Table 1.
Data Collection and Refinement Statistics
| Data collection | |
| space group | P31 |
| unit-cell parameters (Å,°) | 63.6, 63.6, 222.5 |
| Wavelength (Å) | 0.9791 |
| resolution range (Å) | 50.0–2.8 (2.85–2.80)a |
| reflections: measured | 177049 |
| reflections: unique | 24528 |
| redundancy | 7.2 (7.3) |
| completeness (%) | 98.8 (98.6) |
| average I/ σ | 31.6 (3.75) |
| Rmerge (%) | 9.9 (57.5) |
| Refinement | |
| Rcryst | 0.231 (0.270) |
| Rfree | 0.276 (0.291) |
| no. protein atoms | 5642 |
| no. of ligand atoms | 128 |
| no. water molecules | 108 |
| average B factors (Å2) | 46.0 |
| Ramachandran (%) | |
| most favored | 96.4 |
| allowed | 2.7 |
| Disallowed | 0.9 |
| rms deviations | |
| bond lengths (Å) | 0.013 |
| bond angles (°) | 1.70 |
| Chiral |
a
Values in parentheses are those for the highest-resolution shell.
b
Rmerge = Σ|I(hkl) – I| ~1/Σ|I(hkl)|, where the average intensity I is taken over all symmetry equivalent measurements and I(hkl) is the measured intensity for a given reflection.
c
Rfactor = Σ|F(obs) – F(calc)| / Σ | F(obs)|, where Rwork refers to the Rfactor for the data utilized in the refinement and Rfree refers to the Rfactor for 5% of the data that were excluded from the refinement.