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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Full-length cross-linked Contactin 2 (FN1 apart) | |||||||||
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![]() | contactins / adhesion molecule / protein structure / conformational changes / homodimer / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() establishment of protein localization to juxtaparanode region of axon / presynaptic membrane organization / reduction of food intake in response to dietary excess / L1CAM interactions / clustering of voltage-gated potassium channels / protein localization to juxtaparanode region of axon / dendrite self-avoidance / NrCAM interactions / cell-cell adhesion mediator activity / axon initial segment ...establishment of protein localization to juxtaparanode region of axon / presynaptic membrane organization / reduction of food intake in response to dietary excess / L1CAM interactions / clustering of voltage-gated potassium channels / protein localization to juxtaparanode region of axon / dendrite self-avoidance / NrCAM interactions / cell-cell adhesion mediator activity / axon initial segment / node of Ranvier / juxtaparanode region of axon / NCAM1 interactions / fat cell differentiation / homophilic cell adhesion via plasma membrane adhesion molecules / side of membrane / synapse organization / axon guidance / brain development / myelin sheath / postsynaptic membrane / cell adhesion / axon / synapse / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.77 Å | |||||||||
![]() | Liu JL / Fan SF / Ren GR / Rudenko GR | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular mechanism of Contactin 2 homophilic interaction Authors: Fan SF / Liu JL / Chofflett NC / Bailey AB / Russell WR / Zhang ZZ / Takahashi HT / Ren GR / Rudenko GR | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 105.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.6 KB 15.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.6 KB | Display | ![]() |
Images | ![]() | 56.4 KB | ||
Filedesc metadata | ![]() | 5.4 KB | ||
Others | ![]() ![]() | 115.9 MB 115.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 729.4 KB | Display | ![]() |
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Full document | ![]() | 729 KB | Display | |
Data in XML | ![]() | 18.4 KB | Display | |
Data in CIF | ![]() | 23.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9ba4C ![]() 9ba5C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.05 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_44397_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_44397_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Contactin-2 full length (Ig1-FN4)
Entire | Name: Contactin-2 full length (Ig1-FN4) |
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Components |
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-Supramolecule #1: Contactin-2 full length (Ig1-FN4)
Supramolecule | Name: Contactin-2 full length (Ig1-FN4) / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Contactin 2 (full-length)
Macromolecule | Name: Contactin 2 (full-length) / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: ELGTGLE SQ TTFGPVFE D QPLSVLFPE ESTEEQVLLA CRARASPPA T YRWKMNGT EM KLEPGSR HQL VGGNLV IMNP TKAQD AGVYQ CLAS NPVGTV VSR EAILRFG FL QEFSKEER D PVKAHEGWG VMLPCNPPAH YPGLSYRWL L NEFPNFIP TD ...String: ELGTGLE SQ TTFGPVFE D QPLSVLFPE ESTEEQVLLA CRARASPPA T YRWKMNGT EM KLEPGSR HQL VGGNLV IMNP TKAQD AGVYQ CLAS NPVGTV VSR EAILRFG FL QEFSKEER D PVKAHEGWG VMLPCNPPAH YPGLSYRWL L NEFPNFIP TD GRHFVSQ TTG NLYIAR TNAS DLGNY SCLAT SHMD FSTKSV FSK FAQLNLA AE DTRLFAPS I KARFPAETY ALVGQQVTLE CFAFGNPVP R IKWRKVDG SL SPQWTTA EPT LQIPSV SFED EGTYE CEAEN SKGR DTVQGR IIV QAQPEWL KV ISDTEADI G SNLRWGCAA AGKPRPTVRW LRNGEPLAS Q NRVEVLAG DL RFSKLSL EDS GMYQCV AENK HGTIY ASAEL AVQA LAPDFR LNP VRRLIPA AR GGEILIPC Q PRAAPKAVV LWSKGTEILV NSSRVTVTP D GTLIIRNI SR SDEGKYT CFA ENFMGK ANST GILSV RDATK ITLA PSSADI NLG DNLTLQC HA SHDPTMDL T FTWTLDDFP IDFDKPGGHY RRTNVKETI G DLTILNAQ LR HGGKYTC MAQ TVVDSA SKEA TVLVR GPPGP PGGV VVRDIG DTT IQLSWSR GF DNHSPIAK Y TLQARTPPA GKWKQVRTNP ANIEGNAET A QVLGLTPW MD YEFRVIA SNI LGTGEP SGPS SKIRT REAAP SVAP SGLSGG GGA PGELIVN WT PMSREYQN G DGFGYLLSF RRQGSTHWQT ARVPGADAQ Y FVYSNESV RP YTPFEVK IRS YNRRGD GPES LTALV YSAEE EPRV APTKVW AKG VSSSEMN VT WEPVQQDM N GILLGYEIR YWKAGDKEAA ADRVRTAGL D TSARVSGL HP NTKYHVT VRA YNRAGT GPAS PSANA TTMKP PPRR PPGNIS WTF SSSSLSI KW DPVVPFRN E SAVTGYKML YQNDLHLTPT LHLTGKNWI E IPVPEDIG HA LVQIRTT GPG GDGIPA EVHI VRN G SASTSHHHHH H UniProtKB: Contactin-2 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.05 mg/mL | |||||||||
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Buffer | pH: 8 Component:
Details: 10 mM HEPES pH 8.0, 50 mM NaCl | |||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 281 K / Instrument: LEICA EM GP |
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Electron microscopy
Microscope | TFS KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 9049 / Average exposure time: 7.39 sec. / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 81000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Protocol: FLEXIBLE FIT |
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