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- EMDB-70679: Herpes simplex virus type 1 (HSV-1) B-capsid pUL6 portal protein,... -
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Open data
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Basic information
Entry | ![]() | |||||||||||||||||||||||||||
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Title | Herpes simplex virus type 1 (HSV-1) B-capsid pUL6 portal protein, dodecameric complex | |||||||||||||||||||||||||||
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![]() | Complex / VIRAL PROTEIN | |||||||||||||||||||||||||||
Function / homology | ![]() assemblin / nuclear capsid assembly / viral release from host cell / chromosome organization / virion component / host cell cytoplasm / serine-type endopeptidase activity / host cell nucleus / proteolysis / identical protein binding Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||||||||||||||||||||
![]() | Crofut EH / Kashyap S / Stevens A / Jih J / Liu Y-T / Zhou ZH | |||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of a new capsid form and comparison with A-, B- and C-capsids clarify herpesvirus assembly Authors: Stevens A / Kashyap S / Crofut EH / Alvarez-Cabrera AL / Jih J / Liu Y-T / Zhou ZH | |||||||||||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 397.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 21.2 KB 21.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 15.8 KB | Display | ![]() |
Images | ![]() | 114.2 KB | ||
Masks | ![]() | 421.9 MB | ![]() | |
Filedesc metadata | ![]() | 6.8 KB | ||
Others | ![]() ![]() | 390.2 MB 390.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9op5MC ![]() 9op4C ![]() 9op8C ![]() 9opbC ![]() 9opcC ![]() 9opvC 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: 1.1 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_70679_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_70679_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Dodecameric complex of pUL6 with bound loops from scaffolding protein
Entire | Name: Dodecameric complex of pUL6 with bound loops from scaffolding protein |
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Components |
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-Supramolecule #1: Dodecameric complex of pUL6 with bound loops from scaffolding protein
Supramolecule | Name: Dodecameric complex of pUL6 with bound loops from scaffolding protein type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Capsid scaffolding protein
Macromolecule | Name: Capsid scaffolding protein / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 66.501609 KDa |
Sequence | String: MAADAPGDRM EEPLPDRAVP IYVAGFLALY DSGDSGELAL DPDTVRAALP PDNPLPINVD HRAGCEVGRV LAVVDDPRGP FFVGLIACV QLERVLETAA SAAIFERRGP PLSREERLLY LITNYLPSVS LATKRLGGEA HPDRTLFAHV ALCAIGRRLG T IVTYDTGL ...String: MAADAPGDRM EEPLPDRAVP IYVAGFLALY DSGDSGELAL DPDTVRAALP PDNPLPINVD HRAGCEVGRV LAVVDDPRGP FFVGLIACV QLERVLETAA SAAIFERRGP PLSREERLLY LITNYLPSVS LATKRLGGEA HPDRTLFAHV ALCAIGRRLG T IVTYDTGL DAAIAPFRHL SPASREGARR LAAEAEIALS GRTWAPGVEA LTHTLLSTAV NNMMLRDRWS LVAERRRQAG IA GHTYLQA SEKFKMWGAE PVSAPARGYK NGAPESTDIP PGSIAAAPQG DRCPIVRQRG VALSPVLPPM NPVPTSGTPA PAP PGDGSY LWIPASHYNQ LVAGHAAPQP QPHSAFGFPA AAGAVAYGPH GAGLSQHYPP HVAHQYPGVL FSGPSPLEAQ IAAL VGAIA ADRQAGGQPA AGDPGVRGSG KRRRYEAGPS ESYCDQDEPD ADYPYYPGEA RGGPRGVDSR RAARQSPGTN ETITA LMGA VTSLQQELAH MRARTSAPYG MYTPVAHYRP QVGEPEPTTT HPALCPPEAV YRPPPHSAPY GPPQGPASHA PTPPYA PAA CPPGPPPPPC PSTQTRAPLP TEPAFPPAAT GSQPEASNAE AGALVNASSA AHVDVDTARA ADLFVSQMMG AR UniProtKB: Capsid scaffolding protein |
-Macromolecule #2: Capsid portal protein
Macromolecule | Name: Capsid portal protein / type: protein_or_peptide / ID: 2 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 74.162523 KDa |
Sequence | String: MTAPRSWAPT TRARGDTEAL CSPEDGWVKV HPTPGTMLFR EILHGQLGYT EGQGVYNVVR SSEATTRQLQ AAIFHALLNA TTYRDLEAD WLGHVAARGL QPQRLVRRYR NAREADIAGV AERVFDTWRN TLRTTLLDFA HGLVACFAPG GPSGPSSFPK Y IDWLTCLG ...String: MTAPRSWAPT TRARGDTEAL CSPEDGWVKV HPTPGTMLFR EILHGQLGYT EGQGVYNVVR SSEATTRQLQ AAIFHALLNA TTYRDLEAD WLGHVAARGL QPQRLVRRYR NAREADIAGV AERVFDTWRN TLRTTLLDFA HGLVACFAPG GPSGPSSFPK Y IDWLTCLG LVPILRKRQE GGVTQGLRAF LKQHPLTRQL ATVAEAAERA GPGFFELALA FDSTRVADYD RVYIYYNHRR GD WLVRDPI SGQRGECLVL WPPLWTGDRL VFDSPVQRLF PEIVACHSLR EHAHVCRLRN TASVKVLLGR KSDSERGVAG AAR VVNKVL GEDDETKAGS AASRLVRLII NMKGMRHVGD INDTVRAYLD EAGGHLIDAP AVDGTLPGFG KGGNSRGSAG QDQG GRAPQ LRQAFRTAVV NNINGVLEGY INNLFGTIER LRETNAGLAT QLQERDRELR RATAGALERQ QRAADLAAES VTGGC GSRP AGADLLRADY DIIDVSKSMD DDTYVANSFQ HPYIPSYAQD LERLSRLWEH ELVRCFKILC HRNNQGQETS ISYSSG AIA AFVAPYFESV LRAPRVGAPI TGSDVILGEE ELWDAVFKKT RLQTYLTDIA ALFVADVQHA ALPPPPSPVG ADFRPGA SP RGRSRSRSPG RTAPGAPDQG GGIGHRDGRR DGRR UniProtKB: Capsid portal protein |
-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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Grid | Model: Quantifoil / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 45.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 81000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |