In addition to the cleavage sites PheB25 and TyrB26, we hypothesized that their adjacent residues along the N-terminal direction, namely, the P1 residues according to Schechter-Berger nomenclature were also important. In Schechter-Berger nomenclature, the residues N-terminal to the cleavage site are denoted as P1, P2, P3, . . . etc., while the residues in the opposite direction are denoted as P1', P2', P3' ... etc. See Figure . Specifically, the hydrophobicity of the P1 residue was found to be important in the molecular recognition of 𝛼-chymotrypsin , as the deep hydrophobic pocket formed by Ser189, Gly216, and Gly226 in 𝛼-chymotrypsin requires the P1 residue to be hydrophobic as well . Given the fact that the P1 residue itself needed to be sufficiently solvent-exposed to contact and fit in this hydrophobic pocket of 𝛼-chymotrypsin, we hypothesized that a glycoform would be more proteolytically stable if its P1 sites were less solvent accessible due to the steric hindrance by the glycan moiety. Therefore, we calculated the residue SASA of PheB24 and PheB25, which were the P1 sites corresponding to the cleavage sites PheB25 and TyrB26, respectively. DCLM was used to generate the SASA time series, which was then truncated and decorrelated with the same method as the one used in Metric 1. Similarly, the final reported value of each glycoform is the value averaged across simulations starting from the five different wild-type structures, with the uncertainty being the standard deviation of the 5 runs. The monotonicity of the relationship between the metric and the experimental data was assessed by Kendall's tau correlation coefficient (𝜏) , with its uncertainty calculated using the method described in section 2.3. Additionally, in the supporting information (Figures S4), we examined the correlations between any two of the four SASA measures in Metric 1 and Metric 2, including the scissile bond SASA of B26-B27 and P1 site SASA of residues B24 and B25.