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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.