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Results for submission 1H, 13C and 15N resonance assignment of truncated SUMO from Trypanosoma brucei.

BMRB ID: 15194

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Graph for 1H, 13C and 15N resonance assignment of truncated SUMO from Trypanosoma brucei

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_0006_114_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0006_114_0001.pdb 4.5932
S_0016_354_0001.pdb 6.3653
S_0009_222_0001.pdb 7.2877
S_0007_36_0001.pdb 6.2177
S_0021_171_0001.pdb 3.9170
S_0015_46_0001.pdb 3.9987
S_0010_197_0001.pdb 8.3603
S_0017_130_0001.pdb 5.8339
S_0010_101_0001.pdb 7.8698
S_0014_191_0001.pdb 5.4251
Averaged Ca-rmsd 5.987 +/- 1.549

RMSD against lowest energy structure for residues 24-87, 93-93, 95-95

Structure Score
S_0006_114_0001.pdb 1.5362
S_0016_354_0001.pdb 1.6711
S_0009_222_0001.pdb 4.0781
S_0007_36_0001.pdb 1.8814
S_0021_171_0001.pdb 2.1762
S_0015_46_0001.pdb 2.1859
S_0010_197_0001.pdb 1.9787
S_0017_130_0001.pdb 1.9539
S_0010_101_0001.pdb 3.6871
S_0014_191_0001.pdb 1.5510
Averaged Ca-rmsd 2.270 +/- 0.885

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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