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. 2021 Jul 19;9(7):800. doi: 10.3390/vaccines9070800

Figure 2.

Figure 2

Predicted 3D structure of PB1 showing mutations in residues 48 and 391 and respective molecular interactions between them. Three-dimensional structure predictions using iTASSER of the B/Bris PB1 protein sequence and potential interactions at the interface of amino acids 48 and 391. Blue lines represent the presence of hydrogen bonds. Dotted yellow lines indicate predicted distances in angstroms (Å). (A) Potential interaction via a single hydrogen bond and a predicted distance of 1.856 Å between amino acids 48E and 391K in the wt PB1. (B) Lack of predicted hydrogen bonds and a predicted distance of 5.714 Å between amino acids 48E and 391E in the PB1 3M protein. (C) Amino acids 48K and 391E restore the predicted single hydrogen bond interaction and a distance of 1.809 Å between these two amino acids in the PB1att 4M protein.