Table 1.
Crystallographic data processing and refinement statistics
| Cell dimensions (Å) | a = 126.9, b = 101.3, c = 82.0 |
| Space group | P212I2 4 mole/a.u. |
| Resolution (Å) | 40.0–2.8 |
| No. of measurements | 144123 |
| No. of unique reflections | 26185 |
| Completeness (%) | 95.8 (61.3)a |
| I/σ | 6.4 (5.3) |
| Rmerge (%)b | 10.8 (28.5) |
| Refinement | |
| Rcryst (%)c | 21.4 |
| Rfree (%)d | 28.0 |
| No. of protein atoms | 7031 |
| No. of water molecules | 143 |
| Temperature factors (Å2) | |
| Main chaine | 28.4, 30.1, 24.9, 43.5 |
| Side chain | 30.4, 33.2, 28.5, 45.1 |
| Zinc ligands | 29.3, 34.2, 23.2, 52.0 |
| Zinc ion (average) | 48.0 |
| RMSD in bond lengths (Å) | 0.007 |
| RMSD in bond angles (°) | 1.32 |
a Outermost shell 2.9–2.8 Å.
bRmerge = Σ(│Ij − <I>│)/Σ<I>, where Ij is the observed intensity of reflection j and <I> is the average intensity of multiple observations.
cRcryst = Σ││Fo│ − │Fc││/Σ│Fo│, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
d 5% of the data that were used for the calculation of Rfree were randomly excluded from the refinement.
e Temperature factors for individual molecules are quoted.