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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 At3g28950.1 from Arabidopsis thaliana.

BMRB ID: 15295

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Graph for Solution structure At3g28950.1 from Arabidopsis thaliana

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_0009_65_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0009_65_0001.pdb 9.3054
S_0019_358_0001.pdb 11.2413
S_0001_218_0001.pdb 9.1750
S_0018_28_0001.pdb 14.1050
S_0020_150_0001.pdb 11.4705
S_0017_461_0001.pdb 13.2093
S_0003_419_0001.pdb 11.1888
S_0010_443_0001.pdb 10.4622
S_0006_277_0001.pdb 11.3349
S_0008_370_0001.pdb 10.8935
Averaged Ca-rmsd 11.239 +/- 1.523

RMSD against lowest energy structure for residues 78-87, 90-102

Structure Score
S_0009_65_0001.pdb 3.4316
S_0019_358_0001.pdb 2.9154
S_0001_218_0001.pdb 2.8938
S_0018_28_0001.pdb 2.7127
S_0020_150_0001.pdb 2.9625
S_0017_461_0001.pdb 3.2276
S_0003_419_0001.pdb 3.2577
S_0010_443_0001.pdb 3.2620
S_0006_277_0001.pdb 3.0670
S_0008_370_0001.pdb 3.2785
Averaged Ca-rmsd 3.101 +/- 0.225

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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