Refinement statistics.
| Resolution range | 18.0 to 1.77 Å |
| Reflections in working set | 82,005 |
| Reflections in test set | 2541 |
| R cryst * | 20.20% |
| R free † | 22.7% |
| Number of non-hydrogen protein atoms | 5554 |
| Number of solvent molecules | 751 |
| RMS deviation from ideal | |
| Bond lengths | 0.0050 Å |
| Bond angles | 1.13° |
| Bfactor | |
| Average protein | 26.5 |
| Average solvent | 38.5 |
| RMS bonded atoms | 0.554 |
↵* Rcryst = Σhkl∥Fobs| − |Fcalc∥/Σ|Fobs|, where Fobs and Fcalc are the observed and calculated structure factor amplitudes, respectively, for the hklreflections.
↵† Rfree is calculated for a set of reflections that were not included in atomic refinement (33). Both Rcryst andRfree are calculated with no σ cutoff.