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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 NMR Structure of Salmonella typhimurium LT2 Secreted Protein STM0082: Northeast Structural Genomics Consortium Target StR109.

BMRB ID: 15090

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Graph for Solution NMR Structure of Salmonella typhimurium LT2 Secreted Protein STM0082: Northeast Structural Genomics Consortium Target StR109

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_00283

RMSD against lowest energy structure for all residues

Structure Score
S_00283.pdb 7.1937
S_08313.pdb 8.8093
S_02783.pdb 7.0271
S_00149.pdb 7.1058
S_08279.pdb 7.4867
S_06245.pdb 6.9517
S_07467.pdb 5.4370
S_07884.pdb 9.0137
S_06722.pdb 7.3942
S_08613.pdb 5.9469
Averaged Ca-rmsd 7.237 +/- 1.094

RMSD against lowest energy structure for residues 27-96

Structure Score
S_00283.pdb 2.4371
S_08313.pdb 2.1007
S_02783.pdb 3.0202
S_00149.pdb 2.0174
S_08279.pdb 2.4667
S_06245.pdb 2.4266
S_07467.pdb 1.8448
S_07884.pdb 1.4997
S_06722.pdb 1.4321
S_08613.pdb 2.0559
Averaged Ca-rmsd 2.130 +/- 0.480

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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