Table 1.

NMR and Refinement Statistics for the Model Structure of MESD45–184

	Protein
NMR Distance and Dihedral Constraints
Distance constraints
Total NOE	656
Intraresidue	0
Inter-residue	656
Sequential (|i − j| = 1)	296
Medium range (|i − j| ≤ 4)	108
Long range (|i − j| > 4)	252
Hydrogen bonds	106
Total dihedral angle restraints (Talos; Cornilescu et al. [1999])	226
ϕ	113
Ψ	113
Total RDCs	36
Within α1	4
Structure statistics
Violations (average of 20 conformers)
Distance constraints (>0.3 Å)	0.1
Dihedral angle constraints (>5°)	0.05
Maximum dihedral angle violation (°)	5.5
Maximum distance constraint violation (Å)	0.36
Deviations from idealized geometry
Bond lengths (Å)	0.006
Bond angles (°)	0.7
Average pairwise rmsd among 20 refined structures (Å)
Heavy	1.2
Backbone	0.7
MolProbity Clashscore (raw score/Z score)220	26.35/−3.00