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Fig. S1. Stabilization along the reaction by the enzyme environment (MM region) .

Fig. S2. Free energy profiles (potentials of mean force) obtained from AM1/CHARMM27 umbrella-sampling MD simulations.

Fig. S3. Potential energy along RC1 of the QM region and the MM region only for seven AM1/CHARMM27 profiles.

Fig. S4. Structures from AM1/CHARMM27 profiles indicating the conformational changes that allow solvation of Asp38 Oδ1.

Table S1. Geometric measurements in key structures from the B3LYP/6-31+G(d)/CHARMM27 optimized potential energy profile.

Table S2. Geometric measurements from QM and QM/MM optimized conformations of methanol hydrogen bonded to O3 in the reactant, intermediate and product of the 5–androstene-3,17–dione to 4–androstene–3,17–dione reaction.

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