9yax

Localized reconstruction of the asymmetric unit of the low pH treated back neutralized SINV/EEEV in complex with Fab fragment of the antibody EEEV-179

Method: ELECTRON MICROSCOPY Dmax: 242.3 Å Quality: GOOD

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

E1

Eastern equine encephalitis virus

UniProt W8RHT7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 17 其他Polymer 4 PDB declaration: 17-meric(17) Consistent with protein copy count Chain A; UniProt 802–1238 Chain B; UniProt 802–1238 Chain C; UniProt 802–1238 Chain D; UniProt 802–1238 Chain E; UniProt 802–1238 Not recorded EEEV-179 Heavy chain × 1 EEEV-179 Light chain × 1 Capsid protein × 5 (Q88793) E2 × 5 (E9KXL2) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name W8RHT7_EEEV
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–437; UniProt 802–1238 Author chain B; PDBConstruct 1–437; UniProt 802–1238 Author chain C; PDBConstruct 1–437; UniProt 802–1238 Author chain D; PDBConstruct 1–437; UniProt 802–1238 Author chain E; PDBConstruct 1–437; UniProt 802–1238

Capsid protein

Eastern equine encephalitis virus

UniProt Q88793

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 17 其他Polymer 4 PDB declaration: 17-meric(17) Consistent with protein copy count Chain P; UniProt 102–261 Chain Q; UniProt 102–261 Chain R; UniProt 102–261 Chain S; UniProt 102–261 Chain T; UniProt 102–261 Fragment:Capsid protein c-terminal domain EEEV-179 Heavy chain × 1 EEEV-179 Light chain × 1 E1 × 5 (W8RHT7) E2 × 5 (E9KXL2) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q88793_EEEV
Isoform
PDB entities 4
Chains and sequence ranges Author chain P; PDBConstruct 1–160; UniProt 102–261 Author chain Q; PDBConstruct 1–160; UniProt 102–261 Author chain R; PDBConstruct 1–160; UniProt 102–261 Author chain S; PDBConstruct 1–160; UniProt 102–261 Author chain T; PDBConstruct 1–160; UniProt 102–261

E2

Eastern equine encephalitis virus

UniProt E9KXL2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 17 其他Polymer 4 PDB declaration: 17-meric(17) Consistent with protein copy count Chain a; UniProt 325–744 Chain b; UniProt 325–744 Chain c; UniProt 325–744 Chain d; UniProt 325–744 Chain e; UniProt 325–744 Fragment:UNP residues 325-744 EEEV-179 Heavy chain × 1 EEEV-179 Light chain × 1 E1 × 5 (W8RHT7) Capsid protein × 5 (Q88793) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

10 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E9KXL2_EEEV
Isoform
PDB entities 5
Chains and sequence ranges Author chain a; PDBConstruct 1–420; UniProt 325–744 Author chain b; PDBConstruct 1–420; UniProt 325–744 Author chain c; PDBConstruct 1–420; UniProt 325–744 Author chain d; PDBConstruct 1–420; UniProt 325–744 Author chain e; PDBConstruct 1–420; UniProt 325–744

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 9yax

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yax
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9yax
Deposition date deposition_date2025-09-16
Structure title titleLocalized reconstruction of the asymmetric unit of the low pH treated back neutralized SINV/EEEV in complex with Fab fragment of the antibody EEEV-179
Keywords keywords;Eastern Equine Encephalitis Virus, Cryo-EM, Single Particle Averaging, localized reconstruction, asymmetric unit, low pH back neutralization., VIRUS ;; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier71.70
Radius of gyration Rg (electron density) rg_electron71.22
Forward intensity I(0) i05145660000.00
Molecular weight molecular_weight588170.0 kDa
Excluded volume excluded_volume727910 ų
Envelope volume envelope_volume1409000 ų
Hydration-shell volume shell_volume164510 ų
Envelope diameter envelope_diameter240.9
Shell Rg shell_rg74.10
Envelope Rg envelope_rg67.33
Shape Rg shape_rg71.17
Total Rg total_rg71.45
Total atoms total_atoms41372
Residues n_residues5533
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 dmax242.3
Rg (real space) rg_real71.43
Rg uncertainty (real space) rg_real_error2.75
I(0) (real space) i0_real5.1460e+09
I(0) uncertainty (real space) i0_real_error1.1870e+08
Rg (reciprocal space) rg_reciprocal72.48
I(0) (reciprocal space) i0_reciprocal5156000000.0000
Solution quality estimate total_estimate0.8765
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary99.1
Skewness Skewness skewness0.038
Kurtosis Kurtosis kurtosis-0.583
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha251700000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.893

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)