Table 2. Analyses of dimer structures.
ASA, solvent-accessible surface area (2); A np, interface nonpolar area (2); G binding, free-energy changes for alanine mutation (kcalmol1); ND, not detected.
| MST1 | MST1RASSF5 | MST2 | |
|---|---|---|---|
| Calculation of interface area | |||
| ASA of chain A | 5367.2 | 4549.6 | 5174.5 |
| ASA of chain B | 5349.6 | 4846.8 | 5120.5 |
| ASA of complex (chains A and B) | 7858.5 | 7069.3 | 7316.0 |
| Interface area of complex (chains A and B) | 2858.3 | 2327.1 | 2979.0 |
| Nonpolar surface area of chain A | 3297.3 | 2922.0 | 3324.9 |
| Nonpolar surface area of chain B | 3336.3 | 2998.8 | 3308.6 |
| Nonpolar surface area of complex (chains A and B) | 4266.6 | 4051.4 | 4239.3 |
| Interface nonpolar area (A np) | 2367.0 | 1869.4 | 2394.2 |
| Energy for h2 helices (kcalmol1) | |||
| Van der Waals energy | 589.142 | 628.296 | 622.624 |
| Electrostatic energy | 8.645 | 9.171 | 8.323 |
| Total energy | 158.142 | 221.464 | 200.955 |
| Computational alanine scan | |||
| No. of residues with G binding > 1.0 kcalmol1 | 18 | 24 | 24 |
| No. of polar residues with G binding > 1.0 kcalmol1 | 3 | 7 | 5 |
| Polar contacts | |||
| No. of inter-protomer direct hydrogen bonds | 3 | 10 | 8 |
| No. of water molecules mediating the inter-protomer interaction | ND | 6 | 1 |