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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | B25M05 Fab bound to HPV16 L1 pentamer | |||||||||
![]() | Sharpened map of B25M05 bound to HPV16 L1 pentamer | |||||||||
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![]() | HPV / antibody / IMMUNE SYSTEM | |||||||||
Function / homology | ![]() T=7 icosahedral viral capsid / endocytosis involved in viral entry into host cell / virion attachment to host cell / host cell nucleus / structural molecule activity Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
![]() | Hurlburt NK / Singh S / Rodarte JV / Pancera M | |||||||||
Funding support | ![]()
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![]() | ![]() Title: HPV16 neutralizing monoclonal antibodies show evidence for common developmental pathways and public epitopes Authors: Carter JJ / Hurlburt NK | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 22.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18 KB 18 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.3 KB | Display | ![]() |
Images | ![]() | 140.5 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() | 39.8 MB 39.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 905.5 KB | Display | ![]() |
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Full document | ![]() | 905.1 KB | Display | |
Data in XML | ![]() | 13.8 KB | Display | |
Data in CIF | ![]() | 19.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9ml3MC ![]() 9ml1C ![]() 9ml2C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | Sharpened map of B25M05 bound to HPV16 L1 pentamer | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.122 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half map B
File | emd_48346_half_map_1.map | ||||||||||||
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Annotation | Half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map A
File | emd_48346_half_map_2.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : HPV16 L1 pentamer bound to B25M05 Fab
Entire | Name: HPV16 L1 pentamer bound to B25M05 Fab |
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Components |
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-Supramolecule #1: HPV16 L1 pentamer bound to B25M05 Fab
Supramolecule | Name: HPV16 L1 pentamer bound to B25M05 Fab / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 280 KDa |
-Macromolecule #1: Major capsid protein L1
Macromolecule | Name: Major capsid protein L1 / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 47.534574 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: AVVSTDEYVA RTNIYYHAGT SRLLAVGHPY FPIKKPNNNK ILVPKVSGLQ YRVFRIHLPD PNKFGFPDTS FYNPDTQRLV WACVGVEVG RGQPLGVGIS GHPLLNKLDD TENASAYAAN AGVDNRECIS MDYKQTQLCL IGCKPPIGEH WGKGSPCTNV A VQPGDCPP ...String: AVVSTDEYVA RTNIYYHAGT SRLLAVGHPY FPIKKPNNNK ILVPKVSGLQ YRVFRIHLPD PNKFGFPDTS FYNPDTQRLV WACVGVEVG RGQPLGVGIS GHPLLNKLDD TENASAYAAN AGVDNRECIS MDYKQTQLCL IGCKPPIGEH WGKGSPCTNV A VQPGDCPP LELINTVIQD GDMVDTGFGA MDFTTLQANK SEVPLDICTS ICKYPDYIKM VSEPYGDSLF FYLRREQMFV RH LFNRAGT VGENVPDDLY IKGSGSTANL ASSNYFPTPS GSMVTSDAQI FNKPYWLQRA QGHNNGICWG NQLFVTVVDT TRS TNMSLC AAISTSETTY KNTNFKEYLR HGEEYDLQFI FQLCKITLTA DVMTYIHSMN STILEDWNGG SGGEDPLKKY TFWE VNLKE KFSADLDQFP LGRKFLLQLG L UniProtKB: Major capsid protein L1 |
-Macromolecule #2: B25M05 Fab Heavy Chain
Macromolecule | Name: B25M05 Fab Heavy Chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 25.864021 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: QVQLQQWGAG LLKPSETLSL TCAVNGGSFS IYYWSWIRQP PGKGLDWIGE INQSGSTNYN PSLKSRVTMS VDTSKSQFSL RMTSVTAAD TAIYYCARAP RIRWGSYRLK QTNFDSWGQG TLVTVSSRST KGPSVFPLAP SSKSTSGGTA ALGCLVKDYF P EPVTVSWN ...String: QVQLQQWGAG LLKPSETLSL TCAVNGGSFS IYYWSWIRQP PGKGLDWIGE INQSGSTNYN PSLKSRVTMS VDTSKSQFSL RMTSVTAAD TAIYYCARAP RIRWGSYRLK QTNFDSWGQG TLVTVSSRST KGPSVFPLAP SSKSTSGGTA ALGCLVKDYF P EPVTVSWN SGALTSGVHT FPAVLQSSGL YSLSSVVTVP SSSLGTQTYI CNVNHKPSNT KVDKRVEPKS CDKTHHHHHH |
-Macromolecule #3: B25M05 Fab Light Chain
Macromolecule | Name: B25M05 Fab Light Chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 22.902104 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: QSALTQPASV SGSPGQSITI SCTGTSNDVG DYDYVSWYQL HPGKAPKLLI FDVSRRPSGV SDRFSGSKSG DTASLTISGL QAEDEADYY CSSYTGSSTY VFGTGTKVSV LSQPKANPTV TLFPPSSEEL QANKATLVCL ISDFYPGAVT VAWKADSSPV K AGVETTTP ...String: QSALTQPASV SGSPGQSITI SCTGTSNDVG DYDYVSWYQL HPGKAPKLLI FDVSRRPSGV SDRFSGSKSG DTASLTISGL QAEDEADYY CSSYTGSSTY VFGTGTKVSV LSQPKANPTV TLFPPSSEEL QANKATLVCL ISDFYPGAVT VAWKADSSPV K AGVETTTP SKQSNNKYAA SSYLSLTPEQ WKSHRSYSCQ VTHEGSTVEK TVAPTECS |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.6 mg/mL |
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Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.8 µm / Nominal magnification: 36000 |