Table 2 X-ray data collection and crystallographic refinement statistics.
| Â | H3_3I14 | H3_D93N | H6_D93N | H10_3I14 |
|---|---|---|---|---|
PDB ID | 6WF0 | 6WEZ | 6WEX | 6WF1 |
Data collection | ||||
 Space group | P63 | P63 | R32 | P321 |
 Cell dimensions | ||||
  a (Å) | 130.32 | 130.84 | 117.81 | 127.02 |
  b (Å) | 130.32 | 130.84 | 117.81 | 127.02 |
  c (Å) | 188.55 | 189.34 | 438.26 | 158.37 |
  α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
 Resolution (Å) | 42.66–3.46 (3.58–3.45) | 39.02–3.21 (3.32–3.21) | 48.26–3.49 (3.60–3.49) | 41.58–4.19 (4.34–4.19) |
 Unique reflections | 23,612 (2349) | 29,818 (2918) | 15,294 (1421) | 9561 (775) |
 Total reflections | 130,821 (12,953) | 140,225 (14,027) | 144,741 (13,615) | 32,231 (1783) |
  Rmerge | 0.196 (0.992) | 0.141 (1.147) | 0.168 (0.649) | 0.110 (0.581) |
  Rpim | 0.090 (0.459) | 0.072 (0.581) | 0.058 (0.219) | 0.063 (0.406) |
  I/σI | 8.9 (1.7) | 10.2 (1.2) | 9.9 (3.2) | 8.8 (1.5) |
  CC1/2 | 0.989 (0.390) | 0.996 (0.596) | 0.995 (0.86) | 0.987 (0.646) |
 Completeness (%) | 99.1 (98.7) | 98.8 (97.6) | 99.3 (94.5) | 84.5 (70.2) |
 Redundancy | 5.5 (5.5) | 4.7 (4.8) | 9.5 (9.6) | 3.4 (2.3) |
Refinement | ||||
 Resolution (Å) | 42.66–3.46 | 39.02–3.21 | 48.26–3.49 | 41.58–4.19 |
 Unique reflections | 23,516 (2353) | 29,741 (2964) | 15,291 (1421) | 9564 (778) |
 Rwork/Rfree | 0.231/0.282 | 0.232/0.281 | 0.276/0.333 | 0.261/0.309 |
 No. atoms: | ||||
  Protein | 6959 | 6959 | 7109 | 6959 |
  Ligand | 211 | 206 | 14 | 14 |
 B-factors (Å2) | ||||
  Average | 100 | 95 | 112 | 244 |
  Hemagglutinin | 79 | 73 | 86 | 235 |
  Glycans | 121 | 111 | 108 | 257 |
  Antibody | 124 | 120 | 145 | 256 |
 R.m.s. deviations | ||||
  Bond lengths (Å) | 0.003 | 0.003 | 0.002 | 0.002 |
  Bond angles (°) | 0.66 | 0.68 | 0.63 | 0.49 |
 Ramachandran | ||||
  Favored (%) | 92.16 | 94.92 | 92.31 | 94.51 |
  Allowed (%) | 7.84 | 5.08 | 7.58 | 5.49 |
  Outliers (%) | 0 | 0 | 0.11 | 0 |
