Figure 4. In silico characterization of the SNARE complexes bearing the Asp68His and the Ile51Ser variant.

1. Representation of the SNARE complex with Asp68 highlighted (top). BET1^Asp68 is involved in a hydrogen bond with SEC22b^Lys169, with the most probable conformation of His68 in the mutant variant (bottom).
2. Stability of hydrogen bonds between BET1^Asp68 and BET1^Asp72 respectively was estimated using molecular dynamics simulation in three replicas. Parameter occupancy could be more than 100% if several stable hydrogen bonds could be established by residue. Bars represent average fraction of the simulated time the residue is involved in a hydrogen bond(s). Data represented are mean ± SD.
3. Sequence conservation of the corresponding regions of BET1 and SEC22b animal proteins. The relevant residues involved in hydrogen bond network are highlighted by color, hydrogen bonds are shown.
4. Representation of the SNARE complex with Ile51 (upper) and Ser51 (lower) residues highlighted.
5. Sequence conservation of the corresponding regions of BET1 and SEC22b and the relevant residues involved in the hydrophobic patch formed by Ile51 BET and SEC22b^Ile148.