| At a functional site |
4 |
0 |
0 |
| Closer than 4 Å to a critical site |
7 |
2 |
1 |
| Closer than 3 Å to a critical site |
2 |
1 |
0 |
| Closer than 4 Å to a ligand |
11 |
8 |
4 |
| Closer than 3 Å to a ligand |
4 |
3 |
0.6 |
| Normalised accessibility (ACC) ≤ 5% |
41 |
23 |
17 |
| ACC ≤ 5% and change in hydrophobic propensity >0.75 |
21 |
6 |
2 |
| ACC ≤ 5% and change in volume >60 Å3 (overpacking) |
6 |
2 |
0 |
| ACC ≤ 5% and change in volume >–60 Å3 (cavity creation) |
2 |
2 |
0.6 |
| ACC ≤ 5% and change in electrostatic charge |
12 |
4 |
1 |
| ACC < 25% |
67 |
45 |
34 |
| ACC < 25% and absolute change in hydrophobic propensity >0.75 |
33 |
14 |
5 |
| ACC < 25% and change in volume >60 Å3 (overpacking) |
9 |
4 |
1 |
| ACC < 25% and change in volume >–60 Å3 (cavity) |
5 |
4 |
1 |
| ACC < 25% and change in electrostatic charge |
22 |
9 |
4 |
| Normalised crystallographic B-factor <–0.5 |
44 |
29 |
24 |
| Loss of a hydrogen bond |
13 |
8 |
5 |
| Loss of a disulphide bridge |
1.3 |
0.6 |
0 |
| Proline in α-helix |
3 |
1.2 |
0.4 |
| Substitution of Gly with torsion angles forbidden for other amino acids |
1.2 |
0.9 |
0.4 |
