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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 1H, 13C, and 15N Backbone Assignments and 13C Aliphatic Sidechain Assignments for PKA Phosphorylated CFTR Regulatory Region.

BMRB ID: 15340

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Graph for 1H, 13C, and 15N Backbone Assignments and 13C Aliphatic Sidechain Assignments for PKA Phosphorylated CFTR Regulatory Region

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_07980

RMSD against lowest energy structure for all residues

Structure Score
S_07980.pdb 10.7677
S_04941.pdb 15.4909
S_01873.pdb 16.7031
S_00215.pdb 14.6518
S_00621.pdb 16.1204
S_00154.pdb 13.7231
S_03042.pdb 16.3385
S_00630.pdb 17.2038
S_05893.pdb 16.4051
S_06096.pdb 16.3222
Averaged Ca-rmsd 15.373 +/- 1.916

RMSD against lowest energy structure for residues 81-84

Structure Score
S_07980.pdb 2.4516
S_04941.pdb 2.3742
S_01873.pdb 2.5210
S_00215.pdb 2.5534
S_00621.pdb 2.4932
S_00154.pdb 2.3488
S_03042.pdb 2.5220
S_00630.pdb 2.5521
S_05893.pdb 2.3968
S_06096.pdb 2.6209
Averaged Ca-rmsd 2.483 +/- 0.088

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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