8a8n

Structure of self-assembling engineered protein nanocage (EPN) fused with hepatitis A pX protein

Method: ELECTRON MICROSCOPY Dmax: 51.9 Å Quality: GOOD

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

EPN-pX

Human immunodeficiency virus type 1 BH10

UniProt Q9WXS1

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–205 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7;PBS cryo-EM vitrification conditions:Cryogen ETHANE;Blot time 4-5 s. Resolution 6.70 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.

16 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9WXS1_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 19–222; UniProt 2–205

EPN-pX

Human immunodeficiency virus type 1 BH10

UniProt V9Z3B5

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 38–108 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7;PBS cryo-EM vitrification conditions:Cryogen ETHANE;Blot time 4-5 s. Resolution 6.70 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name V9Z3B5_9PICO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 232–302; UniProt 38–108

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 8a8n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8a8n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8a8n
Deposition date deposition_date2022-06-23
Structure title titleStructure of self-assembling engineered protein nanocage (EPN) fused with hepatitis A pX protein
Keywords keywordshepatitis A, pX, VP1-pX, nanocage, icosahedral, protein nanoparticle, virus assembly, enveloped viruses, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier17.29
Radius of gyration Rg (electron density) rg_electron16.06
Forward intensity I(0) i07547200.00
Molecular weight molecular_weight21655.0 kDa
Excluded volume excluded_volume27818 ų
Envelope volume envelope_volume30757 ų
Hydration-shell volume shell_volume15917 ų
Envelope diameter envelope_diameter51.7
Shell Rg shell_rg22.20
Envelope Rg envelope_rg16.30
Shape Rg shape_rg16.02
Total Rg total_rg17.28
Total atoms total_atoms1522
Residues n_residues202
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 dmax51.9
Rg (real space) rg_real17.16
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real7.5470e+06
I(0) uncertainty (real space) i0_real_error8.4420e+04
Rg (reciprocal space) rg_reciprocal17.18
I(0) (reciprocal space) i0_reciprocal7547000.0000
Solution quality estimate total_estimate0.8984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2452000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)