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Figure S1. EGP enhances Db/complex stability dependent on the aromatic ring of Y159

Figure S2. The Db/EGS complex is stable at 25°C

Table I. Statistics of data collection and structure refinement

eji2764-sup-0002-suppmat.mp418037KVideo S1. Representative runs of the MD simulations performed for Db/EGS (left panel) and Db/EGP (right panel) at 350 K. The peptide-binding grove is shown in grey and the peptide in blue and orange for EGS and EGP, respectively. Peptide positions 1 and 3 as well as Y159 are highlighted. The interaction between Y159 and p3P remains conserved throughout the simulation in Db/EGP, whereas Db/EGS displays a muchincreased conformational freedom, particularly around the N terminus of the peptide.

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