Table 2.
Data Collection and Refinement Statistics
| 6X HIV PR–2 | |
|---|---|
| Crystal Form | |
| Space Group | P43 |
| Unit cell parameters | |
| a (Å) | 86.61 |
| b (Å) | 86.61 |
| c (Å) | 33.66 |
| α=β=γ (°) | 90.0 |
| Solvent Content (%)/Vm (Å3/Da) | 50.0 (2.46) |
| No. Molecules per asymm. unit | 2 |
| Data Collection | |
| Resolution (Å) | 61.2-1.3 |
| No. of Unique Reflections | 57,347 |
| No. of Observations | 95,706 |
| Rmerge1 (%) | 3.9 (43.8) |
| I/σI | 10.1 (1.6) |
| Data Completeness (%) | 92.7 (74.1) |
| Mean Multiplicity | 1.67 (1.30) |
| Refinement | |
| No. of Reflections used in refinement | 57,347 |
| Rcryst ‡ (%) | 15.6 |
| Rfree ‡ (%) | 18.9 |
| % Reflections used in Rfree(|F|>0) | 5.0 |
| R.m.s. deviations, bond (Å) lengths | 0.011 |
| R.m.s. deviations, bond angles (°) | 1.24 |
| Ramachandran plot (% most favored, % additional allowed residues, % disallowed residues) | 96.8 |
| 3.2 | |
| 0.0 | |
| Estimated standard uncertainty2 (Å) | 0.070 |
| Coordinate error (Luzatti plot) (Å) | 0.237 |
| Model | |
| No. of atoms | |
| Protein (including alternate conformations) | 1518 |
| Water molecules | 286 |
| Average B-factors (Å2) | |
| Protein main chain atoms | 16.9 |
| Protein side chain atoms | 21.5 |
| Ligand | 15.2 |
| Water molecules | 29.5 |
1
Rsym=ΣhklΣi|Ii(hkl)- I(hkl)|/ ΣhklΣi(I(hkl)) where Ii(hkl) is the intensity of an individual measurement, and I(hkl) is the mean intensity of this reflection.
‡
R factor = Σ hkl |Fobs| - |Fcalc | / Σ hkl | Fobs |, where |Fobs| and |Fcalc| are observed and calculated structure factor amplitudes, respectively. The values in parentheses for completeness, Rsym and I/σ correspond to the highest resolution shell.
2
Estimated standard uncertainty, diffraction precision index (DPI), based on Rfree 46