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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 NMR Assignments of the apo Corynebacterium diphtheria Heme Oxygenase-G135A.

BMRB ID: 15070

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Graph for NMR Assignments of the apo Corynebacterium diphtheria Heme Oxygenase-G135A

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_01076

RMSD against lowest energy structure for all residues

Structure Score
S_01076.pdb 12.9450
S_09743.pdb 14.3998
S_05528.pdb 13.6404
S_07737.pdb 11.8255
S_04503.pdb 12.9829
S_07655.pdb 14.4951
S_00343.pdb 12.9983
S_01000.pdb 15.8169
S_04843.pdb 12.7569
S_06457.pdb 14.9344
Averaged Ca-rmsd 13.680 +/- 1.207

RMSD against lowest energy structure for residues 54-70

Structure Score
S_01076.pdb 2.3041
S_09743.pdb 2.4852
S_05528.pdb 1.9842
S_07737.pdb 2.0985
S_04503.pdb 2.3846
S_07655.pdb 2.3187
S_00343.pdb 2.2230
S_01000.pdb 2.4199
S_04843.pdb 2.1737
S_06457.pdb 2.0862
Averaged Ca-rmsd 2.248 +/- 0.162

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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