TABLE 1.
Data collection and refinement statistics
Each data set was obtained from a single crystal. The values in parentheses are for the highest resolution shell.
| BI 201335 | Analog 1 | |
|---|---|---|
| Data collection | ||
| Space group | P61 | P61 |
| Cell dimensions | ||
| a, b, c (Å) | 94.9, 94.9, 81.9 | 95.0, 95.0, 81.8 |
| α, β, γ (°) | 90.0, 90.0, 120.0 | 90.0, 90.0, 120.0 |
| Resolution (Å) | 40.0-1.9 (1.97-1.90) | 40.0-2.3 (2.38-2.30) |
| Rmerge | 7.3 (61.2) | 4.8 (38.3) |
| I/σI | 12.6 (2.3) | 23.2 (4.9) |
| Completeness (%) | 98.0 (85.4) | 98.6 (88.6) |
| Redundancy | 10.6 (5.8) | 10.6 (7.7) |
| Refinement | ||
| Resolution (Å) | 1.9 | 2.3 |
| No. reflections | 30638 | 17940 |
| Rwork/Rfree | 20.2/24.2 | 21.7/25.5 |
| No. atoms | ||
| Protein | 2834 | 2834 |
| Ligand/ion | 116 | 114 |
| Water | 176 | 66 |
| B-factors | ||
| Protein | 37.9 | 48.5 |
| Ligand/ion | 32.5 | 46.7 |
| Water | 45.8 | 44.9 |
| Root mean square deviations | ||
| Bond lengths (Å) | 0.010 | 0.009 |
| Bond angles (°) | 1.13 | 0.98 |