[English] 日本語
Yorodumi
- EMDB-51021: Mouse Teneurin2 dimer variant A0B1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-51021
TitleMouse Teneurin2 dimer variant A0B1
Map dataSharpened map
Sample
  • Complex: Dimeric complex of mouse Teneurin2 A0B1 variant
    • Protein or peptide: Teneurin transmembrane protein 2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
Keywordscell adhesion molecule / complex / homodimer / CELL ADHESION
Function / homology
Function and homology information


filopodium / PML body / growth cone / dendritic spine / postsynaptic membrane / cell adhesion / endoplasmic reticulum / Golgi apparatus / signal transduction / protein homodimerization activity
Similarity search - Function
: / : / Teneurin intracellular, N-terminal / : / : / : / Teneurin Intracellular Region / Teneurin-3-like, galactose-binding domain-like / Teneurin antibiotic-binding-like domain / Teneurin 1-4, FN-plug domain ...: / : / Teneurin intracellular, N-terminal / : / : / : / Teneurin Intracellular Region / Teneurin-3-like, galactose-binding domain-like / Teneurin antibiotic-binding-like domain / Teneurin 1-4, FN-plug domain / Teneurin TTR-like domain / Teneurin NHL domain / Teneurin YD-shell / Teneurin N-terminal domain profile. / Tox-GHH domain / : / GHH signature containing HNH/Endo VII superfamily nuclease toxin / YD repeat / Teneurin EGF domain / Rhs repeat-associated core / Carboxypeptidase-like, regulatory domain superfamily / Six-bladed beta-propeller, TolB-like / Epidermal growth factor-like domain. / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.48 Å
AuthorsBerbeira-Santana M / Zhou JC / el Omari K / Baker L / Seiradake E
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Wellcome Trust226647/Z/22/Z United Kingdom
CitationJournal: To Be Published
Title: Mouse Teneurin2 dimer variant A0B1
Authors: Berbeira-Santana M / Zhou JC / el Omari K / Baker L / Seiradake E
History
DepositionJul 12, 2024-
Header (metadata) releaseJan 21, 2026-
Map releaseJan 21, 2026-
UpdateJan 21, 2026-
Current statusJan 21, 2026Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_51021.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.94 Å/pix.
x 350 pix.
= 329. Å
0.94 Å/pix.
x 350 pix.
= 329. Å
0.94 Å/pix.
x 350 pix.
= 329. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.94 Å
Density
Contour LevelBy AUTHOR: 0.134
Minimum - Maximum-0.031162169 - 1.9253443
Average (Standard dev.)0.0016174912 (±0.027728163)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions350350350
Spacing350350350
CellA=B=C: 329.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Additional map: Raw map

Fileemd_51021_additional_1.map
AnnotationRaw map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half map A

Fileemd_51021_half_map_1.map
AnnotationHalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half map B

Fileemd_51021_half_map_2.map
AnnotationHalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Dimeric complex of mouse Teneurin2 A0B1 variant

EntireName: Dimeric complex of mouse Teneurin2 A0B1 variant
Components
  • Complex: Dimeric complex of mouse Teneurin2 A0B1 variant
    • Protein or peptide: Teneurin transmembrane protein 2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

-
Supramolecule #1: Dimeric complex of mouse Teneurin2 A0B1 variant

SupramoleculeName: Dimeric complex of mouse Teneurin2 A0B1 variant / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Details: Dimeric complex purified by SEC after recombinant expression in HEK293T cells.
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 266.8826 KDa

-
Macromolecule #1: Teneurin transmembrane protein 2

MacromoleculeName: Teneurin transmembrane protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 267.175906 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: ETGHHHHHHR GGLNDIFEAQ KIEWHEGGST GHLLGLNWQL QPADGHTFNN GVRTGLPGND DVATVPSGGK VPWSLKNSSI DSGEAEVGR RVTQEVPPGV FWRSQIHISQ PQFLKFNISL GKDALFGVYI RRGLPPSHAQ YDFMERLDGK EKWSVVESPR E RRSIQTLV ...String:
ETGHHHHHHR GGLNDIFEAQ KIEWHEGGST GHLLGLNWQL QPADGHTFNN GVRTGLPGND DVATVPSGGK VPWSLKNSSI DSGEAEVGR RVTQEVPPGV FWRSQIHISQ PQFLKFNISL GKDALFGVYI RRGLPPSHAQ YDFMERLDGK EKWSVVESPR E RRSIQTLV QNEAVFVQYL DVGLWHLAFY NDGKDKEMVS FNTVVLDSVQ DCPRNCHGNG ECVSGLCHCF PGFLGADCAK AA CPVLCSG NGQYSKGTCQ CYSGWKGAEC DVPMNQCIDP SCGGHGSCID GNCVCAAGYK GEHCEEVDCL DPTCSSHGVC VNG ECLCSP GWGGLNCELA RVQCPDQCSG HGTYLPDSGL CSCDPNWMGP DCSVEVCSVD CGTHGVCIGG ACRCEEGWTG AACD QRVCH PRCIEHGTCK DGKCECREGW NGEHCTIDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC NVAMETSCAD NKDNE GDGL VDCLDPDCCL QSACQNSLLC RGSRDPLDII QQGQTDWPAV KSFYDRIKLL AGKDSTHIIP GDNPFNSSLV SLIRGQ VVT MDGTPLVGVN VSFVKYPKYG YTITRQDGTF DLIANGGSAL TLHFERAPFM SQERTVWLPW NSFYAMDTLV MKTEENS IP SCDLSGFVRP DPIIISSPLS TFFSASPASN PIVPETQVLH EEIELPGTNV KLRYLSSRTA GYKSLLKITM TQSTVPLN L IRVHLMVAVE GHLFQKSFQA SPNLAYTFIW DKTDAYGQRV YGLSDAVVSV GFEYETCPSL ILWEKRTALL QGFELDPSN LGGWSLDKHH TLNVKSGILH KGTGENQFLT QQPAIITSIM GNGRRRSISC PSCNGLAEGN KLLAPVALAV GIDGSLFVGD FNYIRRIFP SRNVTSILEL RNKEFKHSNS PGHKYYLAVD PVTGSLYVSD TNSRRIYRVK SLSGAKDLAG NSEVVAGTGE Q CLPFDEAR CGDGGKAVDA TLMSPRGIAV DKNGLMYFVD ATMIRKVDQN GIISTLLGSN DLTAVRPLSC DSSMDVAQVR LE WPTDLAV NPMDNSLYVL ENNVILRITE NHQVSIIAGR PMHCQVPGID YSLSKLAIHS ALESASAIAI SHTGVLYITE TDE KKINRL RQVTTNGEIC LLAGAASDCD CKNDVNCICY SGDDAYATDA ILNSPSSLAV APDGTIYIAD LGNIRIRAVS KNKP VLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS ADNDVTELID NNGNSLKIRR DSSGMPRHLL MPDNQ IITL TVGTNGGLKA VSTQNLELGL MTYDGNTGLL ATKSDETGWT TFYDYDHEGR LTNVTRPTGV VTSLHREMEK SITIDI ENS NRDDDVTVIT NLSSVEASYT VVQDQVRNSY QLCNNGTLRV MYANGMAVSF HSEPHVLAGT ITPTIGRCNI SLPMENG LN SIEWRLRKEQ IKGKVTIFGR KLRVHGRNLL SIDYDRNIRT EKIYDDHRKF TLRIIYDQVG RPFLWLPSSG LAAVNVSY F FNGRLAGLQR GAMSERTDID KQGRIVSRMF ADGKVWSYSY LDKSMVLLLQ SQRQYIFEYD SSDRLHAVTM PSVARHSMS THTSIGYIRN IYNPPESNAS VIFDYSDDGR ILKTSFLGTG RQVFYKYGKL SKLSEIVYDS TAVTFGYDET TGVLKMVNLQ SGGFSCTIR YRKVGPLVDK QIYRFSEEGM INARFDYTYH DNSFRIASIK PVISETPLPV DLYRYDEISG KVEHFGKFGV I YYDINQII TTAVMTLSKH FDTHGRIKEV QYEMFRSLMY WMTVQYDSMG RVIKRELKLG PYANTTKYTY DYDGDGQLQS VA VNDRPTW RYSYDLNGNL HLLNPGNSAR LMPLRYDLRD RITRLGDVQY KIDDDGYLCQ RGSDIFEYNS KGLLTRAYNK ASG WSVQYR YDGVGRRASY KTNLGHHLQY FYSDLHNPTR ITHVYNHSNS EITSLYYDLQ GHLFAMESSS GEEYYVASDN TGTP LAVFS INGLMIKQLQ YTAYGEIYYD SNPDFQMVIG FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWRNVGK EPAPF NLYM FKNNNPLSNE LDLKNYVTDV KSWLVMFGFQ LSNIIPGFPR AKMYFVPPPY ELSESQASEN GQLITGVQQT TERHNQ AFL ALEGQVITKK LHASIREKAG HWFATTTPII GKGIMFAIKE GRVTTGVSSI ASEDSRKVAS VLNNAYYLDK MHYSIEG KD THYFVKIGAA DGDLVTLGTT IGRKVLESGV NVTVSQPTLL VNGRTRRFTN IEFQYSTLLL SIRYGLTPDT LDEEKARV L DQARQRALGT AWAKEQQKAR DGREGSRLWT EGEKQQLLST GRVQGYEGYY VLPVEQYPEL ADSSSNIQFL RQNEMGKRG T

UniProtKB: Teneurin-2

-
Macromolecule #5: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 5 / Number of copies: 9 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration0.35 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
300.0 mMNaClsodium chloride
25.0 mMHEPES

Details: 25 mM HEPES, 300 mM NaCl, pH 7.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 120 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.0001 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 294.15 K / Instrument: FEI VITROBOT MARK IV
DetailsSample was monodisperse

-
Electron microscopy

MicroscopeFEI TALOS ARCTICA
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 5212 / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.75 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 150000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

+
Image processing

Particle selectionNumber selected: 1037437
CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.48 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 116348
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final 3D classificationNumber classes: 3 / Software - Name: cryoSPARC
FSC plot (resolution estimation)

-
Atomic model buiding 1

Initial modelChain - Source name: SwissModel / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9g41:
Mouse Teneurin2 dimer variant A0B1

+
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