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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 structure of V21C/V59C Lymphotactin/XCL1.

BMRB ID: 15110

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Graph for Solution structure of V21C/V59C Lymphotactin/XCL1

This run appears to have converged (based on the residues marked non-flexible). That means that the results may be a meaningful prediction of the real structure. Please validate the structure against your experimental data.

Lowest energy structure: S_0028_33_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0028_33_0001.pdb 0.7449
S_0011_253_0001.pdb 0.5298
S_0007_137_0001.pdb 0.6543
S_0008_268_0001.pdb 2.3187
S_0029_182_0001.pdb 0.5731
S_0002_37_0001.pdb 0.5372
S_0024_18_0001.pdb 0.6698
S_0001_323_0001.pdb 0.4539
S_0010_50_0001.pdb 0.5189
S_0018_166_0001.pdb 0.6276
Averaged Ca-rmsd 0.763 +/- 0.553

RMSD against lowest energy structure for residues 1-55

Structure Score
S_0028_33_0001.pdb 0.7047
S_0011_253_0001.pdb 0.5293
S_0007_137_0001.pdb 0.6230
S_0008_268_0001.pdb 2.3387
S_0029_182_0001.pdb 0.5623
S_0002_37_0001.pdb 0.5416
S_0024_18_0001.pdb 0.6741
S_0001_323_0001.pdb 0.4526
S_0010_50_0001.pdb 0.5139
S_0018_166_0001.pdb 0.6232
Averaged Ca-rmsd 0.756 +/- 0.561

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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