BMRB

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 The Trp-cage: Optimizing the Stability of a Globular Miniprotein.

BMRB ID: 15169

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 The Trp-cage: Optimizing the Stability of a Globular Miniprotein

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_08333

RMSD against lowest energy structure for all residues

Structure Score
S_08333.pdb 0.4283
S_05417.pdb 0.3435
S_01838.pdb 0.3169
S_02977.pdb 0.3252
S_01057.pdb 0.6625
S_00641.pdb 0.3455
S_05276.pdb 0.2167
S_00043.pdb 0.2176
S_01087.pdb 0.2171
S_08511.pdb 0.3040
Averaged Ca-rmsd 0.338 +/- 0.133

RMSD against lowest energy structure for residues 1-20

Structure Score
S_08333.pdb 0.2707
S_05417.pdb 0.2033
S_01838.pdb 0.1970
S_02977.pdb 0.2249
S_01057.pdb 0.5985
S_00641.pdb 0.1863
S_05276.pdb 0.1484
S_00043.pdb 0.1474
S_01087.pdb 0.1513
S_08511.pdb 0.2372
Averaged Ca-rmsd 0.237 +/- 0.134

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