6mw9

CryoEM structure of chimeric Eastern Equine Encephalitis Virus with Fab of EEEV-3 antibody

Method: ELECTRON MICROSCOPY Dmax: 235.3 Å Quality: GOOD

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

E1

Eastern equine encephalitis virus

UniProt E9KXM2

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 × 960 PDB declaration: 960-meric(960) Consistent with protein copy count Chain A; UniProt 802–1242 Chain E; UniProt 802–1242 Chain I; UniProt 802–1242 Chain M; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 240 (E9KXL2) EEEV-3 antibody heavy chain × 240 EEEV-3 antibody light chain × 240 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 802–1242 Chain E; UniProt 802–1242 Chain I; UniProt 802–1242 Chain M; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 4 (E9KXL2) EEEV-3 antibody heavy chain × 4 EEEV-3 antibody light chain × 4 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
3 Protein heterocomplex Heteromer Protein × 80 PDB declaration: 80-meric(80) Consistent with protein copy count Chain A; UniProt 802–1242 Chain E; UniProt 802–1242 Chain I; UniProt 802–1242 Chain M; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 20 (E9KXL2) EEEV-3 antibody heavy chain × 20 EEEV-3 antibody light chain × 20 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
4 Protein heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain A; UniProt 802–1242 Chain E; UniProt 802–1242 Chain I; UniProt 802–1242 Chain M; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 24 (E9KXL2) EEEV-3 antibody heavy chain × 24 EEEV-3 antibody light chain × 24 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
5 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 802–1242 Chain E; UniProt 802–1242 Chain I; UniProt 802–1242 Chain M; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 4 (E9KXL2) EEEV-3 antibody heavy chain × 4 EEEV-3 antibody light chain × 4 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 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.

9 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E9KXM2_EEEV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–441; UniProt 802–1242 Author chain E; PDBConstruct 1–441; UniProt 802–1242 Author chain I; PDBConstruct 1–441; UniProt 802–1242 Author chain M; PDBConstruct 1–441; UniProt 802–1242

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 Protein heterocomplex Heteromer Protein × 960 PDB declaration: 960-meric(960) Consistent with protein copy count Chain B; UniProt 325–744 Chain F; UniProt 325–744 Chain J; UniProt 325–744 Chain N; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 240 (E9KXM2) EEEV-3 antibody heavy chain × 240 EEEV-3 antibody light chain × 240 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain B; UniProt 325–744 Chain F; UniProt 325–744 Chain J; UniProt 325–744 Chain N; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 4 (E9KXM2) EEEV-3 antibody heavy chain × 4 EEEV-3 antibody light chain × 4 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
3 Protein heterocomplex Heteromer Protein × 80 PDB declaration: 80-meric(80) Consistent with protein copy count Chain B; UniProt 325–744 Chain F; UniProt 325–744 Chain J; UniProt 325–744 Chain N; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 20 (E9KXM2) EEEV-3 antibody heavy chain × 20 EEEV-3 antibody light chain × 20 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
4 Protein heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain B; UniProt 325–744 Chain F; UniProt 325–744 Chain J; UniProt 325–744 Chain N; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 24 (E9KXM2) EEEV-3 antibody heavy chain × 24 EEEV-3 antibody light chain × 24 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
5 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain B; UniProt 325–744 Chain F; UniProt 325–744 Chain J; UniProt 325–744 Chain N; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 4 (E9KXM2) EEEV-3 antibody heavy chain × 4 EEEV-3 antibody light chain × 4 (G0YP42) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 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 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E9KXL2_EEEV
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–420; UniProt 325–744 Author chain F; PDBConstruct 1–420; UniProt 325–744 Author chain J; PDBConstruct 1–420; UniProt 325–744 Author chain N; PDBConstruct 1–420; UniProt 325–744

EEEV-3 antibody light chain

OrganismNot specified

UniProt G0YP42

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 × 960 PDB declaration: 960-meric(960) Consistent with protein copy count Chain D; UniProt 117–233 Chain H; UniProt 117–233 Chain L; UniProt 117–233 Chain P; UniProt 117–233 Fragment:Fab E1 × 240 (E9KXM2) E2 × 240 (E9KXL2) EEEV-3 antibody heavy chain × 240 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain D; UniProt 117–233 Chain H; UniProt 117–233 Chain L; UniProt 117–233 Chain P; UniProt 117–233 Fragment:Fab E1 × 4 (E9KXM2) E2 × 4 (E9KXL2) EEEV-3 antibody heavy chain × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
3 Protein heterocomplex Heteromer Protein × 80 PDB declaration: 80-meric(80) Consistent with protein copy count Chain D; UniProt 117–233 Chain H; UniProt 117–233 Chain L; UniProt 117–233 Chain P; UniProt 117–233 Fragment:Fab E1 × 20 (E9KXM2) E2 × 20 (E9KXL2) EEEV-3 antibody heavy chain × 20 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
4 Protein heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain D; UniProt 117–233 Chain H; UniProt 117–233 Chain L; UniProt 117–233 Chain P; UniProt 117–233 Fragment:Fab E1 × 24 (E9KXM2) E2 × 24 (E9KXL2) EEEV-3 antibody heavy chain × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 Å
5 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain D; UniProt 117–233 Chain H; UniProt 117–233 Chain L; UniProt 117–233 Chain P; UniProt 117–233 Fragment:Fab E1 × 4 (E9KXM2) E2 × 4 (E9KXL2) EEEV-3 antibody heavy chain × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 7.30 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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0YP42_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 98–214; UniProt 117–233 Author chain H; PDBConstruct 98–214; UniProt 117–233 Author chain L; PDBConstruct 98–214; UniProt 117–233 Author chain P; PDBConstruct 98–214; UniProt 117–233

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 6mw9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mw9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mw9
Deposition date deposition_date2018-10-29
Structure title titleCryoEM structure of chimeric Eastern Equine Encephalitis Virus with Fab of EEEV-3 antibody
Keywords keywordsAlphavirus, EEEV, Eastern Equine Encephalitis Virus, Sindbis, Fab, 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_guinier69.54
Radius of gyration Rg (electron density) rg_electron69.71
Forward intensity I(0) i03673450000.00
Molecular weight molecular_weight504980.0 kDa
Excluded volume excluded_volume628830 ų
Envelope volume envelope_volume1024800 ų
Hydration-shell volume shell_volume127160 ų
Envelope diameter envelope_diameter252.1
Shell Rg shell_rg65.63
Envelope Rg envelope_rg68.16
Shape Rg shape_rg69.68
Total Rg total_rg69.72
Total atoms total_atoms35528
Residues n_residues4616
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 dmax235.3
Rg (real space) rg_real69.55
Rg uncertainty (real space) rg_real_error2.35
I(0) (real space) i0_real3.6730e+09
I(0) uncertainty (real space) i0_real_error8.0550e+07
Rg (reciprocal space) rg_reciprocal69.41
I(0) (reciprocal space) i0_reciprocal3672000000.0000
Solution quality estimate total_estimate0.8542
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary81.8
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha109500000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.615

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)