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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 1H, and 15N Chemical Shift Assignments for the N-terminal domain of Myxococcus xantus CarA protein..

BMRB ID: 15023

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Graph for 1H, and 15N Chemical Shift Assignments for the N-terminal domain of Myxococcus xantus CarA protein.

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_01556

RMSD against lowest energy structure for all residues

Structure Score
S_01556.pdb 6.6586
S_05465.pdb 4.7000
S_01974.pdb 10.2121
S_07731.pdb 6.2349
S_03762.pdb 3.7500
S_02301.pdb 5.7166
S_04944.pdb 4.4533
S_00044.pdb 4.5278
S_08085.pdb 4.5737
S_04060.pdb 3.7227
Averaged Ca-rmsd 5.455 +/- 1.940

RMSD against lowest energy structure for residues 42-80

Structure Score
S_01556.pdb 1.6913
S_05465.pdb 2.4606
S_01974.pdb 2.4001
S_07731.pdb 1.7227
S_03762.pdb 1.6336
S_02301.pdb 1.5034
S_04944.pdb 1.6814
S_00044.pdb 2.3175
S_08085.pdb 1.8527
S_04060.pdb 1.4334
Averaged Ca-rmsd 1.870 +/- 0.380

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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