The folding and unfolding kinetics of single molecules, such as proteins or nucleic acids, can be explored by mechanical pulling experiments. Determining intrinsic kinetic information, at zero stretching force, usually requires an extrapolation by fitting a theoretical model. Here, we apply a recent theoretical approach describing molecular rupture in the presence of force to unfolding kinetic data obtained from coarse-grained simulations of ubiquitin. Unfolding rates calculated from simulations over a broad range of stretching forces, for different pulling directions, reveal a remarkable "turnover" from a force-independent process at low force to a force-dependent process at high force, akin to the "roll-over" in unfolding rates sometimes seen in studies using chemical denaturant. While such a turnover in rates is unexpected in one dimension, we demonstrate that it can occur for dynamics in just two dimensions. We relate the turnover to the quality of the pulling direction as a reaction coordinate for the intrinsic folding mechanism. A novel pulling direction, designed to be the most relevant to the intrinsic folding pathway, results in the smallest turnover. Our results are in accord with protein engineering experiments and simulations which indicate that the unfolding mechanism at high force can differ from the intrinsic mechanism. The apparent similarity between extrapolated and intrinsic rates in experiments, unexpected for different unfolding barriers, can be explained if the turnover occurs at low forces.