Table 1. X-ray Diffraction Data Collection and Refinement of Monoclinic Structures^a.

	AA	NAD+	apo
beamline	APS 19-ID-C	ALS 4.2.2	APS 24-ID-E
space group	C2	C2	C2
unit cell parameters	a = 154.4 Å	a = 155.7 Å	a = 157.0 Å
	b =  162.5 Å	b =  161.6 Å	b =  162.5 Å
	c =  158.7 Å	c =  158.9 Å	c =  160.0 Å
	β = 95.0°	β = 94.8°	β = 94.1°
wavelength	0.979	1.000	0.979
resolution (Å)	47.9–1.76 (1.79–1.76)	62.9–2.00 (2.03–2.00)	16.0–2.40 (2.44–2.40)
no. of observations	1405606	995590	559499
no. of unique reflections	381768	261450	153212
Rmerge(I)	0.066 (0.657)	0.106 (1.050)	0.150 (0.313)
Rmeas(I)	0.078 (0.773)	0.123 (1.224)	0.176 (0.370)
Rpim(I)	0.040 (0.404)	0.063 (0.626)	0.063 (0.626)
mean I/σ	12.3 (1.9)	12.7 (1.3)	6.3 (3.1)
mean CC1/2	0.998 (0.682)	0.997 (0.632)	0.967 (0.874)
completeness (%)	99.4 (99.8)	99.5 (96.1)	98.2 (99.7)
multiplicity	3.7 (3.6)	3.8 (3.7)	3.7 (3.5)
no. of protein chains	8	8	8
no. of protein residues	4070	4062	4056
no. of protein atoms	30562	30440	29450
no. of AA atoms	88	–	–
no. of NAD+ atoms	–	200	–
no. of water molecules	1899	1345	557
Rcryst	0.168 (0.261)	0.171 (0.288)	0.226 (0.243)
Rfreeb	0.206 (0.308)	0.218 (0.352)	0.275 (0.312)
rmsd for bond lengths (Å)	0.006	0.007	0.003
rmsd for bond angles (deg)	1.000	1.021	0.738
Ramachandran plotc (%)
favored	96.97	96.91	96.93
outliers	0.25	0.20	0.02
all-atom Clashscorec	2.1	2.5	2.3
average B factor (Å2)
protein	24.5	30.0	37.4
AA	31.3	–	–
NAD+	–	40.0	–
water	29.3	29.7	28.4
coordinate error (Å)d	0.20	0.24	0.36
PDB entry	4ZUL	4ZUK	4ZVW

^aValues for the outer resolution shell of data are given in parentheses.

^bThe 5% test set.

^cGenerated with MolProbity via PHENIX refine.

^dMaximum likelihood-based coordinate error estimate reported by PHENIX refine.