Determination of protein structures consistent with NMR order parameters

Order parameters obtained from NMR experiments characterize distributions of bond vector orientations. Their interpretation, however, usually requires the assumption of a particular motional model. We propose a multiple-copy simulation method in which the experimental order parameters are used as restraints in conjunction with a standard molecular force field. The latter effectively acts as a sophisticated motional model, allowing ensembles of structures consistent with the experimental order parameters to be determined.