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- PDB-22ll: Structure of neutralizing antibody G4 with MPXV M1R -

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Basic information

Entry
Database: PDB / ID: 22ll
TitleStructure of neutralizing antibody G4 with MPXV M1R
Components
  • Entry-fusion complex associated protein OPG095
  • G4 heavy chain
  • G4 light chain
KeywordsANTIVIRAL PROTEIN / Cryo-EM / Complex
Function / homologyVirion membrane protein, poxvirus L1-related / Lipid membrane protein of large eukaryotic DNA viruses / viral envelope / symbiont entry into host cell / virion attachment to host cell / virion membrane / Entry-fusion complex associated protein OPG095
Function and homology information
Biological speciesMacaca fascicularis (crab-eating macaque)
Monkeypox virus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsZai, X.D. / Chen, L.
Funding support China, 2items
OrganizationGrant numberCountry
Other private2023QNRC001 China
National Natural Science Foundation of China (NSFC)32571110 China
CitationJournal: To Be Published
Title: Structure of neutralizing antibody G4 with MPXV M1R
Authors: Zai, X.D. / Chen, L.
History
DepositionJan 15, 2026Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Sep 2, 2026Provider: repository / Type: Initial release
Revision 1.0Sep 2, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
Ha: G4 heavy chain
Hb: G4 heavy chain
La: G4 light chain
Lb: G4 light chain
Aa: Entry-fusion complex associated protein OPG095
Ab: Entry-fusion complex associated protein OPG095


Theoretical massNumber of molelcules
Total (without water)134,3606
Polymers134,3606
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Antibody G4 heavy chain


Mass: 23797.732 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Macaca fascicularis (crab-eating macaque)
Production host: Homo sapiens (human)
#2: Antibody G4 light chain


Mass: 23219.723 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Macaca fascicularis (crab-eating macaque)
Production host: Homo sapiens (human)
#3: Protein Entry-fusion complex associated protein OPG095 / IMV membrane protein M1R / EFC-associated protein OPG095 / Protein L1


Mass: 20162.510 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Monkeypox virus / Gene: OPG099, MPXVgp080 / Production host: Escherichia coli (E. coli) / References: UniProt: M1LBP0
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: G4 FAB_M1R COMPLEX / Type: COMPLEX / Entity ID: #3, #1-#2 / Source: RECOMBINANT
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
21Macaca fascicularis (crab-eating macaque)9541
31Monkeypox virus10244
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
21Homo sapiens (human)9606
31Homo (humans)9605
Buffer solutionpH: 7.4 / Details: PBS
SpecimenConc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 300 divisions/in.
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 1400 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1CryoSMARTparticle selection
2PHENIX2.0_5885model refinement
13CryoSMART3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 17196 / Symmetry type: POINT
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 111.53 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00489356
ELECTRON MICROSCOPYf_angle_d0.786112718
ELECTRON MICROSCOPYf_chiral_restr0.04691468
ELECTRON MICROSCOPYf_plane_restr0.00561634
ELECTRON MICROSCOPYf_dihedral_angle_d16.16753362

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