4ivj

Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, I222 form

Method: X-RAY DIFFRACTION Dmax: 121.2 Å Quality: GOOD

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

Non-haem bromoperoxidase BPO-A2, Matrix protein 1

Influenza A virus

UniProt P03485

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 Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 3–165 Chain B; UniProt 3–165 Chain C; UniProt 3–165 Mutation:K118A, L279Q, Q24T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.4;298 K;0.1M Na Citrate pH 4.4, 10% PEG 3000, vapor diffusion, hanging drop, temperature 298K Resolution 7.35 Å R-free 0.288

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.

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name M1_I34A1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 287–449; UniProt 3–165 Author chain B; PDBConstruct 287–449; UniProt 3–165 Author chain C; PDBConstruct 287–449; UniProt 3–165

Non-haem bromoperoxidase BPO-A2, Matrix protein 1

Influenza A virus

UniProt P29715

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 Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–278 Chain B; UniProt 1–278 Chain C; UniProt 1–278 Mutation:K118A, L279Q, Q24T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.4;298 K;0.1M Na Citrate pH 4.4, 10% PEG 3000, vapor diffusion, hanging drop, temperature 298K Resolution 7.35 Å R-free 0.288

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.

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BPOA2_STRAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–278; UniProt 1–278 Author chain B; PDBConstruct 1–278; UniProt 1–278 Author chain C; PDBConstruct 1–278; UniProt 1–278

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 4ivj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ivj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ivj
Deposition date deposition_date2013-01-23
Structure title titleStructure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, I222 form
Keywords keywordsprotein design, bionanotechnology, protein assembly, symmetric oligomeric domains, biomaterials, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.90
Radius of gyration Rg (electron density) rg_electron37.47
Forward intensity I(0) i0307892000.00
Molecular weight molecular_weight144200.0 kDa
Excluded volume excluded_volume181010 ų
Envelope volume envelope_volume233710 ų
Hydration-shell volume shell_volume52042 ų
Envelope diameter envelope_diameter120.0
Shell Rg shell_rg43.43
Envelope Rg envelope_rg37.18
Shape Rg shape_rg37.38
Total Rg total_rg38.12
Total atoms total_atoms10194
Residues n_residues1320
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 dmax121.2
Rg (real space) rg_real37.76
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real3.0790e+08
I(0) uncertainty (real space) i0_real_error4.6460e+06
Rg (reciprocal space) rg_reciprocal37.85
I(0) (reciprocal space) i0_reciprocal307900000.0000
Solution quality estimate total_estimate0.8292
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.9
Skewness Skewness skewness0.162
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha105600000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)