Models of the binding of PR66 with V179 and V192 in the hydrophobic pocket in VP1. (a) Molecular-docking model of PR66 in the hydrophobic pocket of VP1 was prepared using Discovery Studio (ver. 4.1; Accelrys, San Diego, CA, USA). (b) Cartoon of the docking result. Arrow indicates the interaction of PR66 with the side chains of valines at the 179 and 192 positions of VP1. V179F and V192M are mutations that orient toward the hydrophobic pocket and diminish it in size, which reduces the contact and interaction with PR66. L247 is distal to the hydrophobic pocket, but—based on the dimensions—there is no evidence suggesting that L247V is involved in the interaction between PR66 and the pocket. However, it possibly plays a role in stabilizing the overall structure. This figure appears in colour in the online version of JAC and in black and white in the print version of JAC.