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8ur7

I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-6heptad-I53_dn5 (local refinement of TH-6heptad)

Method: ELECTRON MICROSCOPY Dmax: 109.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Trimer head HA,Hemagglutinin HA1 chain

synthetic construct

UniProt Q289M7

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 64–280 Chain B； UniProt 64–280 Chain C； UniProt 64–280 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.90 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.

Other PDB Difference from Current Entry 8UR7 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7MFG Cryo-EM structure of the VRC310 clinical trial, vaccine-elicited, human antibody 310-030-1D06 Fab in complex with an H1 NC99 HA trimer Deposited 2021-04-09 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 344–519（176 aa）
Chain D 344–519（176 aa）
Chain I 344–519（176 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.87 Å
7SCN Structure of H1 NC99 influenza hemagglutinin bound to Fab 310-63E6 Deposited 2021-09-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 18–339（322 aa）
Chain B 343–520（178 aa）
Chain C 18–339（322 aa）
Chain D 343–520（178 aa）
Chain G 18–339（322 aa）
Chain I 343–520（178 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；TBS buffer, PH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Blotting time: 5.5 s Blotting force: 0 Waiting time: 7 s
Resolution 3.02 Å
7SCO Structure of H1 influenza hemagglutinin bound to Fab 310-39G10 Deposited 2021-09-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 18–339（322 aa）
Chain B 343–520（178 aa）
Chain C 18–339（322 aa）
Chain D 343–520（178 aa）
Chain G 18–339（322 aa）
Chain I 343–520（178 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；TBS buffer, PH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；Blotting time: 5.5 s Blotting force: 0 Waiting time: 7 s
Resolution 3.37 Å
8D21 Cryo-EM structure of the VRC321 clinical trial, vaccine-elicited, human antibody 1B06 in complex with a stabilized NC99 HA trimer Deposited 2022-05-27 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric
Chain B 344–519（176 aa）
Chain C 344–519（176 aa）
Chain G 344–519（176 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.96 Å
8UR5 I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-1heptad-I53_dn5 (local refinement of TH-1heptad) Deposited 2023-10-25 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 64–280（217 aa）
Chain B 64–280（217 aa）
Chain C 64–280（217 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_I00A1
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 31–247； UniProt 64–280 Author chain B； PDBConstruct 31–247； UniProt 64–280 Author chain C； PDBConstruct 31–247； UniProt 64–280

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 8ur7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ur7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ur7
Deposition date deposition_date2023-10-25
Structure title titleI53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-6heptad-I53_dn5 (local refinement of TH-6heptad)
Keywords keywords;Influenza virus, Hemagglutinin nanoparticle vaccine, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier31.49 Å
Radius of gyration Rg (electron density) rg_electron30.92 Å
Forward intensity I(0) i098451900.00
Molecular weight molecular_weight81072.0 kDa
Excluded volume excluded_volume102510 ų
Envelope volume envelope_volume137980 ų
Hydration-shell volume shell_volume38972 ų
Envelope diameter envelope_diameter116.1 Å
Shell Rg shell_rg35.96 Å
Envelope Rg envelope_rg30.92 Å
Shape Rg shape_rg30.90 Å
Total Rg total_rg31.47 Å
Total atoms total_atoms5772
Residues n_residues789
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax109.8 Å
Rg (real space) rg_real31.59 Å
Rg uncertainty (real space) rg_real_error0.95 Å
I(0) (real space) i0_real9.8450e+07
I(0) uncertainty (real space) i0_real_error1.5020e+06
Rg (reciprocal space) rg_reciprocal31.55 Å
I(0) (reciprocal space) i0_reciprocal98450000.0000
Solution quality estimate total_estimate0.8290
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.5 Å
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis0.353
Angular range angular_range— – 0.2500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21510000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.646; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.837
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)