HRV14 native particle solved by cryoEM. Determined by electron microscopy at 2.6 Å resolution. Released 19 May 2021.
Explore 7BG6 in 3D Show helices and sheets RCSB PDB PDBe
7BG6 contains 39 α-helices and 55 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-20 | 3 | 1 |
| β-strand | 23 | 1 | 2 |
| β-strand | 34-35 | 2 | 3 |
| α-helix | 37-39 | 3 | |
| α-helix | 47-50 | 4 | |
| β-strand | 53 | 1 | 2 |
| β-strand | 56-57 | 2 | 1 |
| α-helix | 63-65 | 3 | |
| β-strand | 66 | 1 | 4 |
| α-helix | 67-70 | 4 | |
| β-strand | 75-84 | 10 | 5 |
| β-strand | 99-103 | 5 | 6 |
| α-helix | 110-116 | 7 | |
| β-strand | 119-135 | 17 | 5 |
| β-strand | 147-153 | 7 | 6 |
| α-helix | 166-169 | 4 | |
| β-strand | 175-179 | 5 | 6 |
| β-strand | 180 | 1 | 7 |
| β-strand | 182 | 1 | 7 |
| β-strand | 183-188 | 6 | 5 |
| β-strand | 197-198 | 2 | 5 |
| β-strand | 203 | 1 | 8 |
| α-helix | 212 | 1 | |
| α-helix | 217-219 | 3 | |
| β-strand | 223-228 | 6 | 6 |
| β-strand | 237-255 | 19 | 5 |
| α-helix | 257-258 | 2 | |
| β-strand | 259 | 1 | 9 |
| α-helix | 262-263 | 2 | |
| α-helix | 275-277 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-18 | 5 | 10 |
| β-strand | 21-25 | 5 | 10 |
| β-strand | 28 | 1 | 11 |
| β-strand | 32-33 | 2 | 11 |
| α-helix | 34-36 | 3 | |
| α-helix | 41-43 | 3 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54 | 1 | 11 |
| α-helix | 57-59 | 3 | |
| β-strand | 64-71 | 8 | 11 |
| β-strand | 78-82 | 5 | 12 |
| α-helix | 84-86 | 3 | |
| α-helix | 90-98 | 9 | |
| β-strand | 99-111 | 13 | 11 |
| β-strand | 119-128 | 10 | 12 |
| α-helix | 132-133 | 2 | |
| β-strand | 134 | 1 | 13 |
| α-helix | 140-143 | 4 | |
| α-helix | 144-147 | 4 | |
| β-strand | 154-155 | 2 | 12 |
| α-helix | 159-160 | 2 | |
| α-helix | 164 | 1 | |
| β-strand | 165 | 1 | 13 |
| α-helix | 166 | 1 | |
| α-helix | 169-171 | 3 | |
| β-strand | 176 | 1 | 9 |
| α-helix | 178-183 | 6 | |
| β-strand | 186-190 | 5 | 12 |
| β-strand | 196-201 | 6 | 11 |
| α-helix | 202-203 | 2 | |
| β-strand | 210 | 1 | 11 |
| β-strand | 215 | 1 | 8 |
| β-strand | 218-229 | 12 | 12 |
| α-helix | 230-231 | 2 | |
| β-strand | 238-254 | 17 | 11 |
| α-helix | 257-259 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-7 | 2 | |
| β-strand | 23 | 1 | 5 |
| α-helix | 28-33 | 6 | |
| β-strand | 39-40 | 2 | 5 |
| β-strand | 42 | 1 | 4 |
| α-helix | 43-46 | 4 | |
| β-strand | 51-52 | 2 | 3 |
| α-helix | 64-67 | 4 | |
| β-strand | 68-71 | 4 | 3 |
| β-strand | 73 | 1 | 14 |
| β-strand | 79-84 | 6 | 14 |
| α-helix | 90-92 | 3 | |
| α-helix | 96-101 | 6 | |
| β-strand | 104-108 | 5 | 15 |
| β-strand | 111-117 | 7 | 3 |
| β-strand | 124-132 | 9 | 14 |
| α-helix | 137-139 | 3 | |
| α-helix | 142-145 | 4 | |
| β-strand | 149-155 | 7 | 14 |
| β-strand | 160-165 | 6 | 3 |
| β-strand | 174-175 | 2 | 15 |
| β-strand | 186-196 | 11 | 14 |
| α-helix | 197-198 | 2 | |
| β-strand | 205-213 | 9 | 3 |
| β-strand | 218-222 | 5 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-40 | 2 | |
| α-helix | 50-53 | 4 | |
| β-strand | 56 | 1 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA-octamer (5'-R(P*UP*GP*UP*UP*UP*UP*UP*A)-3') | C | RNA | 8 | Rhinovirus B14 | |
| Genome polyprotein | 1 | protein | 273 | Human rhinovirus 14 | P03303 (AlphaFold model) |
| Genome polyprotein | 2 | protein | 262 | Human rhinovirus 14 | P03303 (AlphaFold model) |
| Genome polyprotein | 3 | protein | 236 | Human rhinovirus 14 | P03303 (AlphaFold model) |
| Genome polyprotein | 4 | protein | 68 | Human rhinovirus 14 | P03303 (AlphaFold model) |
>7BG6_1 RNA-octamer (5'-R(P*UP*GP*UP*UP*UP*UP*UP*A)-3') (chains C) UGUUUUUA
>7BG6_2 Genome polyprotein (chains 1) TVASISSGPKHTQKVPILTANETGATMPVLPSDSIETRTTYMHFNGSETDVECFLGRAAC VHVTEIQNKDATGIDNHREAKLFNDWKINLSSLVQLRKKLELFTYVRFDSEYTILATASQ PDSANYSSNLVVQAMYVPPGAPNPKEWDDYTWQSASNPSVFFKVGDTSRFSVPYVGLASA YNCFYDGYSHDDAETQYGITVLNHMGSMAFRIVNEHDEHKTLVKIRVYHRAKHVEAWIPR APRALPYTSIGRTNYPKNTEPVIKKRKGDIKSY
>7BG6_3 Genome polyprotein (chains 2) SPNVEACGYSDRVQQITLGNSTITTQEAANAVVCYAEWPEYLPDVDASDVNKTSKPDTSV CRFYTLDSKTWTTGSKGWCWKLPDALKDMGVFGQNMFFHSLGRSGYTVHVQCNATKFHSG CLLVVVIPEHQLASHEGGNVSVKYTFTHPGERGIDLSSANEVGGPVKDVIYNMNGTLLGN LLIFPHQFINLRTNNTATIVIPYINSVPIDSMTRHNNVSLMVIPIAPLTVPTGATPSLPI TVTIAPMCTEFSGIRSKSIVPQ
>7BG6_4 Genome polyprotein (chains 3) GLPTTTLPGSGQFLTTDDRQSPSALPNYEPTPRIHIPGKVHNLLEIIQVDTLIPMNNTHT KDEVNSYLIPLNANRQNEQVFGTNLFIGDGVFKTTLLGEIVQYYTHWSGSLRFSLMYTGP ALSSAKLILAYTPPGARGPQDRREAMLGTHVVWDIGLQSTIVMTIPWTSGVQFRYTDPDT YTSAGFLSCWYQTSLILPPETTGQVYLLSFISACPDFKLRLMKDTQTISQTVALTE
>7BG6_5 Genome polyprotein (chains 4) GAQVSTQKSGSHENQNILTNGSNQTFTVINYYKDAASTSSAGQSLSMDPSKFTEPVKDLM LKGAPALN
ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating. Hrebik, D., Fuzik, T., Gondova, M. et al. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2024251118 · PubMed
Other PDB entries of the same protein (UniProt P03303 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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