Table 2.
X-ray diffraction data and refinement statistics.
| Data collection | |
| Space group | P4 21 2 |
| Cell dimensions | |
| a, b, c (Å) | 159.45, 159.45, 163.90 |
| α, β, γ (°) | 90.00, 90.00, 90.00 |
| Resolution (Å) | 46.45–2.5 (2.589–2.5)* |
| Total reflections | 1,202,979 (120,250) |
| No. of unique reflections | 73,419 (7223) |
| Rmerge | 0.2617 (2.503) |
| I/σI | 11.52 (1.30) |
| Completeness (%) | 99.81 (99.81) |
| Redundancy | 16.4 (16.6) |
| Refinement | |
| Resolution (Å) | |
| No. reflections | 73,312 (7214) |
| Rwork/Rfree | 0.1847/0.2341 |
| No. atoms | 2038 |
| Protein | 1275 |
| Ligand/ion | 188 |
| Water | 575 |
| Wilson B-factors | 47.35 |
| B-factors | |
| Protein | 61.26 |
| Ligand/ion | 89.53 |
| Water | 53.87 |
| R.m.s deviations | |
| Bond lengths (Å) | 0.002 |
| Bond angles (°) | 0.45 |
| Ramachandran statistics | |
| Favored (%) | 95.31 |
| Allowed (%) | 3.97 |
| Outliers (%) | 0.71 |
*Highest resolution shell is shown in parentheses.