Bound water molecules at the interface between the HIV-1 protease and a potent inhibitor, KNI-272, determined by NMR

The binding interactions between HIV-1 protease and the peptidomimetic transition state analog inhibitor KNI-221 in water were examined via 2D water/NOESY and water/ROESY experiments. The results revealed the presence of well-ordered water molecules bound to the protease/KNI-221 complex which have long residence times and short interproton distances to the Ile50/150, Ala28/128 and Asp29/129 amide protons.