Table 1.

Structural Statistics for the Solution Structure of BaSrtC_Δ55^a

	〈SA〉	${(\overline{\text{SA}})}_{\mathrm{r}}$
rmsd from NOE restraints (Å)b
all (2330)	0.029 ± 0.001	0.046
sequential (|i − j| = 1) (617)	0.032 ± 0.001	0.058
medium-range (|i − j| ≤ 4) (292)	0.039 ± 0.002	0.054
long-range (|i − j| ≥ 5) (977)	0.027 ± 0.001	0.040
intraresidue (444)	0.021 ± 0.001	0.034
rmsd from dihedral angles restraints (deg)c (196) deviation from idealized covalent geometry	0.182 ± 0.087	0.095
bonds (Å)	0.007 ± 0.003	0.004
angles (deg)	0.414 ± 0.172	0.523
impropers (deg)	0.191 ± 0.081	0.493
PROCHECK results (%)d
most favorable region	85.6 ± 2.6	89.0
additionally allowed region	14.4 ± 2.6	11.0
generously allowed region	0.0 ± 0.0	0.0
disallowed region	0.0 ± 0.0	0.0
coordinate precision (Å)e,f
protein backbone	0.42 ± 0.07
protein heavy atoms	0.82 ± 0.05

^aThe notation of the NMR structures is as follows. 〈SA〉 represents the final 20 simulated annealing structures. ${(\overline{\text{SA}})}_{\mathrm{r}}$ represents the average energy-minimized structure. The number of terms for each restraint is given in parentheses.

^bNone of the structures exhibited distance violations of >0.5 Å or dihedral angle violations of >5°.

^cThe experimental dihedral angle restraints were as follows: 95 ϕ, 94 ψ, and 39 χ₁ angular restraints.

^dDetermined using PROCHECK.⁶²

^eThe coordinate precision is defined as the average atomic rmsd of the 20 individual SA structures and their mean coordinates. These values are for residues 63−85, 94−113, 124−172, and 182−198 of BaSrtC_Δ55. Backbone atoms are N, C^α, and C′. Assignments were made for residues 58−89, 93−115, 122−183, and 184−198 of BaSrtC_Δ55.

^fStructure calculations also included 58 hydrogen bonds. These bonds were included in xplor structure calculations as HBDB terms as described in ref 32.