Table 1. Summary of diffraction data and structure refinement statistics.
| Diffraction data | |
| Wavelength (Å) | 0.9786 |
| Space group | C2 |
| Cell parameters | |
| a, b, c (Å) | 126.4, 39.3, 87.7 |
| α, β, γ (°) | 90.0, 122.1, 90.0 |
| Resolution (Å) | 50.0–2.40 (2.49–2.40)a |
| Observed reflections | 52 870 |
| Unique reflections (I/σ(I) > 0) | 14 322 |
| Average redundancy | 3.7 (3.7) |
| Average I/σ(I) | 18.0 (3.6) |
| Completeness (%) | 97.9 (97.9) |
| R merge (%)b | 7.8 (52.2) |
| Refinement and structure model | |
| Reflections (Fo ≥ 0σ(Fo)) | |
| Working set | 12 912 |
| Test set | 680 |
| R-factor/Free R-factorc | 0.233/0.260 |
| Average B factor (Å2) | |
| All atoms | 49.0 |
| Protein | 49.4 |
| Ligand/ion | 40.2/41.1 |
| Water | 38.5 |
| RMS deviations | |
| Bond lengths (Å) | 0.007 |
| Bond angles (°) | 1.2 |
| Ramachandran plot (%) | |
| Most favored regions | 95.8 |
| Allowed regions | 3.9 |
aNumbers in parentheses refer to the highest resolution shell.
b R merge = ΣhklΣi|Ii(hkl)i - <I(hkl)> |/ΣhklΣiIi(hkl).
c R-factor = Σhkl| |Fo | - |Fc | |/Σhkl|Fo |.