TABLE 2.
Substrate binding to the dimer and the monomer
| Vdwa | Elecb | Innerc | ||
|---|---|---|---|---|
| kcal/mol | ||||
| The full substrate | ||||
| DIMER | Protomer AD | -15.57 | -890.00 | 132.64 |
| Protomer BD | -4.34 | -860.44 | 162.96 | |
| MONO | Protomer AD | -6.60 | -850.55 | 134.96 |
| Protomer BD | -4.45 | -828.80 | 128.93 | |
| P1 position of substrate | ||||
| DIMER | Protomer AD | -5.04 | -253.85 | 39.87 |
| Protomer BD | -0.42 | -217.21 | 52.28 | |
| MONO | Protomer AD | -1.82 | -219.83 | 40.20 |
| Protomer BD | 4.17 | -208.58 | 41.82 | |
a
The van der Waals energy between the substrate and the enzyme.
b
The electrostatic energy between the substrate and the enzyme.
c
The internal energy of the substrate.