8r1d

SD1-3 Fab in complex with SARS-CoV-2 BA.2.12.1 Spike Glycoprotein

Method: ELECTRON MICROSCOPY Dmax: 154.6 Å Quality: GOOD

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

Spike glycoprotein,Fibritin

Enterobacteria phage T4

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–1208 Chain B; UniProt 1–1208 Chain C; UniProt 1–1208 Not recorded SD1-3 Fab Heavy Chain × 3 SD1-3 Fab Light Chain × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.37 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 A; PDBConstruct 1–1205; UniProt 1–1208 Author chain B; PDBConstruct 1–1205; UniProt 1–1208 Author chain C; PDBConstruct 1–1205; UniProt 1–1208

Spike glycoprotein,Fibritin

Enterobacteria phage T4

UniProt P10104

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 458–484 Chain B; UniProt 458–484 Chain C; UniProt 458–484 Not recorded SD1-3 Fab Heavy Chain × 3 SD1-3 Fab Light Chain × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.37 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.

104 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WAC_BPT4
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1208–1234; UniProt 458–484 Author chain B; PDBConstruct 1208–1234; UniProt 458–484 Author chain C; PDBConstruct 1208–1234; UniProt 458–484

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 8r1d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r1d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r1d
Deposition date deposition_date2023-11-01
Structure title titleSD1-3 Fab in complex with SARS-CoV-2 BA.2.12.1 Spike Glycoprotein
Keywords keywords;SARS-CoV-2, Spike, Glycoprotein, Coronavirus, antibody, Fab, SD1 domain, therapeutic, complex, neutralisingm convalescent sera, viral protein, immune system, SD1-3, BA.2.12.1, omicron variant, virus, BA.2.86 ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.65
Radius of gyration Rg (electron density) rg_electron51.13
Forward intensity I(0) i02615760000.00
Molecular weight molecular_weight432120.0 kDa
Excluded volume excluded_volume541710 ų
Envelope volume envelope_volume741020 ų
Hydration-shell volume shell_volume116460 ų
Envelope diameter envelope_diameter164.2
Shell Rg shell_rg57.69
Envelope Rg envelope_rg50.51
Shape Rg shape_rg51.16
Total Rg total_rg51.22
Total atoms total_atoms30450
Residues n_residues3876
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 dmax154.6
Rg (real space) rg_real51.45
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real2.6160e+09
I(0) uncertainty (real space) i0_real_error4.2540e+07
Rg (reciprocal space) rg_reciprocal51.81
I(0) (reciprocal space) i0_reciprocal2617000000.0000
Solution quality estimate total_estimate0.8580
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.8
Skewness Skewness skewness0.145
Kurtosis Kurtosis kurtosis-0.554
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha304900000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.970; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.262

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)