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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 Dynein Light Chain LC8 at pH 5.5.

BMRB ID: 15076

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Graph for Dynein Light Chain LC8 at pH 5.5

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_0002_59_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0002_59_0001.pdb 1.0109
S_0022_288_0001.pdb 0.7271
S_0007_252_0001.pdb 1.5920
S_0014_156_0001.pdb 0.7932
S_0012_137_0001.pdb 0.8417
S_0001_18_0001.pdb 1.0304
S_0027_51_0001.pdb 3.3407
S_0009_12_0001.pdb 1.4414
S_0010_339_0001.pdb 0.7867
S_0028_101_0001.pdb 0.6670
Averaged Ca-rmsd 1.223 +/- 0.805

RMSD against lowest energy structure for residues 1-83

Structure Score
S_0002_59_0001.pdb 1.0162
S_0022_288_0001.pdb 0.7104
S_0007_252_0001.pdb 1.5709
S_0014_156_0001.pdb 0.7965
S_0012_137_0001.pdb 0.8363
S_0001_18_0001.pdb 1.0297
S_0027_51_0001.pdb 3.3406
S_0009_12_0001.pdb 1.4443
S_0010_339_0001.pdb 0.7898
S_0028_101_0001.pdb 0.6479
Averaged Ca-rmsd 1.218 +/- 0.806

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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