[English] 日本語
Yorodumi
- EMDB-49042: The capsid structure of AAVpo.1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-49042
TitleThe capsid structure of AAVpo.1
Map data
Sample
  • Virus: Adeno-associated virus
    • Protein or peptide: VP3
KeywordsAAVpo.1 / porcine adeno-associated virus / gene therapy / vector / cryo-EM / VIRUS
Function / homologyParvovirus coat protein VP2 / Parvovirus coat protein VP1/VP2 / Parvovirus coat protein VP2 / Capsid/spike protein, ssDNA virus / T=1 icosahedral viral capsid / structural molecule activity / VP3
Function and homology information
Biological speciesAdeno-associated virus - Po1 / Adeno-associated virus
Methodsingle particle reconstruction / cryo EM / Resolution: 1.79 Å
AuthorsNelson A / Mietzsch M / McKenna R
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM082946 United States
CitationJournal: To Be Published
Title: Structural insights into porcine adeno-associated viruses
Authors: Nelson A / Mietzsch M / Eby J / Chipman P / McKenna R
History
DepositionFeb 4, 2025-
Header (metadata) releaseApr 16, 2025-
Map releaseApr 16, 2025-
UpdateApr 16, 2025-
Current statusApr 16, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_49042.map.gz / Format: CCP4 / Size: 282.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)X (Row.)Y (Col.)
0.83 Å/pix.
x 420 pix.
= 348.6 Å
0.83 Å/pix.
x 420 pix.
= 348.6 Å
0.83 Å/pix.
x 420 pix.
= 348.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 2.0
Minimum - Maximum-7.2216706 - 15.571158
Average (Standard dev.)0.000000003361142 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderYXZ
Origin-210-210-210
Dimensions420420420
Spacing420420420
CellA=B=C: 348.6 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_49042_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_49042_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Adeno-associated virus

EntireName: Adeno-associated virus
Components
  • Virus: Adeno-associated virus
    • Protein or peptide: VP3

-
Supramolecule #1: Adeno-associated virus

SupramoleculeName: Adeno-associated virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 272636 / Sci species name: Adeno-associated virus / Sci species strain: AAVpo.1 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No

-
Macromolecule #1: VP3

MacromoleculeName: VP3 / type: protein_or_peptide / ID: 1 / Number of copies: 60 / Enantiomer: LEVO
Source (natural)Organism: Adeno-associated virus - Po1 / Strain: AAVpo.1
Molecular weightTheoretical: 60.185117 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSAGGGSPLG DNNQGADGVG NASGDWHCDS TWMGDRVITK STRTWVLPSY NNHQYLEIHS GSVDGSNANA YFGYSTPWGY FDFNRFHSH WSPRDWQRLV NNYWGFRPRS LKVKIFNIQV KEVTTQDGTT TIANNLTSTV QVFTDNDYQL PYVIGNGTEG C LPAFPPQV ...String:
MSAGGGSPLG DNNQGADGVG NASGDWHCDS TWMGDRVITK STRTWVLPSY NNHQYLEIHS GSVDGSNANA YFGYSTPWGY FDFNRFHSH WSPRDWQRLV NNYWGFRPRS LKVKIFNIQV KEVTTQDGTT TIANNLTSTV QVFTDNDYQL PYVIGNGTEG C LPAFPPQV FTLPQYGYAT LNRNNTDDPT ERSSFFCLEY FPSKMLRTGN NFEFTYSFEE VPFHCSFAPS QNLFKLANPL VD QYLYRFV STDTSGNLQF QKNLKARYAN TYKNWFPGPM CRTQGWYTSA GTYNNKGVAN FDTSNKMELE GASYQVNPQP NGM TNTLQD SNKYALENTM IFNAQNAPPG TTSLYQENNL LITSESETQP VNRLAYNTGG QVSNNNQNSN THPTVGVYNH QEVL PGSVW MDRDVYLQGP IWAKIPETGA HFHPSPAMGG FGLKHPPPMM LIKNTPVPSN VAAFSDVPVK SFITQYSTGQ VTVEI EWEL KKENSKRWNP EIQYTNNYNN PTFVDFAPDT SGEYRTTRAI GTRYLTRPL

UniProtKB: VP3

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 1.79 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 512823
Initial angle assignmentType: COMMON LINE
Final angle assignmentType: COMMON LINE

+
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