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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

Lowest energy structure: S_0008_278_0001

RMSD against lowest energy structure for all residues

StructureScore
S_0008_278_0001.pdb8.6633
S_0017_262_0001.pdb7.3845
S_0015_112_0001.pdb7.6241
S_0017_157_0001.pdb7.7075
S_0012_281_0001.pdb9.7756
S_0012_246_0001.pdb10.3349
S_0004_72_0001.pdb7.5368
S_0008_218_0001.pdb8.8372
S_0017_226_0001.pdb6.9418
S_0026_106_0001.pdb8.0044
Averaged Ca-rmsd8.281 +/- 1.100

RMSD against lowest energy structure for residues 4-38

StructureScore
S_0008_278_0001.pdb2.4577
S_0017_262_0001.pdb3.5462
S_0015_112_0001.pdb2.2111
S_0017_157_0001.pdb2.0459
S_0012_281_0001.pdb2.0643
S_0012_246_0001.pdb4.5788
S_0004_72_0001.pdb1.9554
S_0008_218_0001.pdb2.8386
S_0017_226_0001.pdb2.2720
S_0026_106_0001.pdb2.1856
Averaged Ca-rmsd2.616 +/- 0.838

This entry was calculated with Rosetta version 3.5 and version 3.2 of the CS-Rosetta Toolbox.

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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