1. Volume 3, Issue 1, Pages 33-40 (January 1995)
Crystal structures of HIV-2 protease in complex with inhibitors containing the hydroxyethylamine dipeptide isostere 
Liang Tong, Susan Pav, Suet Mui, Daniel Lamarre, Christiane Yoakim, Pierre Beaulieu, Paul C Anderson 
Structure 
Volume 3, Issue 1, Pages (January 1995)
DOI: /S (01)

2. Figure 1
HIV protease inhibitors. The long inhibitors (1–3 ), contain a (quinolinecarbonyl)valyl group at the P2 and P3 positions and the short inhibitors (4–8 ), contain a novel dimethylphenoxyacetyl group .
Structure 1995 3, 33-40DOI: ( /S (01) )

3. Figure 2
Ramachandran plot for the complex with inhibitor 1 at 1.7 Å resolution. Glycine residues are shown as crosses, prolines as pentagons, and other residues as dots .
Structure 1995 3, 33-40DOI: ( /S (01) )

4. Figure 3
Plot of the average main-chain (N, Cα , C and O) temperature factor values (Å2 ) for the two HIV-2 protease monomers in the complex with inhibitor 1 . Thick line, residues 1–99; thin line, residues 1'–99' .
Structure 1995 3, 33-40DOI: ( /S (01) )

5. Figure 4
Electron density for inhibitor 1 at 1.7 Å resolution. The 2Fo–Fc electron density is shown, calculated before the inhibitor was included in the atomic model. The atomic models for the observed orientation of the inhibitor (thick lines) and the alternative orientation (thin lines), obtained by applying the local two-fold axis of the protease, are also shown. The contour level is at 1σ . Electron density for the pyridyl group becomes visible when the contour level is reduced to 0.5σ .
Structure 1995 3, 33-40DOI: ( /S (01) )

6. Figure 5
The binding modes of the inhibitors. (a) Overlap of the bound conformation of the long inhibitors 1 (red), 2 (cyan) and 3 (black). (b) Overlap of the bound conformation of the short inhibitors 4 (black), 5 (cyan), 6 (pink) and 7 (green). (c ) Overlap of the bound conformation of the long inhibitor 1 (red) and the short inhibitor 7 (green) .
Structure 1995 3, 33-40DOI: ( /S (01) )

7. Figure 5
The binding modes of the inhibitors. (a) Overlap of the bound conformation of the long inhibitors 1 (red), 2 (cyan) and 3 (black). (b) Overlap of the bound conformation of the short inhibitors 4 (black), 5 (cyan), 6 (pink) and 7 (green). (c ) Overlap of the bound conformation of the long inhibitor 1 (red) and the short inhibitor 7 (green) .
Structure 1995 3, 33-40DOI: ( /S (01) )

8. Figure 5
The binding modes of the inhibitors. (a) Overlap of the bound conformation of the long inhibitors 1 (red), 2 (cyan) and 3 (black). (b) Overlap of the bound conformation of the short inhibitors 4 (black), 5 (cyan), 6 (pink) and 7 (green). (c ) Overlap of the bound conformation of the long inhibitor 1 (red) and the short inhibitor 7 (green) .
Structure 1995 3, 33-40DOI: ( /S (01) )

9. Figure 6
(a) Hydrogen-bonding interactions between inhibitor 1 and the protease. (b) The interactions between the hydroxyl of the isostere and the catalytic aspartic acid residues .
Structure 1995 3, 33-40DOI: ( /S (01) )

10. Figure 6
(a) Hydrogen-bonding interactions between inhibitor 1 and the protease. (b) The interactions between the hydroxyl of the isostere and the catalytic aspartic acid residues .
Structure 1995 3, 33-40DOI: ( /S (01) )

11. Figure 7
Stereo plot of conformational changes in the HIV-2 protease in complexes with the short inhibitors. Residues 27'–31' and the (quinolinecarbonyl)valyl group of the complex with inhibitor 1 (red) are shown superimposed on the corresponding residues and the dimethylphenoxyacetyl group of the complex with inhibitor 7 (green).
Structure 1995 3, 33-40DOI: ( /S (01) )

12. Figure 8
Stereo plot of the superposition of inhibitor 1 (thin lines) and JG-365 (thick lines). The water molecules (W301 and W302) are shown as crosses .
Structure 1995 3, 33-40DOI: ( /S (01) )