Table 1.
Structural statistics of the APETx1 structures in the present study (recombinant protein; 20 conformers) and previous study (natural product; 25 conformers) [27]
| Natural product [27] | Recombinant protein | |
|---|---|---|
| PDB code | 1WQK | 7BWI |
| Experimental conditions | pH 3.0 and 280 K | pH 6.0 and 298 K |
| Distance restraints | ||
| Total NOE-derived restraints | 751 | 766 |
| Intraresidue restraints (|i-j| = 0) | 366 | 131 |
| Sequential restraints (|i-j| = 1) | 140 | 216 |
| Short-range restraints (2 ≤ |i-j| ≤ 4) | 61 | 94 |
| Long-range restraints (|i-j| ≥ 5) | 184 | 325 |
| Disulfide bond restraints | 9 | 12 |
| Dihedral angle restraints | 20 | 41 |
| Hydrogen-bond restraints | 36 | – |
| Root-mean-square deviation (RMSD) from mean coordinate structure (Å)a | ||
| Backbone heavy atoms | ||
| Residues 1–42 | 0.82 ± 0.17 | 0.66 ± 0.21 |
| Residues 2–41 | 0.63 ± 0.13 | 0.48 ± 0.12 |
| All heavy atoms | ||
| Residues 1–42 | 1.28 ± 0.17 | 1.01 ± 0.15 |
| Residues 2–41 | 1.13 ± 0.15 | 0.95 ± 0.14 |
| Analysis of the Ramachandran plot (%)b | ||
| Residues in favored regions | 84.3 | 93.7 |
| Residues in allowed regions | 14.0 | 5.6 |
| Ramachandran outliers | 1.7 | 0.6 |
aRoot-mean-square deviation (RMSD) is calculated by MOLMOL [30]. bStereochemical quality is evaluated according to MolProbity (http://molprobity.biochem.duke.edu/)