Table 1.

Structural statistics and root-mean-square deviation for 20 structures of S. pneumoniae CMP kinase

Structural statisticsa	≤SA>	≤>r
Rmsd from experimental distance restraints (Å)b
All (3100)	0.014 ± 0.001	0.014
Intraresidue (906)	0.016 ± 0.001	0.016
Sequential (777)	0.017 ± 0.001	0.017
Medium range (597)	0.011 ± 0.001	0.010
0    Long range (712)	0.010 ± 0.002	0.010
Hydrogen bond (108)	0.012 ± 0.001	0.011
Rmsd from experimental torsional angle restraints (deg)c
φ and ξ angles (326)	0.24 ± 0.02	0.25
CNX potential energies (kcal mole−1)
Etot	144 ± 5	140
Ebond	6 ± 0.3	6
Eang	85 ± 2	84
Eimp	7 ± 0.6	7
Erepel	12 ± 1	12
Enoe	33 ± 3	30
Ecdih	1 ± 0.2	1
Rmsd from idealized geometry
Bonds (Å)	0.00 ± 0.00	0.00
Angles (deg)	0.29 ± 0.00	0.29
Impropers (deg)	0.16 ± 0.01	0.15
Cartesian coordinate rmsd (Å)	N, Cα, and C′	All heavy
≤SA> vs. ≤>d	1.04 ± 0.21	1.46 ± 0.19
≤SA> vs. ≤>e	0.74 ± 0.15	1.13 ± 0.12

^a Where ≤SA> is the ensemble of 20 NMR-derived solution structures of S. pneumoniae CMP kinase; ≤> is the mean atomic structure; ≤>_r is the energy-minimized average structure. The CNX F_repel function was used to simulate van der Waals interactions using a force constant of 4.0 kcal mole⁻¹ Å⁻⁴ with the atomic radii set to 0.8 times their CHARMM values (Brooks et al. 1983).

^b Distance restraints were used with a square-well potential (F_noe = 50 kcal mole⁻¹ Å⁻²). Hydrogen bonds were given bounds of 1.8–2.4 Å (H−O) and 2.7–3.3 Å (N−O). No distance restraint was violated by more than 0.3 Å in any of the final structures.

^c Torsional restraints were applied with values derived from an analysis of the C′, N, C_α, H_α, and C_β chemical shifts using the TALOS program (Cornilescu et al. 1999). A force constant of 200 kcal mole⁻¹ rad⁻² was applied for all torsional restraints.

^d Rmsd for the residues 16–234.

^e Rmsd for the residues 16–161 and 208–234 in the core and substrate-binding domains.