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

  1. *Pairwise r.m.s. deviation was calculated among 20 refined structures for residues 2–17.