Dataset S1: QM/MM Energy Decomposition of PEP-Inhibitory Peptides — Supporting Data for Hsu et al. 2026

Supporting dataset for the manuscript: "Post-MD QM/MM Energy Decomposition Reveals Proline-Linked Electronic Determinants of Peptide Inhibition of Prolyl Endopeptidase" (submitted to Journal of Chemical Information and Modeling). This dataset contains QM/MM interaction energy decomposition (B3LYP-D3(BJ)/def2-SVP, ORCA 6.1.0) and MM-PBSA binding free energy data for 14 food-derived prolyl endopeptidase (PEP)-inhibitory peptides (Ki = 1.27–43.83 μM). Contents (10 sheets):- README: Dataset description, naming conventions, computational details- 1-Peptide_Info: Peptide sequences, source proteins, Ki, IC50, inhibition type, Pro count- 2-QMMM_Energy_Summary: Mean ΔE_int, ΔE_SCF, ΔE_D3, CT per peptide (kcal/mol)- 3-Per_Snapshot_Energies: Individual snapshot energies (126 data points)- 4-Hirshfeld_Residue_CT: Hirshfeld charges per residue (150 residues)- 5-Pro_CT_Summary: Proline residue charge transfer analysis (27 Pro)- 6-Correlation_Statistics: Pearson/Spearman correlations (24 tests)- 7-Leverage_Analysis: Cook's distance and leave-one-out- 8-Regression_Models: R² comparison of descriptors- 9-MMPBSA_Comparison: Per-peptide MM-PBSA energy components Energy naming convention:- ΔE_int^{DFT-D3}: Total supramolecular interaction energy- ΔE_SCF: SCF/non-dispersion interaction energy- ΔE_D3: D3(BJ) pairwise dispersion interaction energy PEP structure: PDB 3DDU. MD: 100 ns, CHARMM27, GROMACS 2025.2.