We demonstrate here a dynamic structure of bacteriorhodopsin (bR) as revealed by $^{13}$ C NMR studies on [3_$^{13}$ C]_,[1-$^{13}$ C]Ala- and/or Val-labeled wild type and a variety of site-directed mutants at ambient temperature. For this purpose, well-resolved (up to twelve) I$^{13}$ C NMR peaks were assigned with reference to the displacement of peaks due to the conformation-dependent I$^{13}$ C chemical shifts and reduced peak-intensities due to site-directed mutations. Revealed bR structure was not rigid as anticipated from 2D crystals of hexagonal array but a dynamically heterogeneous, undergoing a variety of local fluctuations depending upon specific site with frequency range of 10$^2$ -10$^{8}$ Hz. In particular, dynamics- dependent suppression of peaks turned out to be very sensitive to the motion of 10$^{-4}$ s and 10$^{-5}$ s interfered with frequency of magic angle spinning and proton decoupling, respectively. It is also noteworthy that such dynamic feature is strongly dependent upon the manner of 2D crystalline packing: $^{13}$ C NMR peaks of monomeric bR yielded either highly broadened or completely suppressed signals, depending upon the type of $^{13}$ C-labeled amino-acid residues.