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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Cryo-EM structure of PRV gB and FAB 16f9 complex | |||||||||
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![]() | Cryo-EM / PRV gB / FAB 16F9 / Herpe svirus / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex | |||||||||
Function / homology | ![]() host cell endosome / host cell Golgi apparatus / viral envelope / symbiont entry into host cell / virion attachment to host cell / host cell plasma membrane / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.78 Å | |||||||||
![]() | Li Y / Zheng Q / Li S / Wu Y | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Cryo-EM structure of PRV gB and FAB 16f9 complex Authors: Li Y / Zheng Q / Li S | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 446.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17 KB 17 KB | Display Display | ![]() |
Images | ![]() | 46.2 KB | ||
Filedesc metadata | ![]() | 6.2 KB | ||
Others | ![]() ![]() | 475.1 MB 475.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 898 KB | Display | ![]() |
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Full document | ![]() | 897.5 KB | Display | |
Data in XML | ![]() | 18.4 KB | Display | |
Data in CIF | ![]() | 21.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9jmrMC M: atomic model generated by this map 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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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.65 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_61611_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_61611_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : PRV gB and FAB 16F9 complex
Entire | Name: PRV gB and FAB 16F9 complex |
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Components |
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-Supramolecule #1: PRV gB and FAB 16F9 complex
Supramolecule | Name: PRV gB and FAB 16F9 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Glycoprotein B
Macromolecule | Name: Glycoprotein B / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 83.648797 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MPAGGGLWRG PRGHRPGHHG GAGLGRLWPA PHHAAAARGA VALALLLLAL AAAPPCGAAA VTRAASASPT PVPGSPGLTP NDVSAEASL EEIEAFTPGP SEAPDGEYGD LDARTAVRAA ATERDRFYVC PPPSGSTVVR LEPEQACPEY SQGRNFTEGI A VLFKENIA ...String: MPAGGGLWRG PRGHRPGHHG GAGLGRLWPA PHHAAAARGA VALALLLLAL AAAPPCGAAA VTRAASASPT PVPGSPGLTP NDVSAEASL EEIEAFTPGP SEAPDGEYGD LDARTAVRAA ATERDRFYVC PPPSGSTVVR LEPEQACPEY SQGRNFTEGI A VLFKENIA PHKFKAHIYY KNVIVTTVWS GSTYAAITNR FTDRVPVPVQ EITDVIDRRG KCVSKAEYVR NNHKVTAFDR DE NPVEVDL RPSRLNALGT RGWHTTNDTH TKIGAAGFYH TGTSVNCIVE EVEARSVYPY DSFALSTGDI VYMSPFYGLR EGA HGEHIG YAPGRFQQVE HYYPIDLDSR LRASESVTRN FLRTPHFTVA WDWAPKTRRV CSLAKWREAE EMIRDETRDG SFRF TSRAL GASFVSDVTQ LDLQRVHLGD CVLREASEAI DAIYQRRYNN THVLAGDRPE VYLARGGFVV AFRPLISNEL AQLYA RELE RLGLAGVVGP ASPAAAGSAS RAAGQAGTPE PPAVNGTGHL RITTGSAEFA RLQFTYDHIQ AHVNDMLGRI AAAWCE LQN KDRTLWSEMS RLNPSAVATA ALGQRVSARM LGDVMAISRC VEVRGGVYVQ NSMRVPGERG TCYSRPLVTF EHNGTGV IE GQLGDDNELL ISRDLIEPCT GNHRRYFKLG SGYVYYEDYS YVRMVEVPET ISTRVTLNLT LLEDREFLPL EVYTREEL A DTGLLDYSEI QRRNQLHALK FYDIDRVVKV DHHHHHH UniProtKB: Glycoprotein B |
-Macromolecule #2: 16F9 VH
Macromolecule | Name: 16F9 VH / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 52.536238 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MGRLTSSFLL LIVPAYVLSE VQLQQSGPEL VKPGASVKIS CKASGYTFAD YTMHWVKQSH GKSLEWIGYI NPYSLFIDSN QKFKNKATL TVDNSSYTAY MELRSLTSED SAVYYCARFP PYYGFDSHFD YWGQGTALTV SSAKTTPPSV YPLAPGCGDT T GSSVTLGC ...String: MGRLTSSFLL LIVPAYVLSE VQLQQSGPEL VKPGASVKIS CKASGYTFAD YTMHWVKQSH GKSLEWIGYI NPYSLFIDSN QKFKNKATL TVDNSSYTAY MELRSLTSED SAVYYCARFP PYYGFDSHFD YWGQGTALTV SSAKTTPPSV YPLAPGCGDT T GSSVTLGC LVKGYFPESV TVTWNSGSLS SSVHTFPALL QSGLYTMSSS VTVPSSTWPS QTVTCSVAHP ASSTTVDKKL EP SGPISTI NPCPPCKECH KCPAPNLEGG PSVFIFPPNI KDVLMISLTP KVTCVVVDVS EDDPDVRISW FVNNVEVHTA QTQ THREDY NSTIRVVSAL PIQHQDWMSG KEFKCKVNNK DLPSPIERTI SKIKGLVRAP QVYILPPPAE QLSRKDVSLT CLVV GFNPG DISVEWTSNG HTEENYKDTA PVLDSDGSYF IYSKLDIKTS KWEKTDSFSC NVRHEGLKNY YLKKTISRSP GK |
-Macromolecule #3: 16F9 VL
Macromolecule | Name: 16F9 VL / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 25.464201 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MGWSCIILFL VATATGVHSQ IVLSQSPAIL SASPGEKVTM TCRASSSVSY IYWYQQKPES SPKPWIYATS NLASGVPGRF SGSGSGTSY SLTISRVEAE DAATYYCQQW SYNPYTFGGG TKLEIRRADA APTVSIFPPS SEQLTSGGAS VVCFLNNFYP K DINVKWKI ...String: MGWSCIILFL VATATGVHSQ IVLSQSPAIL SASPGEKVTM TCRASSSVSY IYWYQQKPES SPKPWIYATS NLASGVPGRF SGSGSGTSY SLTISRVEAE DAATYYCQQW SYNPYTFGGG TKLEIRRADA APTVSIFPPS SEQLTSGGAS VVCFLNNFYP K DINVKWKI DGSERQNGVL NSWTDQDSKD STYSMSSTLT LTKDEYERHN SYTCEATHKT STSPIVKSFN RNEC |
-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 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TECNAI F30 |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.9 µm |
Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |