Table 1.

Cryo-EM data collection, processing, refinement and validation statistics

	F518HCa (EMD-15914) (PDB 8B8J)	F518HnoCa (EMD-15913) (PDB 8B8G)	F518HCaND (EMD-15919) (PDB 8B8Q)	N562ACacc (EMD-15916) (PDB 8B8K)	N562ACaoc (EMD-15917) (PDB 8B8M)
Data collection and processing
Magnification	130.000	130.000	130.000	130.000	130.000
Voltage (kV)	300	300	300	300	300
Electron exposure (e–/Å2)	66.6/68.1	69.8	76 (UltrAuFoil tilt)/ 84.2 (UltrAufoil)/66.6 (GO)	62.4	62.4
Defocus range (μm)	−1 to −2.4	−1 to −2.4	−1 to −2.4	−1 to −2.4	−1 to −2.4
Pixel size (Å)	1.302	1.302	1.302	1.302	1.302
Symmetry imposed	C2	C2	C1	C2	C1
Initial particle images (no.)	1,600,461	2,901,588	3,399,184	1,168,595	1,168,595
Final particle images (no.)	394,821	181,753	282,719	239,346	124,276
Map resolution (Å)	2.96	3.39	2.93	3.01	3.49
FSC threshold	0.143	0.143	0.143	0.143	0.143
Map resolution range (Å)	2.7–4.0	2.9–5.0	2.8–5.0	2.8–3.5	3.0–5.0
Refinement
Initial model used (PDB code)	6QP6	6QPB	6QP6	6QP6	6QP6
Model resolution (Å)	3.1	3.6	3.1	3.0	3.7
FSC threshold	0.5	0.5	0.5	0.5	0.5
Model resolution range (Å)	2.8–3.1	3.2–3.6	2.8–3.1	2.7– 3.0	3.2– 3.7
Map sharpening B factor (Å2)	108.3	112.9	85	97.7	78.5
Model vs. Map CC (mask)	0.76	0.82	0.78	0.81	0.76
Model composition
Non-hydrogen atoms	11,686	12,086	11,370	12,324	11,758
Protein residues	1418	1464	1382	1482	1423
Ligands	6 Ca2+		6 Ca2+	6 Ca2+ + 2 P1O	6 Ca2+
B factors (Å2)
Protein	136.63	114.71	120.20	113.15	109.84
Ligand	124.86		109.53	112.40	99.04
R.m.s. deviations
Bond lengths (Å)	0.003	0.004	0.003	0.003	0.003
Bond angles (°)	0.464	0.556	0.486	0.500	0.532
Validation
MolProbity score	1.53	2.52	2.50	1.85	2.26
Clashscore	6.85	10.96	9.87	6.75	9.98
Poor rotamers (%)	1.25	7.59	7.36	2.92	4.46
Ramachandran plot
Favored (%)	97.54	95.75	95.32	97.36	96.32
Allowed (%)	2.46	4.25	4.68	2.64	3.68
Disallowed (%)	0.00	0.00	0.00	0.00	0.00