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. 2016 Aug 2;24(8):1380–1386. doi: 10.1016/j.str.2016.06.009

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 (|ij| = 1) 655 839
 Medium-range (2 ≤ |ij| ≤ 4) 530 758
 Long-range (|ij| ≥ 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
a

Statistics are calculated and averaged over an ensemble of the 20 lowest-energy water-refined structures out of 100 calculated structures.

b

Ramachandran statistics calculated using PROCHECK.