4qes

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

Method: X-RAY DIFFRACTION Dmax: 117.4 Å Quality: EXCELLENT

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

Non-haem bromoperoxidase BPO-A2, Matrix protein 1 chimera

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 3–164 Chain B; UniProt 3–164 Chain C; UniProt 3–164 Fragment:SEE REMARK 999 Mutation:K118A, L279Q, Q24T, Y51A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.4;298 K;0.1 M sodium citrate, pH 4.4, 11% PEG3000, 200 mM sodium chloride, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 4.19 Å R-free 0.295

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 287–448; UniProt 3–164 Author chain B; PDBConstruct 287–448; UniProt 3–164 Author chain C; PDBConstruct 287–448; UniProt 3–164

Non-haem bromoperoxidase BPO-A2, Matrix protein 1 chimera

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 Fragment:SEE REMARK 999 Mutation:K118A, L279Q, Q24T, Y51A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.4;298 K;0.1 M sodium citrate, pH 4.4, 11% PEG3000, 200 mM sodium chloride, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 4.19 Å R-free 0.295

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 4qes

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4qes
Deposition date deposition_date2014-05-18
Structure title titleStructure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, quadruple mutant, I222 form
Keywords keywordsprotein design, bionanotechnology, protein assembly, symmetry, biomaterials, OXIDOREDUCTASE, VIRAL PROTEIN; OXIDOREDUCTASE, VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.46
Radius of gyration Rg (electron density) rg_electron36.96
Forward intensity I(0) i0305369000.00
Molecular weight molecular_weight143260.0 kDa
Excluded volume excluded_volume179710 ų
Envelope volume envelope_volume231070 ų
Hydration-shell volume shell_volume51904 ų
Envelope diameter envelope_diameter116.8
Shell Rg shell_rg43.29
Envelope Rg envelope_rg36.66
Shape Rg shape_rg36.88
Total Rg total_rg37.61
Total atoms total_atoms10128
Residues n_residues1323
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 dmax117.4
Rg (real space) rg_real37.29
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real3.0540e+08
I(0) uncertainty (real space) i0_real_error5.1620e+06
Rg (reciprocal space) rg_reciprocal37.40
I(0) (reciprocal space) i0_reciprocal305400000.0000
Solution quality estimate total_estimate0.9004
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.1
Skewness Skewness skewness0.131
Kurtosis Kurtosis kurtosis-0.561
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha112400000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.903

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)