TABLE 1.
Crystallographic data
| Data collection statistics | |
| Space group | P212121 |
| Number of molecules per asymmetric unit | 1 |
| a (Å) | 42.348 |
| b (Å) | 47.868 |
| c (Å) | 90.715 |
| α = β = γ (°) | 90 |
| Wavelength (Å) | 1.5418 |
| Resolution range (Å)a | 1.70–10.52 (1.70–1.76) |
| Completeness (%)a | 97.2 (93.9) |
| Redundancya | 11.7 (9.5) |
| Rmerge (%)a | 6.4 (47.3) |
| Refinement statistics | |
| Total number of reflections (reflections in R-free set) | 20,304 (2,066) |
| Rfactor (%) | 17.93 |
| Rfree (10% free test set) (%) | 22.30 |
| Number of atoms | 1719 |
| Protein | 1507 |
| Water | 138 |
| Ions | 41 |
| Inhibitor | 33 |
| r.m.s.d. | |
| Bond length (Å) | 0.012 |
| Bond angle (°) | 1.417 |
| Average atomic B-factor (Å2) | 16.372 |
| Protein (Å2) | 14.99 |
| Water (Å2) | 30.57 |
| Ions (Å2) | 35.20 |
| Inhibitor (Å2) | 15.78 |
| Wilson B-factor (Å2) | 21.585 |
| Luzzati sigma A coordinate error (observed) (Å) | 0.12 |
| Luzzati sigma A coordinate error (R-free set) (Å) | 0.11 |
| Ramachandran plot (non-Gly, non-Pro residues) | 159 (100%) |
| Residues in favored positions | 146 (91.8%) |
| Residues in allowed positions | 13 (8.2%) |
| Residues in disallowed positions | 0 (0%) |
a Items in parentheses refer to the highest resolution shell.