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A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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Results for submission Northeast Structural Genomics Consortium Target ER411.

BMRB ID: 15088

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Graph for Northeast Structural Genomics Consortium Target ER411

Lowest energy structure: S_05183

RMSD against lowest energy structure for all residues

StructureScore
S_05183.pdb3.3257
S_06208.pdb4.9197
S_06370.pdb3.9368
S_06167.pdb3.4309
S_04076.pdb3.1078
S_04129.pdb4.2966
S_06917.pdb2.8763
S_08938.pdb2.8340
S_04732.pdb3.3417
S_07545.pdb4.0784
Averaged Ca-rmsd3.615 +/- 0.674

RMSD against lowest energy structure for residues 10-105

StructureScore
S_05183.pdb1.1034
S_06208.pdb1.5378
S_06370.pdb1.3028
S_06167.pdb1.3364
S_04076.pdb0.9422
S_04129.pdb1.4632
S_06917.pdb1.0059
S_08938.pdb1.5452
S_04732.pdb1.5055
S_07545.pdb1.1781
Averaged Ca-rmsd1.292 +/- 0.225

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