The standard GOLD PLP molecular scoring function is used. This parameter set with 8 islands and 150000 operations, and select pressure 1.1, gives a more thorough calculational search for the protein-ligand energy minimum than the default setting. All amino acids that contribute to the docking score are listed in the GOLD output files, in addition are the score components, hydrogen bonding contributions, and any rotations of protein target side-chains, available for download. Of the 3 AlphaFold structures generated for each 197 P and 197 S sequences, the most reliable one is used and this is ranked by AF in a confidence estimate. In order to determine any variability in the local binding of Chlorsulfuron using the docking software GOLD, 3 spheres with different radii were used to find any dependence on the search size in Angstroms. These 3 spheres explore the surface terrain of the protein to ensure the binding site is well-defined, and it is as was found due to no change in the binding distribution from altering the search radius too much. (A very large sphere permits the docked molecule to find spots far away that may have local energy minima but no effect on protein function, i.e. multiple energy minima in binding.) There is typically a small set of major conformational modes of the ligand in a binding site, and the 3 docking limited spheres of radii 4,7,15 contain the same set and binding location, as expected if the site is welldefined. There are 500 independent docking runs used to sample the computational epitopes, each randomly initialized with different dihedral angles, and there are 6 combinations of P197/S197 with sphere radii 4,7, and 15 A.