Table 1. aFractional side-chain accessible surface area (asa) (fractional) of MotB residues that are conserved in OmpA-like PG-binding proteins.
Gly161/Gly195 | 0.00/0.00 |
Asp164/Asp198 | 0.01/0.04 |
Leu179/Leu214 | 0.00/0.00 |
Arg183/Arg218 | 0.00/0.02 |
Arg226/Arg260 | 0.01/0.03 |
Residue numbering is as in H. pylori MotB-C/periplasmic domain of Salmonella MotB.
Asa values for H. pylori MotB-C were averaged over all subunits in the asymmetric units of Form A and Form B crystals. The average values for the Salmonella MotB domain were calculated using the coordinates for the high-resolution crystal form (Research Collaboration for Structural Bioinformatics (RCSB) Protein Data Bank code 2zvy [7]).