Table 2. Residue-wise electrostatic interaction energies between KLK7 and the bound peptide. Electrostatic terms from the applied force field have been extracted to investigate energetic consequences of the observed transition in the binding mode and are presented as average and standard deviation in brackets. All residues show a net gain of electrostatic interactions when comparing the native binding pose (0.0–2.0 μs) with the inverted mode (3.0–10.0 μs).

Eel/kcal/mol	Ala-1	Ala-2	Pro-3	Phe-4
0.0–2.0 μs	−5.0 (1.7)	−5.8 (1.9)	−1.7 (1.9)	−16.2 (5.0)
3.0–10.0 μs	−5.6 (4.2)	−6.2 (2.8)	−6.0 (2.7)	−16.6 (5.6)
Difference	−0.7	−0.4	−4.3	−0.3