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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 T4 Bacteriophage Helicase Uvsw.1.

BMRB ID: 15252

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Graph for Solution Structure of T4 Bacteriophage Helicase Uvsw.1

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_01983

RMSD against lowest energy structure for all residues

Structure Score
S_01983.pdb 2.9455
S_06397.pdb 4.2456
S_03657.pdb 3.9005
S_00931.pdb 6.9540
S_02223.pdb 6.7721
S_07475.pdb 8.4732
S_09601.pdb 3.0636
S_03829.pdb 5.0461
S_09789.pdb 4.6272
S_06947.pdb 4.4915
Averaged Ca-rmsd 5.052 +/- 1.799

RMSD against lowest energy structure for residues 15-25, 27-27, 30-74

Structure Score
S_01983.pdb 1.2217
S_06397.pdb 3.4273
S_03657.pdb 1.8668
S_00931.pdb 2.1452
S_02223.pdb 1.9316
S_07475.pdb 4.9880
S_09601.pdb 1.7432
S_03829.pdb 2.0198
S_09789.pdb 2.2353
S_06947.pdb 2.2901
Averaged Ca-rmsd 2.387 +/- 1.071

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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