TABLE 1.
Crystallographic data collection and refinement statistics
| Parameter (unit) | Value |
|---|---|
| Space group | C-2 |
| Molecules per asymmetric unit | 2 |
| Cell constants | |
| a (Å) | 118.46 |
| b (Å) | 76.91 |
| c (Å) | 98.01 |
| β (degree) | 116.16 |
| Resolution (Å)a | 1.80 (1.84-1.80) |
| Total observations | 230,232 |
| Unique reflections | 64,997 |
| Rmerge (%) | 6.2 (17.9) |
| Completeness (%) | 88.9 (96.4) |
| 〈I〉c/〈σ〉 | 29.1 (7.5) |
| Resolution range for refinement (Å) | 20-1.80 |
| No. of protein residues | 709 |
| No. of water molecules | 254 |
| Rmsd bond lengths (Å) | 0.015 |
| Rmsd bond angles (degree) | 1.77 |
| R factor (%) | 20.5 |
| Rfree (%)b | 25.1 |
| Average B factor, protein atoms (Å2) | 31.9 |
| Average B factor, ligand atoms (Å2) | 43.2 |
| Average B factor, solvent atoms (Å2) | 36.1 |
a
Values in parentheses are for the highest resolution shell.
b
Rfree was calculated with a percentage of 4.0 of reflections set aside randomly.
c
〈I〉, average intensity.