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. 2004 Aug 23;87(5):2990–2999. doi: 10.1529/biophysj.104.047886

TABLE 4.

Helix-helix interactions; pairs of residues separated by 3–5 Å

Helix intersection Residue pairs
H2–3 87–95
H2–4 122–68, 123–68, 123–71, 123–64, 123–67, 126–68, 126–69, 126–72, 127–71, 127–75, 129–72, 130–72, 130–76, 131–75, 133–72, 134–83, 135–83, 135–87, 139–87, 142–87, 142–88
H2–7 290–65
H2–11 405–77, 409–77, 409–74, 412–70, 412–72, 412–73, 412–69, 416–66, 416–67, 416–70, 420–63, 420–66
H4–5 148–151, 152–144, 152–141, 152–145, 155–144, 156–141, 156–144, 159–140, 159–144,
H5–7 289–172
H5–8 306–172, 307–173, 307–176, 310–169, 310–173, 310–172, 311–169, 311–173, 313–169, 314–165, 314–169, 317165, 318–165, 318–166, 322–162
H7–8 306–289, 309–288
H7–10 369–284, 369–288, 372–284, 373–284, 373–285, 376–277, 376–280, 377–281, 380–277, 381–278, 384–270, 384–274, 387–270, 388–270, 388–267, 388–271
H7–11 403–271, 403–274, 406–271, 407–274, 407–275, 407–278, 408–278, 410–275, 411–275, 411–278, 411–279, 412–282, 414–279, 415–283, 415–279, 420–287, 279–411HB
H8–10 366–308, 366–309, 366–312, 369–309, 369–313, 370–316, 373–317, 373–313, 374–320, 375–320, 379–320, 379–324, 365–305HB
H10–11 399–388, 400–385, 400–388, 400–389, 400–386, 402–388, 403–385, 403–388, 404–385

Bold, pathogenic residues; italicized, residues crucial for transport. All interactions are hydrophobic except those labeled HB (hydrogen bond). Interactions involving helices 1, 3, 6, and 9 omitted (data available upon request).