9fmw

Omicron BA.1 Spike protein with neutralizing NTD specific mAb K501SP6

Method: ELECTRON MICROSCOPY Dmax: 164.4 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–1207 Chain B; UniProt 1–1207 Chain C; UniProt 1–1207 Not recorded Fab of neutralizing mAb K501SP6 heavy chain × 1 Fab of neutralizing mAb K501SP6 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;TBS, pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 1–1204; UniProt 1–1207 Author chain B; PDBConstruct 1–1204; UniProt 1–1207 Author chain C; PDBConstruct 1–1204; UniProt 1–1207

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 458–484 Chain B; UniProt 458–484 Chain C; UniProt 458–484 Not recorded Fab of neutralizing mAb K501SP6 heavy chain × 1 Fab of neutralizing mAb K501SP6 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;TBS, pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 1
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 9fmw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fmw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fmw
Deposition date deposition_date2024-06-07
Structure title titleOmicron BA.1 Spike protein with neutralizing NTD specific mAb K501SP6
Keywords keywordsNeutralizing Antibody, Conserved Epitope, Covid-19, Spike, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.22
Radius of gyration Rg (electron density) rg_electron49.77
Forward intensity I(0) i01960770000.00
Molecular weight molecular_weight376160.0 kDa
Excluded volume excluded_volume472950 ų
Envelope volume envelope_volume665560 ų
Hydration-shell volume shell_volume108240 ų
Envelope diameter envelope_diameter164.3
Shell Rg shell_rg55.86
Envelope Rg envelope_rg49.12
Shape Rg shape_rg49.82
Total Rg total_rg49.82
Total atoms total_atoms26529
Residues n_residues3360
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 dmax164.4
Rg (real space) rg_real50.09
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real1.9610e+09
I(0) uncertainty (real space) i0_real_error3.6690e+07
Rg (reciprocal space) rg_reciprocal50.31
I(0) (reciprocal space) i0_reciprocal1961000000.0000
Solution quality estimate total_estimate0.8190
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.3
Skewness Skewness skewness0.228
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha331700000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)