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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 SOLUTION STRUCTURE OF HUMAN BETA-MICROSEMINOPROTEIN.

BMRB ID: 15036

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Graph for SOLUTION STRUCTURE OF HUMAN BETA-MICROSEMINOPROTEIN

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_09686

RMSD against lowest energy structure for all residues

Structure Score
S_09686.pdb 5.8527
S_07622.pdb 7.0666
S_08128.pdb 9.2639
S_04082.pdb 6.8011
S_08918.pdb 8.0771
S_08516.pdb 7.6279
S_08867.pdb 5.9627
S_06421.pdb 6.7115
S_06395.pdb 10.0822
S_01510.pdb 6.2392
Averaged Ca-rmsd 7.368 +/- 1.411

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

Structure Score
S_09686.pdb 1.9664
S_07622.pdb 1.9837
S_08128.pdb 2.4699
S_04082.pdb 3.1247
S_08918.pdb 2.8049
S_08516.pdb 2.6859
S_08867.pdb 2.3043
S_06421.pdb 2.0540
S_06395.pdb 5.0232
S_01510.pdb 3.2053
Averaged Ca-rmsd 2.762 +/- 0.912

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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