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 Solution structure of the Bright/ARID domain from the human JARID1C protein..

BMRB ID: 15348

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 Solution structure of the Bright/ARID domain from the human JARID1C protein.

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_0005_139_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0005_139_0001.pdb 1.8348
S_0023_188_0001.pdb 4.2521
S_0002_155_0001.pdb 1.4163
S_0018_136_0001.pdb 2.4396
S_0011_164_0001.pdb 2.0408
S_0018_295_0001.pdb 2.9133
S_0013_60_0001.pdb 1.7780
S_0007_236_0001.pdb 1.6175
S_0022_341_0001.pdb 2.3124
S_0022_231_0001.pdb 2.4497
Averaged Ca-rmsd 2.305 +/- 0.819

RMSD against lowest energy structure for residues 2-93

Structure Score
S_0005_139_0001.pdb 1.8344
S_0023_188_0001.pdb 4.1845
S_0002_155_0001.pdb 1.3881
S_0018_136_0001.pdb 2.4178
S_0011_164_0001.pdb 1.9118
S_0018_295_0001.pdb 2.8942
S_0013_60_0001.pdb 1.7456
S_0007_236_0001.pdb 1.6195
S_0022_341_0001.pdb 2.2857
S_0022_231_0001.pdb 2.4166
Averaged Ca-rmsd 2.270 +/- 0.809

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