Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set.
J Mol Biol. 2011 May 23;
Authors: Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A
The CS-RDC-NOE Rosetta program was used to generate the solution structure of a 27-kDa fragment of the Escherichia coli BamC protein from a limited set of NMR data. The BamC protein is a component of the essential five-protein ?-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC(101-344) forms two well-defined domains connected by an ~18-residue linker, where the relative orientation of the domains was not defined. Both domains adopt a helix-grip fold previously observed in the Bet v 1 superfamily. (15)N relaxation data indicated a high degree of conformational flexibility for the linker connecting the N-terminal domain and the C-terminal domain in BamC. The results here show that CS-RDC-NOE Rosetta is robust and has a high tolerance for misassigned nuclear Overhauser effect restraints, greatly simplifying NMR structure determinations.
PMID: 21624375 [PubMed - as supplied by publisher]
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Structure Calculation Using CS-DP ROSETTA from NESG Wiki
Structure Calculation Using CS-DP ROSETTA
This is a copy of instructions for CS-DP Rosetta from NESG Wiki that was created on 8/20/19. Please go to the original post at http://www.nmr2.buffalo.edu/nesg.wiki/Structure_Calculation_Using_CS-DP_ROSETTA
for a more up-to-date version.
Introduction
The CS-DP-Rosetta approach merges the ideas of model generation using CS-Rosetta with model filtering by agreement to NOESY data via the DP-score from the RPF program to generate high accuracy protein structures. This hybrid approach uses both local backbone chemical shift data...
Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set.
Linear Mode
