001.pdb 1.2312
S_0001_79_0001.pdb 2.3839
S_0002_272_0001.pdb 1.6465
S_0028_193_0001.pdb 0.9389
S_0009_198_0001.pdb 1.4550
Averaged Ca-rmsd 1.593 +/- 0.833

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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