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Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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Results for submission The solution structure of the protein coded by gene RHOS4_12090 of R. sphaeroides. Northeast structural genomics target RhR5.

BMRB ID: 15344

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Graph for The solution structure of the protein coded by gene RHOS4_12090 of R. sphaeroides. Northeast structural genomics target RhR5

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_0015_163_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0015_163_0001.pdb 1.9981
S_0001_228_0001.pdb 2.1056
S_0021_305_0001.pdb 1.7270
S_0008_103_0001.pdb 1.8001
S_0021_107_0001.pdb 1.8898
S_0015_281_0001.pdb 1.7881
S_0010_294_0001.pdb 2.9465
S_0023_238_0001.pdb 3.4864
S_0005_255_0001.pdb 6.6567
S_0023_209_0001.pdb 2.0943
Averaged Ca-rmsd 2.649 +/- 1.519

RMSD against lowest energy structure for residues 1-52, 57-57, 60-61, 64-64

Structure Score
S_0015_163_0001.pdb 1.8897
S_0001_228_0001.pdb 1.9961
S_0021_305_0001.pdb 1.7203
S_0008_103_0001.pdb 1.8820
S_0021_107_0001.pdb 1.8886
S_0015_281_0001.pdb 1.7872
S_0010_294_0001.pdb 3.0255
S_0023_238_0001.pdb 3.3488
S_0005_255_0001.pdb 7.0318
S_0023_209_0001.pdb 1.8981
Averaged Ca-rmsd 2.647 +/- 1.639

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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