The authors have disclosed no conflicts of interest. The data that support the findings of this study are available on request from the corresponding author. The data are not publicly available due to privacy or ethical restrictions. Figure S1. Schematic diagrams of wild-type and mutant structures of the B119 protein, with Ramachandran plot analysis assessing the stereochemical quality of the predicted models. Predicted structures of the wild-type (A) and mutant (B) B119 protein. Structural comparison of site P234 in the wild-type (C) and site L234 in the mutant (D). The Ramachandran plots for wild-type (E) and mutant (F) B119 protein display the distribution of φ (phi) and ψ (psi) dihedral angles for all residues. Residues in most favored, additionally allowed, generously allowed, and disallowed regions are indicated. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Shi et al. (Thu,) studied this question.