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Results for submission 1H, 15N, and 13C chemical shift assignments for CaBP1.

BMRB ID: 15197

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Graph for 1H, 15N, and 13C chemical shift assignments for CaBP1

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_0004_232_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0004_232_0001.pdb 8.2797
S_0012_169_0001.pdb 8.5287
S_0019_77_0001.pdb 7.7374
S_0010_381_0001.pdb 10.6272
S_0016_314_0001.pdb 9.3387
S_0016_378_0001.pdb 12.3272
S_0005_487_0001.pdb 9.3922
S_0012_455_0001.pdb 9.9930
S_0016_278_0001.pdb 9.1762
S_0018_277_0001.pdb 8.6934
Averaged Ca-rmsd 9.409 +/- 1.323

RMSD against lowest energy structure for residues 88-94, 100-115, 117-117, 119-119

Structure Score
S_0004_232_0001.pdb 3.0509
S_0012_169_0001.pdb 3.4715
S_0019_77_0001.pdb 3.0749
S_0010_381_0001.pdb 2.9258
S_0016_314_0001.pdb 3.6450
S_0016_378_0001.pdb 3.4842
S_0005_487_0001.pdb 3.8658
S_0012_455_0001.pdb 3.3138
S_0016_278_0001.pdb 3.4693
S_0018_277_0001.pdb 3.6224
Averaged Ca-rmsd 3.392 +/- 0.299

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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