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. 2020 Jul 28;11(4):e00745-20. doi: 10.1128/mBio.00745-20

TABLE 1.

Crystallographic data collection and refinement statistics for native and complexed NJPyV and HPyV12 VP1 structures

Parametera Value for indicated structureb
NJPyV VP1
(6Y5X)c 		NJPyV VP1-
3′SL (6Y5Y)		 HPyV12 VP1
(6Y5Z)		 HPyV12 VP1-
3′SLN (6Y60)
Data collection statistics
    Space group P21 P21 P21 P212121
    Unit cell dimensions
        a, b, c (Å) 86.48, 151.76,
130.91		 86.38, 151.08,
130.62		 61.22, 136.42,
85.38		 83.32, 141.72,
251.30
        β (°) 106.85 106.56 109.57 90
    Resolution range (Å) 48.30–2.30
(2.36–2.30)		 48.20–1.80
(1.91–1.80)		 44.10–1.55
(1.64–1.55)		 47.40–1.80
(1.91–1.80)
    No. of unique reflections 143,046
(10,546)		 295,110
(47,350)		 181,696
(28,058)		 274,251
(42,872)
    Total no. of reflections 828,661
(60,401)		 1,695,688
(255,694)		 689,847
(106,706)		 1,930,655
(294,756)
    Rmeas (%) 25.1 (104.5) 15.6 (106.4) 5.6 (45.6) 12.5 (177.2)
    I/σI 6.7 (1.6) 9.8 (1.6) 16.4 (2.9) 12.2 (1.3)
    CC1/2 (%) 98.4 (63.8) 99.6 (66.6) 99.9 (85.5) 99.9 (72.5)
    Completeness (%) 99.9 (99.9) 99.8 (99.3) 95.0 (90.9) 99.4 (97.0)
    Wilson B-factors (Å2) 29.3 26.0 24.2 33.3
Refinement statistics
    Rwork/Rfree (%) 18.9/24.4 15.9/19.6 14.3/16.9 20.4/24.3
    No. of atoms
        Protein 21,197 21,615 10,318 19,809
        Water 839 2,796 1,547 1,829
        Glycan 430 287
    B-factor (Å2)
        Protein 29.8 23.3 17.5 33.3
        Water 24.4 33.4 30.4 37.5
        Glycan 31.9 41.1
    RMSD
        Bond length (Å) 0.008 0.010 0.009 0.009
        Bond angle (°) 1.578 1.656 1.548 1.629
a

Rmeas, data redundancy-independent R-factor; I/σI, intensity-to-noise ratio; CC1/2, half-set correlation coefficient; Rwork, refinement R-factor of work set; Rfree, refinement R-factor of test set.

b

Values in parentheses correspond to the highest data resolution shell.

c

PDB accession numbers are given in parentheses after the structure designations.