. Author manuscript; available in PMC: 2011 Mar 1.

Published in final edited form as: J Biomol NMR. 2009 Dec 30;46(3):199–204. doi: 10.1007/s10858-009-9395-y

Table 1.

Average secondary chemical shift and standard deviation for backbone and ¹³C^β and ¹³C^γ nuclei of Pro residues preceded by a cis or trans peptide bond.^a

X	$< Δ δ_{cis}^{X} >$	$σ_{cis}^{X}$	$< Δ δ_{trans}^{X} >$	$σ_{trans}^{X}$
¹H^α	0.17	0.53	−0.03	0.39
¹³C’	−1.78	1.45	−0.26	1.58
¹³C^α	−0.19	1.07	0.55	1.47
¹³C^β	2.42	1.27	0.21	0.97
¹³C^γ ^b	24.41	0.74	27.45	0.86

Using the random coil chemical shifts used by TALOS+ (Shen et al. 2009a).

The regular chemical shift instead of the secondary chemical shift is reported