[English] 日本語
Yorodumi
- EMDB-64090: AcrIE10-Cas7-IR complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-64090
TitleAcrIE10-Cas7-IR complex
Map dataAcrIE10-Cas7-IR complex map
Sample
  • Complex: AcrIE10-Cas7*-IR complex
    • DNA: DNA (5'-D(P*TP*GP*TP*AP*TP*GP*AP*CP*AP*TP*CP*TP*GP*TP*CP*AP*TP*AP*C)-3')
    • DNA: DNA (5'-D(P*GP*TP*AP*TP*GP*AP*CP*AP*GP*AP*TP*GP*TP*CP*AP*TP*AP*CP*AP*A)-3')
    • Protein or peptide: AcrIE10
    • Protein or peptide: CRISPR-associated protein Cse4
KeywordsAnti-CRISPR / Transcription inhibitor / TRANSCRIPTION
Function / homologyCRISPR-associated protein, CT1975 / CT1975-like protein / Uncharacterized protein / CRISPR-associated protein Cse4
Function and homology information
Biological speciesKlebsiella pneumoniae (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.64 Å
AuthorsTsui WT / Ma JB
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: To Be Published
Title: Cryo-EM structure of AcrIE10-Cas7-IR complex
Authors: Tsui WT / Ma JB
History
DepositionApr 9, 2025-
Header (metadata) releaseApr 15, 2026-
Map releaseApr 15, 2026-
UpdateApr 15, 2026-
Current statusApr 15, 2026Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_64090.map.gz / Format: CCP4 / Size: 22.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationAcrIE10-Cas7-IR complex map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.96 Å/pix.
x 180 pix.
= 172.8 Å
0.96 Å/pix.
x 180 pix.
= 172.8 Å
0.96 Å/pix.
x 180 pix.
= 172.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.96 Å
Density
Contour LevelBy AUTHOR: 0.119
Minimum - Maximum-0.5461344 - 0.8528598
Average (Standard dev.)0.0035821514 (±0.029437503)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions180180180
Spacing180180180
CellA=B=C: 172.8 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_64090_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_64090_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : AcrIE10-Cas7*-IR complex

EntireName: AcrIE10-Cas7*-IR complex
Components
  • Complex: AcrIE10-Cas7*-IR complex
    • DNA: DNA (5'-D(P*TP*GP*TP*AP*TP*GP*AP*CP*AP*TP*CP*TP*GP*TP*CP*AP*TP*AP*C)-3')
    • DNA: DNA (5'-D(P*GP*TP*AP*TP*GP*AP*CP*AP*GP*AP*TP*GP*TP*CP*AP*TP*AP*CP*AP*A)-3')
    • Protein or peptide: AcrIE10
    • Protein or peptide: CRISPR-associated protein Cse4

-
Supramolecule #1: AcrIE10-Cas7*-IR complex

SupramoleculeName: AcrIE10-Cas7*-IR complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Cas7* binds to AcrIE10-IR complex
Source (natural)Organism: Klebsiella pneumoniae (bacteria)
Molecular weightTheoretical: 200 KDa

-
Macromolecule #1: DNA (5'-D(P*TP*GP*TP*AP*TP*GP*AP*CP*AP*TP*CP*TP*GP*TP*CP*AP*TP*AP...

MacromoleculeName: DNA (5'-D(P*TP*GP*TP*AP*TP*GP*AP*CP*AP*TP*CP*TP*GP*TP*CP*AP*TP*AP*C)-3')
type: dna / ID: 1 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Klebsiella pneumoniae (bacteria)
Molecular weightTheoretical: 5.794771 KDa
SequenceString:
(DT)(DG)(DT)(DA)(DT)(DG)(DA)(DC)(DA)(DT) (DC)(DT)(DG)(DT)(DC)(DA)(DT)(DA)(DC)

-
Macromolecule #2: DNA (5'-D(P*GP*TP*AP*TP*GP*AP*CP*AP*GP*AP*TP*GP*TP*CP*AP*TP*AP*CP...

MacromoleculeName: DNA (5'-D(P*GP*TP*AP*TP*GP*AP*CP*AP*GP*AP*TP*GP*TP*CP*AP*TP*AP*CP*AP*A)-3')
type: dna / ID: 2 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Klebsiella pneumoniae (bacteria)
Molecular weightTheoretical: 6.16603 KDa
SequenceString:
(DG)(DT)(DA)(DT)(DG)(DA)(DC)(DA)(DG)(DA) (DT)(DG)(DT)(DC)(DA)(DT)(DA)(DC)(DA)(DA)

-
Macromolecule #3: AcrIE10

MacromoleculeName: AcrIE10 / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Klebsiella pneumoniae (bacteria)
Molecular weightTheoretical: 13.185825 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
VKKEISRNPS FTPSPKLRAH LNSHREGVTE RLNNIFDRYA HLVRACALPL DDDETQVLLN VLNGSVVEPA FIEYLAQEIR DSDDYLEGI PAAKSLYEKC QSATYPQLLA TVERLDR

UniProtKB: Uncharacterized protein

-
Macromolecule #4: CRISPR-associated protein Cse4

MacromoleculeName: CRISPR-associated protein Cse4 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Klebsiella pneumoniae (bacteria)
Molecular weightTheoretical: 38.323203 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MTTFIQLHLL TAYPAANLNR DDTGAPKTVM LGGATRLRIS SQSLKRAWRT SELFEHALAG HIGIRSGRIA REAAEILVKS GIEPRKAVD YVKAIGECFG KVKTKADQND PLKCSETEQL AHISPAEFDA VKALAHRLAE EKRAATKEEA ALLRHDRMAV D IAMFGRML ...String:
MTTFIQLHLL TAYPAANLNR DDTGAPKTVM LGGATRLRIS SQSLKRAWRT SELFEHALAG HIGIRSGRIA REAAEILVKS GIEPRKAVD YVKAIGECFG KVKTKADQND PLKCSETEQL AHISPAEFDA VKALAHRLAE EKRAATKEEA ALLRHDRMAV D IAMFGRML ADQPTYNVEA ACQVAHAFGV SETIVEDDFF TAVDDLRAAS EDAGAGHLGE TGFGSALFYT YICIDKDLLV NN LNGNEEL ANKTLRAFTE AALKVSPTGK QNSFASRAYA SWALAEKGTD QPRSLAAAFY QPINGGDQLD VAVQRITALR ENM NTVYGQ QTAFQHFDVM NKQGSMNDVL DFICA

UniProtKB: CRISPR-associated protein Cse4

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration1 mg/mL
BufferpH: 7.8 / Details: 20mM Tris-HCl, 150mM NaCl
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 60 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK I

-
Electron microscopy

MicroscopeFEI POLARA 300
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average exposure time: 1.2 sec. / 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: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Tecnai Polara / 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: 3.64 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 108754
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

-
Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9uer:
AcrIE10-Cas7-IR complex

+
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