Table 2. The strong interactions in the hydrophobic core that are responsible for maintaining insulin in its closed conformation.

Interaction	Distance in the crystal structure [Å]	Average distance during MD simulations where insulin stays at its closed conformation [Å]
F24(Aromatic)–L15(C)	5.2	4.6±0.5
Y26 (Aromatic)–I2A(C)	5.2	5.5±2.1
Y26(Aromatic)–L11(C)	5.2	5.8±1.3
Y26(Aromatic)–V12(C)	3.8	4.5±1.0

The distances were calculated from the center of the benzene ring (aromatic) to the nearest C atom. The same trajectory data as in Table 1 were used in calculating the average distances.