Table 1. Paraplegin crystal structure: Data collection and refinement statistics.
| Structure | Paraplegin |
| Ligand | ADP |
| PDB entry | 2QZ4 |
| Beamline | ID 14-2 |
| Wavelength (Å) | 0.9330 |
| Space group | P4322 |
| Cell dimensions | |
| a, b, c (Å) | 57.2, 57.2, 157.2 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Resolution (Å) | 40.0–2.2 (2.3–2.2) |
| Rsym | 0.069 (0.203) |
| I/(σI) | 23.7 (7.2) |
| Completeness (%) | 99.1 (62.7) |
| Redundancy | 10.6 (4.7) |
| Refinement | |
| Resolution (Å) | 39.1 – 2.2 |
| No. reflections | 12529 |
| Rwork †/Rfree ‡ | 0.209/0.269 |
| No. atoms | |
| Protein | 1680 |
| Ligands | 27 |
| Water | 55 |
| B-factors (Å2) | |
| Protein | 56.1 |
| Ligands | 40.2 |
| Water | 55.6 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.015 |
| Bond angles (°) | 1.6 |
| Ramachandran plot | |
| Favored regions (%) | 94.9 |
| Disallowed regions (%) | 0.9 |
Values for the highest resolution shell are shown in parentheses.
†
Rwork is defined as Σ||Fobs|−|Fcalc||/Σ |Fobs|, where Fobs and Fcalc are observed and calculated structure-factor amplitudes, respectively.
‡
Rfree is the R factor for the test set (5–10% of the data).