Table 1.

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

amino acid	position	δC	δH	HMBC (1H–13C)
Phe	C1	172.1, qC
	C2	55.8, CH	4.55, m	C1, C3
	C3	36.2, CH2	3.00, m; 3.05, m	C2, C9
	C4	139.7, qC
	C5,5′	129.5, CH	7.37, t; 16.0, 9.0 Hz	C9, C7
	C6,6′	128.1, CH	7.28, t; 15.0, 8.0 Hz	C8, C7
	C7	126.1, CH	7.18, t; 15.0, 7.5 Hz	C6, C5
	NH		7.44, d; 9.2 Hz	C2, C10
Ile	C1	170.5, qC
	C2	53.9, CH	4.53, m	C10, C12, C13, C14
	C3	38.2, CH	1.70, m	C13, C14, C15
	C4	14.8, CH3	0.89, d; 7.0 Hz	C11, C12, C14
	C5	24.1, CH2	1.20, m; 1.51, m	C12, C13, C15
	C6	10.2, CH3	0.86, m	C12, C14
	NH		8.95, d; 8.4 Hz	C16
Pro1 (cis)	C1	171.5, qC
	C2	60.9, CH	4.17, d; 8.0 Hz	C16, C18, C19
	C3	31.5, CH2	2.11, m; 2.30, m	C17, C20
	C4	21.9, CH2	1.61, m; 1.72, m	C17
	C5	46.8, CH2	3.25, m; 3.41, m	C17, C18
Tyr	C1	169.3, qC
	C2	53.0, CH	4.55, m	C21, C23
	C3	36.3, CH2	3.27, m; 3.25, m	C21, C22, C29
	C4	127.1, qC
	C5,5′	131.1, CH	6.98, d; 8.5 Hz	C26, C27, C29
	C6,6′	115.1, CH	6.78, d; 8.5 Hz	C27, C28, C24
	C7	156.5, qC
	NH		6.77, d; 4.8 Hz	C30
Pro2 (cis)	C1	170.2, qC
	C2	61.9, CH	4.42, m	C30, C32, C34
	C3	31.8, CH2	2.11, m	C31
	C4	22.2, CH2	1.97, m	C31
	C5	46.3, CH2	3.48, m; 3.62, m	C31
Leu	C1	170.9, qC
	C2	52.2, CH	4.71, m	C37, C35, C38
	C3	38.8, CH2	1.35, m; 1.62, m	C39, C40
	C4	24.9, CH	1.17, m	C39, C40
	C5	20.7, CH3	1.02, d; 6.5 Hz	C38, C40
	C6	23.4, CH3	0.88, d; 6.5 Hz	C38, C40
	NH		8.15, d; 3.6 Hz	C41
Pro3 (cis)	C1	172.7, qC
	C2	58.6, CH	4.58, m	C44, C45, C1
	C3	30.7, CH2	1.85, m; 2.01, m
	C4	21.7, CH2	1.54, m; 1.51, m	C42
	C5	47.12, CH2	3.72, 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.