Table 2. Binding Free Energies and Selected Individual Energy Contributions of PfSUB1-Peptide Complex Structuresa.
| sequence | processing site identity | ΔGEff | ΔGnonpolar | ΔGGBELE |
|---|---|---|---|---|
| LVSAD↓NIDIS | PfSUB1 | –89.6 ± 0.1 | –94.6 ± 0.1 | 5.0 ± 0.1 |
| KITAQ↓DDEES | SERA4 site 1 | –79.1 ± 0.2 | –86.3 ± 0.2 | 7.2 ± 0.1 |
| EIKAE↓TEDDD | SERA5 site 1 | –77.8 ± 0.2 | –84.1 ± 0.2 | 6.3 ± 0.1 |
| KVKAQ↓DDFNP | SERA6 site 1 | –91.8 ± 0.1 | –102.9 ± 0.1 | 11.2 ± 0.1 |
| VVTGE↓AISVT | MSP1–42 | –95.3 ± 0.1 | –104.1 ± 0.1 | 8.8 ± 0.1 |
a
All values are given in kcal/mol (±standard error of the mean); calculated for trajectory range 10–50 ns. ΔGEff = sum of the gas-phase interaction energy and the electrostatic and nonpolar contributions to desolvation upon peptide binding (ΔGEff= ΔGMM+ ΔGGB+ ΔGSA). ΔGnonpolar = sum of van der Waals contribution from the molecular mechanics force field and the nonpolar contribution to the solvation free energy (ΔGnonpolar= ΔGMM-VDW+ ΔGGBSUR). ΔGGBELE = sum of electrostatic energy as calculated by the molecular mechanics force field and the electrostatic contribution to the solvation free energy (ΔGGBELE= ΔGMM-ELE+ ΔGGB).