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 structure of p1 from the infectious bursal disease virus (IBDV) in dodecylphosphocholin (DPC)..

BMRB ID: 15108

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Graph for NMR structure of p1 from the infectious bursal disease virus (IBDV) in dodecylphosphocholin (DPC).

This run appears to have converged (based on the residues marked non-flexible). That means that the results may be a meaningful prediction of the real structure. Please validate the structure against your experimental data.

Lowest energy structure: S_07079

RMSD against lowest energy structure for all residues

Structure Score
S_07079.pdb 1.7889
S_02869.pdb 2.9482
S_09402.pdb 2.0069
S_09035.pdb 3.5339
S_09997.pdb 2.6425
S_04559.pdb 2.8651
S_03618.pdb 1.9689
S_09906.pdb 3.1590
S_03022.pdb 2.8534
S_05432.pdb 2.2669
Averaged Ca-rmsd 2.603 +/- 0.574

RMSD against lowest energy structure for residues 2-42

Structure Score
S_07079.pdb 1.2642
S_02869.pdb 1.5380
S_09402.pdb 1.1453
S_09035.pdb 2.6445
S_09997.pdb 1.2396
S_04559.pdb 1.7476
S_03618.pdb 1.4654
S_09906.pdb 2.1553
S_03022.pdb 2.0992
S_05432.pdb 1.9116
Averaged Ca-rmsd 1.721 +/- 0.482

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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