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 NMR assignments of the binary hvDHFR1:folate complex.

BMRB ID: 15253

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Graph for NMR assignments of the binary hvDHFR1:folate complex

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_0009_187_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0009_187_0001.pdb 5.1498
S_0011_443_0001.pdb 7.0855
S_0012_354_0001.pdb 4.2057
S_0020_471_0001.pdb 4.8742
S_0001_91_0001.pdb 8.4164
S_0010_61_0001.pdb 5.5610
S_0021_141_0001.pdb 10.1096
S_0012_320_0001.pdb 4.8351
S_0004_412_0001.pdb 5.9634
S_0021_370_0001.pdb 7.4201
Averaged Ca-rmsd 6.362 +/- 1.867

RMSD against lowest energy structure for residues 33-120

Structure Score
S_0009_187_0001.pdb 1.8112
S_0011_443_0001.pdb 5.6914
S_0012_354_0001.pdb 2.0859
S_0020_471_0001.pdb 2.2877
S_0001_91_0001.pdb 3.0606
S_0010_61_0001.pdb 2.1341
S_0021_141_0001.pdb 2.4139
S_0012_320_0001.pdb 2.2801
S_0004_412_0001.pdb 1.2739
S_0021_370_0001.pdb 1.6882
Averaged Ca-rmsd 2.473 +/- 1.226

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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