Table 2. Statistics for the top 20 NMR structures of Dec.

Experimental restraints
Total number of NMR restraints	1009
Total number of NOE distance restraints	767
Ambiguous	73
Unambiguous	694
Long range (|i-j| > 4)	124
Medium range (|i-j|)≤4)	93
Sequential (|i-j|)=1)	281
Intra-residue NOEs	269
Total number of dihedral restraints	174
φ/ ψ	127
χ1	47
Hydrogen bond restraints (34*2)	68
RMSD from experimental restraints*
NOE distance (Å)	0.054 ± 0.003
Dihedral (°)	0.42 ± 0.14
RMSD from ideal geometry
Bonds (Å)	0.0042 ± 0.0001
Angles (°)	0.55 ± 0.02
Improper angles (°)	1.68 ± 0.12
EL-J (kcal/mol)	- 316 ± 44
RMSD from mean NMR structure	Backbone†	All Heavy Atoms
Entire protein 1–134 (Å)	>9.5	>9.5
Folded regions 12–86 (Å)	1.33 ± 0.21	1.95 ± 0.32
OB-fold 18–77 (Å)	1.08 ± 0.18	1.66 ± 0.25
OB-fold 2o structure‡ (Å)	0.84 ± 0.15	1.57 ± 0.31
Procheck Ramachandran Plot Statistics§
Most favored (%)	89.1
Additionally allowed (%)	10.9
Generously allowed (%)	0.0
Disallowed (%)	0.0
Quality Z Scores from PSVSe
Procheck (ϕ,ψ)	−2.64
Molprobity Clash	−1.19

^* Structures had no NOE violations > 0.5 Å nor dihedral violations > 5 degrees.

^† Atoms: Cα, N, C, O.

^‡ Calculated over residues in the OB-fold portion: 21–32 (β1), 35–40 (β2), 47–50 (β3), 52–59 (α_OB), 63–68 (β4), 73–77 (β5), a total of 41 amino acids.

^§ Calculated with the PSVS server (http://psvs-1_5-dev.nesg.org) using only the folded parts of Dec (residues 12–89).