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 Tubulin polymerization-promoting protein family member 3 from Homo sapiens. Northeast Structural Genomics target HR387..

BMRB ID: 15329

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Graph for Solution NMR structure of Tubulin polymerization-promoting protein family member 3 from Homo sapiens. Northeast Structural Genomics target HR387.

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_0012_476_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0012_476_0001.pdb 4.7290
S_0012_380_0001.pdb 5.0533
S_0012_399_0001.pdb 6.5435
S_0007_520_0001.pdb 5.9494
S_0012_416_0001.pdb 4.9282
S_0017_386_0001.pdb 8.0743
S_0017_460_0001.pdb 7.9250
S_0008_412_0001.pdb 4.3081
S_0008_513_0001.pdb 5.5167
S_0002_444_0001.pdb 7.0212
Averaged Ca-rmsd 6.005 +/- 1.338

RMSD against lowest energy structure for residues 27-27, 30-32, 34-38, 46-84, 87-88

Structure Score
S_0012_476_0001.pdb 2.8408
S_0012_380_0001.pdb 2.9948
S_0012_399_0001.pdb 2.5824
S_0007_520_0001.pdb 3.2030
S_0012_416_0001.pdb 2.6704
S_0017_386_0001.pdb 2.2855
S_0017_460_0001.pdb 3.4832
S_0008_412_0001.pdb 2.6567
S_0008_513_0001.pdb 3.0224
S_0002_444_0001.pdb 2.6095
Averaged Ca-rmsd 2.835 +/- 0.348

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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