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. Author manuscript; available in PMC: 2021 May 10.
Published in final edited form as: Biochemistry. 2020 Nov 2;59(44):4238–4249. doi: 10.1021/acs.biochem.0c00724

Table 2.

1H ring current shifts for residues in helix G of FeHsARD. All δ values are reported in ppm relative to tetramethylsilane external reference. Values in parentheses are changes relative to average values (www.bmrb.wisc.edu). For diastereomeric methylene pairs, the Δδ is reported for the larger shift difference. For Ile 81, the Hγ shift is for the γ2 methyl group resonance.

Residue δ HN δ Hα (Δδ) δ Hβ (Δδ) δ Hγ (Δδ)
Lys 80 7.39 2.25 (−2.0) −0.02,0.86 (−1.77) 0.49 (−0.86)
Ile 81 7.40 2.68 (−1.5) 1.13 (−0.65) 0.28 (−0.5)
Lys 82 6.04 3.18 (−1.1) 1.00,1.05 (−.75) 0.68,0.92 (−0.67)
Met 83 5.76 1.65 (−2.8) −0.82,0.10 (−1.2) −0.43,−0.24 (−2.8)