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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Integrin aEb7 bound to fab LF61 with an open I domain | |||||||||
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![]() | T cell residence / Adhesion / Signaling / Cell-cell interaction / IMMUNE SYSTEM | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
![]() | Hollis JA / Campbell MG / Malik HS | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Evolutionary origin and structural ligand mimicry mediated by the inserted domain of alpha-integrin proteins Authors: Hollis JA / Campbell MG / Malik HS / Chan MC | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 67.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14 KB 14 KB | Display Display | ![]() |
Images | ![]() | 101.9 KB | ||
Filedesc metadata | ![]() | 5.3 KB | ||
Others | ![]() ![]() | 124.9 MB 124.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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: 1.122 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_42608_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_42608_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Trimeric complex of heterodimeric aEb7 bound to fab LF61
Entire | Name: Trimeric complex of heterodimeric aEb7 bound to fab LF61 |
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Components |
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-Supramolecule #1: Trimeric complex of heterodimeric aEb7 bound to fab LF61
Supramolecule | Name: Trimeric complex of heterodimeric aEb7 bound to fab LF61 type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Integrin Beta-7
Macromolecule | Name: Integrin Beta-7 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Sequence | String: ELDAKIPSTG DATEWRNPHL SMLGSCQPAP SCQKCILSHP SCAWCKQLNF TASGEAEARR CARREELLAR GCPLEELEEP RGQQEVLQDQ PLSQGARGEG ATQLAPQRVR VTLRPGEPQQ LQVRFLRAEG YPVDLYYLMD LSYSMKDDLE RVRQLGHALL VRLQEVTHSV ...String: ELDAKIPSTG DATEWRNPHL SMLGSCQPAP SCQKCILSHP SCAWCKQLNF TASGEAEARR CARREELLAR GCPLEELEEP RGQQEVLQDQ PLSQGARGEG ATQLAPQRVR VTLRPGEPQQ LQVRFLRAEG YPVDLYYLMD LSYSMKDDLE RVRQLGHALL VRLQEVTHSV RIGFGSFVDK TVLPFVSTVP SKLRHPCPTR LERCQSPFSF HHVLSLTGDA QAFEREVGRQ SVSGNLDSPE GGFDAILQAA LCQEQIGWRN VSRLLVFTSD DTFHTAGDGK LGGIFMPSDG HCHLDSNGLY SRSTEFDYPS VGQVAQALSA ANIQPIFAVT SAALPVYQEL SKLIPKSAVG ELSEDSSNVV QLIMDAYNSL SSTVTLEHSS LPPGVHISYE SQCEGPEKRE GKAEDRGQCN HVRINQTVTF WVSLQATHCL PEPHLLRLRA LGFSEELIVE LHTLCDCNCS DTQPQAPHCS DGQGHLQCGV CSCAPGRLGR LCECSVAELS SPDLESGCRA PNGTGPLCSG KGHCQCGRCS CSGQSSGHLC ECDDASCERH EGILCGGFGR CQCGVCHCHA NRTGRACECS GDMDSCISPE GGLCSGHGRC KCNRCQCLDG YYGALCDQCP GCKTPCERHR DCAECGAFRT GPLATNCSTA CAHTNVTLAL APILDDGWCK ERTLDNQLFF FLVEDDARGT VVLRVRPQEK GADHDTSGLE VLFQGPGKNA QCKKKLQALK KKNAQLKWKL QALKKKLAQG GHHHHHH |
-Macromolecule #2: Integrin Alpha-E
Macromolecule | Name: Integrin Alpha-E / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Sequence | String: FNVDVARPWL TPKGGAPFVL SSLLHQDPST NQTWLLVTSP RTKRTPGPLH RCSLVQDEIL CHPVEHVPIP KGRHRGVTVV RSHHGVLICI QVLVRRPHSL SSELTGTCSL LGPDLRPQAQ ANFFDLENLL DPDARVDTGD CYSNKEGGGE DDVNTARQGG ALEKEEEEDK ...String: FNVDVARPWL TPKGGAPFVL SSLLHQDPST NQTWLLVTSP RTKRTPGPLH RCSLVQDEIL CHPVEHVPIP KGRHRGVTVV RSHHGVLICI QVLVRRPHSL SSELTGTCSL LGPDLRPQAQ ANFFDLENLL DPDARVDTGD CYSNKEGGGE DDVNTARQGG ALEKEEEEDK EEEEDEEEEE AGTEIAIILD GSGSIDPPDF QRAKDFISNM MRNFYEKCFE CNFALVQYGG VIQTEFDLRD SQDVMASLAR VQNITQVGSV TKTASAMQHV LDSIFTSSHG SRRKASKVMV VLTDGGIFED PLNLTTVINS PKMQGVERFA IGVGEEFKSA RTARELNLIA SDPDETHAFK VTNYMALDGL LSKLRYNIIS MEGTVGDALH YQLAQIGFSA QILDERQVLL GAVGAFDWSG GALLYDTRSR RGRFLNQTAA AAADAEAAQY SYLGYAVAVL HKTCSLSYIA GAPRYKHHGA VFELQKEGRE ASFLPVLEGE QMGSYFGSEL CPVDIDMDGS TDFLLVAAPF YHVHGEEGRV YVYRLSEQDG SFSLARILSG HPGFTNARFG FAMAAMGDLS QDKLTDVAIG APLEGFGADD GASFGSVYIY NGHWDGLSAS PSQRIRASTV APGLQYFGMS MAGGFDISGD GLADITVGTL GQAVVFRSRP VVRLKVSMAF TPSALPIGFN GVVNVRLCFE ISSVTTASES GLREALLNFT LDVDVGKQRR RLQCSDVRSC LGCLREWSSG SQLCEDLLLM PTEGELCEED CFSNASVKVS YQLQTPEGQT DHPQPILDRY TEPFAIFQLP YEKACKNKLF CVAELQLATT VSQQELVVGL TKELTLNINL TNSGEDSYMT SMALNYPRNL QLKRMQKPPS PNIQCDDPQP VASVLIMNCR IGHPVLKRSS AHVSVVWQLE ENAFPNRTAD ITVTVTNSNE RRSLANETHT LQFRHGFVAV LSKPSIMYVN TGQGLSHHKE FLFHVHGENL FGAEYQLQIC VPTKLRGLQV VAVKKLTRTQ ASTVCTWSQE RACAYSSVQH VEEWHSVSCV IASDKENVTV AAEISWDHSE ELLKDVTELQ ILGEISFNKS LYEGLNAENH RTKITVVFLK DEKYHGTGGL EVLFQGPGEN AQCEKELQAL EKENAQLEWE LQALEKELAQ WSHPQFEK |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.2 mg/mL |
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Buffer | pH: 7.4 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 379901 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |