. Author manuscript; available in PMC: 2020 Oct 24.

Published in final edited form as: J Phys Chem B. 2019 Oct 14;123(42):8939–8953. doi: 10.1021/acs.jpcb.9b05869

Table 1.

X-ray Crystallography and Data Collection and Refinement Statistics

PDB code	6DUJ
Beamline	SSRL SMB 9–2
Wavelength (Å)	1.07
Resolution range (Å)	33.32–1.82 (1.89–1.82)^*
Space group	C 2 2 2₁
Unit cell dimensions
a, b, c (Å)	62.4, 184.4, 35.7
α, β, γ (°)	90, 90, 90
Unique reflections	18770 (1878)^*
Multiplicity	6.5 (5.3)^*
Completeness (%)	98.7 (99)^*
Mean I/σ(I)	24.5 (6.1)^*
Wilson B-factor	21.98
R_sym^†	0.07 (0.27)^*
Refinement
R_work^§	0.184 (0.292)^*
R_free^§	0.235 (0.317)^*
Number of total atoms	1787
protein	1610
heme	86
solvent	91
Total protein residues	210
RMS (bonds, Å)	0.02
RMS (angles, °)	1.62
Ramachandran favored (%)^††	98
Rotamer outliers (%)^††	0
Average B-factor (Å²)	32.34
macromolecules (Å²)	33.00
heme (Å²)	13.90
solvent (Å²)	38.80

Data for highest resolution shell are given in brackets.

^†

R_sym =∑_hkl ∑_i | I_i (hkl)- 〈I (hkl)〉|/ ∑_hkl ∑_i I_i (hkl) where I_i (hkl) is the ith observation of the intensity of the reflection hkl.

^§

R_work =∑_hkl || F_obs|-|F_calc||/ ∑_hkl |F_obs|, where F_obs and F_calc are the observed and calculated structure-factor amplitudes for each reflection hkl. R_free was calculated with 5% of the diffraction data that were selected randomly and excluded from refinement.

^††

Calculated using MolProbity.⁵²