TABLE 2.
Structure refinement statistics
| Statistics | |
|---|---|
| Resolution range (Å) | 38.4−1.55 (1.59−1.55) |
| Reflections | 56,424 (4,241) |
| σ cutoff | None |
| R-value (all) (%) | 12.67 |
| R-value (R-work) (%) | 12.39 (18.1) |
| Free R-value (%) | 17.99 (24.9) |
| Root mean square deviations from ideal geometry | |
| Bond length (Å) | 0.013 |
| Angle (degrees) | 1.61 |
| Chiral (Å) | 0.102 |
| No. of atoms | |
| Protein | 3,175 |
| CAPSO | 30 |
| Water | 451 |
| Mean B-factor (Å2) | |
| All atoms | 22.2 |
| Protein atoms | 20.6 |
| Protein main chain | 18.2 |
| protein side chain | 23.1 |
| CAPSO | 30.4 |
| Water | 33.8 |
| Molprobity Ramachandran plot statistics | |
| Residues in favored regions (%) | 99.6 |
| Residues in allowed regions (%) | 100.0 |
| Residues in disallowed region (%) | 0.0 |