Table 1.

NMR and refinement statistics for protein structures

	Protein
NMR distance and dihedral constraints
Distance constraints
Total NOE	1206
Intraresidue	4
Interresidue	1202
Sequential (|i-j|= 1)	432
Medium range (|i-j|<4)	429
Long range (|i-j| >4)	294
Ambiguous	47
Hydrogen bonds	26
Total dihedral angle restraints	0
Structure statistics
Violations (mean ± SD)
Distance constraints (Å)	0.0354 ± 0.0007
Maximum distance constraint violation (Å)	0.437
Deviations from idealized geometry
Bond lengths (Å)	0.0171 ± 0.0003
Bond angles (°)	2.04 ± 0.04
Impropers (°)	2.3 ± 0.1
Avg. rmsd of 20 structures to the mean (Å)
Heavy (ordered regions)	1.19 ± 0.16 (0.83 ± 0.13)
Backbone (ordered regions)	0.47 ± 0.11 (0.32 ± 0.10)