Table 1.

Summary of experimental constraints and structure calculation statistics for ψ₃₂-ACSL^Phe

Constraint
NOE distance constraints
Intraresiduea	88
Interresidue	150
Mean number per residue	14.0
NOE constraints by category
Very strong (1.8–3.0 Å)	7
Strong (1.8–4.0 Å)	24
Medium (1.8–5.0 Å)	70
Weak (1.8–6.0 Å)	88
Very weak (1.8–7.0 Å)	49
Base pair constraints
Totalb	36
Dihedral angle constraints
Ribose ringc	26
Backbone	48
Mean number per residue	4.3
Violations
Average distance constraints > 0.3Åd	0
RMSDs for distance constraints (Å)	0.027
Average dihedral constraints > 0.5e	3.7
RMSDs for dihedral constraints (°)	0.26
RMSD from ideal geometryf
Bonds (Å)	0.006
Angles (°)	1.4

^aOnly conformationally restrictive constraints are included.

^bThe number of base pair constraints includes U₃₃•A₃₇ base pair constraints.

^cThree torsion angles within each ribose ring were used to constrain the ring to either the C2′-endo or C3′-endo conformation. The ring pucker of residues U₃₃ and A₃₇ were not constrained.

^dA distance violation of 0.3 Å corresponds to 5.0 kcal energy penalty.

^eA dihedral angle violation of 0.5° corresponds to 0.05 kcal energy penalty.

^fCalculated for the minimized average structure.