Table 2.

¹³C and ¹H NMR Data of Stylisin 2 (2)^a

amino acid	position	δC	δH	HMBC (1H–13C)
Phe	C1	168.5, qC
	C2	53.3, CH	4.34, m	C42, C5
	C3	38.1, CH2	3.06, m; 3.21, m	C4, C6, C3
	C4	136.9, qC
	C5,5′	130.0, CH	7.11, t; 13.8,7.2 Hz	C1, C2, C5, C43
	C6,6′	128.4, CH	7.27; 14.0, 7.8 Hz	C44, C3, C1
	C7	127.1, CH	7.26, t; 15.0, 7.8 Hz	C2, C3
	NH		6.79, d; 9.6 Hz	C7
Pro2 (cis)	C1	171.3, qC
	C2	61.3, CH	3.62, m	C7, C10
	C3	31.4, CH2	1.47, m	C11, C10
	C4	22.3, CH2	1.88, m	C8
	C5	47.5, CH2	3.64, m	C8
Pro3 (cis)	C1	169.4, qC
	C2	57.2, CH	4.22, d, 7.8 Hz	C12
	C3	29.7, CH2	1.90, m	C16
	C4	21.5, CH2	1.85, m	C13
	C5	47.0, CH2	3.50, m, 3.52, m	C14
Tyr	C1	172.0, qC
	C2	52.0, CH	4.62, q, 10.0, 6.0 Hz	C17, C19
	C3	38.2, CH2	2.70, q, 12.0, 5.5 Hz; 2.83, m	C20, C21
	C4	136.9, qC
	C5,5′	130.6, CH	6.95, d; 8.4 Hz	C21, C22
	C6,6′	115.5, CH	6.80, d; 9.0 Hz	C22, C23
	C7	156.7, qC		C23, C24
	NH		7.62, d; 4.8 Hz	C26
Pro4 (trans)	C1	170.7, qC
	C2	61.3, CH	3.57, m	C26, C29
	C3	28.1, CH2	2.19, m	C30
	C4	21.9, CH2	1.61, m	C27
	C5	46.5, CH2	3.57, m	C27, C31
Ile	C1	171.6, qC
	C2	58.4, CH	4.18, d, 8.4 Hz	C31, C34
	C3	35.5, CH	2.08, m	C36, C34
	C4	15.8, CH3	0.80, d; 7.8 Hz	C35, C32
	C5	25.8, CH2	1.27, m; 1.4, m	C36, C33
	C6	10.6, CH3	0.82, t; 6.6, 3.0 Hz	C35, C33
	NH		8.98, d; 3.6 Hz	C37
Pro1 (trans)	C1	170.8, qC
	C2	59.3, CH	4.44, m	C37, C41
	C3	31.3, CH2	2.69, q; 5.4, 12.0 Hz	C37, C41
	C4	25.6, CH2	2.08, m; 2.21, m	C38
	C5	46.2, CH2	3.25, m	C42

^aIn acetone-d₆, 600 MHz for ¹H and 150 MHz for ¹³C NMR. Carbon multiplicities were determined by DEPT experiments. Coupling constants (J) are in Hz.