Table 3.
Structural statistics for the family of 30 P2 structures
| Measurement | Value |
|---|---|
| rmsd from experimental distance and torsion angle restraints* | |
| NOE restraints (83), Å | 0.022 |
| La3+ ion restraints (6), Å | 0.022 |
| ϕ angles (14), ° | 0.014 |
| rmsd from idealized covalent geometry | |
| Bond lengths, Å | 0.001 |
| Angles, ° | 0.239 |
| Impropers, ° | 0.206 |
| x-plor potential energies (±SD), kcal·mol−1† | |
| Etotal | 11.6 (±0.7) |
| Erepel | 2.2 (±0.2) |
| ENOE | 1.5 (±0.4) |
| Ebond | 0.5 (±0.0) |
| Eangle | 3.3 (±0.4) |
| Eimproper | 0.7 (±0.1) |
| Edihedral | 0.0 (±0.0) |
| Eharm | 3.5 (±0.2) |
| rmsd of cartesian coordinates‡, Å | |
| Backbone N, Cα and C (residues 1–16) | 0.30 |
| All heavy atoms (residues 1–16) | 0.84 |
| Backbone N, Cα and C (residues 8–16) | 0.10 |
| All heavy atoms (residues 8–16) | 0.25 |
*
The total number of restraints is given in parentheses. None of the 30 structures showed distance violations of more than 0.20 Å or dihedral angle violations of more than 2.0°. No distance or dihedral angle restraints were consistently violated by more than 0.10 Å or 1.0°, respectively.
†
Etot, total energy, Erepel, repulsive energy term, ENOE, effective NOE energy term. The harmonic energy term (Eharm) was used to maintain the geometry of the six La3+ ion ligands.
‡
rmsd values result from a superposition on the N, Ca, and C atoms of the protein backbone and were calculated by averaging the individual rmsds between the average structure and each member of the family.