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Results for submission 1H,13C and 15N NMR Assignments of the Yellow Fever Envelope Protein Domain III.

BMRB ID: 15034

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Graph for 1H,13C and 15N NMR Assignments of the Yellow Fever Envelope Protein Domain III

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_0008_278_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0008_278_0001.pdb 8.6633
S_0017_262_0001.pdb 7.3845
S_0015_112_0001.pdb 7.6241
S_0017_157_0001.pdb 7.7075
S_0012_281_0001.pdb 9.7756
S_0012_246_0001.pdb 10.3349
S_0004_72_0001.pdb 7.5368
S_0008_218_0001.pdb 8.8372
S_0017_226_0001.pdb 6.9418
S_0026_106_0001.pdb 8.0044
Averaged Ca-rmsd 8.281 +/- 1.100

RMSD against lowest energy structure for residues 4-38

Structure Score
S_0008_278_0001.pdb 2.4577
S_0017_262_0001.pdb 3.5462
S_0015_112_0001.pdb 2.2111
S_0017_157_0001.pdb 2.0459
S_0012_281_0001.pdb 2.0643
S_0012_246_0001.pdb 4.5788
S_0004_72_0001.pdb 1.9554
S_0008_218_0001.pdb 2.8386
S_0017_226_0001.pdb 2.2720
S_0026_106_0001.pdb 2.1856
Averaged Ca-rmsd 2.616 +/- 0.838

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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