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 Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation..

BMRB ID: 15180

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Graph for Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation.

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_0003_21_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0003_21_0001.pdb 7.3746
S_0019_9_0001.pdb 8.0469
S_0012_132_0001.pdb 10.6228
S_0018_16_0001.pdb 10.5347
S_0016_162_0001.pdb 10.1817
S_0022_318_0001.pdb 10.7291
S_0009_194_0001.pdb 8.8990
S_0022_60_0001.pdb 9.8189
S_0021_300_0001.pdb 10.7524
S_0024_193_0001.pdb 10.3533
Averaged Ca-rmsd 9.731 +/- 1.209

RMSD against lowest energy structure for residues 53-57

Structure Score
S_0003_21_0001.pdb 2.6812
S_0019_9_0001.pdb 2.9861
S_0012_132_0001.pdb 2.4007
S_0018_16_0001.pdb 2.6286
S_0016_162_0001.pdb 2.3181
S_0022_318_0001.pdb 2.2446
S_0009_194_0001.pdb 2.7041
S_0022_60_0001.pdb 2.1607
S_0021_300_0001.pdb 2.4165
S_0024_193_0001.pdb 2.4062
Averaged Ca-rmsd 2.495 +/- 0.251

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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