Table 1.
Configuration of the peptide bond in front of proline residuesa
| Amino acid | Cβ (ppm) |
Cγ (ppm) |
Δβγ (ppm) |
Strong NOE | Isomer |
|---|---|---|---|---|---|
| P21 | 32.11 | 27.27 | 4.84 | –b | trans |
| P33 | 31.65 | 26.96 | 4.69 | Hα(32)–Hδ(33) | trans |
| P71 | 31.33 | 27.74 | 3.59 | HN(70)–Hδ(71) | trans |
| P106 | 32.74 | 26.49 | 6.25 | Hα(105)–Hδ(106) | trans |
| P122 | 32.27 | 26.80 | 5.47 | –b | trans |
| P135 | 31.33 | –c | − | –b | ? |
| P138 | 31.18 | 26.80 | 4.38 | Hα(137)–Hδ(138) | trans |
| P149 | 31.78 | –c | − | –b | ? |
| P171 | 32.43 | 26.33 | 6.10 | Hα(170)–Hδ(171) | trans |
aThe peptide bond configuration was determined from the chemical shift difference ∆βγ of the Cβ and Cγ shifts of the proline residues according to (Schubert et al. 2002) and/or from the NOEs between the amino acid X preceding the proline residue and the proline residue according to Wüthrich et al. (1984)
bResonances could not be assigned
cNo unambiguous NOEs could be found