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Results for submission Resonance assignment of the first and second KH (hnRNP-K homology) domains of human poly(C)-binding protein-2 (PCBP2).

BMRB ID: 15049

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Graph for Resonance assignment of the first and second KH (hnRNP-K homology) domains of human poly(C)-binding protein-2 (PCBP2)

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_0008_57_0001

RMSD against lowest energy structure for all residues

Structure Score
S_0008_57_0001.pdb 2.1258
S_0009_485_0001.pdb 2.1632
S_0002_174_0001.pdb 7.5069
S_0006_108_0001.pdb 1.7987
S_0011_142_0001.pdb 2.3523
S_0008_259_0001.pdb 3.7523
S_0001_104_0001.pdb 2.0398
S_0018_462_0001.pdb 2.1901
S_0009_19_0001.pdb 2.1126
S_0001_266_0001.pdb 2.3988
Averaged Ca-rmsd 2.844 +/- 1.722

RMSD against lowest energy structure for residues 1-78, 81-81, 83-125, 131-138, 140-154

Structure Score
S_0008_57_0001.pdb 1.8885
S_0009_485_0001.pdb 1.8565
S_0002_174_0001.pdb 5.8234
S_0006_108_0001.pdb 1.4925
S_0011_142_0001.pdb 1.9663
S_0008_259_0001.pdb 3.3438
S_0001_104_0001.pdb 1.9712
S_0018_462_0001.pdb 2.0174
S_0009_19_0001.pdb 1.7735
S_0001_266_0001.pdb 1.9839
Averaged Ca-rmsd 2.412 +/- 1.294

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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