Abstract
We have recently developed various restraint potentials for residual dipolar coupling in solution NMR [1] as well as dipolar coupling and chemical shift in solid-state NMR [2]. In principle, NMR observables are time- and ensemble-averaged, thus the structure determination needs to be based on the average property of an ensemble rather than the collection of multiple independent structure determination. In this work, we have further formulated and implemented the ensemble-average orientational restraint potentials, such as residual dipolar coupling (RDC), dipolar coupling, and peptide plane chemical shift, to explore the flexible nature of proteins embedded in such experimental observables.
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