Sequence alignment for human CR3 and LFA-1 and the vWF-A1, -A2, and -A3 domains. The vWF sequence numbering is indicated at the start and end of each vWF-A sequence. The α-helix and β-strand secondary structures in the CR3 and LFA-1 crystal structures and the three vWF-A models are denoted by A1 to A7 and BA to BF, respectively. Residues that were rebuilt as new loops are denoted in bold and underlined. The DSSP analysis is represented as follows: E, β-strand; B, single residue β-ladders; T, turn; G, 3₁₀helix; and H, α-helix. The COMPARER sidechain solvent accessibilities are on a scale of 0 to 9 for each residue, where 0 corresponds to 0% to 9% solvent exposure, 1 to 11% to 19% solvent exposure, and so on, and buried residues have accessibilities of 0 or 1.