Table 1 Data collection and refinement statistics.

	SeMet-serpin18	serpin18
Data collection
Space group	P4₁2₁2	P4₁2₁2
Unit cell (Å,°)	109.64, 109.64, 72.92 90, 90, 90	109.30, 109.30, 72.55 90, 90, 90
Molecules per asymmetric unit	1	1
Resolution range (Å)^a	50.00–1.60 (1.63–1.60)^a	50.00–1.65 (1.71–1.65)^a
Unique reflections	58,521 (2,856)^a	53,389 (5, 240)^a
Completeness (%)	100.0 (100.0)^a	99.9 (100.0)^a
<I/σ(I)>	83.52 (13.46)^a	23.74 (7.44)^a
R_merge^b (%)	19.4 (69.7)^a	10.1 (44.5)^a
Average redundancy	29.0	12.1
Structure refinement
Resolution range (Å)		50.00–1.65 (1.69–1.65)^a
R-factor^c/R-free^d (%)		17.7/20.7
Number of protein atoms		3032
Number of water atoms		518
RMSD^e bond lengths (Å)		0.011
RMSD bond angles (º)		1.496
Mean B factors (Å²)		21.07
Ramachandran plot^f
Most favored (%)		98.4
Additional allowed (%)		1.6
PDB entry		4R9I

^aValues in parentheses are for the highest resolution shell.
^bR_merge = ∑_hkl∑_i|I_i(hkl)–<I(hkl)>| / ∑_hkl∑_i|I_i(hkl)|, where I_i(hkl) is the intensity of an observation and <I(hkl)> is the mean value for its unique reflection; Summations are over all reflections.
^cR-factor = ∑_h||Fo(h)|–|Fc(h)||/∑_h|Fo(h)|, where Fo and Fc are the observed and calculated structure-factor amplitudes, respectively.
^dR-free was calculated with 5% of the data excluded from the refinement.
^eRoot-mean square-deviation from ideal values.
^fCategories as defined by MolProbity.

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