Table 2.

Structural statistics for the 100 accepted (<SA>) and the energy minimized average (<SA>_r) NMR structures of [113-122]apoJ associated with DPC micelle

Experimental restraints
Intraresidue NOEs		41
Sequential NOEs		23
Medium and long range NOEs		19
(i,i+2; i,i+3; and i,i+4)
Other NOEs		8
Hydrogen bonds (H-O distance)		7
Φ angles		9
Ψ angles		8
Total		115
Mean r.m.s.d.a from experimental restraints		<SA> ± SDb
Distance restraints (Å)		0.022±0.004
Dihedral angle (°)		0.054±0.123
Mean r.m.s.d. from ideal geometry		<SA> ± SD
Bonds (Å)		0.001±0.000(4)
Angles (°)		0.473±0.029
Impropers (°)		0.374±0.038
Ramachandran statistics from PROCHECK-NMRc
Residues in most favored α helical region		100 %
r.m.s.d. from the average structure (Å)
Backbone N, Cα, C		0.296
All heavy atoms		1.371
Pairwise r.m.s.d. analysis
Average backbone pairwise r.m.s.d. (Å)		0.420 (±0.122)
Average non-hydrogen atom pairwise r.m.s.d. (Å)		1.875 (±0.264)
X-PLOR potential energies (kcal/mol)
	<SA> ± SD	(<SA>r)d
Eoverall	15.039±2.489	14.774
Ebond	0.378±0.147	0.408
Eangle	11.095±1.446	10.971
Eimpropers	1.969±0.424	1.809
Evdw	0.328±0.532	0.0
ENOE	1.248±0.522	1.585
Ecdih	0.018±0.072	0.0

^aRoot mean square deviation.

^bStandard deviation.

^cRef. [41]

^d200 cycles of conjugate gradient minimization were used. All of the NMR constraints were enforced during the energy minimization of the average coordinates.