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Table 2 The occurrence of π-turns with different conformational designations and the average backbone torsion angles (°) in the turn region

From: pi-Turns: types, systematics and the context of their occurrence in protein structures

Class

Cα-Cα distance (Å)

φi+1

ψi+1

φi+2

ψi+2

φi+3

ψi+3

φi+4

ψi+4

Ï€-HB turns

AAAa (59%)

5.4 (0.4)

-66 (9)

-33 (14)

-71 (13)

-36 (14)

-97 (15)

-6 (12)

65 (16)

38 (17)

PgAA (9%)

6.3 (0.7)

-62 (7)

130 (7)

85 (13)

-8 (17)

-113 (15)

-64 (17)

-101 (19)

-18 (19)

AAAA (6%)

5.8 (1.0)

-63 (9)

-24 (15)

-87 (15)

-15 (23)

-115 (18)

-71 (37)

-99 (26)

-18 (23)

Schellman motif π-turns (SCH+β)

AAAa (98%)

5.3 (0.4)

-65 (5)

-42 (6)

-63 (6)

-30 (8)

-90 (11)

4 (10)

76 (19)

24 (17)

Ï€-NHB turns

AEAA (11%)

5.8 (0.5)

-85 (19)

-14 (19)

-101 (34)

150 (22)

-62 (11)

-25 (13)

-89 (16)

-3 (17)

EAAa (10%)

5.3 (0.3)

-89 (15)

179 (10)

-64 (9)

-20 (12)

-92 (12)

4 (10)

84 (13)

11 (11)

EAAA (8%)

5.8 (0.5)

-94 (34)

150 (24)

-58 (9)

-30 (12)

-80 (15)

-24 (18)

-110 (21)

-13 (21)

EAAE (6%)

4.8 (0.7)

-120 (28)

177 (19)

-64 (11)

-28 (14)

-105 (19)

-16 (23)

-146 (22)

144 (28)

AAaA (6%)

5.7 (0.4)

-67 (19)

-26 (17)

-92 (19)

-3 (13)

74 (15)

14 (18)

-96 (20)

-17 (19)

AEEa (6%)

5.8 (0.5)

-89 (19)

-12 (17)

-101 (31)

144 (30)

-57 (8)

134 (10)

81 (16)

2 (20)

  1. The standard deviations are in the parentheses. The classes are defined using the conformational designations shown in Figure 2a.