Docking the C-Terminal Tyrosine Cluster into the Active Site. To verify whether the conformational change of the P-Y574 side chain would be sufficient to allow for the entry of the tyrosine substrate to the active site and interact with catalytic residues, we synthesized the C-terminal Tyr cluster peptide (YSYGYNYYGYSYSEKE). Unfortunately, this peptide was insoluble, likely because of multiple tyrosines, which are prone to aggregation. We therefore docked this peptide into the active site of the P-Y574 model, resulting from the 10 ns MD simulation using AutoDock (version 4.02).