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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Mouse Teneurin2 dimer variant A0B0 | |||||||||
Map data | Sharpened map | |||||||||
Sample |
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Keywords | cell adhesion molecule / complex / homodimer / CELL ADHESION | |||||||||
| Function / homology | Function and homology informationfilopodium / PML body / growth cone / dendritic spine / postsynaptic membrane / cell adhesion / endoplasmic reticulum / Golgi apparatus / signal transduction / protein homodimerization activity Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.82 Å | |||||||||
Authors | Berbeira-Santana M / Zhou JC / el Omari K / Baker L / Seiradake E | |||||||||
| Funding support | United Kingdom, 1 items
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Citation | Journal: To Be PublishedTitle: Mouse Teneurin2 dimer variant A0B0 Authors: Berbeira-Santana M / Zhou CJ / el Omari K / Baker L / Seiradake E | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_51022.map.gz | 139.7 MB | EMDB map data format | |
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| Header (meta data) | emd-51022-v30.xml emd-51022.xml | 24.3 KB 24.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51022_fsc.xml | 11.6 KB | Display | FSC data file |
| Images | emd_51022.png | 70.9 KB | ||
| Filedesc metadata | emd-51022.cif.gz | 8.2 KB | ||
| Others | emd_51022_additional_1.map.gz emd_51022_half_map_1.map.gz emd_51022_half_map_2.map.gz | 79.3 MB 126.4 MB 126.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51022 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51022 | HTTPS FTP |
-Validation report
| Summary document | emd_51022_validation.pdf.gz | 951.5 KB | Display | EMDB validaton report |
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| Full document | emd_51022_full_validation.pdf.gz | 951.1 KB | Display | |
| Data in XML | emd_51022_validation.xml.gz | 20.4 KB | Display | |
| Data in CIF | emd_51022_validation.cif.gz | 26.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51022 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51022 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9g42MC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_51022.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Sharpened map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Raw map
| File | emd_51022_additional_1.map | ||||||||||||
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| Annotation | Raw map | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half map A
| File | emd_51022_half_map_1.map | ||||||||||||
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| Annotation | Half map A | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half map B
| File | emd_51022_half_map_2.map | ||||||||||||
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| Annotation | Half map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Dimeric complex of mouse Teneurin2 A0B0 variant
| Entire | Name: Dimeric complex of mouse Teneurin2 A0B0 variant |
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| Components |
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-Supramolecule #1: Dimeric complex of mouse Teneurin2 A0B0 variant
| Supramolecule | Name: Dimeric complex of mouse Teneurin2 A0B0 variant / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 Details: Dimeric complex purified by SEC after recombinant expression in HEK293T cells. |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 266.01164 KDa |
-Macromolecule #1: Teneurin transmembrane protein 2
| Macromolecule | Name: Teneurin transmembrane protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 266.301906 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: 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 RNSPGHKYYL AVDPVTGSLY VSDTNSRRIY RVKSLSGAKD LAGNSEVVAG TGEQCLPFDE A RCGDGGKA VDATLMSPRG IAVDKNGLMY FVDATMIRKV DQNGIISTLL GSNDLTAVRP LSCDSSMDVA QVRLEWPTDL AV NPMDNSL YVLENNVILR ITENHQVSII AGRPMHCQVP GIDYSLSKLA IHSALESASA IAISHTGVLY ITETDEKKIN RLR QVTTNG EICLLAGAAS DCDCKNDVNC ICYSGDDAYA TDAILNSPSS LAVAPDGTIY IADLGNIRIR AVSKNKPVLN AFNQ YEAAS PGEQELYVFN ADGIHQYTVS LVTGEYLYNF TYSADNDVTE LIDNNGNSLK IRRDSSGMPR HLLMPDNQII TLTVG TNGG LKAVSTQNLE LGLMTYDGNT GLLATKSDET GWTTFYDYDH EGRLTNVTRP TGVVTSLHRE MEKSITIDIE NSNRDD DVT VITNLSSVEA SYTVVQDQVR NSYQLCNNGT LRVMYANGMA VSFHSEPHVL AGTITPTIGR CNISLPMENG LNSIEWR LR KEQIKGKVTI FGRKLRVHGR NLLSIDYDRN IRTEKIYDDH RKFTLRIIYD QVGRPFLWLP SSGLAAVNVS YFFNGRLA G LQRGAMSERT DIDKQGRIVS RMFADGKVWS YSYLDKSMVL LLQSQRQYIF EYDSSDRLHA VTMPSVARHS MSTHTSIGY IRNIYNPPES NASVIFDYSD DGRILKTSFL GTGRQVFYKY GKLSKLSEIV YDSTAVTFGY DETTGVLKMV NLQSGGFSCT IRYRKVGPL VDKQIYRFSE EGMINARFDY TYHDNSFRIA SIKPVISETP LPVDLYRYDE ISGKVEHFGK FGVIYYDINQ I ITTAVMTL SKHFDTHGRI KEVQYEMFRS LMYWMTVQYD SMGRVIKREL KLGPYANTTK YTYDYDGDGQ LQSVAVNDRP TW RYSYDLN GNLHLLNPGN SARLMPLRYD LRDRITRLGD VQYKIDDDGY LCQRGSDIFE YNSKGLLTRA YNKASGWSVQ YRY DGVGRR ASYKTNLGHH LQYFYSDLHN PTRITHVYNH SNSEITSLYY DLQGHLFAME SSSGEEYYVA SDNTGTPLAV FSIN GLMIK QLQYTAYGEI YYDSNPDFQM VIGFHGGLYD PLTKLVHFTQ RDYDVLAGRW TSPDYTMWRN VGKEPAPFNL YMFKN NNPL SNELDLKNYV TDVKSWLVMF GFQLSNIIPG FPRAKMYFVP PPYELSESQA SENGQLITGV QQTTERHNQA FLALEG QVI TKKLHASIRE KAGHWFATTT PIIGKGIMFA IKEGRVTTGV SSIASEDSRK VASVLNNAYY LDKMHYSIEG KDTHYFV KI GAADGDLVTL GTTIGRKVLE SGVNVTVSQP TLLVNGRTRR FTNIEFQYST LLLSIRYGLT PDTLDEEKAR VLDQARQR A LGTAWAKEQQ KARDGREGSR LWTEGEKQQL LSTGRVQGYE GYYVLPVEQY PELADSSSNI QFLRQNEMGK RGT UniProtKB: Teneurin-2 |
-Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 10 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.17 mg/mL | |||||||||
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| Buffer | pH: 7.5 Component:
Details: 25 mM HEPES, 300 mM NaCl, pH 7.5 | |||||||||
| Grid | Model: 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 | |||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV | |||||||||
| Details | Sample was monodisperse |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Software | Name: EPU |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 6108 / Average electron dose: 41.503 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: SwissModel / Chain - Initial model type: in silico model |
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| Software | Name: Coot |
| Refinement | Space: REAL / Protocol: RIGID BODY FIT |
| Output model | ![]() PDB-9g42: |
Movie
Controller
About Yorodumi




Keywords
Authors
United Kingdom, 1 items
Citation





Z (Sec.)
Y (Row.)
X (Col.)












































Homo sapiens (human)
FIELD EMISSION GUN

