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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 NMR Structure of 50S Ribosomal Protein L14e from Sulfolobus Solfataricus; Northeast Structural Genomics Consortium Target SSR105..

BMRB ID: 15210

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Graph for NMR Structure of 50S Ribosomal Protein L14e from Sulfolobus Solfataricus; Northeast Structural Genomics Consortium Target SSR105.

This run appears to have converged (based on the residues marked non-flexible). That means that the results may be a meaningful prediction of the real structure. Please validate the structure against your experimental data.

Lowest energy structure: S_0005_92_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0005_92_0001.pdb 1.6214
S_0007_231_0001.pdb 1.7052
S_0008_29_0001.pdb 2.3402
S_0008_272_0001.pdb 1.4557
S_0029_311_0001.pdb 2.7732
S_0016_21_0001.pdb 1.3508
S_0019_189_0001.pdb 1.9818
S_0023_20_0001.pdb 1.9601
S_0004_240_0001.pdb 1.8023
S_0013_284_0001.pdb 2.2812
Averaged Ca-rmsd 1.927 +/- 0.438

RMSD against lowest energy structure for residues 2-89

Structure Score
S_0005_92_0001.pdb 1.5861
S_0007_231_0001.pdb 1.6733
S_0008_29_0001.pdb 2.3058
S_0008_272_0001.pdb 1.4588
S_0029_311_0001.pdb 2.6394
S_0016_21_0001.pdb 1.3507
S_0019_189_0001.pdb 1.9572
S_0023_20_0001.pdb 1.9618
S_0004_240_0001.pdb 1.7907
S_0013_284_0001.pdb 2.2245
Averaged Ca-rmsd 1.895 +/- 0.406

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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