Table 1.

NMR and refinement statistics for DsbB protein structures.

	DsbB[CSSC]	DsbB[CSSC] – UQ2
NMR distance and dihedral constraints
Distance constraints
NOEs
Intra-residue	41	44
Inter-residue
Sequential (|i − j| = 1)	191	191
Medium-range (1 < |i − j| < 5)	216	216
Long-range (|i − j| > 4)	39	39
Intermolecular	NA	10
Ambiguous	14	14
Hydrogen bonds	97	97
Paramagnetic relaxation enhancements
Upper bound	871	872
Lower bound	273	274
Total dihedral angle restraints
ϕ	144	144
ψ	151	151
Residual dipolar couplings
1DHN	114	114
1DNC’	109	109
1DC’Cα	114	114
Structure statistics	20 structures	20 structures
Violations (mean and s.d.)
Distance constraints (Å)	0.0099±0.0008	0.0098±0.0009
Dihedral angle constraints (°)	0.204±0.031	0.206±0.027
Residual dipolar couplings (Hz)
HN	2.64±0.08	2.63±0.06
NC’	0.049±0.001	0.049±0.001
C’Cα	1.20±0.02	1.21±0.01
Deviations from idealized geometry
Bond lengths (Å)	0.0017±0.0000	0.0017±0.0000
Bond angles (°)	0.402±0.003	0.403±0.002
Impropers (°)	0.248±0.005	0.250±0.004
Ramachandran plot statistics* (%)
Residues in most favored regions	86.9	90.0
Residues in additionally allowed regions	10.0	9.2
Residues in generously allowed regions	3.1	0.8
Residues in disallowed regions	0	0
Average pairwise r.m.s. deviation*(Å)
Heavy	1.75	1.67
Backbone	0.80	0.70

^*Statistics applied in structure rigid regions (aa 4–97and 114–164, see Figure 3C).