[English] 日本語
Yorodumi
- EMDB-77390: Structure of the PhiX174 bacteriophage -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-77390
TitleStructure of the PhiX174 bacteriophage
Map dataStructure of the PhiX174 bacteriophage
Sample
  • Virus: Sinsheimervirus
    • Protein or peptide: DNA-binding protein J
    • Protein or peptide: Capsid protein F
    • Protein or peptide: Major spike protein G
KeywordsPhage / Microviridae / Icosahedral / Bacteriophage / VIRUS
Function / homology
Function and homology information


T=1 icosahedral viral capsid / viral capsid / host cell cytoplasm / symbiont entry into host cell / structural molecule activity / DNA binding
Similarity search - Function
Microvirus J protein-like / Microvirus J protein / Microviridae F protein / Microviridae F protein superfamily / Capsid protein (F protein) / Capsid/spike protein, ssDNA virus
Similarity search - Domain/homology
: / Capsid protein F / DNA-binding protein J
Similarity search - Component
Biological speciesSinsheimervirus
Methodsingle particle reconstruction / cryo EM / Resolution: 2.76 Å
AuthorsLi DB / King SH / Driscoll CL / Wilkinson ME / Hie BL
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Generative design of novel bacteriophages with genome language models
Authors: King SH / Driscoll CL / Li DB / Guo D / Merchant AT / Brixi G / Wilkinson ME / Hie BL
History
DepositionJun 1, 2026-
Header (metadata) releaseJun 17, 2026-
Map releaseJun 17, 2026-
UpdateJun 17, 2026-
Current statusJun 17, 2026Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_77390.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationStructure of the PhiX174 bacteriophage
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.92 Å/pix.
x 512 pix.
= 472.576 Å
0.92 Å/pix.
x 512 pix.
= 472.576 Å
0.92 Å/pix.
x 512 pix.
= 472.576 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.923 Å
Density
Contour LevelBy AUTHOR: 0.03
Minimum - Maximum-0.03566774 - 0.11276686
Average (Standard dev.)0.00041453916 (±0.007959928)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 472.576 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: Half Map A

Fileemd_77390_half_map_1.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half Map B

Fileemd_77390_half_map_2.map
AnnotationHalf Map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Sinsheimervirus

EntireName: Sinsheimervirus
Components
  • Virus: Sinsheimervirus
    • Protein or peptide: DNA-binding protein J
    • Protein or peptide: Capsid protein F
    • Protein or peptide: Major spike protein G

-
Supramolecule #1: Sinsheimervirus

SupramoleculeName: Sinsheimervirus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Purified from E. coli culture / NCBI-ID: 1910954 / Sci species name: Sinsheimervirus / Sci species strain: PhiX174 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No

-
Macromolecule #1: DNA-binding protein J

MacromoleculeName: DNA-binding protein J / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sinsheimervirus
Molecular weightTheoretical: 4.239017 KDa
Recombinant expressionOrganism: Escherichia coli C (bacteria)
SequenceString:
MSKGKKRSGA RPGRPQPLRG TKGKRKGARL WYVGGQQF

UniProtKB: DNA-binding protein J

-
Macromolecule #2: Capsid protein F

MacromoleculeName: Capsid protein F / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sinsheimervirus
Molecular weightTheoretical: 48.535523 KDa
Recombinant expressionOrganism: Escherichia coli C (bacteria)
SequenceString: MSNIQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL RLSPLRRGLA IDSTVDIFTF YVPHRHVYGE QWIKFMKDG VNATPLPTVN TTGYIDHAAF LGTINPDTNK IPKHLFQGYL NIYNNYFKAP WMPDRTEANP NELNQDDARY G FRCCHLKN ...String:
MSNIQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL RLSPLRRGLA IDSTVDIFTF YVPHRHVYGE QWIKFMKDG VNATPLPTVN TTGYIDHAAF LGTINPDTNK IPKHLFQGYL NIYNNYFKAP WMPDRTEANP NELNQDDARY G FRCCHLKN IWTAPLPPET ELSRQMTTST TSIDIMGLQA AYANLHTDQE RDYFMQRYHD VISSFGGKTS YDADNRPLLV MR SNLWASG YDVDGTDQTS LGQFSGRVQQ TYKHSVPRFF VPEHGTMFTL ALVRFPPTAT KEIQYLNAKG ALTYTDIAGD PVL YGNLPP REISMKDVFR SGDSSKKFKI AEGQWYRYAP SYVSPAYHLL EGFPFIQEPP SGDLQERVLI RHHDYDQCFQ SVQL LQWNS QVKFNVTVYR NLPTTRDSIM TS

UniProtKB: Capsid protein F

-
Macromolecule #3: Major spike protein G

MacromoleculeName: Major spike protein G / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sinsheimervirus
Molecular weightTheoretical: 19.062637 KDa
Recombinant expressionOrganism: Escherichia coli C (bacteria)
SequenceString:
MFQTFISRHN SNFFSDKLVL TSVTPASSAP VLQTPKATSS TLYFDSLTVN AGNGGFLHCI QMDTSVNAAN QVVSVGADIA FDADPKFFA CLVRFESSSV PTTLPTAYDV YPLDGRHDGG YYTVKDCVTI DVLPRTPGNN VYVGFMVWSN FTATKCRGLV S LNQVIKEI ICLQPLK

UniProtKB: UNIPROTKB: A3FJA7

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4
Component:
ConcentrationFormulaName
100.0 mMNaClsodium chloride
20.0 mMTris
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 41.15 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 150000

+
Image processing

Particle selectionNumber selected: 91377 / Details: Circular blob picked
CTF correctionSoftware - Name: cryoSPARC (ver. 4.6.2) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 2.76 Å / Resolution method: FSC 0.143 CUT-OFF / Software: (Name: cryoSPARC (ver. 4.6.2), RELION (ver. 5.0)) / Number images used: 24547
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC (ver. cryoSPARC)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC (ver. cryoSPARC)
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