The accuracy of force fields is of utmost importance in molecular modeling of proteins. Despite successful applications of force fields for about the past 30 years, some inherent flaws lying in force fields, such as biased secondary propensities and fixed atomic charges, have been observed in different aspects of biomolecular research; hence, a correction to current force fields is desirable. Because of the simplified functional form and the limited number of parameters for main chain torsion (MCT) in traditional force fields, it is not easy to propose an exquisite force field that is well-balanced among various conformations. Recently, AMBER-compatible force fields with coupled MCT term have been proposed, which show some improvement over AMBER03 and AMBER99SB force fields. In this work, further calibration of the torsional parameters has been conducted by changing the solvation model in quantum mechanical calculation and minimizing the deviation from the nuclear magnetic resonance experiments for some benchmark model systems and a folded protein. The results show that the revised force fields give excellent agreement with experiments in J coupling, chemical shifts, and secondary structure populations. In addition, the polarization effect is found to be crucial for the systems with ordered secondary structures.