Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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CS-Rosetta Results Access

Results for submission chemical shift assignments of PA4090 from Pseudomonas aeruginosa.

BMRB ID: 15246

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Graph for chemical shift assignments of PA4090 from Pseudomonas aeruginosa

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_04737

RMSD against lowest energy structure for all residues

Structure Score
S_04737.pdb 3.7860
S_03735.pdb 8.3851
S_08209.pdb 7.8458
S_01638.pdb 5.0363
S_00035.pdb 3.6985
S_02035.pdb 4.5769
S_04838.pdb 4.7602
S_01044.pdb 5.0202
S_07761.pdb 11.8037
S_00848.pdb 6.9704
Averaged Ca-rmsd 6.188 +/- 2.561

RMSD against lowest energy structure for residues 34-118

Structure Score
S_04737.pdb 2.6392
S_03735.pdb 2.0105
S_08209.pdb 2.4984
S_01638.pdb 3.1782
S_00035.pdb 1.9060
S_02035.pdb 2.3366
S_04838.pdb 2.3786
S_01044.pdb 2.4633
S_07761.pdb 3.0117
S_00848.pdb 3.3639
Averaged Ca-rmsd 2.579 +/- 0.479

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.

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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

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