Table 2.

NMR and refinement statistics for structures of apo- and p53 DBD-bound BCL-xL

	Apo-BCL-xLΔC	p53 DBD-bound BCL-xLΔC
NMR distance and dihedral constraints
Distance constraints
Total NOE	607	766
Intra-residue	59	54
Inter-residue	548	712
Sequential (|i − j| = 1)	225	283
Medium-range (|i − j| < 4)	164	266
Long-range (|i − j| > 5)	159	163
Intermolecular	0	0
Hydrogen bonds	48	70
Total dihedral angle restraints	216	208
ϕ	108	104
ψ	108	104
Structure statistics
Violations (mean ± s.d.)
Distance constraints (Å)	0.019 (0.002)	0.016 (0.003)
Dihedral angle constraints (°)	0.73 (0.16)	0.73 (0.17)
Max. dihedral angle violation (°)	5.25	4.69
Max. distance constraint violation (Å)	0.33	0.35
Deviations from idealized geometry
Bond lengths(Å)	0.013	0.013
Bond angles (°)	1.7	1.7
Impropers(°)
Average pairwise r.m.s. deviation** (Å)
Heavy	2.2	1.8
Backbone	1.6	1.1

^**r.m.s.d. calculated for the 20 lowest energy structures of each model and folded core residues 3–20, 87–193.