We report a new solid-state multidimensional NMR approach based on the cross-polarization with variable-contact pulse sequence [Paluch, P.; Pawlak, T.; Amoureux, J.-P.; Potrzebowski, M. J. J. Magn. Reson. 233, 2013, 56], with 1H inverse detection and very fast magic angle spinning (νR = 60 kHz), dedicated to the measurement of local molecular motions of 1H–15N vectors. The introduced three-dimensional experiments, 1H–15N–1H and hCA(N)H, are particularly useful for the study of molecular dynamics of proteins and other complex structures. The applicability and power of this methodology have been revealed by employing as a model sample the GB-1 small protein doped with Na2CuEDTA. The results clearly prove that the dispersion of 1H–15N dipolar coupling constants well correlates with higher order structure of the protein. Our approach complements the conventional studies and offers a fast and reasonably simple method.