Table 1 Structural statistics for the family of 20 structures of HaSCP-2 in aqueous solution.

From: NMR structure and function of Helicoverpa armigera sterol carrier protein-2, an important insecticidal target from the cotton bollworm

Unambiguous distance restraints

 

 Intraresidue (i-j = 0)

930

 Sequential (|i-j| = 1)

415

 Medium range (2 ≤ |i-j| ≤ 4)

227

 Long range (|i-j| ≥ 5)

386

 Hydrogen bonds

29

Ambiguous distance restraints

275

Total

2262

Dihedral angle restraints

 Φ

109

 Ψ

110

Total

219

Mean r.m.s. deviations from the experimental restraints

 Distance (Å)

0.30 ± 0.0015

 Dihedral angle (o)

0.53 ± 0.10

Mean r.m.s. deviations from idealized covalent geometry

 Bond (Å)

0.0038 ± 0.00012

 Angle (o)

0.54 ± 0.015

 Improper (o)

1.40 ± 0.072

Ramachandran plota

 Well-ordered residuesb in HaSCP-2% residues in the most favorable regions

90.8

 additional allowed regions

8.6

 generously allowed regions

0.7

 Disallowed regions

0.0

Atomic r.m.s. differences (Å)

Residues 19–128

 

 Backbone heavy atoms (N, Cα and C’)

0.398

 Heavy atoms

0.840

  1. None of the structures exhibits distance violations greater than 0.3 Å or dihedral angle violations greater than 4˚.
  2. aThe program PROCHECK (http://www.biochem.ucl.ac.uk/~roman/procheck_nmr/procheck_nmr.html) was used to assess the overall quality of the structures.
  3. bResidues 18–79,82–117,120–134.
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