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 Backbone assignment of human IgG1 CH3 domain.

BMRB ID: 15204

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Graph for Backbone assignment of human IgG1 CH3 domain

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_0006_2_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0006_2_0001.pdb 0.5647
S_0011_272_0001.pdb 0.7422
S_0019_205_0001.pdb 1.0310
S_0006_143_0001.pdb 0.5864
S_0008_252_0001.pdb 1.3922
S_0014_310_0001.pdb 1.0946
S_0018_116_0001.pdb 0.6355
S_0009_164_0001.pdb 0.5400
S_0006_92_0001.pdb 0.9461
S_0004_252_0001.pdb 0.8099
Averaged Ca-rmsd 0.834 +/- 0.279

RMSD against lowest energy structure for residues 1-100

Structure Score
S_0006_2_0001.pdb 0.5400
S_0011_272_0001.pdb 0.7019
S_0019_205_0001.pdb 1.0120
S_0006_143_0001.pdb 0.5840
S_0008_252_0001.pdb 1.3932
S_0014_310_0001.pdb 1.0642
S_0018_116_0001.pdb 0.6304
S_0009_164_0001.pdb 0.5365
S_0006_92_0001.pdb 0.9260
S_0004_252_0001.pdb 0.8073
Averaged Ca-rmsd 0.820 +/- 0.279

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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