Table 1 Structural statistics of the 20 final NMR structure of the HPLW at 318 K.
From: Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptide
Number of the distance restraints | |
Unambiguous NOE | 110 |
Ambiguous NOE | 71 |
Total NOE | 181 |
Divided into | |
Intra-residue NOE | 45 |
Sequential NOE | 50 |
Medium, Long-range NOE | 15 |
Number of dihedral angle restraints | 81 |
Residual NOE violations | |
Number > 0.1° | ±1 |
Maximum, Å | 0.18 ± 0.02 |
Residual angle violations | |
Number > 2.0° | 0 ± 0 |
Maximum, Å | 0 |
Amber energies, KJ/mol | |
Total | −410 ± 25 |
Van der Waals | −215 ± 20 |
Electrostatic | −282 ± 18 |
R.m.s.d (Å) to a mean structure | |
Backbone (residues 5–13) | 0.49 ± 0.05 |
Heavy atoms (residues 5–13) | 1.33 ± 0.09 |
