Table S1 - Changing Folding and Binding Stability in a Viral Coat Protein: A Comparison between Substitutions Accessible through Mutation and Those Fixed by Natural Selection

FoldX estimates of ΔΔGfold and ΔΔGbind for all 8094 possible single substitutions in the φX174 F protein relative to the reference sequence. site is the residue number. Note in protein F the first amino acid, methionine, is removed after translation. Numbering begins after its removal. aa.from and aa.to are the amino acids in the reference and the mutant respectively. within.1.DNA.change indicates substitutions that can be accessed by a single DNA change from the reference sequence (1 = yes, 0 = no). wild.phg.sub indicates substitutions we infer occurred in the evolution of the φX174-like wild phage by comparison of them with their consensus sequence (1 = yes, 0 = no). lab.exp.sub indicates substitutions found in a lab adaptation experiment (see paper for source of experiments; 1 = yes, 0 = no). ddG.fold and ddG.bind give changes in folding and binding stability, ΔΔGfold and ΔΔGbind, respectively. (TXT)