Fig. 4

Superposition of some residues in the inhibitor binding area. In each residue, 147 inhibitor-bound units are superimposed so that the RMSD targeting main chain (N, Cα and C atoms) would be minimized based on a specific inhibitor-bound unit. Excluding some exceptions, O and N atoms are colored red and blue, respectively, and the carbon skeleton of inhibitors is shadowed in green. a Arg358: The units close to the inhibitor (<4 Å) have the Nη atom colored cyan and the water O atom colored yellow. b Arg125. c and d Tyr547: The Tyr547 side chains were divided into c the first and d the second group. In the second group, the Oη atom is colored cyan and the water O atom is colored yellow. e Ser630: The units in which inhibitor forms a covalent bond have the Oγ atom colored cyan, the inhibitor drawn by a line and the water O atom colored yellow. The image of the different angle is drawn at the lower left in this Figure. f Ser209: Some units close to the inhibitor (<4 Å) have the Oγ atom colored cyan and the water O atom colored yellow. g Var711: The units in which the Cγ atoms have an opposite direction to the other units have the Cγ atom marked by a “sphere”. h Asn710: Some units in which the Oδ and Nδ atoms are switched to each other have the water O atom colored yellow