Table 1.
Data collection and refinement statistics
| Data collection | |
|---|---|
| Space group | C2 |
| Cell dimensions | |
| a, b, c (Å) | 634.9, 122.0, 264.4 |
| α, β, γ (°) | 90.00, 112.9, 90.00 |
| Resolution (Å) | 48.8–6.0 (6.27–6.0) |
| R meas | 0.34 (2.53) |
| I/σI | 5.17 (0.92) |
| Completeness (%) | 99.5 (99.9) |
| Redundancy | 6.2 (6.4) |
| Refinement | |
|---|---|
| Resolution (Å) | 48.8–6.0 |
| No. reflections | 46729 |
| R work/R free | 28.9/32.2 |
| No. atoms | |
| Protein/Ligand | 34,018/422 |
| B‐factors (Å2) | |
| Protein/Ligand | 352.3/528.0 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.004 |
| Bond angles (°) | 0.911 |
| Clash score | 1.54 |
| Ramachandran plot (%) | |
| Favored/Allowed/Outliers | 95.3/4.2/0.5 |
Data from two crystals were merged. The resolution limit was chosen according to CC(½), which has values of 0.99 and 0.31 for the resolution shells 48.8–6.0 and 6.27–6.0 Å, respectively. Using I/σ(I) = 2 in the outer shell as criteria, the maximum resolution would be around 7 Å. Refinement statistics does not include any contribution from FP, and the model is therefore only 82% complete. R meas is the redundancy independent R‐factor on intensities. Values in parentheses are for highest resolution shell.