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

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

^bRamachandran statistics calculated using PROCHECK.