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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.