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- EMDB-23252: CryoEM structure of the HCMV Trimer gHgLgO in complex with neutra... -

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Basic information

Entry
Database: EMDB / ID: EMD-23252
TitleCryoEM structure of the HCMV Trimer gHgLgO in complex with neutralizing fabs 13H11 and MSL-109
Map dataComposite map of Trimer gHgLgO bound to fabs 13H11 and Msl-109 used for model refinement
Sample
  • Complex: HCMV Trimer gHgLgO bound to neutralizing fabs 13H11 and MSL-109
    • Complex: HCMV Trimer gHgLgO
      • Protein or peptide: Envelope glycoprotein H
      • Protein or peptide: Envelope glycoprotein L
      • Protein or peptide: Envelope glycoprotein O
    • Complex: neutralizing fabs 13H11 and MSL-109
      • Protein or peptide: Fab 13H11 light chain
      • Protein or peptide: Fab 13H11 heavy chain
      • Protein or peptide: Fab MSL-109 light chain
      • Protein or peptide: Fab MSL-109 heavy chain
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: alpha-D-mannopyranose
Function / homology
Function and homology information


host cell endosome membrane / HCMV Late Events / HCMV Early Events / host cell Golgi apparatus / entry receptor-mediated virion attachment to host cell / symbiont entry into host cell / fusion of virus membrane with host plasma membrane / viral envelope / host cell plasma membrane / virion membrane / plasma membrane
Similarity search - Function
Betaherpesvirus glycoprotein L (gL) domain profile. / Herpesvirus UL74, glycoprotein / Herpes UL74 glycoproteins / Cytomegalovirus glycoprotein L / Cytomegalovirus glycoprotein L / Herpesvirus glycoprotein H main domain / Herpesvirus glycoprotein H / Herpesvirus glycoprotein H, C-terminal / Herpesvirus glycoprotein H, C-terminal domain superfamily / Herpesvirus glycoprotein H C-terminal domain
Similarity search - Domain/homology
Envelope glycoprotein L / Envelope glycoprotein H / Envelope glycoprotein O
Similarity search - Component
Biological speciesHuman cytomegalovirus / Homo sapiens (human) / Human cytomegalovirus (strain Merlin)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsKschonsak M / Rouge L / Arthur CP / Hoangdung H / Patel N / Kim I / Johnson M / Kraft E / Rohou AL / Gill A ...Kschonsak M / Rouge L / Arthur CP / Hoangdung H / Patel N / Kim I / Johnson M / Kraft E / Rohou AL / Gill A / Martinez-Martin N / Payandeh J / Ciferri C
CitationJournal: Cell / Year: 2021
Title: Structures of HCMV Trimer reveal the basis for receptor recognition and cell entry.
Authors: Marc Kschonsak / Lionel Rougé / Christopher P Arthur / Ho Hoangdung / Nidhi Patel / Ingrid Kim / Matthew C Johnson / Edward Kraft / Alexis L Rohou / Avinash Gill / Nadia Martinez-Martin / ...Authors: Marc Kschonsak / Lionel Rougé / Christopher P Arthur / Ho Hoangdung / Nidhi Patel / Ingrid Kim / Matthew C Johnson / Edward Kraft / Alexis L Rohou / Avinash Gill / Nadia Martinez-Martin / Jian Payandeh / Claudio Ciferri /
Abstract: Human cytomegalovirus (HCMV) infects the majority of the human population and represents the leading viral cause of congenital birth defects. HCMV utilizes the glycoproteins gHgLgO (Trimer) to bind ...Human cytomegalovirus (HCMV) infects the majority of the human population and represents the leading viral cause of congenital birth defects. HCMV utilizes the glycoproteins gHgLgO (Trimer) to bind to platelet-derived growth factor receptor alpha (PDGFRα) and transforming growth factor beta receptor 3 (TGFβR3) to gain entry into multiple cell types. This complex is targeted by potent neutralizing antibodies and represents an important candidate for therapeutics against HCMV. Here, we determine three cryogenic electron microscopy (cryo-EM) structures of the trimer and the details of its interactions with four binding partners: the receptor proteins PDGFRα and TGFβR3 as well as two broadly neutralizing antibodies. Trimer binding to PDGFRα and TGFβR3 is mutually exclusive, suggesting that they function as independent entry receptors. In addition, Trimer-PDGFRα interaction has an inhibitory effect on PDGFRα signaling. Our results provide a framework for understanding HCMV receptor engagement, neutralization, and the development of anti-viral strategies against HCMV.
History
DepositionJan 7, 2021-
Header (metadata) releaseMar 10, 2021-
Map releaseMar 10, 2021-
UpdateMar 17, 2021-
Current statusMar 17, 2021Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 3.2
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 3.2
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7lbe
  • Surface level: 3.2
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7lbe
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_23252.png

Downloads & links

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Map

FileDownload / File: emd_23252.map.gz / Format: CCP4 / Size: 70.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationComposite map of Trimer gHgLgO bound to fabs 13H11 and Msl-109 used for model refinement
Voxel sizeX=Y=Z: 1.3514 Å
Density
Contour LevelBy AUTHOR: 3.2 / Movie #1: 3.2
Minimum - Maximum-15.498942 - 31.33147
Average (Standard dev.)-0.032898095 (±0.63407326)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions264264264
Spacing264264264
CellA=B=C: 356.7696 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.35140151515151.35140151515151.3514015151515
M x/y/z264264264
origin x/y/z0.0000.0000.000
length x/y/z356.770356.770356.770
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ264264264
MAP C/R/S321
start NC/NR/NS000
NC/NR/NS264264264
D min/max/mean-15.49931.331-0.033

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Supplemental data

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Additional map: Overall map of Trimer bound to fabs 13H11...

Fileemd_23252_additional_1.map
AnnotationOverall map of Trimer bound to fabs 13H11 and Msl-109, non-sharpened used for composite map generation
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focussed map of gO and part. gL, sharpened...

Fileemd_23252_additional_2.map
AnnotationFocussed map of gO and part. gL, sharpened used for composite map generation
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focussed map of part. gL and part. gH,...

Fileemd_23252_additional_3.map
AnnotationFocussed map of part. gL and part. gH, sharpened used for composite map generation
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focussed map of part gH and Fv regions...

Fileemd_23252_additional_4.map
AnnotationFocussed map of part gH and Fv regions of fabs, sharpened used for composite map generation
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focussed map of part gH and Fv regions of fabs, non-sharpened

Fileemd_23252_additional_5.map
AnnotationFocussed map of part gH and Fv regions of fabs, non-sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focussed map of part. gL and part. gH, non-sharpened

Fileemd_23252_additional_6.map
AnnotationFocussed map of part. gL and part. gH, non-sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focussed map of gO and part. gL, non-sharpened

Fileemd_23252_additional_7.map
AnnotationFocussed map of gO and part. gL, non-sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : HCMV Trimer gHgLgO bound to neutralizing fabs 13H11 and MSL-109

EntireName: HCMV Trimer gHgLgO bound to neutralizing fabs 13H11 and MSL-109
Components
  • Complex: HCMV Trimer gHgLgO bound to neutralizing fabs 13H11 and MSL-109
    • Complex: HCMV Trimer gHgLgO
      • Protein or peptide: Envelope glycoprotein H
      • Protein or peptide: Envelope glycoprotein L
      • Protein or peptide: Envelope glycoprotein O
    • Complex: neutralizing fabs 13H11 and MSL-109
      • Protein or peptide: Fab 13H11 light chain
      • Protein or peptide: Fab 13H11 heavy chain
      • Protein or peptide: Fab MSL-109 light chain
      • Protein or peptide: Fab MSL-109 heavy chain
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: alpha-D-mannopyranose

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Supramolecule #1: HCMV Trimer gHgLgO bound to neutralizing fabs 13H11 and MSL-109

SupramoleculeName: HCMV Trimer gHgLgO bound to neutralizing fabs 13H11 and MSL-109
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7
Molecular weightTheoretical: 275 KDa

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Supramolecule #2: HCMV Trimer gHgLgO

SupramoleculeName: HCMV Trimer gHgLgO / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#3
Source (natural)Organism: Human cytomegalovirus
Recombinant expressionOrganism: Homo sapiens (human)

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Supramolecule #3: neutralizing fabs 13H11 and MSL-109

SupramoleculeName: neutralizing fabs 13H11 and MSL-109 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #4-#7
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #1: Envelope glycoprotein H

MacromoleculeName: Envelope glycoprotein H / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human cytomegalovirus (strain Merlin) / Strain: Merlin
Molecular weightTheoretical: 87.311273 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRPGLPSYLI ILAVCLFSHL LSSRYGAEAV SEPLDKAFHL LLNTYGRPIR FLRENTTQCT YNSSLRNSTV VRENAISFNF FQSYNQYYV FHMPRCLFAG PLAEQFLNQV DLTETLERYQ QRLNTYALVS KDLASYRSFS QQLKAQDSLG EQPTTVPPPI D LSIPHVWM ...String:
MRPGLPSYLI ILAVCLFSHL LSSRYGAEAV SEPLDKAFHL LLNTYGRPIR FLRENTTQCT YNSSLRNSTV VRENAISFNF FQSYNQYYV FHMPRCLFAG PLAEQFLNQV DLTETLERYQ QRLNTYALVS KDLASYRSFS QQLKAQDSLG EQPTTVPPPI D LSIPHVWM PPQTTPHGWT ESHTTSGLHR PHFNQTCILF DGHDLLFSTV TPCLHQGFYL IDELRYVKIT LTEDFFVVTV SI DDDTPML LIFGHLPRVL FKAPYQRDNF ILRQTEKHEL LVLVKKDQLN RHSYLKDPDF LDAALDFNYL DLSALLRNSF HRY AVDVLK SGRCQMLDRR TVEMAFAYAL ALFAAARQEE AGAQVSVPRA LDRQAALLQI QEFMITCLSQ TPPRTTLLLY PTAV DLAKR ALWTPNQITD ITSLVRLVYI LSKQNQQHLI PQWALRQIAD FALKLHKTHL ASFLSAFARQ ELYLMGSLVH SMLVH TTER REIFIVETGL CSLAELSHFT QLLAHPHHEY LSDLYTPCSS SGRRDHSLER LTRLFPDATV PATVPAALSI LSTMQP STL ETFPDLFCLP LGESFSALTV SEHVSYIVTN QYLIKGISYP VSTTVVGQSL IITQTDSQTK CELTRNMHTT HSITVAL NI SLENCAFCQS ALLEYDDTQG VINIMYMHDS DDVLFALDPY NEVVVSSPRT HYLMLLKNGT VLEVTDVVVD ATDGTKLG P EQKLISEEDL NSAVDGSGLN DIFEAQKIEW HENLYFQGHH HHHHHH

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Macromolecule #2: Envelope glycoprotein L

MacromoleculeName: Envelope glycoprotein L / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human cytomegalovirus (strain Merlin) / Strain: Merlin
Molecular weightTheoretical: 30.846492 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MCRRPDCGFS FSPGPVILLW CCLLLPIVSS AAVSVAPTAA EKVPAECPEL TRRCLLGEVF EGDKYESWLR PLVNVTGRDG PLSQLIRYR PVTPEAANSV LLDEAFLDTL ALLYNNPDQL RALLTLLSSD TAPRWMTVMR GYSECGDGSP AVYTCVDDLC R GYDLTRLS ...String:
MCRRPDCGFS FSPGPVILLW CCLLLPIVSS AAVSVAPTAA EKVPAECPEL TRRCLLGEVF EGDKYESWLR PLVNVTGRDG PLSQLIRYR PVTPEAANSV LLDEAFLDTL ALLYNNPDQL RALLTLLSSD TAPRWMTVMR GYSECGDGSP AVYTCVDDLC R GYDLTRLS YGRSIFTEHV LGFELVPPSL FNVVVAIRNE ATRTNRAVRL PVSTAAAPEG ITLFYGLYNA VKEFCLRHQL DP PLLRHLD KYYAGLPPEL KQTRVNLPAH SRYGPQAVDA R

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Macromolecule #3: Envelope glycoprotein O

MacromoleculeName: Envelope glycoprotein O / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human cytomegalovirus
Molecular weightTheoretical: 58.298504 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGRKEDMRSI SKLFFIISLT VLLFSIINCK VVRPPGRYWL GTVLSTIGKQ KLDKFKLEIL KQLEREPYTK YFNMTRQHVK NLTMNMTQF PQYYILAGPI RNDSITYLWF DFYSTQLRKP AKYVYSQYNH TAKTITFRPP SCGTVPSMTC LSEMLNVSKR N DTGEQGCG ...String:
MGRKEDMRSI SKLFFIISLT VLLFSIINCK VVRPPGRYWL GTVLSTIGKQ KLDKFKLEIL KQLEREPYTK YFNMTRQHVK NLTMNMTQF PQYYILAGPI RNDSITYLWF DFYSTQLRKP AKYVYSQYNH TAKTITFRPP SCGTVPSMTC LSEMLNVSKR N DTGEQGCG NFTTFNPMFF NVPRWNTKLY VGPTKVNVDS QTIYFLGLTA LLLRYAQRNC THSFYLVNAM SRNLFRVPKY IN GTKLKNT MRKLKRKQAP VKEQLEKKTK KSQSTTTPYF SYTTSTALNV TTNATYRVTT SAKRIPTSTI AYRPDSSFMK SIM ATQLRD LATWVYTTLR YRNEPFCKPD RNRTAVSEFM KNTHVLIRNE TPYTIYGTLD MSSLYYNETM SVENETASDN NETT PTSPS TRFQKTFIDP LWDYLDSLLF LDKIRNFSLQ LPAYGNLTPP EHRRAVNLST LNSLWWWLQG SENLYFQGSA WSHPQ FEKG GGSGGGSGGG SAWSHPQFEK

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Macromolecule #4: Fab 13H11 light chain

MacromoleculeName: Fab 13H11 light chain / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.78002 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKKNIAFLLA SMFVFSIATN AYADIQMTQS PSSLSASVGD RVTITCRASQ GINNYLAWYQ QKPGKVPKLL IYAASTLQSG VPSRFSGSG SGTAFTLTIL SLQPEDVATY YCQKYNSAPF TFGPGTKVDI KRTVAAPSVF IFPPSDEQLK SGTASVVCLL N NFYPREAK ...String:
MKKNIAFLLA SMFVFSIATN AYADIQMTQS PSSLSASVGD RVTITCRASQ GINNYLAWYQ QKPGKVPKLL IYAASTLQSG VPSRFSGSG SGTAFTLTIL SLQPEDVATY YCQKYNSAPF TFGPGTKVDI KRTVAAPSVF IFPPSDEQLK SGTASVVCLL N NFYPREAK VQWKVDNALQ SGNSQESVTE QDSKDSTYSL SSTLTLSKAD YEKHKVYACE VTHQGLSSPV TKSFNRGEC

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Macromolecule #5: Fab 13H11 heavy chain

MacromoleculeName: Fab 13H11 heavy chain / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.600086 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKKNIAFLLA SMFVFSIATN AYAQVQLVQS GAEVKKPGAS VKVSCKASGY TFTNYYIHWV RQAPGQGLEW MGIIHPSSGG TSYAQKFQG RVTMTRDTST STVSMDLSSL RSEDTAVYYC GRAFRILGLS DVFVNDWGQG TVVTVSSAST KGPSVFPLAP S SKSTSGGT ...String:
MKKNIAFLLA SMFVFSIATN AYAQVQLVQS GAEVKKPGAS VKVSCKASGY TFTNYYIHWV RQAPGQGLEW MGIIHPSSGG TSYAQKFQG RVTMTRDTST STVSMDLSSL RSEDTAVYYC GRAFRILGLS DVFVNDWGQG TVVTVSSAST KGPSVFPLAP S SKSTSGGT AALGCLVKDY FPEPVTVSWN SGALTSGVHT FPAVLQSSGL YSLSSVVTVP SSSLGTQTYI CNVNHKPSNT KV DKKVEPK SCD

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Macromolecule #6: Fab MSL-109 light chain

MacromoleculeName: Fab MSL-109 light chain / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.355809 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKKNIAFLLA SMFVFSIATN AYADIVMTQS PLSLSVTPGE PASISCRSSQ SLLHTNGYNY LDWYVQKPGQ SPQLLIYLAS NRASGVPDR FSGSGSGTDF TLKISRVETE DVGVYYCMQA LQIPRTFGQG TKVEIKRTVA APSVFIFPPS DEQLKSGTAS V VCLLNNFY ...String:
MKKNIAFLLA SMFVFSIATN AYADIVMTQS PLSLSVTPGE PASISCRSSQ SLLHTNGYNY LDWYVQKPGQ SPQLLIYLAS NRASGVPDR FSGSGSGTDF TLKISRVETE DVGVYYCMQA LQIPRTFGQG TKVEIKRTVA APSVFIFPPS DEQLKSGTAS V VCLLNNFY PREAKVQWKV DNALQSGNSQ ESVTEQDSKD STYSLSSTLT LSKADYEKHK VYACEVTHQG LSSPVTKSFN RG ECGLNDI FEAQKIEWHE

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Macromolecule #7: Fab MSL-109 heavy chain

MacromoleculeName: Fab MSL-109 heavy chain / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.547818 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKKNIAFLLA SMFVFSIATN AYAEEQVLES GGGLVKPGGS LRLSCAASGF TFSPYSVFWV RQAPGKGLEW VSSINSDSTY KYYADSVKG RFTISRDNAE NSIFLQMNSL RAEDTAVYYC ARDRSYYAFS SGSLSDYYYG LDVWGQGTLV TVSSASTKGP S VFPLAPSS ...String:
MKKNIAFLLA SMFVFSIATN AYAEEQVLES GGGLVKPGGS LRLSCAASGF TFSPYSVFWV RQAPGKGLEW VSSINSDSTY KYYADSVKG RFTISRDNAE NSIFLQMNSL RAEDTAVYYC ARDRSYYAFS SGSLSDYYYG LDVWGQGTLV TVSSASTKGP S VFPLAPSS KSTSGGTAAL GCLVKDYFPE PVTVSWNSGA LTSGVHTFPA VLQSSGLYSL SSVVTVPSSS LGTQTYICNV NH KPSNTKV DKKVEPKSCD

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Macromolecule #10: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 10 / Number of copies: 16 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

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Macromolecule #11: alpha-D-mannopyranose

MacromoleculeName: alpha-D-mannopyranose / type: ligand / ID: 11 / Number of copies: 1 / Formula: MAN
Molecular weightTheoretical: 180.156 Da
Chemical component information

ChemComp-MAN:
alpha-D-mannopyranose / Mannose

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation state2D array

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Sample preparation

Concentration0.4 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
0.3 MNaClSodium chloridesodium chloride
0.025 MHEPES

Details: The sample was gently cross-linked with 0.025% (v/v) EM-grade glutaraldehyde for 10 min at RT and quenched with 9 mM Tris pH 7.5
GridModel: C-flat-1.2/1.3 / Mesh: 300 / Pretreatment - Type: PLASMA CLEANING / Details: The grid was coated with Au/Pd 80/20 prior use.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 2.5 seconds before plunging.
DetailsThis sample contained monomeric and dimeric protein complexes.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal magnification: 165000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Number grids imaged: 1 / Number real images: 14717 / Average exposure time: 10.0 sec. / Average electron dose: 50.0 e/Å2 / Details: Images were collected in 50 frames every 0.2 s
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1478640
CTF correctionSoftware - Name: CTFFIND / Software - details: 4.1.13
Startup modelType of model: OTHER / Details: ab-initio reconstruction using cisTEM
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: cisTEM (ver. 1.02)
Final 3D classificationNumber classes: 100 / Software - Name: RELION (ver. 3.1) / Details: selected 52 of 100 classes
Final angle assignmentType: PROJECTION MATCHING / Software - Name: cisTEM (ver. 1.02)
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cisTEM (ver. 1.02)
Details: Used score threshold of 0.25 for final 3D reconstruction. Map used for model building and refinements is a composite map after combining 3 focussed maps with PHENIX
Number images used: 1350211

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-7lbe:
CryoEM structure of the HCMV Trimer gHgLgO in complex with neutralizing fabs 13H11 and MSL-109

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