. 2011 Apr 20;6(4):e18981. doi: 10.1371/journal.pone.0018981

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]).

Table 1. aFractional side-chain accessible surface area (asa) (fractional) of MotB residues that are conserved in OmpA-like PG-binding proteins.

Table 1. ^aFractional side-chain accessible surface area (asa) (fractional) of MotB residues that are conserved in OmpA-like PG-binding proteins.