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: 15176

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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_339_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0003_339_0001.pdb 8.8479
S_0010_117_0001.pdb 13.3226
S_0008_228_0001.pdb 14.0127
S_0010_358_0001.pdb 12.5476
S_0021_255_0001.pdb 11.4332
S_0025_313_0001.pdb 12.9095
S_0004_93_0001.pdb 14.0828
S_0010_87_0001.pdb 12.5653
S_0005_217_0001.pdb 11.7438
S_0019_204_0001.pdb 12.1271
Averaged Ca-rmsd 12.359 +/- 1.514

RMSD against lowest energy structure for residues 2-7

Structure Score
S_0003_339_0001.pdb 2.7778
S_0010_117_0001.pdb 2.9258
S_0008_228_0001.pdb 2.8640
S_0010_358_0001.pdb 2.9741
S_0021_255_0001.pdb 3.1856
S_0025_313_0001.pdb 2.8535
S_0004_93_0001.pdb 2.8743
S_0010_87_0001.pdb 3.1021
S_0005_217_0001.pdb 2.7924
S_0019_204_0001.pdb 2.8048
Averaged Ca-rmsd 2.915 +/- 0.136

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

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