7wp1

Cryo-EM structure of SARS-CoV-2 Mu S6P trimer in complex with neutralizing antibody VacW-209 (local refinement)

Method: ELECTRON MICROSCOPY Dmax: 77.8 Å Quality: GOOD

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

VacW-209 light chain

Homo sapiens

UniProt A0A5C2GQT9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 1–111 Not recorded VacW-209 heavy chain × 1 Spike protein S1 × 1 (P0DTC2) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5C2GQT9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 1–111; UniProt 1–111

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 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 333–521 Not recorded VacW-209 light chain × 1 (A0A5C2GQT9) VacW-209 heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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 3
Chains and sequence ranges Author chain F; PDBConstruct 1–189; UniProt 333–521

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 7wp1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7wp1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7wp1
Deposition date deposition_date2022-01-22
Structure title titleCryo-EM structure of SARS-CoV-2 Mu S6P trimer in complex with neutralizing antibody VacW-209 (local refinement)
Keywords keywordsSARS-CoV-2, Mu variant, spike, neutralizing antibody, Cryo-EM, VIRAL PROTEIN, IMMUNE SYSTEM-VIRAL PROTEIN complex; IMMUNE SYSTEM/VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier23.95
Radius of gyration Rg (electron density) rg_electron22.99
Forward intensity I(0) i037763300.00
Molecular weight molecular_weight46849.0 kDa
Excluded volume excluded_volume58336 ų
Envelope volume envelope_volume72668 ų
Hydration-shell volume shell_volume26286 ų
Envelope diameter envelope_diameter80.4
Shell Rg shell_rg30.09
Envelope Rg envelope_rg23.29
Shape Rg shape_rg22.92
Total Rg total_rg24.05
Total atoms total_atoms3305
Residues n_residues423
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 dmax77.8
Rg (real space) rg_real23.88
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real3.7760e+07
I(0) uncertainty (real space) i0_real_error4.9540e+05
Rg (reciprocal space) rg_reciprocal23.89
I(0) (reciprocal space) i0_reciprocal37760000.0000
Solution quality estimate total_estimate0.8923
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.279
Kurtosis Kurtosis kurtosis-0.342
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8249000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7wp1H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7wp1L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)