Table I.

Combined chemical shift perturbations to NH (amide) correlations of selected residues in CYP-S-CO relative to the shifts of CYP-1-CO (camphor-bound) as a function of substrate. Perturbations were calculated from individual ¹H and ¹⁵N shifts using the equation $\mid \mathrm{\Delta }{\delta }_{NH}\mid ={\left[{(\mathrm{\Delta }{\delta }_H)}^2+{(\mathrm{\Delta }{\delta }_N/5)}^2\right]}^{1/2}$ (Ref ¹⁸).

Residue	|Δδ| (1H, 15N) ppm adamantanone (CYP-2-CO)	|Δδ| (1H, 15N) ppm norcamphor (CYP-3-CO)
Val 247 (I helix)	0.14	0.22
Gly 248 (I helix)	0.07	0.14
Gly 249 (I helix)	0.16	0.31
Thr 252 (I helix)	0.32	0.42
Val 254 (I helix)	Large change	Large change
Val 295 (β3)	Small or none	Small or none
Ala 296 (β3)	0.06	0.13
Gly 298 (β3)	0.03	0.13
Met 323	overlapped	overlapped
Leu 324	None or small	None or small
Ser 325 (K’ helix)	0.33	0.45
Gly 326 (K’ helix)	0.16	0.29
Cys 357 (haem ligand)	0.03	0.11