9yb2

Localized reconstruction of the asymmetric unit of SINV/EEEV at 40C sample.

Method: ELECTRON MICROSCOPY Dmax: 209.6 Å Quality: GOOD

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

E1 glycoprotein

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 × 12 其他Polymer 4 PDB declaration: 12-meric(12) 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 Not recorded Capsid protein × 4 (Q88793) E2 glycoprotein × 4 (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 × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 1
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

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 × 12 其他Polymer 4 PDB declaration: 12-meric(12) 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 Fragment:Capsid c-terminal domain E1 glycoprotein × 4 (W8RHT7) E2 glycoprotein × 4 (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 × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 2
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

E2 glycoprotein

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 × 12 其他Polymer 4 PDB declaration: 12-meric(12) 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 Fragment:UNP residues 325-744 E1 glycoprotein × 4 (W8RHT7) Capsid protein × 4 (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 × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 3
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

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 9yb2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yb2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yb2
Deposition date deposition_date2025-09-16
Structure title titleLocalized reconstruction of the asymmetric unit of SINV/EEEV at 40C sample.
Keywords keywordsEastern Equine Encephalitis Virus, Cryo-EM, Single Particle Averaging, localized reconstruction, asymmetric unit, 40C., VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.95
Radius of gyration Rg (electron density) rg_electron65.46
Forward intensity I(0) i02890700000.00
Molecular weight molecular_weight450660.0 kDa
Excluded volume excluded_volume562860 ų
Envelope volume envelope_volume1009300 ų
Hydration-shell volume shell_volume129050 ų
Envelope diameter envelope_diameter213.0
Shell Rg shell_rg68.05
Envelope Rg envelope_rg62.26
Shape Rg shape_rg65.40
Total Rg total_rg65.72
Total atoms total_atoms31679
Residues n_residues4067
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 dmax209.6
Rg (real space) rg_real65.63
Rg uncertainty (real space) rg_real_error1.54
I(0) (real space) i0_real2.8910e+09
I(0) uncertainty (real space) i0_real_error5.0050e+07
Rg (reciprocal space) rg_reciprocal66.17
I(0) (reciprocal space) i0_reciprocal2893000000.0000
Solution quality estimate total_estimate0.8689
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary87.3
Skewness Skewness skewness0.093
Kurtosis Kurtosis kurtosis-0.616
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha136800000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.444

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)