Table I. Statistics from crystallographic analysis.
| Data collection | |
| data set | native |
| resolution (Å) | 20.0–3.2 |
| total observations | 50 139 |
| unique observations | 12 666 |
| data coverage (%) | 99.5 |
| Rsym | 0.084 |
| mean I/σ(I) | 15.9 |
| highest resolution bin | 3.29–3.20 |
| completeness | 97.2 |
| Rsym | 0.369 |
| mean I/σ(I) | 2.8 |
| Refinement | |
| resolution range (Å) | 20–3.2 |
| number of reflections (I > 0) | 12 171 |
| Rworking/Rfree (%) | 24.8/31.4 |
| number of atoms | 3627 |
| number of water molecules | – |
| r.m.s.d. bond length (Å) | 0.009 |
| r.m.s.d. bond angles (°) | 1.44 |
| mean protein main-chain temperature factor (Å2) | 41.9 |
Rsym= ΣhΣi |Ih,i – Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of symmetry-related reflections of h. R = Σ|Fobs – Fcalc|/ΣFobs, where Fobs = Fp, and Fcalc is the calculated protein structure factor from the atomic model (Rfree was calculated with 5% of the reflections). R.m.s.ds in bond lengths and angles are the deviations from ideal value.