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 NMR structure of the murine DLC2 (deleted in liver cancer -2) SAM (sterile alpha motif) domain.

BMRB ID: 15060

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 NMR structure of the murine DLC2 (deleted in liver cancer -2) SAM (sterile alpha motif) domain

It appears this run did not converge (based on the residues marked non-flexible). While the best predicted structure is displayed, the lack of convergence means that this structure is unlikely to resemble the actual structure. Furthermore, it is not necessarily representative of the ensemble of structures formed.

Lowest energy structure: S_06410

RMSD against lowest energy structure for all residues

Structure Score
S_06410.pdb 8.8716
S_04407.pdb 10.3413
S_09319.pdb 10.6411
S_01112.pdb 8.2244
S_01714.pdb 8.8629
S_00028.pdb 15.0745
S_01357.pdb 8.7234
S_06254.pdb 8.0440
S_02250.pdb 10.0022
S_04751.pdb 11.0757
Averaged Ca-rmsd 9.986 +/- 2.071

RMSD against lowest energy structure for residues 22-38, 42-54

Structure Score
S_06410.pdb 3.2450
S_04407.pdb 3.2788
S_09319.pdb 3.6058
S_01112.pdb 3.3902
S_01714.pdb 3.5428
S_00028.pdb 3.1680
S_01357.pdb 3.2942
S_06254.pdb 3.2450
S_02250.pdb 3.2225
S_04751.pdb 3.0836
Averaged Ca-rmsd 3.308 +/- 0.162

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