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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | TTYH2 in complex with ApoE coexpressed, dataset1 map1 | |||||||||
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![]() | Membrane protein / lipid interactions / apolipoprotein | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.03 Å | |||||||||
![]() | Sukalskaia A / Dutzler R / Plochberger B / Pugnetti A / Karner A / Weber F | |||||||||
Funding support | ![]()
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![]() | ![]() Title: TTYH2 in complex with lipidated ApoE Authors: Sukalskaia A / Dutzler R / Plochberger B / Pugnetti A / Karner A / Weber F | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 38.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.6 KB 16.6 KB | Display Display | ![]() |
Images | ![]() | 33.8 KB | ||
Filedesc metadata | ![]() | 5.3 KB | ||
Others | ![]() ![]() | 37.7 MB 37.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 894.3 KB | Display | ![]() |
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Full document | ![]() | 893.8 KB | Display | |
Data in XML | ![]() | 11.3 KB | Display | |
Data in CIF | ![]() | 13.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | C: citing same article ( |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.302 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_53301_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_53301_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : TTYH2 homodimer in complex with coexpressed ApoE
Entire | Name: TTYH2 homodimer in complex with coexpressed ApoE |
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Components |
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-Supramolecule #1: TTYH2 homodimer in complex with coexpressed ApoE
Supramolecule | Name: TTYH2 homodimer in complex with coexpressed ApoE / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 132 KDa |
-Supramolecule #2: ApoE
Supramolecule | Name: ApoE / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: ![]() |
-Supramolecule #3: TTYH2 homodimer
Supramolecule | Name: TTYH2 homodimer / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: TTYH2 homodimer
Macromolecule | Name: TTYH2 homodimer / type: protein_or_peptide / ID: 1 / Details: contains a C-terminal Myc-tag followed by SBP-tag / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: MSQAARVDYI APWWVVWLHS VPHVGLRLQP VNSTFSPGDE SYQESLLFLG LVAAVCLGLN LIFLVAYLVC ACHCRRDDAV QTKQHHSCCI TWTAVVAGLI CCAAVGVGFY GNSETNDGAY QLMYSLDDAN HTFSGIDALV SGTTQKMKVD LEQHLARLSE IFAARGDYLQ ...String: MSQAARVDYI APWWVVWLHS VPHVGLRLQP VNSTFSPGDE SYQESLLFLG LVAAVCLGLN LIFLVAYLVC ACHCRRDDAV QTKQHHSCCI TWTAVVAGLI CCAAVGVGFY GNSETNDGAY QLMYSLDDAN HTFSGIDALV SGTTQKMKVD LEQHLARLSE IFAARGDYLQ TLKFIQQMAG SVVVQLSGLP VWREVTMELT KLSDQTGYVE YYRWLSYLLL FILDLVICLI ACLGLAKRSK CLLASMLCCG ALSLLLSWAS LAADGSAAVA TSDFCVAPDT FILNVTEGQI STEVTRYYLY CSQSGSSPFQ QTLTTFQRAL TTMQIQVAGL LQFAVPLFST AEEDLLAIQL LLNSSESSLH QLTAMVDCRG LHKDYLDALA GICYDGLQGL LYLGLFSFLA ALAFSTMICA GPRAWKHFTT RNRDYDDIDD DDPFNPQAWR MAAHSPPRGQ LHSFCSYSSG LGSQTSLQPP AQTISNAPVS EYMNQAMLFG RNPRYENVPL IGRASPPPTY SPSMRATYLS VADEHLRHYG NQFPAALEVL FQGPQGTEQK LISEEDLRGA SMDEKTTGWR GGHVVEGLAG ELEQLRARLE HHPQGQREP |
-Macromolecule #2: ApoE coexpressed
Macromolecule | Name: ApoE coexpressed / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: MSKVLWAALL VTFLAGCQAK VEQAVETEPE PELRQQTEWQ SGQRWELALG RFWDYLRWVQ TLSEQVQEEL LSSQVTQELR ALMDETMKEL KAYKSELEEQ LTPVAEETRA RLSKELQAAQ ARLGADMEDV CGRLVQYRGE VQAMLGQSTE ELRVRLASHL RKLRKRLLRD ...String: MSKVLWAALL VTFLAGCQAK VEQAVETEPE PELRQQTEWQ SGQRWELALG RFWDYLRWVQ TLSEQVQEEL LSSQVTQELR ALMDETMKEL KAYKSELEEQ LTPVAEETRA RLSKELQAAQ ARLGADMEDV CGRLVQYRGE VQAMLGQSTE ELRVRLASHL RKLRKRLLRD ADDLQKRLAV YQAGAREGAE RGLSAIRERL GPLVEQGRVR AATVGSLAGQ PLQERAQAWG ERLRARMEEM GSRTRDRLDE VKEQVAEVRA KLEEQAQQIR LQAEAFQARL KSWFEPLVED MQRQWAGLVE KVQAAVGTSA APVPSDNHAL EVLFQGPQGT EQKLISEEDL HHHHHH |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 Component:
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Vitrification | Cryogen name: NITROGEN |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 59.6 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |