Free energy perturbation (FEP)-based absolute binding free energy (ABFE) calculations have emerged as a powerful tool for the accurate prediction of ligand-protein binding affinities in drug discovery. The restraint addition is crucial in FEP-ABFE calculations; however, due to the non-orthogonal couplings between the restrained degrees of freedom, it typically requires numerous λ windows to ensure the phase-space overlap during restraint addition. This study introduces the RED-E-function-based equilibrium parameter finder (REPF), a novel method that relies on harmonic restraints to optimize the equilibrium values in restraints, enhancing phase-space overlap and improving the convergence of the restraint addition. REPF was applied to 44 protein-ligand complexes across 5 targets and compared to restraint schemes reported in the literature. We found that REPF-optimized restraints achieve an accuracy comparable to that of the 12λ approach while using only 2λ simulations, resulting in a significant reduction in computational costs. Extensive tests confirmed the improved convergence behavior and reduced energy fluctuations of REPF-optimized restraints.