Table 1.
Statistics on diffraction data and structural refinement.
| Data collection | |
| Space group | C2 (C121) |
| Unit cell (a, b, c, Å) | 115.01, 115.34, 68.51, 90, 108.1, 90 |
| Resolution (Å) | 30.00 – 1.65 |
| Unique reflections | 92,150 |
| Fold of redundancy | 6.8 |
| Completeness (%) | 90.9 (54.8a) |
| Average I/δ | 13.2 (2.7a) |
| Rmerge | 0.059 (0.285a) |
| Structure refinement | |
| R-factor | 0.203 |
| R-free | 0.223 |
| Reflections | 87,881(8781b) |
| RMS deviation for bond (Å) | 0.005 |
| Angle (degree) | 1.06 |
| Average B-factor (Å2) | |
| Protein(# of atoms) | 31.8 (5272) |
| Waters(# of atoms) | 36.7 (404) |
| Zn(# of atoms) | 26.8 (2) |
| Mg(# of atoms) | 26.0 (2) |
| Ramachandran plot statistics (%) as defined in CCP4 | |
| Most favored regions | 91.7 |
| Additionally allowed regions | 7.7 |
| Generously allowed regions | 0.7 |
| Disallowed regions | 0.0 |
a
For the resolution shell of 1.71–1.65 Å.
b
Reflections omitted for calculation of R-free.