TABLE 2.
Summary of diffraction data and structure refinement
| Statistica (unit) | Result |
|---|---|
| No. of crystals | 1 |
| No. of images | 244 |
| Temp (°C) | −180 |
| Space group | P21 |
| Cell parameter(s) | |
| a, b, c (Å) | 68.7, 170.5, 87.3 |
| β (°) | 95.2 |
| Resolution range (Å) | 15.0-2.70 |
| No. of observed reflections | 139,372 |
| No. of unique reflections (I/σ > 0) | 53,883 |
| Completeness (%) (2.78-2.70 Å bin) | 98.5 (96.8) |
| Rmergeb (%) (2.78-2.70 Å bin) | 9.5 (23.7) |
| Resolution range (Å) | 15.0-2.70 |
| No. of reflections | |
| (Fo ≥ σ [Fo]) (2.78-2.70 Å bin) | 53,756 (4,281) |
| Free R set (2.78-2.70 Å bin) | 2,681 (221) |
| Completeness (%) (2.78-2.70 Å bin) | 98.3 (96.6) |
| R factorc (%) (2.78-2.70 Å bin) | 22.0 (30.3) |
| Free R factor (%) (2.78-2.70 Å bin) | 23.9 (32.4) |
| No. of residues | 457 |
| No. of: | |
| Protein atoms | 3,513 |
| Zn atoms | 2 |
| Water molecules | 126 |
| Average B factor (Å2) of: | 28.8 |
| Protein main chain atoms | 28.0 |
| Protein side chain atoms | 29.8 |
| Zn atoms | 21.9 |
| Water molecules | 26.8 |
| RMS bond lengths (Å) | 0.007 |
| RMS bond angles (°) | 1.4 |
| RMS dihedral angles (°) | 23.3 |
| RMS improper angles (°) | 0.86 |
| Ramachandran plot (%) | |
| Most favored regions | 86.9 |
| Allowed regions | 12.1 |
| Generously allowed | 1.0 |
a
The first group contains statistics for diffraction data, and the second group contains statistics for refinement and model.
b
Rmerge = Σ||Io| − 〈I〉|/Σ〈I〉.
c
R factor = Σ||Fo| − |Fc||/Σ|Fo|.