[English] 日本語
Yorodumi
- EMDB-64647: Cryo-EM Structure of the Vaccinia Virus Entry/Fusion Complex (EFC... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-64647
TitleCryo-EM Structure of the Vaccinia Virus Entry/Fusion Complex (EFC) Lacking the F9 Subunit
Map dataMain_map_sharppen
Sample
  • Complex: The Vaccinia Virus Entry/Fusion Complex (EFC) Lacking the F9 Subunit
    • Protein or peptide: Virion membrane protein OPG143
    • Protein or peptide: Entry-fusion complex protein OPG094
    • Protein or peptide: Envelope protein OPG155
    • Protein or peptide: Protein OPG107
    • Protein or peptide: Entry-fusion complex protein OPG086
    • Protein or peptide: Entry-fusion complex protein OPG094
    • Protein or peptide: Protein OPG104
    • Protein or peptide: Virion membrane protein OPG147
    • Protein or peptide: Entry-fusion complex protein OPG076
KeywordsVaccinia Virus / Entry-Fusion Complex (EFC) / cryo-EM / Single-particle reconstruction / VIRAL PROTEIN
Function / homology
Function and homology information


membrane fusion involved in viral entry into host cell / DNA-templated transcription termination / helicase activity / host cell endoplasmic reticulum membrane / hydrolase activity / fusion of virus membrane with host plasma membrane / viral envelope / symbiont entry into host cell / virion membrane / DNA binding ...membrane fusion involved in viral entry into host cell / DNA-templated transcription termination / helicase activity / host cell endoplasmic reticulum membrane / hydrolase activity / fusion of virus membrane with host plasma membrane / viral envelope / symbiont entry into host cell / virion membrane / DNA binding / ATP binding / membrane
Similarity search - Function
Viral late protein H2 / Poxvirus A28 / Poxvirus A21 / Viral late protein H2 / Poxvirus A28 family / Poxvirus A21 Protein / Poxvirus L5 / Poxvirus G3 / Poxvirus L5 protein family / Chordopoxvirus G3 protein ...Viral late protein H2 / Poxvirus A28 / Poxvirus A21 / Viral late protein H2 / Poxvirus A28 family / Poxvirus A21 Protein / Poxvirus L5 / Poxvirus G3 / Poxvirus L5 protein family / Chordopoxvirus G3 protein / Pox virus entry-fusion-complex G9/A16 / Pox virus entry-fusion-complex G9/A16
Similarity search - Domain/homology
Entry-fusion complex protein OPG094 / Protein OPG104 / Protein OPG107 / Entry-fusion complex protein OPG076 / Virion membrane protein OPG143 / Entry-fusion complex protein OPG086 / Entry-fusion complex protein OPG094 / Envelope protein OPG155 / Virion membrane protein OPG147
Similarity search - Component
Biological speciesOrthopoxvirus vaccinia
Methodsingle particle reconstruction / cryo EM / Resolution: 3.05 Å
AuthorsWang CH / Lin CSH / Chang W
Funding support Taiwan, 2 items
OrganizationGrant numberCountry
Academia Sinica (Taiwan) Taiwan
National Science Council (NSC, Taiwan) Taiwan
CitationJournal: To Be Published
Title: Cryo-EM analysis of Vaccinia Virus Entry Fusion Complex
Authors: Lin CSH / Li CA / Wang CH / Kao CF / Chiu HJ / Yeh MC / Gao HD / Ho MC / Lee HM / Chang W
History
DepositionMay 16, 2025-
Header (metadata) releaseDec 17, 2025-
Map releaseDec 17, 2025-
UpdateDec 17, 2025-
Current statusDec 17, 2025Processing site: PDBj / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_64647.map.gz / Format: CCP4 / Size: 1000 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMain_map_sharppen
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.53 Å/pix.
x 640 pix.
= 339.52 Å
0.53 Å/pix.
x 640 pix.
= 339.52 Å
0.53 Å/pix.
x 640 pix.
= 339.52 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.5305 Å
Density
Contour LevelBy AUTHOR: 0.12
Minimum - Maximum-1.8717633 - 2.5424097
Average (Standard dev.)0.00023518513 (±0.03919966)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions640640640
Spacing640640640
CellA=B=C: 339.52 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Additional map: Main map unsharppen

Fileemd_64647_additional_1.map
AnnotationMain_map_unsharppen
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half-map-A

Fileemd_64647_half_map_1.map
AnnotationHalf-map-A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half-map-B

Fileemd_64647_half_map_2.map
AnnotationHalf-map-B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

+
Entire : The Vaccinia Virus Entry/Fusion Complex (EFC) Lacking the F9 Subunit

EntireName: The Vaccinia Virus Entry/Fusion Complex (EFC) Lacking the F9 Subunit
Components
  • Complex: The Vaccinia Virus Entry/Fusion Complex (EFC) Lacking the F9 Subunit
    • Protein or peptide: Virion membrane protein OPG143
    • Protein or peptide: Entry-fusion complex protein OPG094
    • Protein or peptide: Envelope protein OPG155
    • Protein or peptide: Protein OPG107
    • Protein or peptide: Entry-fusion complex protein OPG086
    • Protein or peptide: Entry-fusion complex protein OPG094
    • Protein or peptide: Protein OPG104
    • Protein or peptide: Virion membrane protein OPG147
    • Protein or peptide: Entry-fusion complex protein OPG076

+
Supramolecule #1: The Vaccinia Virus Entry/Fusion Complex (EFC) Lacking the F9 Subunit

SupramoleculeName: The Vaccinia Virus Entry/Fusion Complex (EFC) Lacking the F9 Subunit
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Orthopoxvirus vaccinia

+
Macromolecule #1: Virion membrane protein OPG143

MacromoleculeName: Virion membrane protein OPG143 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 43.48659 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGAAVTLNRI KIAPGIADIR DKYMELGFNY PEYNRAVKFA EESYTYYYET SPGEIKPKFC LIDGMSIDHC SSFIVPEFAK QYVLIHGEP CSSFKFRPGS LIYYQNEVTP EYIKDLKHAT DYIASGQRCH FIKKDYLLGD SDSVAKCCSK TNTKHCPKIF N NNYKTEHC ...String:
MGAAVTLNRI KIAPGIADIR DKYMELGFNY PEYNRAVKFA EESYTYYYET SPGEIKPKFC LIDGMSIDHC SSFIVPEFAK QYVLIHGEP CSSFKFRPGS LIYYQNEVTP EYIKDLKHAT DYIASGQRCH FIKKDYLLGD SDSVAKCCSK TNTKHCPKIF N NNYKTEHC DDFMTGFCRN DPGNPNCLEW LRAKRKPAMS TYSDICSKHM DARYCSEFIR IIRPDYFTFG DTALYVFCND HK GNRNCWC ANYPKSNSGD KYLGPRVCWL HECTDESRDR KWLYYNQDVQ RTRCKYVGCT INVNSLALKN SQAELTSNCT RTT SAVGDV HPGEPVVKDK IKLPTWLGAA ITLVVISVIF YFISIYSRPK IKTNDINVRR R

UniProtKB: Virion membrane protein OPG143

+
Macromolecule #2: Entry-fusion complex protein OPG094

MacromoleculeName: Entry-fusion complex protein OPG094 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 38.840285 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGGGVSVELP KRDPPPGVPT DEMLLNVDKM HDVIAPAKLL EYVHIGPLAK DKEDKVKKRY PEFRLVNTGP GGLSALLRQS YNGTAPNCC RTFNRTHYWK KDGKISDKYE EGAVLESCWP DVHDTGKCDV DLFDWCQGDT FDRNICHQWI GSAFNRSNRT V EGQQSLIN ...String:
MGGGVSVELP KRDPPPGVPT DEMLLNVDKM HDVIAPAKLL EYVHIGPLAK DKEDKVKKRY PEFRLVNTGP GGLSALLRQS YNGTAPNCC RTFNRTHYWK KDGKISDKYE EGAVLESCWP DVHDTGKCDV DLFDWCQGDT FDRNICHQWI GSAFNRSNRT V EGQQSLIN LYNKMQTLCS KDASVPICES FLHHLRAHNT EDSKEMIDYI LRQQSADFKQ KYMRCSYPTR DKLEESLKYA EP RECWDPE CSNANVNFLL TRNYNNLGLC NIVRCNTSVN NLQMDKTSSL RLSCGLSNSD RFSTVPVNRA KVVQHNIKHS FDL KLHLIS LLSLLVIWIL IVAI

UniProtKB: Entry-fusion complex protein OPG094

+
Macromolecule #3: Envelope protein OPG155

MacromoleculeName: Envelope protein OPG155 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 16.340536 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MNSLSIFFIV VATAAVCLLF IQGYSIYENY GNIKEFNATH AAFEYSKSIG GTPALDRRVQ DVNDTISDVK QKWRCVVYPG NGFVSASIF GFQAEVGPNN TRSIRKFNTM QQCIDFTFSD VININIYNPC VVPNINNAEC QFLKSVL

UniProtKB: Envelope protein OPG155

+
Macromolecule #4: Protein OPG107

MacromoleculeName: Protein OPG107 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 21.568877 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MDKTTLSVNA CNLEYVREKA IVGVQAAKTS TLIFFVIILA ISALLLWFQT SDNPVFNELT RYMRIKNTVN DWKSLTDSKT KLESDRGRL LAAGKDDIFE FKCVDFGAYF IAMRLDKKTY LPQAIRRGTG DAWMVKKAAK VDPSAQQFCQ YLIKHKSNNV I TCGNEMLN ELGYSGYFMS PHWCSDFSNM E

UniProtKB: Protein OPG107

+
Macromolecule #5: Entry-fusion complex protein OPG086

MacromoleculeName: Entry-fusion complex protein OPG086 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 12.814793 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MASLLYLILF LLFVCISYYF TYYPTNKLQA AVMETDRENA IIRQRNDEIP TRTLDTAIFT DASTVASAQI HLYYNSNIGK IIMSLNGKK HTFNLYDDND IRTLLPILLL SK

UniProtKB: Entry-fusion complex protein OPG086

+
Macromolecule #6: Entry-fusion complex protein OPG094

MacromoleculeName: Entry-fusion complex protein OPG094 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 15.062823 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MENVPNVYFN PVFIEPTFKH SLLSVYKHRL IVLFEVFVVF ILIYVFFRSE LNMFFMPKRK IPDPIDRLRR ANLACEDDKL MIYGLPWMT TQTSALSINS KPIVYKDCAK LLRSINGSQP VSLNDVLRR

UniProtKB: Entry-fusion complex protein OPG094

+
Macromolecule #7: Protein OPG104

MacromoleculeName: Protein OPG104 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 15.174698 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MTDEQIYAFC DANKDDIRCK CIYPDKSIVR IGIDTRLPYY CWYEPCKRSD ALLPASLKKN ITKCNVSDCT ISLGNVSITD SKLDVNNVC DSKRVATENI AVRYLNQEIR YPIIDIKWLP IGLLALAILI LAFF

UniProtKB: Protein OPG104

+
Macromolecule #8: Virion membrane protein OPG147

MacromoleculeName: Virion membrane protein OPG147 / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 13.661822 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MITLFLILCY FILIFNIIVP AISEKMRRER AAYVNYKRLN KNFICVDDRL FSYNFTTSGI KAKVAVDNKN VPIPCSKINE VNNNKDVDT LYCDKDRDDI PGFARSCYRA YSDLFFTT

UniProtKB: Virion membrane protein OPG147

+
Macromolecule #9: Entry-fusion complex protein OPG076

MacromoleculeName: Entry-fusion complex protein OPG076 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Orthopoxvirus vaccinia
Molecular weightTheoretical: 4.230069 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MLVVIMFFIA FAFCSWLSYS YLRPYISTKE LNKSR

UniProtKB: Entry-fusion complex protein OPG076

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.2 / Details: 2.5 mM biotin, 0.02% NP-40 in PBS
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.4 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.99 µm / Nominal defocus min: 0.13 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.05 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 474787
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more