Table 1.
NMR and Refinement Statistics for Protein Structures
CSP 1-100 | pCSP 1-100 | |
---|---|---|
NMR Distance and Dihedral Constraints | ||
Distance constraints | ||
Total NOE | 2,450 | 3,120 |
Intra-residue | 851 | 968 |
Inter-residue | 1,599 | 2,152 |
Sequential (|i – j| = 1) | 655 | 839 |
Medium-range (2 ≤ |i – j| ≤ 4) | 530 | 758 |
Long-range (|i – j| ≥ 5) | 414 | 555 |
Total dihedral angle restraints | 187 | 181 |
ϕ | 92 | 90 |
ψ | 95 | 91 |
Structure Statistics | ||
Violations (mean and SD) | ||
Distance constraints (Å) | 0.08 ± 0.06 | 0.07 ± 0.07 |
Dihedral angle constraints (°) | 1.15 ± 0.88 | 1.44 ± 1.10 |
Max. dihedral angle violation (°) | 4.79 | 5.57 |
Max. distance constraint violation (Å) | 0.72 | 1.13 |
Deviations from idealized geometry | ||
Bond lengths (Å) | 0.0041 ± 0.00013 | 0.0050 ± 0.0001 |
Bond angles (°) | 0.59 ± 0.012 | 0.65 ± 0.016 |
Impropers (°) | 1.54 ± 0.056 | 1.59 ± 0.067 |
Average pairwise root-mean-square deviationa (Å) | ||
Heavy | 0.47 | 0.49 |
Backbone | 0.14 | 0.20 |
Ramachandran statisticsb | ||
Most favored/additionally allowed/generously allowed (%) | 88.2/11.8/0.0 | 80.6/18.3/1.1 |
Statistics are calculated and averaged over an ensemble of the 20 lowest-energy water-refined structures out of 100 calculated structures.
Ramachandran statistics calculated using PROCHECK.