9c4n

Infectious B19V capsid

Method: ELECTRON MICROSCOPY Dmax: 27.3 Å Quality: GOOD

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

Inter-alpha-trypsin inhibitor heavy chain H4

OrganismNot specified

UniProt Q14624

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain Y; UniProt 1–930 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITIH4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain Y; PDBConstruct 1–930; UniProt 1–930

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 9c4n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c4n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c4n
Deposition date deposition_date2024-06-04
最后修订 last_revision2024-11-13
Structure title titleInfectious B19V capsid
Keywords keywordsB19, Virion, Capsid, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier8.27
Radius of gyration Rg (electron density) rg_electron6.89
Forward intensity I(0) i049005.30
Molecular weight molecular_weight984.2 kDa
Excluded volume excluded_volume1209 ų
Envelope volume envelope_volume1552 ų
Hydration-shell volume shell_volume2437 ų
Envelope diameter envelope_diameter23.5
Shell Rg shell_rg10.39
Envelope Rg envelope_rg7.02
Shape Rg shape_rg6.87
Total Rg total_rg8.62
Total atoms total_atoms69
Residues n_residues9
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 dmax27.3
Rg (real space) rg_real8.28
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real4.9010e+04
I(0) uncertainty (real space) i0_real_error5.1030e+02
Rg (reciprocal space) rg_reciprocal8.28
I(0) (reciprocal space) i0_reciprocal49010.0000
Solution quality estimate total_estimate0.8922
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary10.0
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4947.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)