Dynamically-driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain.

However, this contribution may not be significant because within the present 30-ns simulations, no obvious dissociation of two protomers occurs, as judged from the comparison of the RMSD values for the WT and N214A dimers, as well as the fact that even more inter-protomer hydrogen bonds with high occupancy are found over the key dimerization interface, namely between the N-finger and active-site residues of N214A.

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