[English] 日本語
Yorodumi
- EMDB-63979: RABV G binding with CTB011 Fab and CTB012 Fab -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-63979
TitleRABV G binding with CTB011 Fab and CTB012 Fab
Map data
Sample
  • Complex: RABV G binding with CTB 011 Fab CTB012 Fab
    • Protein or peptide: Glycoprotein
    • Protein or peptide: CTB011 Fab Heavy chain
    • Protein or peptide: CTB011 Fab light chain
    • Protein or peptide: CTB012 Fab light chain
    • Protein or peptide: CTB012 Fab heavy chain
KeywordsRABV / G protein / Neutralizing antibody / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


viral envelope / virion membrane / membrane
Similarity search - Function
: / Rhabdovirus glycoprotein G PH domain / : / Rhabdovirus spike glycoprotein G central domain / Rhabdovirus glycoprotein / Rhabdovirus spike glycoprotein fusion domain
Similarity search - Domain/homology
Biological speciesLyssavirus rabies / Mus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.94 Å
AuthorsCao L / Zhang C
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Emerg Microbes Infect / Year: 2025
Title: Structural basis for broad neutralization of rabies virus by an antibody cocktail SYN023.
Authors: Lei Cao / Jiagui Qu / Chuziyue Zhang / Ruihong Chen / Jinyue Wang / Christine Fehlner-Gardiner / Michael Niezgoda / Panayampalli Subbian Satheshkumar / Xiangxi Wang / Eric Tsao /
History
DepositionMar 31, 2025-
Header (metadata) releaseJan 7, 2026-
Map releaseJan 7, 2026-
UpdateJan 7, 2026-
Current statusJan 7, 2026Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_63979.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 320 pix.
= 342.4 Å
1.07 Å/pix.
x 320 pix.
= 342.4 Å
1.07 Å/pix.
x 320 pix.
= 342.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.07 Å
Density
Contour LevelBy AUTHOR: 0.46
Minimum - Maximum-0.6927848 - 1.3931949
Average (Standard dev.)0.000060714185 (±0.04304184)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 342.40002 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_63979_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_63979_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : RABV G binding with CTB 011 Fab CTB012 Fab

EntireName: RABV G binding with CTB 011 Fab CTB012 Fab
Components
  • Complex: RABV G binding with CTB 011 Fab CTB012 Fab
    • Protein or peptide: Glycoprotein
    • Protein or peptide: CTB011 Fab Heavy chain
    • Protein or peptide: CTB011 Fab light chain
    • Protein or peptide: CTB012 Fab light chain
    • Protein or peptide: CTB012 Fab heavy chain

-
Supramolecule #1: RABV G binding with CTB 011 Fab CTB012 Fab

SupramoleculeName: RABV G binding with CTB 011 Fab CTB012 Fab / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Lyssavirus rabies

-
Macromolecule #1: Glycoprotein

MacromoleculeName: Glycoprotein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Lyssavirus rabies
Molecular weightTheoretical: 44.823402 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: KFPIYTIPDK LGPWSPIDIH HLSCPNNLVV EDEGCTNLSG FSYMELKVGY ISAIKMNGFT CTGVVTEAET YTNFVGYVTT TFKRKHFRP TPDACRAAYN WKMAGDPRYE ESLHNPYPDY HWLRTVKTTK ESLVIISPSV ADLDPYDRSL HSPVFPGGNC S GVAVSSTY ...String:
KFPIYTIPDK LGPWSPIDIH HLSCPNNLVV EDEGCTNLSG FSYMELKVGY ISAIKMNGFT CTGVVTEAET YTNFVGYVTT TFKRKHFRP TPDACRAAYN WKMAGDPRYE ESLHNPYPDY HWLRTVKTTK ESLVIISPSV ADLDPYDRSL HSPVFPGGNC S GVAVSSTY CSTNHDYTIW MPENPRLGMS CDIFTNSRGK RASKGSETCG FVDERGLYKS LKGACKLKLC GVLGLRLMDG TW VAMQTSN ETKWCPPGQL VNLHDFRSDE IEHLVVEELV KKREECLDAL ESIMTTKSVS FRRLSHLRKL VPGFGKAYTI FNK TLMEAD AHYKSVRTWN EIIPSKGCLR VGGRCHPHVN GVFFNGIILG PDGNVLIPEM QSSLLQQHME LLVSSVIPLM HPL

UniProtKB: Glycoprotein

-
Macromolecule #2: CTB011 Fab Heavy chain

MacromoleculeName: CTB011 Fab Heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 13.165745 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
QVQLVQSGAE VKKPGASVKV SCKASGYSFT DYIMLWVRQA PGQRLEWIGD IYPYYGSTSY NLKFKGKATL TVDTSASTAY MELSSLRSE DTAVYYCARQ GGDGNYVLFD YWGQGTLVTV

-
Macromolecule #3: CTB011 Fab light chain

MacromoleculeName: CTB011 Fab light chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 11.526706 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
DIQMTQSPSS LSASVGDRVT ITCKASQNVG TTVAWYQQKP GKAPKALIYS ASYRYSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQ QYNSYPFTFG QGTKLEI

-
Macromolecule #4: CTB012 Fab light chain

MacromoleculeName: CTB012 Fab light chain / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 12.123598 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
DIVMTQSPLS LPVTPGEPAS ISCKSTKSLL NSDGFTYLDW YLQKPGQSPQ LLIYLVSNRF SGVPDRFSGS GSGTDFTLKI SRVEAEDVG VYYCFQSNYL PFTFGGGTKV EI

-
Macromolecule #5: CTB012 Fab heavy chain

MacromoleculeName: CTB012 Fab heavy chain / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 12.930525 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
EVQLVESGGG LVQPGGSLIL SCAASGFTFS GFAMSWVRQA PGKGLEWVAT ISSGGTYTYS PDSVMGRFTI SRDNAKNSLY LQMNSLRAE DTAVYYCARR LRRNYYSMDY WGQGTMVTV

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TECNAI SPIRIT
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Tecnai Spirit / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.94 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 359068
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD
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