Table 1.
Statistical analysis of NMR and computed structural data for 1
| Distance restraints | Observed |
|---|---|
| Total | 116 |
| Intraresidue | |
| Pentapeptide | 23 |
| Glycans | 10 |
| Sequential (|k-j| = 1) | |
| Pentapeptide | 28 |
| Glycans | 8 |
| Medium range (2 ≦|i-j| ≦4) | |
| Pentapeptide | 1 |
| Glycans | 2 |
| Pentapeptide–Glycans | |
| Self* | 29 |
| Other† | 13 |
| 3-bond J-coupling restraints | |
| Pentapeptide | 5 |
| Glycans | 6 |
| Structure Statistics | Value |
| NOE violations | |
| Number >0.2 Å | 2 |
| Number >0.5 Å | 0 |
| Three-bond J-coupling violations | |
| Number >0.25 Hz | 0 |
| Deviations from ideal covalent geometry | |
| Bond length, Å | 0.013 ± 0.005 |
| Bond angle, Å | 2.7 ± 0.4 |
| Impropers, deg | 1.3 ± 0.4 |
| Pairwise rms deviation among 20 final structures, Å | |
| Peptapeptide backbone + (S1G1, T2G1, T3G1) rings | 1.17 ± 0.55 |
| Pentapeptide + (S1G1, T2G1, T3G1) heavy atoms | 1.36 ± 0.60 |
*
Between peptide residue and its attached glycans. These NOEs were limited to the proximally linked GalNac N-acetyl-methyl group.
†
Between peptide residue and glycans on other peptide residues.