Table 2.

Structure validation parameters for human β2-m conformers from NMR data refinement (DISCOVER)

Parameter	This work	Consensus standarda
Total residues/selected residuesb	100/83	74 ± 39/62 ± 36
Number of conformers	20	20 ± 15
Restraints per residuec,d	10.3	11.3 ± 4.5
NOE rms violation (/10−1 nm)e	0.079	0.061 ± 0.043
Ramachandran qualityb
Residues in most-favored regions	70.5%	73.6 ± 15.5%
Residues in additional allowed regions	28.2%	n.a.
Residues in generously allowed regions	1.0%	n.a.
Residues in disallowed regions	0.3%	n.a.
Average G-factorsb,f
ϕ − Ψ	−1.13	n.a.
χ1 −χ2	−1.03	n.a.
χ1 only	−0.14	n.a.
overall	−0.98	n.a.

n.a., not available.

^a From Doreleijers et al. 1998.

^b According to Doreleijers et al. (1998) the listed parameters, except for the NOE rms violation, were calculated on well-defined segments of the protein, namely only those residues for which the average of the circular variance of the backbone angles φ and Ψ was <0.2 were included in the selected segments.

^c To avoid the redundancy of considering upper and lower bounds, only a single distance bound per internuclear separation was included in the count. Thus, only 789 NOE and 67 dihedral angle restraints were included in the count.

^d Referred to the reduced NOE-restraint set above considered from well-defined segments.

^e Referred to all residues.

^f Low G-factors indicate low-probability conformations (Laskowski et al. 1996). As a rule of thumb, acceptable overall values range around −1.