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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | VAR2CSA-CSA 3D7 | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Plasmodium falciparum / Complex / CSA binding / CELL ADHESION | |||||||||
| Function / homology | Function and homology informationsymbiont-mediated perturbation of host erythrocyte aggregation / infected host cell surface knob / antigenic variation / adhesion of symbiont to microvasculature / cell adhesion molecule binding / cell-cell adhesion / host cell surface receptor binding / host cell plasma membrane / membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Wang L / Wang Z | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Cell Discov / Year: 2021Title: The molecular mechanism of cytoadherence to placental or tumor cells through VAR2CSA from Plasmodium falciparum. Authors: Weiwei Wang / Zhaoning Wang / Xiuna Yang / Yan Gao / Xiang Zhang / Long Cao / Aguang Dai / Jin Sun / Lei Sun / Lubin Jiang / Zhenguo Chen / Lanfeng Wang / ![]() | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_31504.map.gz | 3.8 MB | EMDB map data format | |
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| Header (meta data) | emd-31504-v30.xml emd-31504.xml | 11.8 KB 11.8 KB | Display Display | EMDB header |
| Images | emd_31504.png | 50 KB | ||
| Filedesc metadata | emd-31504.cif.gz | 6.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31504 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31504 | HTTPS FTP |
-Validation report
| Summary document | emd_31504_validation.pdf.gz | 359.4 KB | Display | EMDB validaton report |
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| Full document | emd_31504_full_validation.pdf.gz | 359 KB | Display | |
| Data in XML | emd_31504_validation.xml.gz | 6.5 KB | Display | |
| Data in CIF | emd_31504_validation.cif.gz | 7.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31504 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31504 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7fapMC ![]() 7fasC 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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Map
| File | Download / File: emd_31504.map.gz / Format: CCP4 / Size: 129.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.044 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : VAR2CSA and CSA
| Entire | Name: VAR2CSA and CSA |
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| Components |
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-Supramolecule #1: VAR2CSA and CSA
| Supramolecule | Name: VAR2CSA and CSA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 306 kDa/nm |
-Macromolecule #1: Erythrocyte membrane protein 1, PfEMP1
| Macromolecule | Name: Erythrocyte membrane protein 1, PfEMP1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 306.190219 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MDKSSIANKI EAYLGAKSDD SKIDQSLKAD PSEVQYYGSG GDGYYLRKNI CKITVNHSDS GTNDPCDRIP PPYGDNDQWK CAIILSKVS EKPENVFVPP RRQRMCINNL EKLNVDKIRD KHAFLADVLL TARNEGERIV QNHPDTNSSN VCNALERSFA D IADIIRGT ...String: MDKSSIANKI EAYLGAKSDD SKIDQSLKAD PSEVQYYGSG GDGYYLRKNI CKITVNHSDS GTNDPCDRIP PPYGDNDQWK CAIILSKVS EKPENVFVPP RRQRMCINNL EKLNVDKIRD KHAFLADVLL TARNEGERIV QNHPDTNSSN VCNALERSFA D IADIIRGT DLWKGTNSNL EQNLKQMFAK IRENDKVLQD KYPKDQNYRK LREDWWNANR QKVWEVITCG ARSNDLLIKR GW RTSGKSN GDNKLELCRK CGHYEEKVPT KLDYVPQFLR WLTEWIEDFY REKQNLIDDM ERHREECTSE DHKSKEGTSY CST CKDKCK KYCECVKKWK SEWENQKNKY TELYQQNKNE TSQKNTSRYD DYVKDFFKKL EANYSSLENY IKGDPYFAEY ATKL SFILN SSDANNPSEK IQKNNDEVCN CNESGIASVE QEQISDPSSN KTCITHSSIK ANKKKVCKHV KLGVRENDKD LRVCV IEHT SLSGVENCCC QDFLRILQEN CSDNKSGSSS NGSCNNKNQE ACEKNLEKVL ASLTNCYKCD KCKSEQSKKN NKNWIW KKS SGKEGGLQKE YANTIGLPPR TQSLCLVVCL DEKGKKTQEL KNIRTNSELL KEWIIAAFHE GKNLKPSHEK KNDDNGK KL CKALEYSFAD YGDLIKGTSI WDNEYTKDLE LNLQKIFGKL FRKYIKKNNT AEQDTSYSSL DELRESWWNT NKKYIWLA M KHGAGMNSTT CCGDGSVTGS GSSCDDIPTI DLIPQYLRFL QEWVEHFCKQ RQEKVKPVIE NCKSCKESGG TCNGECKTE CKNKCEVYKK FIEDCKGGDG TAGSSWVKRW DQIYKRYSKY IEDAKRNRKA GTKNCGPSST TNAAENKCVQ SDIDSFFKHL IDIGLTTPS SYLSIVLDDN ICGADKAPWT TYTTYTTTEK CNKETDKSKL QQCNTAVVVN VPSPLGNTPH GYKYACQCKI P TNEETCDD RKEYMNQWSC GSARTMKRGY KNDNYELCKY NGVDVKPTTV RSNSSKLDDK DVTFFNLFEQ WNKEIQYQIE QY MTNTKIS CNNEKNVLSR VSDEAAQPKF SDNERDRNSI THEDKNCKEK CKCYSLWIEK INDQWDKQKD NYNKFQRKQI YDA NKGSQN KKVVSLSNFL FFSCWEEYIQ KYFNGDWSKI KNIGSDTFEF LIKKCGNDSG DGETIFSEKL NNAEKKCKEN ESTN NKMKS SETSCDCSEP IYIRGCQPKI YDGKIFPGKG GEKQWICKDT IIHGDTNGAC IPPRTQNLCV GELWDKRYGG RSNIK NDTK ESLKQKIKNA IQKETELLYE YHDKGTAIIS RNPMKGQKEK EEKNNDSNGL PKGFCHAVQR SFIDYKNMIL GTSVNI YEY IGKLQEDIKK IIEKGTTKQN GKTVGSGAEN VNAWWKGIEG EMWDAVRCAI TKINKKQKKN GTFSIDECGI FPPTGND ED QSVSWFKEWS EQFCIERLQY EKNIRDACTN NGQGDKIQGD CKRKCEEYKK YISEKKQEWD KQKTKYENKY VGKSASDL L KENYPECISA NFDFIFNDNI EYKTYYPYGD YSSICSCEQV KYYEYNNAEK KNNKSLCHEK GNDRTWSKKY IKKLENGRT LEGVYVPPRR QQLCLYELFP IIIKNKNDIT NAKKELLETL QIVAEREAYY LWKQYHAHND TTYLAHKKAC CAIRGSFYDL EDIIKGNDL VHDEYTKYID SKLNEIFDSS NKNDIETKRA RTDWWENEAI AVPNITGANK SDPKTIRQLV WDAMQSGVRK A IDEEKEKK KPNENFPPCM GVQHIGIAKP QFIRWLEEWT NEFCEKYTKY FEDMKSNCNL RKGADDCDDN SNIECKKACA NY TNWLNPK RIEWNGMSNY YNKIYRKSNK ESEDGKDYSM IMEPTVIDYL NKRCNGEING NYICCSCKNI GENSTSGTVN KKL QKKETQ CEDNKGPLDL MNKVLNKMDP KYSEHKMKCT EVYLEHVEEQ LKEIDNAIKD YKLYPLDRCF DDKSKMKVCD LIGD AIGCK HKTKLDELDE WNDVDMRDPY NKYKGVLIPP RRRQLCFSRI VRGPANLRNL KEFKEEILKG AQSEGKFLGN YYNED KDKE KALEAMKNSF YDYEYIIKGS DMLTNIQFKD IKRKLDRLLE KETNNTEKVD DWWETNKKSI WNAMLCGYKK SGNKII DPS WCTIPTTETP PQFLRWIKEW GTNVCIQKEE HKEYVKSKCS NVTNLGAQES ESKNCTSEIK KYQEWSRKRS IQWEAIS EG YKKYKGMDEF KNTFKNIKEP DANEPNANEY LKKHCSKCPC GFNDMQEITK YTNIGNEAFK QIKEQVDIPA ELEDVIYR L KHHEYDKGND YICNKYKNIN VNMKKNNDDT WTDLVKNSSD INKGVLLPPR RKNLFLKIDE SDICKYKRDP KLFKDFIYS SAISEVERLK KVYGEAKTKV VHAMKYSFAD IGSIIKGDDM MENNSSDKIG KILGDGVGQN EKRKKWWDMN KYHIWESMLC GYKHAYGNI SENDRKMLDI PNNDDEHQFL RWFQEWTENF CTKRNELYEN MVTACNSAKC NTSNGSVDKK ECTEACKNYS N FILIKKKE YQSLNSQYDM NYKETKAEKK ESPEYFKDKC NGECSCLSEY FKDETRWKNP YETLDDTEVK NN UniProtKB: Erythrocyte membrane protein 1, PfEMP1 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 6.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 52.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: NONE |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 241954 |
| Initial angle assignment | Type: ANGULAR RECONSTITUTION |
| Final angle assignment | Type: ANGULAR RECONSTITUTION |
-Atomic model buiding 1
| Refinement | Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-7fap: |
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About Yorodumi




Keywords
Authors
China, 1 items
Citation


Z (Sec.)
Y (Row.)
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FIELD EMISSION GUN
