Table 1.

Amino acids composition within the four simulated zones and the corresponding α-helices, together with the Kyte–Doolittle and Rose indexes.

zones	domain	α-helix	AA range	AA numbera	KD indexb	Rose index
1			E16–H105	90	29.1	66.14
	IA	h2	E16–L31	16	11.9	12.66
		h3	P35–D56	22	−2.7	16.04
		h4	S65–T76	12	3.5	9.04
		h5	A88–A92	5	5.1	3.92
		h6	E95–H105	11	−17.7	7.81
2			E208–E280	73	−29.5	52.59
	IIA	h2	E208–F223	16	−5.3	11.62
		h3	E227–H247	21	−1.3	15.56
		h4	L250–E266	17	−0.9	12.49
		h5	L275–E280	6	−2.1	4.43
3			W341–V415	75	−18.2	54.30
	IIB	h3	S342–A362	21	12.5	15.71
		h4	D365–E383	19	−14.4	13.56
	IIIA	h1	P384–L398	15	−8.8	10.74
		h2	Y401–V415	15	−5.9	10.71
4			A510–A582	73	−31.6	50.52
	IIIB	h1	A510–T515	6	6.4	4.59
		h2	E518–K536	19	−23.1	12.86
		h3	E542–K560	19	0.9	13.88
		h4	E565–A582	18	−1.4	12.80

^aThe number of amino acids in the subdomains exceeds the sum of those in the α-helices owing to the presence of regular turns and random strands.

^bKyte–Doolittle index, calculated as the sum of the values for the individual amino acids. A positive hydropathy value indicates hydrophobicity and a negative one hydrophilicity.