8dao

Crystal structure of SARS-CoV-2 spike stem fusion peptide in complex with neutralizing antibody COV44-79

Method: X-RAY DIFFRACTION Dmax: 100.2 Å Quality: EXCELLENT

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

COV44-79 heavy chain constant domain

Homo sapiens

UniProt P0DOX5

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 120–222 Not recorded COV44-79 heavy chain variable domain × 1 COV44-79 light chain variable domain × 1 COV44-79 light chain constant domain × 1 (P01834) Spike protein S2 fusion peptide × 1 (P0DTC2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1 M Tris, pH 8.5, 0.01 M nickel (II) chloride, and 20% PEG monomethyl ether 2000 Resolution 2.80 Å R-free 0.284
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 120–222 Not recorded COV44-79 heavy chain variable domain × 1 COV44-79 light chain variable domain × 1 COV44-79 light chain constant domain × 1 (P01834) Spike protein S2 fusion peptide × 1 (P0DTC2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1 M Tris, pH 8.5, 0.01 M nickel (II) chloride, and 20% PEG monomethyl ether 2000 Resolution 2.80 Å R-free 0.284

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.

105 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–103; UniProt 120–222 Author chain G; PDBConstruct 1–103; UniProt 120–222

COV44-79 light chain constant domain

Homo sapiens

UniProt P01834

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 1–107 Not recorded COV44-79 heavy chain variable domain × 1 COV44-79 light chain variable domain × 1 COV44-79 heavy chain constant domain × 1 (P0DOX5) Spike protein S2 fusion peptide × 1 (P0DTC2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1 M Tris, pH 8.5, 0.01 M nickel (II) chloride, and 20% PEG monomethyl ether 2000 Resolution 2.80 Å R-free 0.284
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 1–107 Not recorded COV44-79 heavy chain variable domain × 1 COV44-79 light chain variable domain × 1 COV44-79 heavy chain constant domain × 1 (P0DOX5) Spike protein S2 fusion peptide × 1 (P0DTC2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1 M Tris, pH 8.5, 0.01 M nickel (II) chloride, and 20% PEG monomethyl ether 2000 Resolution 2.80 Å R-free 0.284

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.

44 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGKC_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–107; UniProt 1–107 Author chain H; PDBConstruct 1–107; UniProt 1–107

Spike protein S2 fusion peptide

OrganismNot specified

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain I; UniProt 809–823 Not recorded COV44-79 heavy chain variable domain × 1 COV44-79 light chain variable domain × 1 COV44-79 heavy chain constant domain × 1 (P0DOX5) COV44-79 light chain constant domain × 1 (P01834) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1 M Tris, pH 8.5, 0.01 M nickel (II) chloride, and 20% PEG monomethyl ether 2000 Resolution 2.80 Å R-free 0.284
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain J; UniProt 809–823 Not recorded COV44-79 heavy chain variable domain × 1 COV44-79 light chain variable domain × 1 COV44-79 heavy chain constant domain × 1 (P0DOX5) COV44-79 light chain constant domain × 1 (P01834) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293.15 K;0.1 M Tris, pH 8.5, 0.01 M nickel (II) chloride, and 20% PEG monomethyl ether 2000 Resolution 2.80 Å R-free 0.284

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 2472 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–15; UniProt 809–823 Author chain J; PDBConstruct 1–15; UniProt 809–823

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 8dao

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8dao
Deposition date deposition_date2022-06-13
Structure title titleCrystal structure of SARS-CoV-2 spike stem fusion peptide in complex with neutralizing antibody COV44-79
Keywords keywordsSARS-CoV-2, coronavirus, antibody, fusion peptide, neutralizing antibody, COVID-19, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.30
Radius of gyration Rg (electron density) rg_electron31.48
Forward intensity I(0) i0156433000.00
Molecular weight molecular_weight98273.0 kDa
Excluded volume excluded_volume122610 ų
Envelope volume envelope_volume161860 ų
Hydration-shell volume shell_volume42586 ų
Envelope diameter envelope_diameter105.5
Shell Rg shell_rg38.99
Envelope Rg envelope_rg30.47
Shape Rg shape_rg31.47
Total Rg total_rg32.19
Total atoms total_atoms6914
Residues n_residues912
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 dmax100.2
Rg (real space) rg_real32.09
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real1.5640e+08
I(0) uncertainty (real space) i0_real_error2.3220e+06
Rg (reciprocal space) rg_reciprocal32.18
I(0) (reciprocal space) i0_reciprocal156400000.0000
Solution quality estimate total_estimate0.9012
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.0
Skewness Skewness skewness0.096
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24690000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8daoA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8daoB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8daoC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8daoD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)