Table 2.

Crystallographic data statistics. PR, wild type HIV-1 protease; PR_V82A, PR with the V82A mutation; PR_I84V, PR with the I84V mutation

Protease	PR_V82A^a	PR^a	PR_V82A^a	PR_I84V	PR	PR_V82A^b	*#Pr^a ^b	PR_V82A
Inhibitor	CA-p2	p2-NC	p2-NC	p2-NC	p6^pol-PR	p6^pol-PR	p1-p6	p1-p6
Space group	P2₁2₁2	P2₁2₁2	P2₁2₁2	P2₁2₁2	P2₁2₁2	P2₁2₁2	P2₁2₁2	P2₁2₁2
Unit cell dimensions (Å)
a	57.89	58.00	58.02	57.80	59.45	58.88	58.91	58.46
b	85.96	85.78	85.89	85.59	87.00	86.27	86.07	85.85
c	46.19	46.53	46.61	46.46	46.32	46.40	46.54	46.39
Resolution range (Å)	50–1.54	50–1.40	50–1.10	50–1.30	50–1.60	50–1.42	50–1.38	50–1.32
Unique reflections	34 544	44 291	95 318	55 009	32 005	40 847	47 418	55 317
R_merge (%) overall (final shell)	6.5 (37.1)	10.1 (45.6)	10.2 (37.7)	7.9 (33.0)	9.1 (41.3)	9.8 (70.8)	10.4 (28.6)	8.4 (57.7)
<I/sigma> overall (final shell)	13.4 (5.8)	8.9 (2.1)	10.4 (2.1)	14.4 (3.2)	13.2 (3.7)	17.1 (2.6)	14.1 (13.8)	10.4 (2.9)
Data range for refinement (Å)	10–1.54	10–1.40	10–1.10	10–1.30	10–1.60	10–1.42	10–1.38	10–1.32
R_work (%)	0.12	0.15	0.13	0.12	0.15	0.18	0.16	0.13
R_free (%)	0.19	0.19	0.17	0.16	0.23	0.23	0.21	0.18
No. of waters (total occupancies)	194	188	206	223.5	155	199	190	297
Completeness (%)overall (final shell)	99.6 (100)	95.6 (66.6)	94.8 (68.4)	96.0 (72.4)	99.2 (93.1)	90.3 (100)	89.2 (96.2)	99.9 (100)
RMS deviation from ideality
Bonds (Å)	0.010	0.011	0.015	0.013	0.009	0.011	0.010	0.012
Angle distance (Å)	0.029	0.029	0.033	0.030	0.029	0.031	0.030	0.034
Average B-factors (Å²)
Main chain	15.9	8.0	9.0	10.6	22.4	16.7	14.2	12.0
Side chain	21.9	12.2	13.7	15.4	27.6	21.1	18.4	17.0
Inhibitor	27.5	14.0	10.6	14.7	29.9	19.1	18.3	24.0
Solvent	31.5	23.7	24.4	25.8	37.9	30.9	27.3	26.7

Diffraction data collected at Advanced Photon Source, beamline SER-CAT 22. All other data were collected at National Synchrotron Light Source, beamline X26C.

Structures in which hydrogen atoms were not added.