8zhf

SARS-CoV-2 spike trimer (6P) in complex with R1-26 Fab, head-to-head aggregate

Method: ELECTRON MICROSCOPY Dmax: 222.7 Å Quality: EXCELLENT

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

Spike glycoprotein,Fibritin,Expression Tag

synthetic construct

UniProt A0A346FJN8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 18 其他Polymer 30 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 458–484 Chain B; UniProt 458–484 Chain C; UniProt 458–484 Chain D; UniProt 458–484 Chain E; UniProt 458–484 Chain I; UniProt 458–484 Not recorded Heavy chain of R1-26 Fab × 6 Light chain of R1-26 Fab × 6 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 30 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.26 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.

17 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A346FJN8_BPT6
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1201–1227; UniProt 458–484 Author chain B; PDBConstruct 1201–1227; UniProt 458–484 Author chain C; PDBConstruct 1201–1227; UniProt 458–484 Author chain D; PDBConstruct 1201–1227; UniProt 458–484 Author chain E; PDBConstruct 1201–1227; UniProt 458–484 Author chain I; PDBConstruct 1201–1227; UniProt 458–484

Spike glycoprotein,Fibritin,Expression Tag

synthetic construct

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 Insufficient information Heteromer Protein × 18 其他Polymer 30 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 11–1208 Chain B; UniProt 11–1208 Chain C; UniProt 11–1208 Chain D; UniProt 11–1208 Chain E; UniProt 11–1208 Chain I; UniProt 11–1208 Not recorded Heavy chain of R1-26 Fab × 6 Light chain of R1-26 Fab × 6 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 30 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.26 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 1–1198; UniProt 11–1208 Author chain B; PDBConstruct 1–1198; UniProt 11–1208 Author chain C; PDBConstruct 1–1198; UniProt 11–1208 Author chain D; PDBConstruct 1–1198; UniProt 11–1208 Author chain E; PDBConstruct 1–1198; UniProt 11–1208 Author chain I; PDBConstruct 1–1198; UniProt 11–1208

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 8zhf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zhf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zhf
Deposition date deposition_date2024-05-10
Structure title titleSARS-CoV-2 spike trimer (6P) in complex with R1-26 Fab, head-to-head aggregate
Keywords keywordsSpike protein, RBD, Antibody, Fab, Viral protein, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier84.85
Radius of gyration Rg (electron density) rg_electron85.08
Forward intensity I(0) i013979800000.00
Molecular weight molecular_weight1006800.0 kDa
Excluded volume excluded_volume1258600 ų
Envelope volume envelope_volume2294100 ų
Hydration-shell volume shell_volume232920 ų
Envelope diameter envelope_diameter329.3
Shell Rg shell_rg83.59
Envelope Rg envelope_rg80.00
Shape Rg shape_rg85.05
Total Rg total_rg85.15
Total atoms total_atoms70929
Residues n_residues8985
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 dmax222.7
Rg (real space) rg_real80.28
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.3290e+10
I(0) uncertainty (real space) i0_real_error2.6550e+08
Rg (reciprocal space) rg_reciprocal84.58
I(0) (reciprocal space) i0_reciprocal13970000000.0000
Solution quality estimate total_estimate0.9163
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary99.0
Skewness Skewness skewness0.126
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.8111
Highest regularization parameter α highest_alpha744200000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.999; Stabil: 0.978; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)