Table 1.
Structure and NMR restraints statistics.a
| eefxPot | REPEL | |
|---|---|---|
| Experiment Restraints | ||
| dihedral angles | 294 | 294 |
| NOE distances (i-j>5) | 146 | 146 |
| H-bonds | 77 | 77 |
| RMSD Agreement with Experimental restraints | ||
| dihedral angle (deg) | 0.598±0.039 | 0.570±0.094 |
| NOE (Å) | 0.040±0.003 | 0.044±0.003 |
| H-bond (Å) | 0.028±0.006 | 0.047±0.003 |
| Idealized Covalent Geometry RMSD | ||
| bonds (Å) | 0.995±0.001 | 1.036±0.000 |
| angles (deg) | 0.267±0.002 | 0.537±0.002 |
| impropers (deg) | 0.320±0.008 | 0.645±0.005 |
| Coordinate Precision as average RMSD from mean (Å)b | ||
| backbone CA, C, N atoms | 1.586 | 2.451 |
| all heavy atoms | 2.164 | 2.960 |
| Ramachandran Plot ϕ/ψ Angle Statistics | ||
| most favored regions | 92.9% | 92.2% |
| additional allowed regions | 5.8% | 4.8% |
| generously allowed regions | 0.8% | 1.7% |
| disallowed regions | 0.5% | 1.4% |
a
Calculated for 10 structures, out of 100 refined structures, selected for lowest energy and lowest experimental restraint violations.
b
Calculated for all 156 protein residues.