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- EMDB-43225: DH270.6 Fab bound to the HIV-1 CH848 DE3 SOSIP -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-43225
TitleDH270.6 Fab bound to the HIV-1 CH848 DE3 SOSIP
Map data
Sample
  • Complex: Antibody Fab bound HIV-1 ectodomain
    • Protein or peptide: CH848 DE3 SOSIP gp120
    • Protein or peptide: CH848 DE3 SOSIP gp41
    • Protein or peptide: DH270.6 Antibody Fab Heavy Chain
    • Protein or peptide: DH270.6 Antibody Fab Light Chain
KeywordsImmunogen / Vaccine / Antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope ...positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / apoptotic process / host cell plasma membrane / virion membrane / structural molecule activity / plasma membrane
Similarity search - Function
Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120
Similarity search - Domain/homology
Envelope glycoprotein gp160
Similarity search - Component
Biological speciesHuman immunodeficiency virus 1 / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsHenderson R / Acharya P
Funding support United States, 4 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)DP2-AI164323 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)UM1AI144371 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI145687 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)U54AI170752 United States
CitationJournal: To Be Published
Title: Engineering immunogens that select for specific mutations in HIV broadly neutralizing antibodies
Authors: Henderson R / Haynes BF
History
DepositionDec 29, 2023-
Header (metadata) releaseOct 2, 2024-
Map releaseOct 2, 2024-
UpdateOct 2, 2024-
Current statusOct 2, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_43225.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 300 pix.
= 324. Å
1.08 Å/pix.
x 300 pix.
= 324. Å
1.08 Å/pix.
x 300 pix.
= 324. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 1.95
Minimum - Maximum-5.467902 - 9.948050500000001
Average (Standard dev.)0.009495078 (±0.2122461)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 324.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_43225_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_43225_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Antibody Fab bound HIV-1 ectodomain

EntireName: Antibody Fab bound HIV-1 ectodomain
Components
  • Complex: Antibody Fab bound HIV-1 ectodomain
    • Protein or peptide: CH848 DE3 SOSIP gp120
    • Protein or peptide: CH848 DE3 SOSIP gp41
    • Protein or peptide: DH270.6 Antibody Fab Heavy Chain
    • Protein or peptide: DH270.6 Antibody Fab Light Chain

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Supramolecule #1: Antibody Fab bound HIV-1 ectodomain

SupramoleculeName: Antibody Fab bound HIV-1 ectodomain / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Human immunodeficiency virus 1

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Macromolecule #1: CH848 DE3 SOSIP gp120

MacromoleculeName: CH848 DE3 SOSIP gp120 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Human immunodeficiency virus 1
Molecular weightTheoretical: 51.665461 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: ENLWVTVYYG VPVWKEAKTT LFCASDARAY EKEVHNVWAT HACVPTDPSP QELVLGNVTE NFNMWKNDMV DQMHEDIISL WDQSLKPCV KLTPLCVTLI CSDATVKTGT VEEMKNCSFN TTTEIRDKEK KEYALFYKPD IVPLSETNNT SEYRLINCNT S ACTQACPK ...String:
ENLWVTVYYG VPVWKEAKTT LFCASDARAY EKEVHNVWAT HACVPTDPSP QELVLGNVTE NFNMWKNDMV DQMHEDIISL WDQSLKPCV KLTPLCVTLI CSDATVKTGT VEEMKNCSFN TTTEIRDKEK KEYALFYKPD IVPLSETNNT SEYRLINCNT S ACTQACPK VTFEPIPIHY CAPAGYAILK CNDETFNGTG PCSNVSTVQC THGIRPVVST QLLLNGSLAE KEIVIRSENL TN NAKIIIV HLHTPVEIVC TRPNNNTRKS VRIGPGQTFY ATGDIIGDIK QAHCNISEEK WNDTLQKVGI ELQKHFPNKT IKY NQSAGG DMEITTHSFN CGGEFFYCNT SNLFNGTYNG TYISTNSSAN STSTITLQCR IKQIINMWQG VGRCMYAPPI AGNI TCRSN ITGLLLTRDG GTNSNETETF RPAGGDMRDN WRSELYKYKV VKIEPLGVAP TRCKRRV

UniProtKB: Envelope glycoprotein gp160

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Macromolecule #2: CH848 DE3 SOSIP gp41

MacromoleculeName: CH848 DE3 SOSIP gp41 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Human immunodeficiency virus 1
Molecular weightTheoretical: 17.179514 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
AVGIGAVFLG FLGAAGSTMG AASMTLTVQA RNLLSGIVQQ QSNLLRAIEA QQHMLQLTVW GIKQLQARVL AVERYLRDQQ LLGIWGCSG KLICCTNVPW NSSWSNRNLS EIWDNMTWLQ WDKEISNYTQ IIYGLLEESQ NQQEKNEQDL LALD

UniProtKB: Envelope glycoprotein gp160

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Macromolecule #3: DH270.6 Antibody Fab Heavy Chain

MacromoleculeName: DH270.6 Antibody Fab Heavy Chain / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.16973 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
QVQLVQSGAQ MKNPGASVKV SCAPSGYTFT DFYIHWLRQA PGQGLQWMGW MNPQTGRTNT ARNFQGRVTM TRDTSIGTAY MELRSLTSD DTAIYYCTTG GWISLYYDSS YYPNFDHWGQ GTLLTVS

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Macromolecule #4: DH270.6 Antibody Fab Light Chain

MacromoleculeName: DH270.6 Antibody Fab Light Chain / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.295555 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
ALTQPASVSG SPGQSITISC TGTKYDVGSH DLVSWYQQYP GKVPKYMIYE VNKRPSGVSN RFSGSKSGNT ASLTISGLRA EDEADYYCC SFGGSATVVC GGGTKVTVL

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.1
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.71 µm / Nominal defocus min: 0.42 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 236154
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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