Table 2.
Chain Interfaces Calculated by PISAa
interface | chain 1:chain 2 | residues | area (Å2) | H-bonds | salt bonds | CSSc | color |
---|---|---|---|---|---|---|---|
1 | dho1(A):dho4(G) | 30:30 | 1082 | 10 | 26 | 0.969 | purple |
2 | atc1(B):atc2(D) | 26:26 | 946 | 19 | 8 | 1.00 | blue |
(2) | atc1(B):atc3(F) | 26:26 | 946 | 19 | 8 | 1.00 | cyan |
3 | atc1(B):dho1(A) | 23:22 | 788 | 9 | 7 | 0.427 | green |
4 | atc1(B):dho4(G) | 20:22 | 768 | 12 | 0 | 0.191 | yellow |
5 | dho1(A):dho5(I) | 12:12 | 389 | 2 | 0 | 0.059 | orange |
6 | dho1(A):atc3(F) | 4:5 | 51 | 2 | 0 | 0.018 | red |
7b | atc1(B):atc* | 11:11 | 114 | 10 | 10 | 0.00 | gray |
The Protein Interfaces, Surfaces, and Assemblies service (PISA) at the European Bioinformatics Institute (http://www.ebi.ac.uk/msd-srv/prot_int/pistart.html) identified six protein interfaces in the DAC dodecamer and one packing contact in the crystal. The six interfaces within the dodecamer are ranked in decreasing order of their buried surface area, which is an approximate measure of the strength of the interaction, and correspondingly colored in descending order of spectral energy (59). The crystal packing contact is colored gray.
Crystal packing contact between two dodecamers in the crystal.
Complexation significance score.