Table 3.
Structural Statistics for the 20 Lowest-Energy Solution Structures of ASPE As Validated by PSVS (the Protein Structure Validation Suite)
| Experimental constraints | |
|---|---|
| total NOE | 517 |
| intraresidue [i = j] | 101 |
| sequential [|i − j| = 1] | 187 |
| medium range [1 < |i − j| < 5] | 63 |
| long range [|i − j| ≥ 5] | 166 |
| dihedral angles | 17 |
| hydrogen bonds | 15 |
| Violations | |
| distance (>0.1 Å) | 0 |
| dihedral angle (>1°) | 0 |
| van der Waals (<1.6 Å) | 0 |
| RMSD from idealized geometrya | |
| bond lengths (Å) | 0.011 |
| bond angles (deg) | 0.8 |
| RMS of distance violation (Å) | 0.01 |
| RMS of dihedral angle violation (deg) | 0.1 |
| Average pairwise RMSD values (Å)a | |
| all backbone atoms | 0.16 |
| all heavy atoms | 0.59 |
| Ramachandran plot statistics from Richardson’s lab (%) | |
| most favored regions | 93.7 |
| allowed regions | 6.3 |
| disallowed regions | 0 |
a
RMSD values were given as the mean value.