Overall, these observations imply moderate predictiveness of the SASA of residue B24, since a low value at this site generally indicates that the structure is very likely to have more, or at least comparable proteolytic stability compared to the wild type. Notably, most proteolytically unstable glycoforms, including GF 2, GF 3, GF 4, GF 6, GF 7, and GF8, had the same level of SASA at residue B24 as the wild type. This could be attributable to the situation where the residue of the wild type is already very solvent-exposed, leaving considerably less space for the proteolytically unstable glycoforms to have an even higher SASA value. This limitation is intrinsic to both Metric 1 and Metric 2, motivating us to look for more reliable predictors for proteolytic stability.