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 ATOMIC STRUCTURE OF TRANSLATION INITIATION FACTOR aIF2 beta-SUBUNIT FROM ARCHAEBACTERIA SULFOLOBUS SOLFATARICUS: HIGH RESOLUTION NMR IN SOLUTION.

BMRB ID: 15229

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 ATOMIC STRUCTURE OF TRANSLATION INITIATION FACTOR aIF2 beta-SUBUNIT FROM ARCHAEBACTERIA SULFOLOBUS SOLFATARICUS: HIGH RESOLUTION NMR IN SOLUTION

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_03142

RMSD against lowest energy structure for all residues

Structure Score
S_03142.pdb 10.6597
S_06984.pdb 11.7310
S_06688.pdb 11.9356
S_05194.pdb 13.1609
S_08943.pdb 11.2959
S_05083.pdb 14.7364
S_06317.pdb 11.3552
S_09247.pdb 14.3873
S_07438.pdb 9.7836
S_08905.pdb 9.5156
Averaged Ca-rmsd 11.856 +/- 1.770

RMSD against lowest energy structure for residues 63-78, 80-86

Structure Score
S_03142.pdb 3.4560
S_06984.pdb 2.5776
S_06688.pdb 2.5558
S_05194.pdb 2.8839
S_08943.pdb 3.3689
S_05083.pdb 4.3954
S_06317.pdb 3.0879
S_09247.pdb 2.8393
S_07438.pdb 3.3695
S_08905.pdb 3.5383
Averaged Ca-rmsd 3.207 +/- 0.549

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