[English] 日本語
Yorodumi
- EMDB-70156: 1C5H TCR bound to R-phycoerythrin -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-70156
Title1C5H TCR bound to R-phycoerythrin
Map dataR-Phycoerythrin
Sample
  • Complex: R-phycoerythrin
    • Protein or peptide: R-phycoerythrin class I alpha subunit
    • Protein or peptide: R-phycoerythrin class I beta subunit
  • Ligand: PHYCOERYTHROBILIN
  • Ligand: PHYCOUROBILIN
KeywordsT-cell / gamma delta TCR / phycoerythrin / direct / IMMUNE SYSTEM
Function / homologyPhycobilisome, alpha/beta subunit / Phycobilisome, alpha/beta subunit superfamily / Phycobilisome protein / phycobilisome / chloroplast thylakoid membrane / photosynthesis / Globin-like superfamily / R-phycoerythrin class I beta subunit / R-phycoerythrin class I alpha subunit
Function and homology information
Biological speciesHomo sapiens (human) / Pyropia tenera (asakusa nori)
Methodsingle particle reconstruction / cryo EM / Resolution: 1.68 Å
AuthorsRashleigh L / Venugopal H / Rossjohn J / Gully BS
Funding support Australia, 1 items
OrganizationGrant numberCountry
Australian Research Council (ARC)DP230102073 Australia
CitationJournal: Structure / Year: 2025
Title: Antibody-like recognition of a gamma delta T cell receptor toward a foreign antigen
Authors: Rashleigh L / Venugopal H / Rice MT / Gunasinghe SD / Sok CL / Gherardin NA / Almeida CF / Van Rhijn I / Moody DB / Godfrey DI / Rossjohn J / Gully BS
History
DepositionApr 10, 2025-
Header (metadata) releaseAug 6, 2025-
Map releaseAug 6, 2025-
UpdateAug 6, 2025-
Current statusAug 6, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_70156.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationR-Phycoerythrin
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 360 pix.
= 295.2 Å
0.82 Å/pix.
x 360 pix.
= 295.2 Å
0.82 Å/pix.
x 360 pix.
= 295.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.82 Å
Density
Contour LevelBy AUTHOR: 0.122
Minimum - Maximum-0.39941567 - 1.6150893
Average (Standard dev.)0.00026216518 (±0.038350385)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 295.2 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Mask #1

Fileemd_70156_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Additional map: sharpened map

Fileemd_70156_additional_1.map
Annotationsharpened map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half Map A

Fileemd_70156_half_map_1.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half Map B

Fileemd_70156_half_map_2.map
AnnotationHalf Map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : R-phycoerythrin

EntireName: R-phycoerythrin
Components
  • Complex: R-phycoerythrin
    • Protein or peptide: R-phycoerythrin class I alpha subunit
    • Protein or peptide: R-phycoerythrin class I beta subunit
  • Ligand: PHYCOERYTHROBILIN
  • Ligand: PHYCOUROBILIN

-
Supramolecule #1: R-phycoerythrin

SupramoleculeName: R-phycoerythrin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

-
Macromolecule #1: R-phycoerythrin class I alpha subunit

MacromoleculeName: R-phycoerythrin class I alpha subunit / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Pyropia tenera (asakusa nori)
Molecular weightTheoretical: 17.707906 KDa
SequenceString:
MKSVITTTIS AADAAGRFPS SSDLESVQGN IQRAASRLEA AEKLAGNHEA VVKEAGDACF AKYPYLKNPG EAGDSQEKIN KCYRDIDHY MRLINYSLVV GGTGPLDEWG IAGAREVYRA LNLPGSSYIA AFVFTRDRLC VPRDMSAQAA VEFSGALDYV I NSLC

UniProtKB: R-phycoerythrin class I alpha subunit

-
Macromolecule #2: R-phycoerythrin class I beta subunit

MacromoleculeName: R-phycoerythrin class I beta subunit / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Pyropia tenera (asakusa nori)
Molecular weightTheoretical: 18.33685 KDa
SequenceString:
MLDAFSRVVV NSDSKAAYVS GSDLQALKTF IADGNKRLDA VNSIVSNASC IVSDAVSGMI CENPGLIAPG GNCYTNRRMA ACLRDGEII LRYTSYALLA GDSSVLEDRC LNGLKETYIA LGVPTNSTAR AVSIMKSSAV AFISNTAPQR KMATAAGDCS A LSSEVASY CDKVSAAI

UniProtKB: R-phycoerythrin class I beta subunit

-
Macromolecule #3: PHYCOERYTHROBILIN

MacromoleculeName: PHYCOERYTHROBILIN / type: ligand / ID: 3 / Number of copies: 24 / Formula: PEB
Molecular weightTheoretical: 588.694 Da
Chemical component information

ChemComp-PEB:
PHYCOERYTHROBILIN

-
Macromolecule #4: PHYCOUROBILIN

MacromoleculeName: PHYCOUROBILIN / type: ligand / ID: 4 / Number of copies: 6 / Formula: PUB
Molecular weightTheoretical: 590.71 Da
Chemical component information

ChemComp-CYB:
PHYCOUROBILIN

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
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: 2.0 µm / Nominal defocus min: 0.4 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 1.68 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 211282
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
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