Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

CS-Rosetta Results Access

Results for submission 1H, 13C, and 15N Chemical Shift Assignments for CutA1 from E. coli.

BMRB ID: 15094

These results are interactive!

Clicking on an image will enlarge it. Clicking again will open it in a Jmol viewer. Click the downward pointing arrow to shrink an image. You can also enlarge the graph and make it interactive by clicking twice. Hold down the right mouse button and drag to zoom in on the interactive graph. Left click on a structure in the graph to pull it up in the Jmol viewer. This enables you to explore any structure in the Jmol viewer.

Graph for 1H, 13C, and 15N Chemical Shift Assignments for CutA1 from E. coli

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_00380

RMSD against lowest energy structure for all residues

Structure Score
S_00380.pdb 4.9462
S_01614.pdb 4.1152
S_04814.pdb 2.3736
S_08556.pdb 3.1158
S_08321.pdb 2.1346
S_01039.pdb 3.0349
S_09683.pdb 3.9868
S_01821.pdb 3.0224
S_00599.pdb 4.0969
S_07214.pdb 2.4626
Averaged Ca-rmsd 3.329 +/- 0.917

RMSD against lowest energy structure for residues 9-112

Structure Score
S_00380.pdb 2.1313
S_01614.pdb 2.2512
S_04814.pdb 1.1300
S_08556.pdb 0.9689
S_08321.pdb 1.0631
S_01039.pdb 1.6006
S_09683.pdb 2.4085
S_01821.pdb 1.2191
S_00599.pdb 3.6404
S_07214.pdb 0.9701
Averaged Ca-rmsd 1.738 +/- 0.868

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.

Download results for best 10 structures Download all results

To have this entry show up in your list of submitted entries please click here.

Please contact us if you encounter any issues.

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

This service made possible by:

CHTC Logo OSG Logo CS-Rosetta Logo