(A) The cartoon representation of SafD-SafANte. The SafD is colored in red and SafANte in green. The residues, Leu4, Gln9, Lys11, Val13, Ile15, Phe17, corresponding the P** and P1-P5 pockets, respectively, are shown in stick representation. (B) The topology diagram of SafD-dsc. The secondary structure of SafD is colored in red. The complementing G strand is colored in green. The artificial linker DNKQ is highlighted with dotted line. (C) Electrostatic surface of SafD-dsc. The surface is colored with electrostatic potential (blue for positive charge and red for negative charge). (D) Structural superimposition of SafD-dsc molecules presented in this report. The residue Tyr13 in LoopA-B is highlighted and shown in stick representation. (E) Sequence alignment of SafD, SefD, AfaD, DraD and AggB adhesins. The β-strands of SafD are shown with arrows on top of the sequences. The highly and relatively conserved residues are indicated with ‘*' and ‘:', respectively. Tyr13 is underscored and colored in red. Residues delineating the P** pocket are shown in green.