Accurate automated protein NMR structure determination using unassigned NOESY data.

ABSTRACT: Conventional NMR structure determination requires nearly complete assignment of the cross peaks of a refined NOESY peak list. Depending on the size of the protein and quality of the spectral data, this can be a time-consuming manual process requiring several rounds of peak list refinement and structure determination. Programs such as Aria, CYANA, and AutoStructure can generate models using unassigned NOESY data but are very sensitive to the quality of the input peak lists and can converge to inaccurate structures if the signal-to-noise of the peak lists is low. Here, we show that models with high accuracy and reliability can be produced by combining the strengths of the high-resolution structure prediction program Rosetta with global measures of the agreement between structure models and e

SUBMITTER: Raman S 

PROVIDER: S-EPMC2841443 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature