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 Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation..

BMRB ID: 15179

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 Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation.

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_0010_31_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0010_31_0001.pdb 3.8504
S_0005_359_0001.pdb 6.2938
S_0021_475_0001.pdb 7.9075
S_0003_78_0001.pdb 4.9475
S_0002_92_0001.pdb 4.8444
S_0011_73_0001.pdb 6.1259
S_0002_195_0001.pdb 4.2252
S_0009_62_0001.pdb 5.9280
S_0010_193_0001.pdb 5.2533
S_0002_387_0001.pdb 4.4933
Averaged Ca-rmsd 5.387 +/- 1.203

RMSD against lowest energy structure for residues 27-48

Structure Score
S_0010_31_0001.pdb 2.1487
S_0005_359_0001.pdb 2.5378
S_0021_475_0001.pdb 3.2572
S_0003_78_0001.pdb 2.0348
S_0002_92_0001.pdb 2.1756
S_0011_73_0001.pdb 2.6414
S_0002_195_0001.pdb 1.9397
S_0009_62_0001.pdb 1.6461
S_0010_193_0001.pdb 2.3675
S_0002_387_0001.pdb 3.2723
Averaged Ca-rmsd 2.402 +/- 0.538

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