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. Author manuscript; available in PMC: 2023 Mar 7.
Published in final edited form as: Nature. 2021 May 26;595(7865):130–134. doi: 10.1038/s41586-021-03579-z

Extended Data Table 1 |. Cryo-EM data collection, refinement and validation statistics.

PCFT-NB (EMDB-12140) (PDB7BC6) PCFT-NB + pemetrexed (EMDB-12141) (PDB7BC7)
Data collection and processing
Magnification 105,000 105,000
Voltage (kV) 300 300
Electron exposure (e-/Å2) 59.1 58.5
Defocus range (μm) 0.8 – 2.5 0.8 – 2.5
Pixel size (Ă) 0.832 0.832
Symmetry imposed C1 C1
Initial particle images (no.) 5,538,959 9,420,673
Final particle images (no.) 174,399 341,318
Map resolution (Å) 3.2 3.3
 FSC threshold 0.143 0.143
Map resolution range (Å) 3.2–3.6 3.2–4.4
Refinement
Initial model used (PDB code) None 7BC6
Model resolution (Å) 3.2 3.3
 FSC threshold 0.143 0.143
Model resolution range (Å) 3.2–3.6 3.2–4.4
Map sharpening B factor (Å2) −95.3 −81.8
Model composition
 Non-hydrogen atoms 4178 4209
 Protein residues 549 549
 Ligands 0 LYA: 1
B factors (Å2)
 Protein 39.19 55.49
 Ligand N/A 60.24
R.m.s. deviations
 Bond lengths (Å) 0.008 0.008
 Bond angles (°) 0.893 0.870
Validation
 MolProbity score 1.95 2.13
 Clashscore 9.52 12.19
 Poor rotamers (%) 0.92 0.23
Ramachandran plot
 Favored (%) 93.03 90.46
 Allowed (%) 6.97 9.36
 Disallowed (%) 0.00 0.18