Table 2. Summary of text linked to residue mentions for a random sample of high-quality predictions.

PDB ID (Chain)	Protein Name	Residue(s)	Text summary
153L (A)	Goose lysozyme	Glu73a	NAG O6 directly hydrogen bonds to Glu73 OE2 [59]
1AB0 (A)	V32D/F57H Adipocyte Lipid-Binding Protein	Asp32, His57, and Cys117b	Phe57 in WT is part of the ligand binding portal, and Asp32 and His57 form a salt bridge in the mutant that controls access to the ligand binding site. Cys117 lies within the internal lipid-binding cavity [60]
1EYJ (A)	Fructose 1,6-Biphosphatase	Asp74b	Asp74 is involved in the forward reaction of this enzyme [61]
1GU9 (A)	Mtb alkhydro-peroxidase	Cys133, His137	Cys133 is a catalytic sulfhydryl group,His137 is involved in a relay to deprotonate Cys133 [62]
1I8B (B)	Chalcone synthase	Phe256a	Gly256 is in the active site in the wild type and the whole paper is about mutations to this residue, including G256F [63]
1LAR (A)	Receptor-like protein tyrosine phosphatase LAR	Leu1644	Leu1644 is responsible for inactivity of the protein and mutation to Tyr conferred robust PTPase activity to D2 domain [64]
1QOB (A)	Anabaena ferrodoxin	Gln70	Gln70 is at an interface that makes contact with a key interface but is not as critical as other residues in determining oxidation kinetics [65]
1TS2 (A)	Toxic shock syndrome toxin-1	His135, Gln136	H135A appears to reduce superantigenicity by altering properties of TCR interaction surface and is tied for the largest joint reduction in superantigenicity and lethality. Q136A causes a dramatic conformational change [66]
1XYH (A)	Human cyclophilin J	Gln52b	Gln52 expected to be an active site based on sequence alignment [67]
1YK3 (A)	Putative antibiotic resistance protein from Mtb	His130, Asp168b	His130 and Asp168 are both in the active site and have a putative roles in substrate binding and catalysis [40]

^aFamily-level NSM annotation available.

^bFamily-level NSM-valid annotation available.