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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 Solution structure of the CUL7-CPH domain from Homo Sapiens; Northeast Structural Genomics Consortium target HT1..

BMRB ID: 15109

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Graph for Solution structure of the CUL7-CPH domain from Homo Sapiens; Northeast Structural Genomics Consortium target HT1.

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_0024_37_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0024_37_0001.pdb 2.3769
S_0010_124_0001.pdb 2.4754
S_0010_324_0001.pdb 4.9001
S_0002_191_0001.pdb 2.3695
S_0006_128_0001.pdb 2.9431
S_0016_271_0001.pdb 2.1825
S_0016_48_0001.pdb 1.5678
S_0007_127_0001.pdb 1.5497
S_0017_241_0001.pdb 1.9499
S_0019_41_0001.pdb 7.7528
Averaged Ca-rmsd 3.007 +/- 1.920

RMSD against lowest energy structure for residues 2-59, 64-76

Structure Score
S_0024_37_0001.pdb 2.3403
S_0010_124_0001.pdb 2.5036
S_0010_324_0001.pdb 4.7775
S_0002_191_0001.pdb 2.1996
S_0006_128_0001.pdb 2.9259
S_0016_271_0001.pdb 2.2303
S_0016_48_0001.pdb 1.5720
S_0007_127_0001.pdb 1.5606
S_0017_241_0001.pdb 1.8280
S_0019_41_0001.pdb 6.6134
Averaged Ca-rmsd 2.855 +/- 1.613

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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