Table 1 Structural statistics of hIAPP (residues 1-37).
From: The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes
NMR distance and dihedral constraints | |
Distance constraints | |
Total NOE | 542 |
Intra-residue | 136 |
Inter-residue | 406 |
Sequential (|i − j| = 1) | 218 |
Medium-range (|i − j| < 4) | 184 |
Long-range (|i − j| > 5) | 4 |
Total dihedral angle restraints | 20 |
ϕ | 10 |
ψ | 10 |
Structure statistics | |
Violations (mean ± s.d.) | |
Distance constraints (Å) | 0.019 ± 0.002 |
Dihedral angle constraints (°) | 0.767 ± 0.133 |
Max. dihedral angle violation (°) | 3.02 |
Max. distance constraint violation (Å) | 0.25 |
Deviations from idealized geometry | |
Bond lengths (Å) | 0.014 ± 0.001 |
Bond angles (°) | 1.636 ± 0.043 |
Impropers (°) | 1.789 ± 0.155 |
Average pairwise r.m.s. deviation* (Å) | |
Heavy | 0.78 ± 0.31 |
Backbone | 0.27 ± 0.09 |
Ramachandran plot statistics (%) | |
Residues in most favoured regions | 68.0 |
Residues in additionally allowed regions | 30.6 |
Residues in generously allowed regions | 0.9 |
Residues in disallowed regions | 0.5 |