To probe whether this plasticity is facilitated by the S/I substitution or by other features of the IsPETase scaffold, we calculated the ꭓ1 and ꭓ2 dihedral torsions of the corresponding tryptophan in all the trajectories. From this data, it can be seen that the tryptophan side chain residue ꭓ1 and ꭓ2 dihedral angles are consistent with the B and C conformers of wild-type