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 Resonance assignments for the discoidin domain of DDR2..

BMRB ID: 15315

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Graph for Resonance assignments for the discoidin domain of DDR2.

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_07860

RMSD against lowest energy structure for all residues

Structure Score
S_07860.pdb 9.7259
S_00605.pdb 11.7375
S_06689.pdb 13.7031
S_01807.pdb 12.9847
S_06367.pdb 13.1730
S_02476.pdb 12.0558
S_00974.pdb 12.8089
S_09596.pdb 12.8685
S_06068.pdb 11.7901
S_02650.pdb 13.2119
Averaged Ca-rmsd 12.406 +/- 1.143

RMSD against lowest energy structure for residues 60-63, 72-81

Structure Score
S_07860.pdb 2.6756
S_00605.pdb 2.8357
S_06689.pdb 2.7696
S_01807.pdb 3.0549
S_06367.pdb 3.3259
S_02476.pdb 2.9408
S_00974.pdb 2.8175
S_09596.pdb 2.9950
S_06068.pdb 3.8273
S_02650.pdb 3.0326
Averaged Ca-rmsd 3.027 +/- 0.335

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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