Abstract
Sequence-specific assignments of the NH, C.alpha.H, and C.beta.H resonances in the NMR spectrum of the histidne-containing protein (HPr) from Escherichia coli are complete [Klevit, R. E., Drobny, G. P., and Waygood, E. B. (1986) Biochemistry]. In addition, the C.gamma.H3 resonances of valyl, threonyl, and isoleucyl residues have been assigned by two-dimensional relayed coherence transfer (RELAY) experiments. In order to rigorously assign the resonances from longer side chains such as leucines, long-range transfer experiments have been applied to HPr. Coherence transfers via isotropic mixing within large spin systems were accomplished by multiple pulse trains applied during the mixing time of a two-dimensional experiment.