9js7

cryoEM of antibody complexed with mature Zika virus

Method: ELECTRON MICROSCOPY Dmax: 176.5 Å Quality: GOOD

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

Genome polyprotein

Zika virus ZIKV/H. sapiens/FrenchPolynesia/10087PF/2013

UniProt A0A024B7W1

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 heterocomplex Heteromer Protein × 420 PDB declaration: 420-meric(420) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Not recorded antibody heavy chain × 120 antibody light chain × 120 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.84 Å
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Not recorded antibody heavy chain × 2 antibody light chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.84 Å
3 Protein heterocomplex Heteromer Protein × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Not recorded antibody heavy chain × 10 antibody light chain × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.84 Å
4 Protein heterocomplex Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Not recorded antibody heavy chain × 12 antibody light chain × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.84 Å
5 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 291–794 Chain B; UniProt 291–794 Chain C; UniProt 291–794 Not recorded antibody heavy chain × 2 antibody light chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.84 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.

35 other PDB entries and 101 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_ZIKVF
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–504; UniProt 291–794 Author chain B; PDBConstruct 1–504; UniProt 291–794 Author chain C; PDBConstruct 1–504; UniProt 291–794

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 9js7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9js7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9js7
Deposition date deposition_date2024-09-30
Structure title titlecryoEM of antibody complexed with mature Zika virus
Keywords keywordsCOMPLEX, VIRUS, VIRUS-IMMUNE SYSTEM complex; VIRUS/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.04
Radius of gyration Rg (electron density) rg_electron56.86
Forward intensity I(0) i0680586000.00
Molecular weight molecular_weight212810.0 kDa
Excluded volume excluded_volume264710 ų
Envelope volume envelope_volume398890 ų
Hydration-shell volume shell_volume64950 ų
Envelope diameter envelope_diameter189.0
Shell Rg shell_rg51.68
Envelope Rg envelope_rg54.82
Shape Rg shape_rg56.87
Total Rg total_rg56.66
Total atoms total_atoms14929
Residues n_residues1974
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 dmax176.5
Rg (real space) rg_real56.64
Rg uncertainty (real space) rg_real_error2.15
I(0) (real space) i0_real6.8060e+08
I(0) uncertainty (real space) i0_real_error1.3750e+07
Rg (reciprocal space) rg_reciprocal55.50
I(0) (reciprocal space) i0_reciprocal679400000.0000
Solution quality estimate total_estimate0.8017
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.4
Skewness Skewness skewness0.524
Kurtosis Kurtosis kurtosis-0.533
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29930000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.835; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)