Residues in the α2I domain structure within 4.2 Å (non-hydrogen atoms) of the bound GFOGER tripeptide and equivalent residues in the other human and lamprey αI domains, and the fragment from the hagfish.

Where available, the sequence numbering is from a three-dimensional structure (PDB codes and resolution are indicated). The metal ion at MIDAS is covalently bound to the tripeptide ligand. Residues from MIDAS (S153, S155 and T221 in α2I, 1DZI) are in italics and two residues, D151 and D254 in α2I (not listed), are absolutely conserved across all of the sequences and bind to the metal at MIDAS via a water molecule (WAT2001).*, no equivalent or aligned residue; ?, residue not present in the sequence fragment;†alignment uncertain at the position - no threonine present nearby in the sequence and replacement of arginine with threonine did not alter binding to collagens of the expressed mutant (data not shown).Residues in the α2I domain structure within 4.2 Å (non-hydrogen atoms) of the bound GFOGER tripeptide and equivalent residues in the other human and lamprey αI domains, and the fragment from the hagfish.