Supplementary data: Computational docking of lactic acid bacteria-derived metabolites against NDM-1

Ten LAB-derived metabolites: benzoic acid, 3-phenyllactic acid, Cyclo(L-Leu-L-Pro) (Gancidin W), Cyclo(L-Phe-L-Pro), reuterin, Cyclo(L-Pro-L-Val), Cyclo(L-Phe-trans-4-hydroxy-L-Pro), phenylacetic acid, 4-hydroxyphenyllactic acid, and diacetyl were evaluated by blind molecular docking against the NDM-1 crystal structure (PDB: 3ZR9) using CB-Dock2. For each ligand, all predicted binding pockets were examined in descending order of Vina score and cross-checked against six catalytic residues (His120, His122, His189, Asp124, Cys208, His250) spanning the enzyme's dizinc active site; the highest-scoring pocket showing genuine catalytic-residue engagement, rather than the highest-scoring pocket overall, was retained as the validated result.