Fig. 6: Structural evaluation of designs.
From: Simultaneous enhancement of multiple functional properties using evolution-informed protein design
A Structural alignment of the crystal structure of 70.a (top, blue), 80.a (middle, yellow) and 80.b (bottom, teal) with WT TEM-1 (PDB: 1XPB, silver). Catalytic residues-E166 and S7074-are circled in red and their side chains are in stick representation. B Highlight of the mutations (red sections of the ribbons) in each design relative to WT TEM-1. Catalytic residues (E166 and S70) marked as in [A]. C Structural superimposition of 70.a (blue), 80.a (yellow) and 80.b (teal) with publicly available β-lactamase structures (silver, 927 protein chains from 542 PDB entries). [C, inset] Distribution of structural similarity (root mean square deviation in Cα atomic positions, RMSD) of each publicly available β-lactamase structure relative to WT TEM-1 (PDB: 1XPB). RMSD of each design: marginal ticks on the x-axis. D The relationship between sequence identity and Cα backbone structural similarity (RMSD) for the same publicly-available β-lactamase structures as in [C] and the three designs. Colors as in [C]. Source data are provided in the Source Data file.
