Hydrogen Bonding in High-Resolution Protein Structures: A New Method To Assess NMR Protein Geometry

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Abstract
An analysis of backbone hydrogen bonds has been performed on nine high-resolution protein X-ray crystal structures. Backbone hydrogen-bond geometry is compared in the context of X-ray crystal structure resolution. A strong correlation between the hydrogen-bond distance, RHO, and the hydrogen-bond angle, θNHO, is observed when the X-ray crystal structure resolution is <1.00 Å. Ab initio calculations were performed to substantiate these results. The angle and distance limits found in our correlation for the backbone hydrogen-bond geometry can be used to evaluate the quality of protein structures and for further NMR structure refinement.