Table 2.

Least-Squares Refinement Statistics.

	Wild-type Protein Complexed with SAM and dTDP-phenol	Wild-type Protein Complexed with SAH and dTDP-Quip3N	H123A Mutant Protein Complexed with SAH and dTDP-Quip3N	H123N Mutant Protein Complexed with SAH and dTDP- Quip3N
resolution limits (Å)	100 – 1.35	100 – 1.79	100 – 1.8	100 – 1.65
aR-factor (overall) %/no. reflections	18.5/55697	21.2/50622	18.6/47216	19.7/60948
R-factor (working)%/no. reflections	18.3/52903	20.9/48053	18.3/44824	19.4/57875
R-factor (free)%/no. reflections	20.9/2794	26.6/2569	24.5/2392	24.5/3073
number of protein atoms	1,842b	3,679d	3,660f	3,688h
number of heteroatoms	334c	604e	513g	544i
average B value (Å2)
protein atoms	15.3	20.0	16.1	15.6
ligands	9.3	13.0	9.6	8.3
solvent	26.6	31.9	25.9	27.3
weighted RMS deviations from ideality
bond lengths (Å)	0.012	0.012	0.013	0.014
bond angles (deg)	2.2	2.1	2.3	2.3
planar groups (Å)	0.008	0.010	0.014	0.014

^aR-factor = (© | F_o − F_c | / © | F_o |) × 100 where F_o is the observed structure-factor amplitude and F_c is the calculated structure-factor amplitude.

^bThese include a multiple conformation for Glu 191

^cHeteroatoms include a dTDP-phenol molecule, a SAM molecule, an ethylene glycol molecule, and 272 waters.

^dThese include a multiple conformation for Arg 183 in subunit 1.

^eHeteroatoms include two dTDP-Quip3N molecules, two SAH molecules, an ethylene glycol molecule, and 478 waters.

^fThese include a multiple conformation for Arg 183 in subunit 1.

^gHeteroatoms include two dTDP-Quip3N molecules, two SAH molecules, an ethylene glycol molecule, and 387 waters.

^hThese include multiple conformations for Arg 183 in subunit 1, and Arg 90, Asn 123, and Glu 191 in subunit 2.

ⁱHeteroatoms include two dTDP-Quip3N molecules, two SAH molecules, two ethylene glycol molecules, and 414 waters.