Before revision:  MD provided a wealth of information about interactions between the MTSL and the residues of the protein and  on the different motional contributions to the overall dynamics of the MTSL . Data obtained from MD were seen to be in good agreement with those obtained from QM but the dynamics of the system revealed more interactions than those observed from QMmethods .
After revision:  MD provided a wealth of information about interactions between the MTSL and the residues of the protein and on the different motional contributions to the overall dynamics of the MTSL that were validated using a multifrequency electron paramagnetic resonance (EPR) approach. The latter relayed on the frequency dependence of the resolution of the fast and slow motions of the spin probe and was used to distinguish the fast internal motion of the spin label from the slow protein tumbling. Data obtained from MD were seen to be in good agreement with those obtained from QM but the dynamics of the system revealed more interactions than those observed from QMmethods .