Table 3. Structure refinement.
Values in parentheses are for the highest resolution shell.
| Resolution range (Å) | 49.23–2.25 (2.31–2.25) |
| Completeness (%) | 92.2 |
| No. of reflections, working set | 188208 |
| No. of reflections, test set | 10062 |
| Final R cryst | 0.183 (0.208) |
| Final R free | 0.230 (0.293) |
| No. of non-H atoms | |
| Protein | 34093 |
| Waters | 1751 |
| Total | 35834 |
| R.m.s.d.s | |
| Bond lengths (Å) | 0.007 |
| Angles (°) | 1.606 |
| Average B factors† (Å2) | |
| Protein | 22.9 |
| Waters | 9.2 |
| Other | 9.9 |
| Ramachandran plot‡ | |
| Most favored (%) | 94.2 |
| Allowed (%) | 99.8 |
| Outliers§ (%) | 0.2 |
| PDB code | 8ed4 |
†
Calculated by BAVERAGE from the CCP4 suite (Winn et al., 2011 ▸).
‡
Calculated using MolProbity (Chen et al., 2010 ▸).
§
The outliers were AspA613, IleA811, AspC668, IleC811, AlaG304, IleG811, PheI105, PheJ105 and PheK105. The 2F o − F c electron-density maps were observed clearly for these residues at 1.1σ and most are consistent between copies in the asymmetric unit and (for AioAB) with the previously published structure.