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. Author manuscript; available in PMC: 2020 May 7.
Published in final edited form as: Nature. 2019 Nov 7;577(7789):275–279. doi: 10.1038/s41586-019-1759-1

Extended Data Table 1 |.

Cryo-EM data collection, structure refinement and model statistics.

HMPV L:P complex (EMDB-20651) (PDB 6U50)
Data collection and processing
Magnification (nominal/calibrated) 31,000/40,322.58
Voltage (kV) 300
Electron exposure (e-/Å2) 48
Defocus range (μm) 1.5–3.0
Pixel size (Å) 1.24
Symmetry imposed Cl
Initial particle images (no.) 5,381,943
Final particle images (no.) 302,346
Map resolution (Å) 3.7
 FSC threshold 0.143
Map resolution range (Å) ∞-3.7
Refinementa
Initial model used (PDB code) -
Model resolution (Å) 3.7
 FSC threshold 0.5
Model resolution range (Å) ∞-3.7
Map sharpening B factor (Å2) −188.25
Model composition
 Non-hydrogen atoms 12,977
 Protein residues 1,623
 Ligands -
B factors (Å2)
 Protein 15.62 (5.27–52.43)
 Ligand -
R.m.s. deviations
 Bond lengths (Å) 0.004
 Bond angles (°) 0.717
Validationb
 MolProbity scorec 1.31 (98th percentile)
 Clashscore 2.13
 Poor rotamers (%) 0.00
Ramachandran plot
 Favored (%) 100.00
 Allowed (%) 0.00
 Disallowed (%) 0.00
1

Refinement statistics were obtained with program Phenix (phenix.real_space_refinement) (ref 30) except otherwise noted.

2

Molprobity score was obtained from the Molprobity online server (100th percentile is the best among structures within the resolution specified) and the present structure is in the 98th percentile (N=27675, 0 – 99Å)

3

The assignment of Pro-1041 as a cis-Proline is supported by electron density showing a hydrogen bond between the carbonyl oxygen atom of Thr-1040 and the N atom of Gln-1353.