Biological Magnetic Resonance Data Bank

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Results for submission The highly cooperative folding of small, naturally occurring proteins is likely the result of natural selection..

BMRB ID: 15132

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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_05627

RMSD against lowest energy structure for all residues

Structure Score
S_05627.pdb 2.6574
S_03939.pdb 5.0787
S_03862.pdb 2.3684
S_00746.pdb 2.0354
S_07966.pdb 3.3099
S_06284.pdb 3.4006
S_04481.pdb 4.3021
S_00136.pdb 3.0969
S_02727.pdb 2.7755
S_07197.pdb 4.3260
Averaged Ca-rmsd 3.335 +/- 0.967

RMSD against lowest energy structure for residues 1-96

Structure Score
S_05627.pdb 0.4612
S_03939.pdb 0.6536
S_03862.pdb 0.7308
S_00746.pdb 0.7869
S_07966.pdb 0.4883
S_06284.pdb 0.4075
S_04481.pdb 0.8991
S_00136.pdb 0.3650
S_02727.pdb 0.6312
S_07197.pdb 0.8582
Averaged Ca-rmsd 0.628 +/- 0.191

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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