Table 2.
Refinement statistics
| TR-I | TR-II | |
|---|---|---|
| Resolution range, Å | 10.0–2.4 | 10.0–2.3 |
| Reflections used in refinement, no. | 18,143 | 10,999 |
| R factor | ||
| Work set | 0.155 | 0.205 |
| Test set | 0.248 | 0.306 |
| Test set size, % | 5 | 6 |
| No. of atoms | ||
| Protein | 3,828 | 1,922 |
| Cofactor | 96 | — |
| Water | 98 | 103 |
| rms deviation from ideal value (protein) | ||
| Bond length, Å | 0.008 | 0.008 |
| Bond angle, degrees | 0.97 | 1.33 |
| Dihedral angle, degrees | 24.73 | 23.37 |
| Improper angle, degrees | 1.72 | 1.10 |
| Residues in most favored regions of Ramachandran plot, % | 90.4 | 90.0 |
| Average B factor, Å2 | ||
| Main chain | 17.22 | 30.17 |
| Side chain | 23.18 | 33.09 |
| Cofactor | 16.10 | — |
| Solvent | 26.99 | 36.44 |
R factor = ∑ (|Fo| − |Fc|)/∑ |Fo|, where |Fo| and |Fc|, respectively, are the observed and calculated structure factor amplitudes.