Biological Magnetic Resonance Data Bank

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Results for submission Assignments of {lambda}-IntCB bound to a DNA half-site.

BMRB ID: 15213

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Graph for Assignments of {lambda}-IntCB bound to a DNA half-site

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_0006_198_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0006_198_0001.pdb 4.7519
S_0024_252_0001.pdb 6.0300
S_0014_317_0001.pdb 6.1540
S_0017_310_0001.pdb 6.1140
S_0013_154_0001.pdb 6.9391
S_0019_142_0001.pdb 5.3812
S_0022_57_0001.pdb 5.9359
S_0007_193_0001.pdb 11.6432
S_0013_30_0001.pdb 6.6775
S_0030_13_0001.pdb 7.5172
Averaged Ca-rmsd 6.714 +/- 1.896

RMSD against lowest energy structure for residues 35-61, 64-64

Structure Score
S_0006_198_0001.pdb 2.2227
S_0024_252_0001.pdb 2.5060
S_0014_317_0001.pdb 3.6374
S_0017_310_0001.pdb 2.1663
S_0013_154_0001.pdb 1.6762
S_0019_142_0001.pdb 2.6175
S_0022_57_0001.pdb 1.3561
S_0007_193_0001.pdb 2.5888
S_0013_30_0001.pdb 2.9534
S_0030_13_0001.pdb 2.5278
Averaged Ca-rmsd 2.425 +/- 0.636

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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