Table 2. Data Collection and Refinement Statistics for gpASNase3.
| uncleaved | cleaved ASP complex | |
|---|---|---|
| PDB entry | 4O47 | 4O48 |
| Data Collectiona | ||
| X-ray source | LS-CAT, ID-G | LS-CAT, ID-G |
| wavelength (Å) | 0.978 57 | 0.979 11 |
| temperature (K) | 100 | 100 |
| resolution (Å) | 30–1.9 (2.01–1.9) | 30–2.29 (2.43–2.29) |
| number of reflections | ||
| observed | 384991 (60228) | 220590 (33863) |
| unique | 83640 (13338) | 47228 (7297) |
| completeness (%) | 99.7 (99.7) | 98.8 (96.0) |
| Rsym (%) | 5.4 (49.6) | 8.2 (59.7) |
| average I/σ(I) | 14.8 (2.6) | 15.7 (3.3) |
| space group | P3221 | P3221 |
| unit cell (Å) | ||
| a = b | 114.87 | 114.58 |
| c | 138.97 | 138.59 |
| Twinning Analysis (xtriage) | ||
| ⟨I2⟩/⟨I⟩2, (untwinned: 2.0), perfect twin: 1.5) | 1.952 | 1.604 |
| ⟨|L|⟩, (untwinned: 0.500), perfect twin: 0.375) | 0.478 | 0.385 |
| ⟨L2⟩, (untwinned: 0.333), perfect twin: 0.200) | 0.310 | 0.210 |
| twin law | no twinning | -h,-k,l |
| Refinement | ||
| refinement program | REFMAC5 | REFMAC5 |
| twinning fraction | 0.4, 0.6 | |
| Rcryst (%) | 19.3 | 18.2 |
| Rfree (%) | 21.3 | 22.1 |
| resolution range (Å) | 28.7–1.90 | 29.7–2.29 |
| no. of protein molecules per asymmetric unit | 2 | 2 |
| no. of atoms | 4456 | 4443 |
| protein (protA, protB) | 2157, 2119 | 2171, 2174 |
| aspartate | 2 × 9 | |
| water molecules | 178 | 78 |
| Na+ | 2 × 1 | 2 × 1 |
| rmsd from ideal | ||
| bond lengths (Å) | 0.013 | 0.011 |
| bond angles (deg) | 1.58 | 1.50 |
| average B factor (Å2) | ||
| protein (protA, protB) | 40.5, 45.9 | 39.5, 45.3 |
| aspartate (protA, protB) | 39.2, 47.1 | |
| water molecules | 43.5 | 37.0 |
| Na+ (protA, protB) | 36.0, 35.3 | 30.7, 36.2 |
| Ramachandran plot (%) | ||
| favored regions | 96.9 | 95.7 |
| additionally allowed regions | 2.8 | 3.9 |
| outlier regions | 0.3 | 0.3 |
a
Data for the last shell are in parentheses.