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 NMR Assignments of the apo Corynebacterium diphtheria Heme Oxygenase.

BMRB ID: 15071

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Graph for NMR Assignments of the apo Corynebacterium diphtheria Heme Oxygenase

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_07693

RMSD against lowest energy structure for all residues

Structure Score
S_07693.pdb 10.9914
S_07952.pdb 13.4486
S_05221.pdb 15.3553
S_09995.pdb 13.5649
S_07882.pdb 14.2724
S_00467.pdb 13.7285
S_06923.pdb 13.5017
S_02833.pdb 14.4762
S_01341.pdb 11.0208
S_04506.pdb 13.1407
Averaged Ca-rmsd 13.350 +/- 1.390

RMSD against lowest energy structure for residues 125-137

Structure Score
S_07693.pdb 2.7830
S_07952.pdb 2.8045
S_05221.pdb 2.8060
S_09995.pdb 2.8032
S_07882.pdb 2.6774
S_00467.pdb 2.7724
S_06923.pdb 2.7320
S_02833.pdb 2.7109
S_01341.pdb 2.7175
S_04506.pdb 2.7013
Averaged Ca-rmsd 2.751 +/- 0.048

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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