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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 SOLUTION STRUCTURE OF HUMAN BETA-MICROSEMINOPROTEIN.

BMRB ID: 15036

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Graph for SOLUTION STRUCTURE OF HUMAN BETA-MICROSEMINOPROTEIN

Lowest energy structure: S_09686

RMSD against lowest energy structure for all residues

StructureScore
S_09686.pdb5.8527
S_07622.pdb7.0666
S_08128.pdb9.2639
S_04082.pdb6.8011
S_08918.pdb8.0771
S_08516.pdb7.6279
S_08867.pdb5.9627
S_06421.pdb6.7115
S_06395.pdb10.0822
S_01510.pdb6.2392
Averaged Ca-rmsd7.368 +/- 1.411

RMSD against lowest energy structure for residues 4-13, 16-56

StructureScore
S_09686.pdb1.9664
S_07622.pdb1.9837
S_08128.pdb2.4699
S_04082.pdb3.1247
S_08918.pdb2.8049
S_08516.pdb2.6859
S_08867.pdb2.3043
S_06421.pdb2.0540
S_06395.pdb5.0232
S_01510.pdb3.2053
Averaged Ca-rmsd2.762 +/- 0.912

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