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. 2007 Jul 27;8:270. doi: 10.1186/1471-2105-8-270

Table 8.

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

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

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 = Ndec/Nnat (Eq. 2) of the decoy ranked first by the 20-class OS2 energy function.