Table 1.

Data collection and refinement statistics

Measurement	Value
Data collection
Resolution, Å	2.15
Measured reflections	54,641
Unique reflections	7,998
Completeness, %	99.7 (99.2)*
Rmerge†	0.066 (0.126)*
Refinement
Resolution range, Å	30.0–2.15
No. of reflections	7,829
Sigma cutoff	None
Rcryst‡	0.213
Rfree§	0.276
No. of protein atoms	1,185
No. of bepridil atoms	81
No. of Ca2+ atoms	3
No. of water molecules	136
rms deviation bond lengths, Å	0.017
rms deviation angles, °	1.48

^*Values for the highest resolution bin (2.23–2.15 Å) are shown in parentheses. 

^†R_merge = Σ_hkl|I − 〈I〉|/ΣI_hkl. 

^‡ R_cryst = Σ_hkl||F_obs| − |F_calc||/Σ_hkl|F_obs|, where F_calc and F_obs are the calculated and observed structure factor amplitudes, respectively. 

^§ R_free is the same as R_cryst except that the summation is over 5% of the reflections, which were randomly selected and excluded from the refinement (21).