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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 GROUP IV WW DOMAIN: A.NIDULANS PINA.

BMRB ID: 15003

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Graph for SOLUTION STRUCTURE OF GROUP IV WW DOMAIN: A.NIDULANS PINA

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_05399

RMSD against lowest energy structure for all residues

Structure Score
S_05399.pdb 6.9293
S_00285.pdb 4.1501
S_07533.pdb 3.1079
S_06779.pdb 4.1979
S_08115.pdb 2.9505
S_07927.pdb 4.2306
S_01653.pdb 6.9689
S_05827.pdb 4.8317
S_01981.pdb 6.8484
S_08388.pdb 3.5518
Averaged Ca-rmsd 4.777 +/- 1.577

RMSD against lowest energy structure for residues 2-34

Structure Score
S_05399.pdb 2.4380
S_00285.pdb 2.6842
S_07533.pdb 1.9879
S_06779.pdb 1.9797
S_08115.pdb 1.8493
S_07927.pdb 1.6160
S_01653.pdb 3.2474
S_05827.pdb 3.0491
S_01981.pdb 3.7976
S_08388.pdb 2.1146
Averaged Ca-rmsd 2.476 +/- 0.704

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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