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Table 8 Native complex discrimination and residue contacts at the interfaces of submitted and target CAPRI structures

From: Recognizing protein–protein interfaces with empirical potentials and reduced amino acid alphabets

  

Interface contactsb

 

Target number

Native ranka

HH

HP

PP

Top decoy's interface contact number Fc

T04

9 8

53 (49.8)

32 (39.7)

15 (10.4)

1.1

T05

64 61

42 (56.8)

51 (34.4)

7 (8.7)

1.4

T06

2 3

46 (43.1)

33 (37.1)

21 (19.9)

1.0

T07

58 62

23 (25.7)

43 (44.9)

35 (29.3)

1.3

T08

84 61

7 (40.2)

77 (42.6)

16 (17.1)

4.3

T09

165 162

27 (39.2)

53 (42.1)

20 (18.6)

2.2

T11

1 1

48 (42.5)

41 (42.8)

11 (14.6)

1.0

T12

9 5

48 (53.5)

41 (36.9)

11 (9.5)

1.1

T13

194 176

65 (64.2)

33 (30.5)

2 (5.3)

1.0

T14

68 121

26 (31.4)

51 (44.2)

23 (24.4)

0.6

T15

12 3

18 (17.3)

44 (48.6)

38 (14.5)

0.8

T18

25 8

36 (49.3)

49 (43.1)

14 (7.6)

1.0

T19

3 38

36 (45.1)

44 (40.0)

20 (14.9)

0.6

  1. aValues for the 20Cl/OS1, OS2 functions, already given in Table 7. bThe percentage of interface contacts of each type, averaged over the 99 decoy structures: hydrophobic-hydrophobic (HH), hydrophobic-polar (HP), polar–polar (PP); values for the native structure in parentheses. cThe relative contact number F = N dec /N nat (Eq. 2) of the decoy ranked first by the 20-class OS2 energy function.