Table 5. X-ray data collection and refinement statistics of the N-terminal truncated (Δl–80) human MetAP1 (tHsMetAP1) in complex with 26d.
| Crystal | tHsMetAP1 w. 26d |
|---|---|
| Space group | P21 |
| Cell dimensions | |
| a (Å) | 47.5 |
| b (Å) | 77.4 |
| c (Å) | 48.0 |
| β (deg) | 90.9 |
| X-ray data collection statistics | |
| X-ray Source | FR-E+/Raxis IV |
| Wavelength (Å) | 1.54178 |
| Resolution range (Å) (HighRes shell) | 50.00-2.09 (2.16-2.09) |
| Collected Reflections | 71,126 |
| Unique Reflections | 20,226 |
| I/σ | 29.6 (2.8) |
| Completeness (%) | 97.9 (86.6) |
| Rmerge (%) | 11.7 (49.0) |
| Refinement statistics | |
| Rcryst (%) | 0.18 (0.27) |
| Rfree (%) | 0.25 (0.33) |
| R.m.s deviations | |
| Bond length (Å) | 0.013 |
| Angle (deg) | 1.1533 |
| Monomer in ASU | 1 |
| Total Atoms | 2,586 |
| Protein atoms | 2,400 |
| Water molecules | 152 |
| Ligand | 34 |
| B-factor (ΔHsMetAP1)(Å2) | 41.8 |
| B-factor (26d)(Å2) | 62.0 |
| B-factor (H2O)(Å2) | 55.0 |