6mx4

CryoEM structure of chimeric Eastern Equine Encephalitis Virus

Method: ELECTRON MICROSCOPY Dmax: 201.4 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 Other combination Heteromer Protein × 720 其他Polymer 240 PDB declaration: 720-meric(720) Consistent with protein copy count Chain A; UniProt 802–1242 Chain D; UniProt 802–1242 Chain G; UniProt 802–1242 Chain J; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 240 (E9KXL2) Capsid × 240 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 240 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 240 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
2 Other combination Heteromer Protein × 12 其他Polymer 4 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 802–1242 Chain D; UniProt 802–1242 Chain G; UniProt 802–1242 Chain J; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 4 (E9KXL2) Capsid × 4 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(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 HELIUM Resolution 4.40 Å
3 Other combination Heteromer Protein × 60 其他Polymer 20 PDB declaration: 60-meric(60) Consistent with protein copy count Chain A; UniProt 802–1242 Chain D; UniProt 802–1242 Chain G; UniProt 802–1242 Chain J; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 20 (E9KXL2) Capsid × 20 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
4 Other combination Heteromer Protein × 72 其他Polymer 24 PDB declaration: 72-meric(72) Consistent with protein copy count Chain A; UniProt 802–1242 Chain D; UniProt 802–1242 Chain G; UniProt 802–1242 Chain J; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 24 (E9KXL2) Capsid × 24 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 24 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
5 Other combination Heteromer Protein × 12 其他Polymer 4 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 802–1242 Chain D; UniProt 802–1242 Chain G; UniProt 802–1242 Chain J; UniProt 802–1242 Fragment:ectodomain (UNP residues 802-1242) E2 × 4 (E9KXL2) Capsid × 4 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(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 HELIUM Resolution 4.40 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 D; PDBConstruct 1–441; UniProt 802–1242 Author chain G; PDBConstruct 1–441; UniProt 802–1242 Author chain J; 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 Other combination Heteromer Protein × 720 其他Polymer 240 PDB declaration: 720-meric(720) Consistent with protein copy count Chain B; UniProt 325–744 Chain E; UniProt 325–744 Chain H; UniProt 325–744 Chain K; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 240 (E9KXM2) Capsid × 240 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 240 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 240 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
2 Other combination Heteromer Protein × 12 其他Polymer 4 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 325–744 Chain E; UniProt 325–744 Chain H; UniProt 325–744 Chain K; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 4 (E9KXM2) Capsid × 4 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(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 HELIUM Resolution 4.40 Å
3 Other combination Heteromer Protein × 60 其他Polymer 20 PDB declaration: 60-meric(60) Consistent with protein copy count Chain B; UniProt 325–744 Chain E; UniProt 325–744 Chain H; UniProt 325–744 Chain K; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 20 (E9KXM2) Capsid × 20 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
4 Other combination Heteromer Protein × 72 其他Polymer 24 PDB declaration: 72-meric(72) Consistent with protein copy count Chain B; UniProt 325–744 Chain E; UniProt 325–744 Chain H; UniProt 325–744 Chain K; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 24 (E9KXM2) Capsid × 24 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 24 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
5 Other combination Heteromer Protein × 12 其他Polymer 4 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 325–744 Chain E; UniProt 325–744 Chain H; UniProt 325–744 Chain K; UniProt 325–744 Fragment:ectodomain (UNP residues 325-744) E1 × 4 (E9KXM2) Capsid × 4 (P27284) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(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 HELIUM Resolution 4.40 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 E; PDBConstruct 1–420; UniProt 325–744 Author chain H; PDBConstruct 1–420; UniProt 325–744 Author chain K; PDBConstruct 1–420; UniProt 325–744

Capsid

Eastern equine encephalitis virus

UniProt P27284

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 × 720 其他Polymer 240 PDB declaration: 720-meric(720) Consistent with protein copy count Chain C; UniProt 1–260 Chain F; UniProt 1–260 Chain I; UniProt 1–260 Chain L; UniProt 1–260 Fragment:N-terminal domain (UNP residues 1-260) E1 × 240 (E9KXM2) E2 × 240 (E9KXL2) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 240 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 240 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
2 Other combination Heteromer Protein × 12 其他Polymer 4 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 1–260 Chain F; UniProt 1–260 Chain I; UniProt 1–260 Chain L; UniProt 1–260 Fragment:N-terminal domain (UNP residues 1-260) E1 × 4 (E9KXM2) E2 × 4 (E9KXL2) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(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 HELIUM Resolution 4.40 Å
3 Other combination Heteromer Protein × 60 其他Polymer 20 PDB declaration: 60-meric(60) Consistent with protein copy count Chain C; UniProt 1–260 Chain F; UniProt 1–260 Chain I; UniProt 1–260 Chain L; UniProt 1–260 Fragment:N-terminal domain (UNP residues 1-260) E1 × 20 (E9KXM2) E2 × 20 (E9KXL2) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
4 Other combination Heteromer Protein × 72 其他Polymer 24 PDB declaration: 72-meric(72) Consistent with protein copy count Chain C; UniProt 1–260 Chain F; UniProt 1–260 Chain I; UniProt 1–260 Chain L; UniProt 1–260 Fragment:N-terminal domain (UNP residues 1-260) E1 × 24 (E9KXM2) E2 × 24 (E9KXL2) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 24 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen HELIUM Resolution 4.40 Å
5 Other combination Heteromer Protein × 12 其他Polymer 4 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 1–260 Chain F; UniProt 1–260 Chain I; UniProt 1–260 Chain L; UniProt 1–260 Fragment:N-terminal domain (UNP residues 1-260) E1 × 4 (E9KXM2) E2 × 4 (E9KXL2) ;2-acetamido-2-deoxy-beta-D-glucopyranose-(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 HELIUM Resolution 4.40 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.

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

View Construct and Data Evidence
UniProt name POLS_EEEV3
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–260; UniProt 1–260 Author chain F; PDBConstruct 1–260; UniProt 1–260 Author chain I; PDBConstruct 1–260; UniProt 1–260 Author chain L; PDBConstruct 1–260; UniProt 1–260

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 6mx4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mx4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mx4
Deposition date deposition_date2018-10-30
Structure title titleCryoEM structure of chimeric Eastern Equine Encephalitis Virus
Keywords keywordsAlphavirus, EEEV, Eastern Equine Encephalitis Virus, Sindbis, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.13
Radius of gyration Rg (electron density) rg_electron62.67
Forward intensity I(0) i02853240000.00
Molecular weight molecular_weight447940.0 kDa
Excluded volume excluded_volume559570 ų
Envelope volume envelope_volume934170 ų
Hydration-shell volume shell_volume124090 ų
Envelope diameter envelope_diameter202.9
Shell Rg shell_rg66.20
Envelope Rg envelope_rg59.86
Shape Rg shape_rg62.61
Total Rg total_rg62.94
Total atoms total_atoms31491
Residues n_residues4039
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 dmax201.4
Rg (real space) rg_real62.85
Rg uncertainty (real space) rg_real_error1.67
I(0) (real space) i0_real2.8530e+09
I(0) uncertainty (real space) i0_real_error5.7590e+07
Rg (reciprocal space) rg_reciprocal63.32
I(0) (reciprocal space) i0_reciprocal2855000000.0000
Solution quality estimate total_estimate0.8337
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary80.6
Skewness Skewness skewness0.092
Kurtosis Kurtosis kurtosis-0.619
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha118100000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)