Our hypothesis suggests that glycoforms whose P1-P3 region has a lower 𝛽-sheet propensity should potentially have higher proteolytic stability. However, most of the residues, including B22, B23, and B24 did not show this trend, while residue B25 did show predictiveness of roughly the same level as Metric 1 since it showed the lowest 𝛽-sheet propensity for the most proteolytically stable structures (GF 10 and GF 13). Notably, even if one of the four residues exhibited moderate predictiveness, the generally large error bars in the 𝛽-sheet propensity undermine its usage as a metric to capture structural determinants that influenced the proteolytic stability of the structure. These large error bars in the case of B22 to B24 also imply that the structure at these sites can adopt a wide range of orientations, contradicting our hypothesis that the glycoforms able to prevent proteolytic degradation should have common orientations at these sites due to high free energy costs of structural re-orientations or transformations. Similar to the first two metrics, we note that these large error bars are not necessarily the results of the starting model bias, since the 𝛽-sheet propensity was calculated from the orientations of just a few atoms, which naturally caused larger fluctuations of the results. Since the metric is insufficient to assess the proteolytic stability, whether or not the large error bars can be ascribed to the starting model bias is not relevant.