Table II.
A | B | E | V | |
---|---|---|---|---|
(A) | ||||
A | 7 | 16 | 11 | 2 |
B | 116 | 85 | 0 | |
E | 133 | 0 | ||
V | 2 | |||
(B) | ||||
A | 0 | 1 | 0 | 0 |
B | 34 | 7 | 0 | |
E | 48 | 0 | ||
V | 0 | |||
(C) | ||||
A | 0 | 15 | 12 | 1 |
B | 52 | 82 | 0 | |
E | 60 | 0 | ||
V | 0 | |||
(D) | ||||
A | 4 | 1 | 9 | 1 |
B | 21 | 3 | 0 | |
E | 10 | 0 | ||
V | 1 | |||
(E) | ||||
A | 14 | 4 | 4 | 0 |
B | 68 | 34 | 0 | |
E | 83 | 0 | ||
V | 1 |
(A) Distribution of homologous interaction pairs considered for the analysis. (B) Distribution of interaction pairs where neither of interactions has a charged residue pair. (C) Distribution of unconserved charged residue pairs (Type 1). (D) Distribution of conserved charged residue pairs (Type 2). (E). Distribution of correlated reappearance charged residue pairs (Type 4). For tables (A and B), position (X,Y) in a table corresponds to the number of interaction pairs from an interface formed by two proteins from kingdom X and an interface formed by two proteins from kingdom Y. For tables (C–E), position (X,Y) in a table corresponds to the number of charged residue pairs of the given type between a pair of residues from an interface formed by two proteins from kingdom X and a residue pair from another interface formed by two proteins from kingdom Y. Note that a single interface can contribute to more than one class of charged residue pairs.