Refinement statistics used in this paper
| Variable | Value |
| Unique reflectionsa | 30,887 |
| R factor | 18.59 |
| Rfree | 24.36 |
| Refined atoms | |
| Protein non-H atoms | 5,375 |
| Solvent | 120 |
| r.m.s. deviations | |
| Bond lengths (Å) | 0.009 |
| Bond angles | 1.173 |
| Ramachandran analysis | |
| Most favored (%) | 92.8 |
| Additionally allowed | 6.5 |
| Generously allowed | 0.3 |
| Disallowed | 0.3 |
| Variable | Value |
| Unique reflectionsa | 30,887 |
| R factor | 18.59 |
| Rfree | 24.36 |
| Refined atoms | |
| Protein non-H atoms | 5,375 |
| Solvent | 120 |
| r.m.s. deviations | |
| Bond lengths (Å) | 0.009 |
| Bond angles | 1.173 |
| Ramachandran analysis | |
| Most favored (%) | 92.8 |
| Additionally allowed | 6.5 |
| Generously allowed | 0.3 |
| Disallowed | 0.3 |
Rfree is the same for the test set (5% of the data). R factor = ∑hkl | |Fo| − k|Fc|/∑hkl |Fo|, in which k is the scaling factor, Fc is the calculated amplitude of the structure factor, and Fo is the observed amplitude of the structure factor. ESRF, European Synchrotron Radiation Facility; r.m.s., root-mean-square.
This number does not include the free R set of reflections (5% of total reflections).