7tpr

Camel nanobodies 7A3 and 8A2 broadly neutralize SARS-CoV-2 variants

Method: ELECTRON MICROSCOPY Dmax: 198.6 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 15–1159 Chain B; UniProt 15–1159 Chain C; UniProt 15–1159 Mutation:F817P, A892P, A899P, A942P, K986P, V987P, and residues 682-685 from RRAR to GSAS Nanobody 8A2 × 2 Nanobody 7A3 × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;PBS cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.39 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 1–1145; UniProt 15–1159 Author chain B; PDBConstruct 1–1145; UniProt 15–1159 Author chain C; PDBConstruct 1–1145; UniProt 15–1159

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 7tpr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7tpr
Deposition date deposition_date2022-01-25
Structure title titleCamel nanobodies 7A3 and 8A2 broadly neutralize SARS-CoV-2 variants
Keywords keywordsNeutralization, nanobody, 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_guinier57.62
Radius of gyration Rg (electron density) rg_electron57.30
Forward intensity I(0) i02871930000.00
Molecular weight molecular_weight449340.0 kDa
Excluded volume excluded_volume561550 ų
Envelope volume envelope_volume817510 ų
Hydration-shell volume shell_volume119860 ų
Envelope diameter envelope_diameter216.2
Shell Rg shell_rg58.80
Envelope Rg envelope_rg56.82
Shape Rg shape_rg57.34
Total Rg total_rg57.21
Total atoms total_atoms31669
Residues n_residues4074
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 dmax198.6
Rg (real space) rg_real57.66
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real2.8720e+09
I(0) uncertainty (real space) i0_real_error5.6770e+07
Rg (reciprocal space) rg_reciprocal57.58
I(0) (reciprocal space) i0_reciprocal2872000000.0000
Solution quality estimate total_estimate0.8660
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.2
Skewness Skewness skewness0.408
Kurtosis Kurtosis kurtosis-0.102
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha229000000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.830

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id7tprA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7tprB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7tprC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily960 — Spike glycoprotein, N-terminal domain
Domain ID domain_id7tprD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7tprE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7tprF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7tprG01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7tprH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)