Table 2. Structure-refinement statistics.

Resolution range	23–1.95
No. of protein atoms	2572
No. of cadmium/chloride ions	1/1
No. of water molecules	226
Rcryst† (%) (No. of reflections)	21.0 (27186)
Rfree† (%) (No. of reflections)	25.7 (1486)
R.m.s.d. bonds (Å)	0.020
R.m.s.d. angles (°)	2.16
Average B factor (Å2)	25.3
Residues not modelled	Monomer A/B, tag residues, 177–183, 1–3; monomer A, 4, 15–18, 126–129
Residues in multiple conformations	B123, B138
Ramachandran plot, nonglycine/proline residues
In most favoured regions	267 (97.1%)
In additionally allowed regions	8 (2.9%)

^† R _cryst = , where F _o is the observed structure-factor amplitude and F _c is the calculated structure-factor amplitude. R _free is calculated based on 5% of reflections not used in refinement.