9x5y

B/Brisbane/60/2008 HA in complex with BO-6B

Method: ELECTRON MICROSCOPY Dmax: 141.3 Å Quality: EXCELLENT

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

Hemagglutinin HA1 chain

Influenza B virus (B/Brisbane/60/2008)

UniProt C0LT38

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 × 12 其他Polymer 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–362 Chain B; UniProt 363–550 Chain E; UniProt 1–362 Chain F; UniProt 363–550 Chain G; UniProt 1–362 Chain I; UniProt 363–550 Not recorded BO-6B heavy chain × 3 BO-6B light chain × 3 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.65 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C0LT38_9INFB
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–362; UniProt 1–362 Author chain E; PDBConstruct 1–362; UniProt 1–362 Author chain G; PDBConstruct 1–362; UniProt 1–362 Author chain B; PDBConstruct 1–188; UniProt 363–550 Author chain F; PDBConstruct 1–188; UniProt 363–550 Author chain I; PDBConstruct 1–188; UniProt 363–550

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 9x5y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x5y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x5y
Deposition date deposition_date2025-10-14
Structure title titleB/Brisbane/60/2008 HA in complex with BO-6B
Keywords keywordsHemagglutinin, HA, antibody, influenza B virus, BO-6B, 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_guinier44.88
Radius of gyration Rg (electron density) rg_electron44.64
Forward intensity I(0) i0774094000.00
Molecular weight molecular_weight225860.0 kDa
Excluded volume excluded_volume281380 ų
Envelope volume envelope_volume384050 ų
Hydration-shell volume shell_volume71362 ų
Envelope diameter envelope_diameter141.3
Shell Rg shell_rg48.36
Envelope Rg envelope_rg45.35
Shape Rg shape_rg44.64
Total Rg total_rg44.80
Total atoms total_atoms15870
Residues n_residues1995
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 dmax141.3
Rg (real space) rg_real44.71
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real7.7410e+08
I(0) uncertainty (real space) i0_real_error1.5070e+07
Rg (reciprocal space) rg_reciprocal44.88
I(0) (reciprocal space) i0_reciprocal774200000.0000
Solution quality estimate total_estimate0.9013
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.5
Skewness Skewness skewness0.119
Kurtosis Kurtosis kurtosis-0.690
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha124600000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.859

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)