. 2000 Apr 1;28(7):1585–1593. doi: 10.1093/nar/28.7.1585

Table 1. Aromatic proton and nitrogen chemical shifts (p.p.m.) for TAR RNA bound to argininamide at 25°C in D₂O.

Residue	δ(¹H2)	δ(¹H5)	δ(¹H8)	δ(¹⁵N1)	δ(¹⁵N3)	δ(¹⁵N7)	δ(¹⁵N9)
Uridine residues
U23		5.58		144.31	160.09
U25		5.96		144.54	157.77
U31		5.78		143.28	157.51
U38		5.41		147.25	161.07
U40		5.49		147.17	160.98
U42		5.31		146.00	161.06
Cytidine residues^a
C18		5.26		151.17
C29		5.12		151.37
C37		5.19		151.88
C39		5.61		150.64
C41		5.67		151.75
C45		5.16		151.32
Adenosine residues
A20	6.92		7.98	220.40	213.61	230.53	170.56
A22	7.14		7.73	223.40	213.94	229.78	170.66
A27	7.49		7.80	221.12	210.93	229.12	169.21
A35	8.24		8.39	^b	218.21	232.20	168.84
Guanosine residues
G16^c			8.12		163.31	233.07	168.28
G16^c			8.13		163.23	232.60	168.15
G17			7.73		^d	233.57	169.67
G21			7.06		162.85	234.33	168.98
G26			7.74		^d	230.50	168.91
G28			7.48		^d	234.10	169.70
G32			7.77		^d	235.99	167.34
G33			7.63		166.50	235.69	169.14
G34			7.89		162.46	236.89	169.02
G36			7.41		162.12	233.69	169.20
G43			7.68		162.08	234.59	169.45
G44			7.32		161.39	233.54	169.08

All proton chemical shifts are referenced to the internal standard TSP and nitrogen shifts are referenced indirectly according to the chemical shift ratio (27).^aCytidine residues 19, 30 and 46 are not assigned due to resonance overlap of the corresponding H5 protons.^bOnly one correlation at the H2 resonance frequency of A35 between the typical N1 and N3 chemical shift regions was observed as seen in Figure 5.^cTwo sets of correlations of similar intensity were observed for the terminal guanosine residue G16, which is likely to be due to 3′-end heterogeneity.^dNot assigned due to resonance overlap.

Table 1. Aromatic proton and nitrogen chemical shifts (p.p.m.) for TAR RNA bound to argininamide at 25°C in D2O.

Table 1. Aromatic proton and nitrogen chemical shifts (p.p.m.) for TAR RNA bound to argininamide at 25°C in D₂O.