. Author manuscript; available in PMC: 2013 May 11.

Published in final edited form as: Biochem Biophys Res Commun. 2012 Mar 24;421(3):413–417. doi: 10.1016/j.bbrc.2012.03.096

Table 4. Protease inhibitor hydrophobic contacts.

Hydrophobic contacts made by compounds 1 and 2. Amino acid residues (represented as single letter amino acid codes) involved in hydrophobic contacts with compounds 1 and 2 are listed for MDR769, NL4-3 and PLM-II. In the case of NL4-3 and MDR769, the protease residues are numbered 1–99 for monomer-A and 101–199 for monomer-B. Both compounds show almost equal number of hydrophobic contacts with the MDR769 HIV-1 protease. Compound 1 shows more hydrophobic contacts than 2 in the docked models of NL4-3 HIV-1 protease. Both compounds show highest number of hydrophobic contacts with PLM-II.

Enzyme	Amino acid residues involved in hydrophobic contacts
Enzyme	Compound 1	Compound 2
MDR769	G27, I50, P81, T82, V84, I147, P181, T182	A28, V32, V84, G148, I150, P181, T182, V184
NL4-3	R8, A28, D30, V32, I47, I50, I84, A128, D129, D130, V132, I147, G149, I150, L176, P181, V182, I184	L23, A28, V82, I84, A128, D129, I147, G149, I150, V182, I184
PLM-II	I14, M15, Y17, I32, D34, G36, S37, M75, N76, Y77, V78, S79, F111, T114, S118, F120, I123, L131, Y192, D214, G216, T217, S218, A219, T221, F244, Q275, N288, I290, L292, F294, I300	I14, M15, Y17, I32, D34, G36, S37, A38, M75, N76, Y77, V78, S79, F111, T114, A117, S118, F120, I123, L131, Y192, I212, D214, G216, T217, S218, A219, T221, F244, I290, L292, F294, I300