Table 2. Refinement statistics.
| High resolution A52 | Low resolution A52 | B14 | |
| Space group | P21 | R3∶H | C2 |
| Resolution limits (Å) a | 33.8–1.9 (1.95–1.90) | 40.1–2.8 (2.89–2.75) | 46.3–2.7 (2.76–2.70) |
| Reflections in working set a | 29,385 (2,161) | 19,183 (2,611) | 36,439 (2,577) |
| Reflections in test set a | 1,571 (86) | 988 (135) | 1,783 (99) |
| R factor of working set a, b | 0.177 (0.252) | 0.181 (0.287) | 0.223 (0.381) |
| R free (%) a, b, c | 0.215 (0.298) | 0.192 (0.302) | 0.244 (0.412) |
| Number of atoms (protein/water) | 2,508/207 | 2,516/0 | 4,632/0 |
| Number of atoms with alternate conformations (protein/water) | 36/0 | 12/– | 0/– |
| Residues in Ramachandran favoured region (%) | 99.3 | 98.0 | 97.7 |
| Ramachandran outliers (%) | 0.0 | 0.0 | 1.4 |
| rmsd bond lengths (Å) | 0.010 | 0.005 | 0.005 |
| rmsd bond angles (°) | 1.107 | 0.816 | 0.777 |
| Average B factors (Å2) (protein/water) | 29.6/38.0 | 81.7/– | 62.5/– |
a
Numbers in parentheses are for the highest resolution shell.
b
R = Σhkl∥F obs (hkl)|−|F calc (hkl)∥/Σhkl |F obs (hkl)|, where |F obs (hkl)| and |F calc (hkl)| are the observed and calculated structure facture amplitudes.
c
R free equals the R-factor of test set (5% of the data removed prior to refinement).