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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | C-hexon capsomer of the VZV C-Capsid | |||||||||
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![]() | VZV / capsid structure / VIRUS | |||||||||
Function / homology | ![]() T=16 icosahedral viral capsid / viral process / viral capsid / host cell nucleus / structural molecule activity Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
![]() | Nan W / Lei C / Xiangxi W | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Insights into varicella-zoster virus assembly from the B- and C-capsid at near-atomic resolution structures Authors: Cao L / Wang N / Lv Z / Chen W / Chen Z / Song L / Sha X / Wang G / Hu Y / Lian X / Cui G / Fan J / Quan Y / Liu H / Hou H / Wang X | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 49.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19.5 KB 19.5 KB | Display Display | ![]() |
Images | ![]() | 104.5 KB | ||
Filedesc metadata | ![]() | 6.7 KB | ||
Others | ![]() ![]() | 40.7 MB 40.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 11.8 KB | Display | |
Data in CIF | ![]() | 13.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8x9xMC ![]() 8x9wC ![]() 8x9yC ![]() 8xa0C ![]() 8xa1C ![]() 8xa2C ![]() 8xa3C 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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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.35 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_38187_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_38187_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Human alphaherpesvirus 3
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Human alphaherpesvirus 3
Supramolecule | Name: Human alphaherpesvirus 3 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10335 / Sci species name: Human alphaherpesvirus 3 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: Yes / Virus empty: No |
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-Macromolecule #1: Major capsid protein
Macromolecule | Name: Major capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 152.267125 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: PAGIIPTGNV LSTIEVCAHR CIFDFFKQIR SDDNSLYSAQ FDILLGTYCN TLNFVRFLEL GLSVACICTK FPELAYVRDG VIQFEVQQP MIARDGPHPV DQPVHNYMVK RIHKRSLSAA FAIASEALSL LSNTYVDGTE IDSSLRIRAI QQMARNLRTV L DSFERGTA ...String: PAGIIPTGNV LSTIEVCAHR CIFDFFKQIR SDDNSLYSAQ FDILLGTYCN TLNFVRFLEL GLSVACICTK FPELAYVRDG VIQFEVQQP MIARDGPHPV DQPVHNYMVK RIHKRSLSAA FAIASEALSL LSNTYVDGTE IDSSLRIRAI QQMARNLRTV L DSFERGTA DQLLGVLLEK APPLSLLSPI NKFQPEGHLN RVARAALLSD LKRRVCADMF FMTRHAREPR LISAYLSDMV SC TQPSVMV SRITHTNTRG RQVDGVLVTT ATLKRQLLQG ILQIDDTAAD VPVTYGEMVL QGTNLVTALV MGKAVRGMDD VAR HLLDIT DPNTLNIPSI PPQSNSDSTT AGLPVNARVP ADLVIVGDKL VFLEALERRV YQATRVAYPL IGNIDITFIM PMGV FQANS MDRYTRHAGD FSTVSEQDPR QFPPQGIFFY NKDGILTQLT LRDAMGTICH SSLLDVEATL VALRQQHLDR QCYFG VYVA EGTEDTLDVQ MGRFMETWAD MMPHHPHWVN EHLTILQFIA PSNPRLRFEL NPAFDFFVAP GDVDLPGPQR PPEAMP TVN ATLRIINGNI PVPLCPISFR DCRGTQLGLG RHTMTPATIK AVKDTFEDRA YPTIFYMLEA VIHGNERNFC ALLRLLT QC IRGYWEQSHR VAFVNNFHML MYITTYLGNG ELPEVCINIY RDLLQHVRAL RQTITDFTIQ GEGHNGETSE ALNNILTD D TFIAPILWDC DALIYRDEAA RDRLPAIRVS GRNGYQALHF VDMAGHNFQR RDNVLIHGRP VRGDTGQAIP ITPHHDREW GILSKIYYYI VIPAFSRGSC CTMGVRYDRL YPALQAVIVP EIPADEEAPT TPEDPRHPLH AHQLVPNSLN VYFHNAHLTV DGDALLTLQ ELMGDMAERT TAILVSSAPD AGAATATTRN MRIYDGALYH GLIMMAYQAY DETIATGTFF YPVPVNPLFA C PEHLASLR GMTNARRVLA KMVPPIPPFL GANHHATIRQ PVAYHVTHSK SDFNTLTYSL LGGYFKFTPI SLTHQLRTGF HP GIAFTVV RQDRFATEQL LYAERASESY FVGQIQVHHH DAIGGVNFTL TQPRAHVDLG VGYTAVCATA ALRCPLTDMG NTA QNLFFS RGGVPMLHDN VTESLRRITA SGGRLNPTEP LPIFGGLRPA TSAGIARGQA SVCEFVAMPV STDLQYFRTA CNPR GRASG MLYMGDRDAD IEAIMFDHTQ SDVAYTDRAT LNPWASQKHS YGDRLYNGTY NLTGASPIYS PCFKFFTPAE VNTNC NTLD RLLMEAKAVA SQSSTDTEYQ FKRPPGSTEM TQDPCGLFQE AYPPLCSSDA AMLRTAHAGE TGADEVHLAQ YLIRDA SPL RGCLPL UniProtKB: Major capsid protein |
-Macromolecule #2: Small capsomere-interacting protein
Macromolecule | Name: Small capsomere-interacting protein / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 10.185611 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: SNPTTFSVEA IAAYTPVALI RLLNASGPLQ PGHRVDIADA RSIYTVGAAA SAARARANHN ANTIRRTAMF AETDPMTWLR PTVGLRRTF NPRII UniProtKB: Small capsomere-interacting protein |
-Macromolecule #3: Tri2A
Macromolecule | Name: Tri2A / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 27.729641 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: AMPFEIEVLL PGELSPAETS ALQKCEGKII TFSTLRHRAS LVDIALSSYY INGAPPDTLS LLEAYRMRFA AVITRVIPGK LLAHAIGVG TPTPGLFIQN TSPVDLCNGD YICLLPPVYG SADSIRLDSV GLEIVFPLTI PQTLMREIIA KVVARAVEDL N LMFSINEG ...String: AMPFEIEVLL PGELSPAETS ALQKCEGKII TFSTLRHRAS LVDIALSSYY INGAPPDTLS LLEAYRMRFA AVITRVIPGK LLAHAIGVG TPTPGLFIQN TSPVDLCNGD YICLLPPVYG SADSIRLDSV GLEIVFPLTI PQTLMREIIA KVVARAVEDL N LMFSINEG CLLILALIPR LLALLIPRLL ALVTREAAQL IHPEAPMLML PIYETISSWI STSSRLGDTL GTRAILRVCV FD GPSTVHP GDRTAVIQV |
-Macromolecule #4: Tri2B
Macromolecule | Name: Tri2B / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 28.721295 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: AMPFEIEVLL PGEISPAETS ALQKCEGKII TFSTLRHRAS LVDIALSSYY INGAPPDTLS LLEAYRMRFA AVITRVIPGK LLAHAIGVG TPTPGLFIQN TSPVDLCNGD YICLLPPVFG SADEIRLDSV GLEIVFPLTI PQTLMREIIA KVVARAVERT A ADVICYNG ...String: AMPFEIEVLL PGEISPAETS ALQKCEGKII TFSTLRHRAS LVDIALSSYY INGAPPDTLS LLEAYRMRFA AVITRVIPGK LLAHAIGVG TPTPGLFIQN TSPVDLCNGD YICLLPPVFG SADEIRLDSV GLEIVFPLTI PQTLMREIIA KVVARAVERT A ADVICYNG RRYELETNLQ HRDGSDAAIR TLVLNLMFSI NEGTTLILTL ITRLLRFPIY EAISSWISTS SRLGDTLGTR AI LRVCVFD GPSTVHPGDR TAVIQV |
-Macromolecule #5: Tri1
Macromolecule | Name: Tri1 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 33.690453 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: AAAAAAAAAA AAAAAAAAAA FKSTTQLIQQ VSLTDFFRPD IEHAGSTVLI LRHPTDLPAL ARHRAPPGRQ TERLAEAWGQ LLEASRAYV TSLSFIAACR AEEYTDKQAA EANRTAIVSA YGCSRMGARL IRFSECLRAM VQCHVFPHRF ISFFGSLLEY T IQDNLCNI ...String: AAAAAAAAAA AAAAAAAAAA FKSTTQLIQQ VSLTDFFRPD IEHAGSTVLI LRHPTDLPAL ARHRAPPGRQ TERLAEAWGQ LLEASRAYV TSLSFIAACR AEEYTDKQAA EANRTAIVSA YGCSRMGARL IRFSECLRAM VQCHVFPHRF ISFFGSLLEY T IQDNLCNI TAVAKGPQEA ARTDKTSTRR VTANIPACVF WDVDKDLHLS ADGLKHVFLV FVYTQRRQRE GVRLHLALSQ LN EQCFGRG IGFLLGARIC MYAAYTLIGT IPSESVRYTR RMERFGGYNV PTIWLEGVVW GGTNTWNEC |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.3 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1755031 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |