Table 1.
Data collection and refinement statistics for HIV-1 protease mutants in complex with 1
| PRI47V | PRL76V | PRV82A | PRN88D | |
|---|---|---|---|---|
| Crystal | ||||
| Space group | P21212 | P21212 | P21212 | P21212 |
| a, b, c (Å) | 58.20, 86.39, 45.95 | 57.82, 86.24, 46.01 | 58.64, 86.46, 45.44 | 58.23, 86.39, 46.07 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Data collection | ||||
| Resolution (Å) | 50-1.25 | 50-1.30 | 50-1.43 | 50-1.55 |
| Completeness (%) | 94.6 (63.7) | 98.1 (86.3) | 90.5 (57.0) | 99.9 (99.5) |
| Rsym (%) | 6.8 (32.6) | 9.4 (41.1) | 9.8 (45.0) | 7.5 (42.5) |
| <I/σ(I)> | 19.9 (2.4) | 14.3 (2.1) | 10.2 (2.0) | 23.1 (4.2) |
| Unique reflections | 61338 | 56338 | 39482 | 34554 |
| Redundancy | 6.1 (2.0) | 5.8 (2.7) | 12.1 (2.0) | 7.1 (6.3) |
| Refinement | ||||
| Resolution (Å) | 10-1.25 | 10-1.30 | 10-1.43 | 10-1.55 |
| Rwork (%) | 14.7 | 13.5 | 16.8 | 14.8 |
| Rfree (%) | 16.9 | 17.2 | 21.8 | 20.7 |
| RMSD bonds (Å) | 0.013 | 0.012 | 0.010 | 0.009 |
| RMSD angle dist. (Å) | 0.033 | 0.032 | 0.029 | 0.028 |
| Protein atoms | 1510 | 1510 | 1510 | 1512 |
| Solvent atoms | 205 | 225 | 129 | 183 |
| Total residues | 198 | 198 | 198 | 198 |
| Average B-factors (Å2) | ||||
| Main chain atoms | 13.4 | 12.5 | 17.7 | 16.1 |
| Side chain atoms | 18.7 | 19.3 | 24.8 | 23.5 |
| Inhibitor | 9.8 | 13.1 | 15.1 | 17.8 |
| Solvent | 24.4 | 23.8 | 24.8 | 24.7 |
| Ramachandran: | ||||
| Favored regions (%) | 100.0 | 100.0 | 100.0 | 100.0 |
| Allowed regions (%) | 100.0 | 100.0 | 100.0 | 100.0 |
| Relative Occup. of 1 | 0.70/0.30 | 1.00 | 0.65/0.35 | 1.00 |
Rsym = Σ|Iobs - Iavg|/ΣIavg; Rwork = Σ∥Fobs - Fcalc∥/ΣFobs; Rfree was calculated using 5% of data and the same sums. Parentheses denote the highest resolution bin.