8sqn

CryoEM structure of Western equine encephalitis virus VLP in complex with the chimeric Du-D1-Mo-D2 MXRA8 receptor

Method: ELECTRON MICROSCOPY Dmax: 198.4 Å Quality: GOOD

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

E1 envelope glycoprotein

Western equine encephalitis virus

UniProt Q1W679

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 798–1235 Chain D; UniProt 321–735 Chain F; UniProt 798–1235 Chain H; UniProt 321–735 Chain J; UniProt 798–1235 Chain L; UniProt 321–735 Chain N; UniProt 798–1235 Chain P; UniProt 321–735 Fragment:UNP residues 798-1235 Fragment:UNP residues 321-735 DuD1MoD2 chimeric MXRA8 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.89 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 Q1W679_WEEV
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain B; PDBConstruct 1–438; UniProt 798–1235 Author chain F; PDBConstruct 1–438; UniProt 798–1235 Author chain J; PDBConstruct 1–438; UniProt 798–1235 Author chain N; PDBConstruct 1–438; UniProt 798–1235 Author chain D; PDBConstruct 1–415; UniProt 321–735 Author chain H; PDBConstruct 1–415; UniProt 321–735 Author chain L; PDBConstruct 1–415; UniProt 321–735 Author chain P; PDBConstruct 1–415; UniProt 321–735

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 8sqn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8sqn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8sqn
Deposition date deposition_date2023-05-04
Structure title titleCryoEM structure of Western equine encephalitis virus VLP in complex with the chimeric Du-D1-Mo-D2 MXRA8 receptor
Keywords keywords;WEEV, MXRA8, Receptor, Alphavirus, Avian, VLP, Structural Genomics, PSI-2, Protein Structure Initiative, Center for Structural Genomics of Infectious Diseases, CSGID, VIRAL PROTEIN-SIGNALING PROTEIN complex ;; VIRAL PROTEIN/SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.31
Radius of gyration Rg (electron density) rg_electron59.03
Forward intensity I(0) i02349400000.00
Molecular weight molecular_weight405260.0 kDa
Excluded volume excluded_volume506360 ų
Envelope volume envelope_volume835700 ų
Hydration-shell volume shell_volume117290 ų
Envelope diameter envelope_diameter203.3
Shell Rg shell_rg62.16
Envelope Rg envelope_rg57.77
Shape Rg shape_rg58.95
Total Rg total_rg59.40
Total atoms total_atoms56304
Residues n_residues3677
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 dmax198.4
Rg (real space) rg_real59.12
Rg uncertainty (real space) rg_real_error2.30
I(0) (real space) i0_real2.3490e+09
I(0) uncertainty (real space) i0_real_error5.5430e+07
Rg (reciprocal space) rg_reciprocal59.45
I(0) (reciprocal space) i0_reciprocal2351000000.0000
Solution quality estimate total_estimate0.8721
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.7
Skewness Skewness skewness0.216
Kurtosis Kurtosis kurtosis-0.383
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha126800000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.798

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)