TABLE 1.
Domain | H3 no.a | H5 no.a | Ind/05b | No. of samplesc | Residue(s) (no. of samples [%])d |
---|---|---|---|---|---|
Conserved interface residue | 95 (98) | 91 | Y | 12 | Y: 12 (100) |
130-loop | 132 | 128 | S | 12 | S: 12 (100) |
133 | 129 | S | 12 | S: 12 (92–100); P: 1 (8) | |
134 | 130 | G | |||
135 | 131 | V | |||
136 | 132 | S | |||
Conserved interface residue | 153 | 149 | W | 60 | W: 60 (97–100) |
Antigenic site | 155 | 151 | I | 60 | I: 60 (98–100) M: 1 (1), N: 1 (2) |
Conserved interface residue | 183 | 179 | H | 59 | H: 59 (98–100); R: 1 (2) |
190-helix | 186 | 182 | N | 59 | N: 59 (95–100); S: 3 (3–5); H: 1 (3) |
187 | 183 | D | 59 | N: 40 (25–100); D: 19 (75–100); T: 1 (100) | |
188 | 184 | A | 59 | E: 38 (3–100); A: 18 (75–100); G: 3 (95–97); K: 3 (2–100); V: 2 (100); T: 1 (6) | |
189 | 185 | A | 59 | A: 58 (98–100); E: 1 (99); K: 1 (1); T: 1 (2) | |
190 | 186 | E | 59 | E: 59 (92–100); G: 5 (1–4); A: 1 (3); K: 1 (3) | |
191 | 187 | Q | 59 | Q: 59 (99–100) | |
192 | 188 | T | 59 | T: 59 (98–100); A: 2 (2–2) | |
193 | 189 | R | 59 | M: 37 (26–100); R: 17 (74–100); K: 6 (100) | |
194 | 190 | L | 59 | L: 59 (99–100) | |
Conserved interface residue | 195 | 191 | Y | 59 | Y: 59 (98.33–100) |
220-loop | 224 | 220 | N | 59 | N: 59 (94–100); D: 1 (4); H: 1 (1); K: 1 (6); S: 1 (3) |
225 | 221 | G | 59 | G: 59 (82–100); E: 2 (2–2.3); R: 1 (18) | |
226 | 222 | Q | 59 | Q: 59 (80–100); R: 4 (2–20); K: 1 (5) | |
227 | 223 | S | 59 | S: 59 (97–100); R: 1 (1) | |
228 | 224 | G | 59 | G: 59 (97–100); R: 1 (3) |
Position according to H3 and H5 numbering after removal of the signal peptide.
Amino acid present in the sequence of reference strain A/Indonesia/5/2005 used in this work.
Number of samples with sequencing data available at the position mentioned.
Residues observed, number of samples in which the amino acid is observed, and proportion or proportion range within the sample(s).