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. 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 3. Protease inhibitor polar contacts.

Polar contacts made by compounds 1 and 2. Amino acid residues (represented as single letter amino acid codes) of MDR 769 A82T HIV-1 protease involved in polar contacts with compounds 1 and 2 are listed with their corresponding number of contacts in parenthesis. In the case of NL4-3 and MDR769, the protease residues are numbered 1–99 for monomer-A and 101–199 for monomer-B. Active site water molecules that are involved in polar contacts with either compound are listed along with the protease residues. Compound 2 shows more contacts than that of compound 1 in all three cases. Both compounds show highest number of polar contacts with PLM-II.

Enzyme Compound 1 Total compound 2 Total
MDR769 N25 (2), N125 (1), H2O (3) 6 N25 (3), N125 (2), H2O (4) 9
NL4-3 R8 (1), D125 (1), G127 (1) 3 D25 (2), G27(2), D29(2), G48 (1), R108 (1), G127 (2), D129 (1), G148 (1) 12
PLM-II D34 (2), G36 (1), S79 (2), Y192 (1), G216 (1), T217 (1) 8 D34 (3), G36 (1), V78 (1), S79 (3), Y192 (2), D214 (1), T217 (1), S218 (2) 14