Nuclear Magnetic Resonance (NMR) is a powerful tool for determining the structures of proteins in the solution state. However, due to a lack of experimental constraints as well as the inherent internal dynamics of proteins in solution, loops and even relative orientations of domains in multi-domain proteins are oftentimes poorly converged in NMR-derived protein structures. Optimal application of NMR-derived protein structures therefore requires an efficacious means to exclude poorly defined structural features. For example, inclusion of ill-converged atomic coordinates in Molecular Replacement (MR) results in poor phasing power, while restricting MR templates to include only a well-defined “core” set of atoms vastly improves the phases obtained. Current methods for delineating a core residue or atom set include FindCore, FindCore2 and Cyrange. In delineating core atom sets, Cyrange and FindCore2 produce larger core residue or atom sets while FindCore provides a more stringent definition for core atom sets. FindCore and FindCore2 are atom-based methods whereas Cyrange is residue based. A previous study (Mao, B., Guan, R., & Montelione, G. T. Structure, 2011, 19: 757-766) has already explored the use of FindCore in MR. We will present our results comparing the more inclusive cores identified by FindCore2 and Cyrange in MR calculations.

Determining proteins structure using NMR: More inclusive cores identified by FindCore2 and Cyrange in MR calculations

251st National Meeting (2016)

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