TABLE 1.
Crystallographic statistics
All numbers in parentheses refer to the highest resolution shell statistics.
| Data collection | |
|---|---|
| Wavelength (Å) | 1.00 |
| Space group | P212121 |
| Cell dimensions | |
| a, b, c (Å) | 69.4, 77.2, 84.3 |
| α, β, γ (°) | 90, 90, 90 |
| Resolution range (Å) | 50–2.4 (2.49–2.40) |
| Redundancy | 4.5 |
| Unique reflections | 17,475 |
| Completeness (%) | 98.5 (99.9) |
| I/σ(I) | 25.9 (2.8) |
| Rsyma | 0.057 (0.607) |
| Refinement | |
| Resolution range (Å) | 37.0–2.40 (2.55–2.40) |
| No. of reflections | 16,795 |
| R-factor/Free R-factorb | 0.203/0.252 |
| No. of atoms | |
| Protein | 2066 |
| Ligand | 24 |
| Water | 53 |
| Average B-values (Å2) | |
| Protein | 50.1 |
| Ligand | 35.7 |
| Water | 40.4 |
| r.m.s.c deviations | |
| Bond lengths (Å) | 0.006 |
| Bond angles (°) | 1.3 |
| Ramachandran plot | 89.3, 9.4, 0.9, 0.4 |
a Rsym = σ |Iavg − Ii|/σIi, where Ii is the observed intensity and Iavg is the average intensity.
b Free R-factor is calculated for 5% of randomly selected reflections excluded from refinement.
c r.m.s., root mean square.