TABLE 2.

Crystallographic data measurement and refinement data

	ClfB(199–542)	ClfB((212–542) )·K10 peptide	ClfB((212–542) )·Fg α-chain peptide
Cell dimensions
a, b, c	96.4, 96.4, 84.1 Å	85.6, 85.6, 84.8 Å	86.2, 86.2, 83.9 Å
α, β, γ	90°	90°	90°
Space group	P43 21 2	P43	P43
Max resolution	2.45 Å	2.60 Å	2.50 Å
Reflections unique	15,061	18,830	21,349
Completeness	98.9% (96.0%)	99.6% (99.8%)	99.8% (100%)
Rmergea	0.061	0.080	0.061
No. of molecules in the asymmetric unit	1	1	1
R-factor/Rfreeb	0.204/0.281	0.182/0.219	0.178/0.207
Average B value	31.3 Å	38.2 Å	25.8 Å
No. of non-hydrogen atoms	2821	2653	2733
Protein	2642	2463	2463
Peptide		56	66
Water	179	134	204
Root mean square deviations from ideal values
Bond lengths	0.006 Å	0.019 Å	0.016 Å
Bond angles	1.20°	1.64°	1.55°

^a R_merge = Σ|I_j − 〈I〉|/Σ I_i; where I_j is the measured and 〈I〉 is the mean intensity of reflection hkl.

^b +R_free is calculated over 5% of randomly selected reflections not included in the refinement.