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Table 3 The triangle constructed from the associated residues in a triplet clique approximates to being equilateral

From: Mapping the distribution of packing topologies within protein interiors shows predominant preference for specific packing motifs

Composition Frequency <r12> <r13> <r23> < Ω1> < Ω2> < Ω3>
ILE LEU VAL 322 5.9 (0.7) 5.9 (0.7) 5.6 (0.5) 56.5 (7.5) 61.6 (9.2) 61.9 (8.6)
ILE LEU LEU 291 6.3 (0.6) 5.6 (0.6) 5.5 (0.6) 55.0 (7.9) 55.9 (5.9) 69.1 (7.1)
PHE ILE LEU 276 5.8 (0.8) 5.4 (0.6) 5.9 (0.6) 63.2 (9.5) 55.5 (9.3) 61.3 (10.9)
VAL LEU LEU 268 5.4 (0.5) 5.9 (0.4) 5.6 (0.6) 59.2(7.8) 65.2 (5.6) 55.5 (5.4)
PHE LEU VAL 246 5.5 (0.6) 5.3 (0.6) 5.6 (0.6) 61.6 (8.2) 57.7 (9.4) 60.7 (9.4)
PHE LEU LEU 237 5.1 (0.5) 5.8 (0.5) 5.6 (0.5) 62.1 (8.4) 65.7 (7.6) 52.1 (5.7)
LEU LEU LEU 202 5.2 (0.5) 6.1 (0.3) 5.7 (0.4) 59.5 (4.2) 67.8 (4.9) 52.6 (4.7)
LEU ILE ILE 187 6.4 (0.5) 5.7 (0.6) 6.3 (0.8) 63.4 (11.7) 52.8 (7.0) 63.8 (7.6)
LEU PHE PHE 162 5.1 (0.5) 5.8 (0.5) 5.5 (0.5) 60.7 (9.3) 66.1 (7.0) 53.3 (5.9)
TYR ILE LEU 151 5.7 (0.8) 5.3 (0.6) 6.0 (0.6) 65.5 (8.8) 53.9 (9.5) 60.5 (11.1)
PHE ILE VAL 150 5.7 (0.7) 5.4 (0.7) 5.9 (0.7) 64.9 (10.6) 55.6 (10.7) 59.5 (10.3)
VAL ILE ILE 134 5.5 (0.6) 6.3 (0.6) 6.2 (0.8) 63.1 (11.1) 64.9 (7.5) 52.0 (7.2)
LEU VAL VAL 128 5.9 (0.4) 5.3 (0.5) 5.7 (0.5) 61.1 (8.0) 54.8 (4.7) 64.1 (6.1)
ILE VAL VAL 119 6.3 (0.5) 5.5 (0.6) 5.7 (0.5) 57.8 (8.1) 54.4 (6.4) 67.8 (5.9)
TYR PHE LEU 117 5.5 (0.6) 5.4 (0.6) 5.4 (0.5) 59.6 (9.0) 59.6 (10.1) 60.7 (9.5)
ILE PHE PHE 105 6.3 (0.6) 5.5 (0.7) 5.5 (0.6) 54.6 (8.5) 54.9 (7.3) 70.5 (7.2)
TYR LEU LEU 104 4.9 (0.4) 5.9 (0.5) 5.5 (0.6) 60.9 (8.5) 67.9 (7.1) 51.2 (6.3)
TYR LEU VAL 98 5.4 (0.6) 5.4 (0.7) 5.5 (0.4) 60.7 (7.6) 59.4 (10.1) 59.9 (10.4)
PHE ILE ILE 94 5.5 (0.6) 6.3 (0.7) 6.4 (0.9) 66.0 (11.3) 63.1 (8.5) 50.8 (6.7)
PHE VAL VAL 88 4.9 (0.6) 5.8 (0.5) 5.7 (0.5) 63.5 (10.0) 65.7 (7.7) 50.8 (6.8)
TYR PHE ILE 85 5.6 (0.5) 5.7 (0.9) 5.8 (0.8) 61.8 (12.1) 59.9 (13.3) 58.2 (9.9)
TYR PHE VAL 77 5.5 (0.6) 5.5 (0.6) 5.5 (0.7) 59.9 (10.7) 59.3 (10.0) 60.7 (9.9)
ILE ILE ILE 70 5.5 (0.6) 6.4 (0.5) 7.0 (0.6) 72.1 (6.2) 59.9 (4.5) 48.0 (5.8)
TYR ILE VAL 69 5.8 (0.9) 5.4 (0.6) 5.9 (0.7) 63.4 (10.6) 55.0 (10.3) 61.5 (11.7)
VAL PHE PHE 67 5.8 (0.5) 5.0 (0.5) 5.4 (0.5) 59.8 (9.0) 52.3 (6.9) 67.8 (8.0)
TRP PHE LEU 56 5.5 (0.6) 5.6 (0.6) 5.4 (0.6) 58.7 (8.5) 61.6 (10.3) 59.7 (9.3)
TYR PHE PHE 53 5.9 (0.5) 5.1 (0.4) 5.5 (0.5) 59.8 (9.2) 52.6 (5.7) 67.5 (8.1)
LEU VAL ALA 50 5.7 (0.5) 4.7 (0.4) 4.7 (0.4) 53.4 (5.3) 53.1 (6.8) 73.5 (7.7)
  1. Average lengths of sides (Å) and internal angles (°) (along with their standard deviations in parentheses) of the triangle formed by joining the origins of the three internal frames corresponding to the constituent residues (in a triplet clique) are tabulated. Only those compositions have been given whose frequencies are greater than equal to 50.