8wfh

Crystal structure of Omicron BA.4/5 in complex with a neutralizing antibody scFv D1

Method: X-RAY DIFFRACTION Dmax: 82.9 Å Quality: GOOD

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

Spike protein S1

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 × 2 PDB declaration: trimeric(3) Count mismatch; review required Chain A; UniProt 333–530 Not recorded D1 scFv × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;25% w/v PEG 1500, SPG Buffer/NaOH pH 8.5 Resolution 2.72 Å R-free 0.250

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 1–198; UniProt 333–530

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 8wfh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wfh
Deposition date deposition_date2023-09-19
Structure title titleCrystal structure of Omicron BA.4/5 in complex with a neutralizing antibody scFv D1
Keywords keywordsRBD, antibody, scFv, BA.4/5, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.46
Radius of gyration Rg (electron density) rg_electron23.84
Forward intensity I(0) i036977700.00
Molecular weight molecular_weight46532.0 kDa
Excluded volume excluded_volume57942 ų
Envelope volume envelope_volume68803 ų
Hydration-shell volume shell_volume24773 ų
Envelope diameter envelope_diameter86.6
Shell Rg shell_rg30.28
Envelope Rg envelope_rg24.11
Shape Rg shape_rg23.76
Total Rg total_rg24.81
Total atoms total_atoms3284
Residues n_residues422
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 dmax82.9
Rg (real space) rg_real24.50
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real3.6980e+07
I(0) uncertainty (real space) i0_real_error5.4610e+05
Rg (reciprocal space) rg_reciprocal24.49
I(0) (reciprocal space) i0_reciprocal36980000.0000
Solution quality estimate total_estimate0.8744
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.405
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8323000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.827; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.928; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)