Table 3.
X-ray data collection, refinement, and validation statistics
| hPNMT-19 | hPNMT-29 | |
|---|---|---|
| Data Collection | ||
| Space group | P43212 | P43212 |
| Cell dimensions: a, b, c (Å) | 94.66, 94.66, 188.46 | 94.15, 94.15, 188.16 |
| Resolution (Å)* | 38.62–1.95 (2.06-1.95) | 38.43–2.2 (2.32-2.2) |
| Total Reflections* | 1,613,327 (222,007) | 277,262 (40,988) |
| Unique Reflections* | 63,094 (8,974) | 43,470 (6,217) |
| Redundancy* | 25.6 (24.7) | 6.4 (6.6) |
| Rpim* | 0.015 (0.426) | 0.023 (0.371) |
| Mn(I/sd)* | 31.1 (1.7) | 20.5 (2.0) |
| Completeness* (%) | 99.8 (98.7) | 99.8 (99.8) |
| Refinement | ||
| Resolution (Å) | 38.62-1.95 | 38.43-2.2 |
| No. reflections | 62,657 | 43,250 |
| Rwork /R free | 0.1824 / 0.2295 | 0.1826 / 0.2207 |
| Residues modeled for molecules | A: 26-280 B: 16-280 |
A: 17-280 B: 26-280 |
| Wilson B factor | 40.22 | 47.57 |
| Number of atoms / B factor | ||
| Protein | 8,135 / 50.60 | 8,115 / 60.67 |
| Ligand (Tris) | 40 / 54.25 | 40 / 65.85 |
| Ligand (Inhibitor) | 128 / 82.59 | 128 / 63.68 |
| Water | 314 / 51 | 181 / 56.18 |
| RMS deviations | ||
| Bond lengths (Å) | 0.013 | 0.013 |
| Bond angles (°) | 1.493 | 1.443 |
| Structure Analysis | ||
| Ramachandran (%) | ||
| Most favored | 98.85 | 98.07 |
| Allowed | 1.15 | 1.93 |
| Disallowed | 0 | 0 |
*
highest resolution shell in parenthese