Table 2.
Characteristics of the intertwined assembly
| No. of swapped residuesa | 9 (158–166) |
| No. of residues in the hinge loopa | 5 (167–171) |
| No. of intermolecular H-bonds (salt bridges)b | 41 (13) |
| Buried interaction area (Å2)a,c | 2375 |
| Total interaction surface (Å2)a,b | 2987 |
| r.m.s.d. wt monomer versus G167 dimer (Chain A) Å (no. of Cα atoms) | 0.4 (79) |
Physico-chemical parameters of the domain swapped dimer. The table lists parameters similar to those cited in (36) to compare our structural features with those of other domain-swap proteins previously characterized.
a
Values are intended as ‘per subunit’.
b
Computed using the PISA software.
c
Calculated by subtracting the solvent accessible surface area of the closed monomer from that of the open monomer.