8jmm

Structure of XBB spike protein (S) dimer-trimer in complex with bispecific antibody G7-Fc at 3.75 Angstroms resolution.

Method: ELECTRON MICROSCOPY Dmax: 299.1 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Spike glycoprotein

Severe acute respiratory syndrome coronavirus 2

UniProt P0DTC2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 28–1208 Chain B; UniProt 28–1208 Chain C; UniProt 28–1208 Chain D; UniProt 28–1208 Chain E; UniProt 28–1208 Chain F; UniProt 28–1208 Not recorded 7F3 Fv × 6 GW01 Fv × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2152 other PDB entries and 2473 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 36–1215; UniProt 28–1208 Author chain B; PDBConstruct 36–1215; UniProt 28–1208 Author chain C; PDBConstruct 36–1215; UniProt 28–1208 Author chain D; PDBConstruct 36–1215; UniProt 28–1208 Author chain E; PDBConstruct 36–1215; UniProt 28–1208 Author chain F; PDBConstruct 36–1215; UniProt 28–1208

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8jmm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8jmm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8jmm
Deposition date deposition_date2023-06-05
Structure title titleStructure of XBB spike protein (S) dimer-trimer in complex with bispecific antibody G7-Fc at 3.75 Angstroms resolution.
Keywords keywordsAntibody, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron109.90
Forward intensity I(0) i013756200000.00
Molecular weight molecular_weight1001800.0 kDa
Excluded volume excluded_volume1253000 ų
Envelope volume envelope_volume2314600 ų
Hydration-shell volume shell_volume203350 ų
Envelope diameter envelope_diameter423.1
Shell Rg shell_rg80.95
Envelope Rg envelope_rg104.00
Shape Rg shape_rg109.90
Total Rg total_rg109.70
Total atoms total_atoms70630
Residues n_residues9099
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax299.1
Rg (real space) rg_real100.10
Rg uncertainty (real space) rg_real_error1.42
I(0) (real space) i0_real1.3160e+10
I(0) uncertainty (real space) i0_real_error2.4520e+08
Rg (reciprocal space) rg_reciprocal94.64
I(0) (reciprocal space) i0_reciprocal13230000000.0000
Solution quality estimate total_estimate0.8877
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary85.5
Skewness Skewness skewness0.478
Kurtosis Kurtosis kurtosis-0.664
Angular range angular_range— – 0.0700 −1
Current regularization parameter α current_alpha0.8216
Highest regularization parameter α highest_alpha1207000000.0000
Real-space data points n_real_points15
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.010; Oscil: 0.874; Stabil: 0.980; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.009

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)