Extended Data Table 3. Crystallographic data collection and refinement statistics.

Crystallographic data collection and refinement statistics for LBD structures.

DATA COLLECTION	(2S,4R)-4-MethylGlu	LY466195 - Glu
Space group	P61	P6122
Unit cell a, b, c (Å)	52.3, 52.3, 170.9	102.8, 102.8, 282.0
a, β, g	90, 90, 120	90, 90, 120
Number per a.u.	1	2
Wavelength (Å)	1.0000	1.0000
Resolution (Å) a	30 – 1.27 (1.29)	30 – 1.8 (1.83)
Unique observations	68757	82330
Mean redundancy b	7.0 (4.7)	14.5 (14.2)
Completeness (%) b	99.4 (95.2)	100 (100)
Rmergebc	0.043 (0.335)	0.058 (> 1)
Rpimbd	0.017 (0.166)	0.017 (0.326)
I/s(I)b	45.6 (3.8)	48.4 (2.8)
REFINEMENT
Resolution (Å)	27.29 – 1.27	29.86 – 1.80
Protein atoms (AC) e	2127 (80)	4125 (95)
Ligand atoms	11	34
Li/Cl/SO4 ions	-/-/-	2/10/2
Water atoms	410	533
Rwork/Rfree (%) f	14.3/16.3	16.4/18.7
rms deviations
Bond lengths (Å)	0.009	0.014
Bond angles °	1.24	1.40
Mean B-Values (Å2)
Protein overall	20.9	27.5
MC/SC g	18.6/23.2	23.4/31.7
Ligand	13.2	19.8
Li/Cl/SO4 ions	-/-/-	23.8/57.1/34.8
Water	34.9	34.1
Ramachandran % h	97.8/0	97.9/0

Superscripts a–h denote the following:

^aValues in parenthesis indicate the low resolution limit for the highest-resolution shell of data.

^bValues in parenthesis indicate statistics for the highest-resolution shell of data.

^cR_merge = (Σ|I_I − <I_I>|)/Σ_I |I_I|, where <I_I> is the mean I_I over symmetry–equivalent reflections.

^d ${\mathrm{R}}_{\text{pim}}=(\sqrt{1/(\mathrm{n}-1)}{\mathrm{\sum }}_{I=1}^{\mathrm{n}}\mathrm{I}{\mathrm{I}}_I\mathrm{I})/{\mathrm{\sum }}_I{\mathrm{I}}_I$, where <I_I> is the mean I_I over symmetry–equivalent reflections.

^eAlternate conformations.

^fR_work = (Σ ||F_o| − |F_c||)/Σ |F_o|, where F_o and F_c denote observed and calculated structure factors, respectively; 5% of the reflections were set aside for the calculation of the R_free value.

^gMain chain/Side chain.

^hPreferred/Disallowed conformations.