were subsequently positioned at the shared binding cavity, thereby forming an initial configuration of the entire antibody-analyte-antibody ternary complex. To minimize the production of sterically clashing ternary complexes, the conformations of the model analytes were automatically adjusted to adopt an extended conformation. Simulations described herein were carried out with the SANDER module of the AMBER 4.1 molecular dynamics simulation package (San Francisco, CA, USA). First, the generated ternary complex structure was solvated and neutralized in a box with TIP3P water with a minimum of 10 Å between the model and a wall of the box. The structure was initially subjected to energy minimization (1000-time steps) to remove unreasonable atomic contacts. Afterward, the prepared system was equilibrated using a canonical (NVT) ensemble, followed by an isothermal-isobaric (NPT) ensemble. Finally, 100 ns molecular dynamics simulations were carried out at normal temperature and pressure (300 K and 1.01325 bar, respectively), wherein a time step of 2 fs was applied using the SHAKE algorithm to fix the bonds involving hydrogen atoms. A brief protocol of the antibody-analyte-antibody ternary complex construction is provided and schematized in the Supplementary Information.