Table 1.
Statistics of diffraction data and structure refinement
| A. Data collection | |
| Space group | P212121 |
| Unit cell dimensions (Å) | a = 72.90, b = 86.38, c = 87.99 |
| Wavelength (Å) | 0.974 |
| Resolution range (Å) | 61.66–1.82 |
| Unique reflections | 49,689 (3441) |
| Completeness (%) | 100 (99) |
| I/σ(I) | 16.68 (3.99) |
| Rsym | 0.055 (0.25) |
| Multiplicity | 10.6 (8.7) |
| B. Refinement | |
| Working set | 47173 |
| Test set (5.1%) | 2516 |
| R-factor / Rfree (%) | 22.54 / 26.86 |
| C. Model compositions | |
| Amino acids (A and B chains) | 520 |
| Total number of protein atoms (partial occupancy) | 4171 (318) |
| Metal atoms | 2 |
| Water molecules | 527 |
| D. Stereochemistry | |
| Bond lengths (Å) | 0.02 |
| Bond angles (°) | 1.49 |
| Chiral center restrains (Å3) | 0.11 |
| E. Ramachandran plot | |
| Residues in most favored regions (%) | 97.1 |
| Residues in additional allowed regions (%) | 2.9 |
| F. Mean B-factors (Å2) | |
| All protein atoms | 15.6 |
| Main-chain atoms | 15.6 |
| Side-chain atoms | 17.1 |
| Metal ions | 13.5 |
| Water molecules | 27.1 |