TABLE 3.
Structural statistics for theoretical model of JCV agnoprotein peptide dimer
| Parameter | Value for JCV agnoprotein peptide dimer |
|---|---|
| Total no. of NOE restraints | |
| Intraresidue | 229 |
| Sequential (|i − j| = 1)a | 90 |
| Medium range (|i − j| ≤ 4) | 49 |
| Intermolecular | 40 |
| RMSD structure statistics | |
| Bonds (Å) | 8.48 × 10−4–9.48 × 10−4 |
| Bond angles (°) | 0.424–0.426 |
| Improper torsions (°) | 0.317–0.320 |
| NOE restraints (Å) | 2.90 × 10−3–5.93 × 10−3 |
| Final energies (kcal/mol) | |
| Total | 70.97–72.98 |
| Bonds | 0.873–1.090 |
| Angles | 60.05–60.69 |
| Improper angles | 9.58–9.75 |
| van der Waals | 0.03–0.79 |
| NOE | 0.37–1.58 |
| Ramachandran plot of residues (%) in: | |
| Most favored regions | 62.3 |
| Additional allowed regions | 30.6 |
| Generously allowed regions | 6.5 |
| Disallowed regions | 0.6 |
| Atomic RMSD (Å) on the backbone atoms (K23 to F39) | |
| Pairwise | 0.89 ± 0.24 |
| To mean structure | 0.60 ± 0.15 |
a
j represents an amino acid different from amino acid i. Residues represented by i and j may be consecutive in the sequence or separated by 1, 2, or 3 residues.