TABLE 2.

Structural statistics for the monomeric structure of JCV agnoprotein peptide

Parametera	Value for JCV agnoprotein peptide monomer
No. of restraints for calculation	452
Unambiguous	369
Ambiguous	83
Total no. of NOE restraints	452
Intraresidue	293
Sequential (|i − j| = 1)a	100
Medium range (|i − j| ≤ 4)	59
RMSD structure statistics
Bonds (Å)	2.7 × 10−3-2.93 × 10−3
Bond angles (°)	0.44–0.50
Improper torsions (°)	0.88–1.23
NOE restraints (Å)	1.34 × 10−2-1.63 × 10−2
Final energies (kcal/mol)
Total	−1,146 to −998.6
Bonds	4.42–5.21
Angles	32.43–41.91
Improper angles	9.78–17.38
Dihedrals	164.5–167.86
van der Waals	−98.55 to −55.67
Electrostatic	−1,270.34 to −1,173.67
NOE	4.08–5.98
Ramachandran plot of residues (%) in:
Most favored regions	80.3
Additional allowed regions	18.0
Generously allowed regions	1.7
Disallowed regions	0
Atomic RMSD (Å) on backbone atoms (K23 to F29)
Pairwise	0.66 ± 0.22
To mean structure	1.04 ± 0.15

^aj 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.