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 NMR chemical shift assignments for E. coli YejL protein: target ER309 of the Northeast Structural Genomics Consortium.

BMRB ID: 15346

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Graph for NMR chemical shift assignments for E. coli YejL protein: target ER309 of the Northeast Structural Genomics Consortium

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_0003_306_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0003_306_0001.pdb 2.4148
S_0010_114_0001.pdb 6.1136
S_0026_148_0001.pdb 2.3990
S_0020_36_0001.pdb 5.5194
S_0030_219_0001.pdb 3.5940
S_0009_106_0001.pdb 6.0691
S_0028_302_0001.pdb 2.7460
S_0014_134_0001.pdb 2.4679
S_0012_305_0001.pdb 2.4534
S_0017_121_0001.pdb 2.4387
Averaged Ca-rmsd 3.622 +/- 1.620

RMSD against lowest energy structure for residues 1-43

Structure Score
S_0003_306_0001.pdb 0.9858
S_0010_114_0001.pdb 1.1891
S_0026_148_0001.pdb 0.6998
S_0020_36_0001.pdb 1.3834
S_0030_219_0001.pdb 1.2826
S_0009_106_0001.pdb 1.0760
S_0028_302_0001.pdb 0.9077
S_0014_134_0001.pdb 0.6078
S_0012_305_0001.pdb 0.5776
S_0017_121_0001.pdb 0.6036
Averaged Ca-rmsd 0.931 +/- 0.300

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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