The process of equilibration of protein states in a three-stranded antiparallel beta-sheet miniprotein is studied using a time-dependent free energy disconnectivity graph. To determine the rates of transitions, the molecular dynamics simulation results of a recent work (Kalgin, I. V.; et al. J. Phys. Chem. B 2013, 117, 6092) are employed. The vertices of the graph are the free energies of characteristic states of the protein, and the edges are the transition state free energies. To determine the latter, the "complete" partition function (Eyring, 1935) is used, which includes the translational partition function corresponding to the ballistic motion of the system along the reaction coordinate. The distance along the reaction coordinate that enters the translational partition function is taken to be proportional to the observation time and thus measures the number of representative points that cross the transition state surface during given time. As the time increases, the free energy barriers between the clusters of characteristic conformations (native-like, helical, and beta-sheet conformations of different degree of organization) decrease and (local) equilibrium between the clusters is established. With time, these clusters are grouped into larger clusters, extending The equilibrium to a larger portion of protein states.