Table 2.

X-ray data collection, phasing, and refinement statistics

	SQLE•FAD• Cmpd-4′′	SeMet-SQLE•FAD•Cmpd-4′′			SQLE•FAD• NB-598	SQLE•FAD
	Native	Peak	Inflection	Remote
	PDB:6C6N				PDB:6C6P	PDB:6C6R
Data collection
Wavelength (Å)	0.97941	0.97909	0.97959	0.96108	0.97915	0.9792
Space group	P3221	P3221	P3221	P3221	P3221	P3221
Cell dimensions
a (Å)	126.96	127.1	127.2	127.23	127.86	126.39
b (Å)	126.36	127.1	127.2	127.23	127.86	126.39
c (Å)	166.12	165.91	166.14	166.24	165.09	166.01
α, β, γ (°)	90, 90, 120	90, 90, 120	90, 90, 120	90, 90, 120	90, 90, 120	90, 90, 120
Resolutiona (Å)	35.79–2.30	50–2.75	50–2.90	50–3.15	40.57–2.50	38.81–3.00
	(2.38–2.30)	(2.80-2.75)	(2.95–2.90)	(3.20–3.15)	(2.59–2.50)	(3.11–3.00)
Rmergea (%)	8.2 (55.5)	9.0 (53.5)	8.0 (51.8)	8.5 (48.9)	8.6 (54.1)	12.4 (68.8)
I/σIa	12.1 (3.0)	52.1 (7.7)	39.7 (5.1)	37.7 (6.4)	15.1 (2.5)	10.6 (2.5)
Completenessa (%)	98.8 (99.7)	100 (100)	100 (100)	99.9 (100)	88.5 (89.3)	99.6 (98.8)
Redundancya	5.2 (5.3)	18.4 (18.8)	9.1 (9.4)	9.1 (9.3)	4.8 (4.7)	7.4 (6.1)
Figure of merit (post-density modification)			0.24/0.74
Rcullis (anomalous)			0.84
Refinement
No. reflections	68379				48318	31143
Rwork/Rfree (%)	18.90/22.00				19.31/23.42	19.01/24.85
No. of atoms
Protein	7058				7050	7060
Ligand	401				363	315
Water	179				170	58
B-factors (Å2)
Protein	53.46				59.69	61.32
Ligand	57.33				61.35	57.17
Water	47.31				55.42	44.68
R.m.s deviations
Bond lengths (Å)	0.003				0.009	0.004
Bond angles (°)	0.58				0.99	0.68

^aValues in parentheses are for highest-resolution shell