Table 1.

Data collection and refinement statistics

	PYL2–Pyrabactin	PYL1–Pyrabactin–ABI1	PYL2 A93F–Pyrabactin	PYL2 A93F–Pyrabactin–HAB1	PYL2 A93F–Pyrabactin–ABI2
Data collection
Space group	C2221	P1	C2221	P212121	P212121
Cell dimensions
a, b, c(Å)	62.27, 105.07, 185.08	59.98, 66.71, 72.60	62.08, 105.57, 182.90	62.08, 105.57, 182.90	62.13, 97.59, 134.50
α,β,γ(°)	90, 90, 90	115.8, 95.4, 105.6	90, 90, 90	90, 90, 90	90, 90, 90
Resolution (Å)	30–1.85 (1.92–1.85)*	30–2.15 (2.23–2.15)	30–2.10 (2.18–2.10)	30–2.55 (2.64–2.55)	30–2.10 (2.18–2.10)
Rsym or Rmerge	0.100 (0.706)	0.098 (0.752)	0.093(0.725)	0.164(0.793)	0.102(0.764)
I/σI	32.2 (3.90)	49.1 (4.5)	27.6 (2.9)	15.9 (2.4)	32.4 (3.7)
Completeness (%)	96.9 (92.8)	97.6 (96.2)	99.9 (99.9)	100.0 (100.0)	100.0 (100.0)
Redundancy	12.7(12.8)	13.4 (2.3)	8.2 (8.4)	8.4 (8.6)	14.7 (14.6)
Refinement
Resolution (Å)	30–1.85	30–2.15	30–2.10	30–2.55	30–2.10
No. reflections	46913	46283	32811	18181	25445
Rwork / Rfree (%)	19.4/23.4	21.2%	23.0%	22.3%	19.4%
No. atoms
Protein	4259	6956	4259	3706	3574
Ligand/ion	66	48	66	34	96
Water	327	180	223	128	171
B-factors
Protein	39.49	48.59	55.39	49.61	46.35
Ligand/ion	67.16	42.23	101.40	84.16	40.79
Water	44.46	49.19	50.00	40.24	47.29
R.m.s. deviations
Bond lengths (Å)	0.016	0.021	0.022	0.018	0.023
Bond angles (°)	1.493	1.73	1.66	1.44	1.74

^*Values in parentheses are for highest-resolution shell. One crystal was used for each structure.