Table 1. Structural statistics for the ensemble of VSTx1 structures.
| Experimental restraints1 | |
| Interproton distance restraints | |
| Intraresidue | 193 |
| Sequential (|i–j| = 1) | 206 |
| Medium range (|i–j| < 5) | 116 |
| Long range (|i–j| ≥ 5) | 179 |
| Disulfide-bond restraints | 9 |
| Dihedral-angle restraints (ϕ, ψ, χ1) | 54 |
| Total number of restraints per residue | 22.5 |
| R.m.s. deviation from mean coordinate structure (Å)2 | |
| Backbone atoms, residues 2–34 | 0.03 ± 0.01 |
| Heavy atoms, residues 2–34 | 0.54 ± 0.11 |
| Stereochemical quality3 | |
| Residues in most favored Ramachandran region (%) | 89.8 ± 1.7 |
| Ramachandran outliers (%) | 0.0 ± 0.0 |
| Unfavorable sidechain rotamers (%) | 15.2 ± 4.6 |
| Clashscore, all atoms4 | 5.8 ± 0.7 |
| Overall MolProbity score | 2.72 ± 0.14 |
All statistics are given as mean ± S.D. 1Only structurally relevant restraints, as defined by CYANA, are included.
2Mean r.m.s. deviation calculated over the entire ensemble of 20 structures.
3According to MolProbity (http://molprobity.biochem.duke.edu).
4Defined as the number of steric overlaps >0.4 Å per thousand atoms.