9eau

RRV DKTA VLP in complex with VLDLR-LBD-Fc

Method: ELECTRON MICROSCOPY Dmax: 210.4 Å Quality: GOOD

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

Spike glycoprotein E1

Ross river virus (STRAIN T48)

UniProt C9DZM3

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain A; UniProt 817–1254 Chain E; UniProt 817–1254 Chain I; UniProt 817–1254 Chain M; UniProt 817–1254 Mutation:K327D, D345K, E348T, D349A Spike glycoprotein E2 × 4 (Q076B2) Capsid protein × 4 (P08491) Very low-density lipoprotein receptor × 2 (P98155) CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name C9DZM3_9VIRU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–438; UniProt 817–1254 Author chain E; PDBConstruct 1–438; UniProt 817–1254 Author chain I; PDBConstruct 1–438; UniProt 817–1254 Author chain M; PDBConstruct 1–438; UniProt 817–1254

Spike glycoprotein E2

Ross river virus (STRAIN T48)

UniProt Q076B2

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain B; UniProt 335–753 Chain F; UniProt 335–753 Chain J; UniProt 335–753 Chain N; UniProt 335–753 Not recorded Spike glycoprotein E1 × 4 (C9DZM3) Capsid protein × 4 (P08491) Very low-density lipoprotein receptor × 2 (P98155) CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q076B2_9VIRU
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–419; UniProt 335–753 Author chain F; PDBConstruct 1–419; UniProt 335–753 Author chain J; PDBConstruct 1–419; UniProt 335–753 Author chain N; PDBConstruct 1–419; UniProt 335–753

Capsid protein

Ross river virus (STRAIN T48)

UniProt P08491

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain C; UniProt 113–270 Chain G; UniProt 113–270 Chain K; UniProt 113–270 Chain O; UniProt 113–270 Not recorded Spike glycoprotein E1 × 4 (C9DZM3) Spike glycoprotein E2 × 4 (Q076B2) Very low-density lipoprotein receptor × 2 (P98155) CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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_RRVT
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–158; UniProt 113–270 Author chain G; PDBConstruct 1–158; UniProt 113–270 Author chain K; PDBConstruct 1–158; UniProt 113–270 Author chain O; PDBConstruct 1–158; UniProt 113–270

Very low-density lipoprotein receptor

Homo sapiens

UniProt P98155

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain Y; UniProt 111–149 Chain Z; UniProt 111–149 Not recorded Spike glycoprotein E1 × 4 (C9DZM3) Spike glycoprotein E2 × 4 (Q076B2) Capsid protein × 4 (P08491) CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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.

25 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VLDLR_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain Y; PDBConstruct 1–39; UniProt 111–149 Author chain Z; PDBConstruct 1–39; UniProt 111–149

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 9eau

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9eau
Deposition date deposition_date2024-11-11
Structure title titleRRV DKTA VLP in complex with VLDLR-LBD-Fc
Keywords keywordsAlphavirus Receptor, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier66.19
Radius of gyration Rg (electron density) rg_electron65.44
Forward intensity I(0) i02968520000.00
Molecular weight molecular_weight452810.0 kDa
Excluded volume excluded_volume563740 ų
Envelope volume envelope_volume985370 ų
Hydration-shell volume shell_volume126440 ų
Envelope diameter envelope_diameter210.7
Shell Rg shell_rg67.78
Envelope Rg envelope_rg62.10
Shape Rg shape_rg65.35
Total Rg total_rg65.77
Total atoms total_atoms31779
Residues n_residues4138
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 dmax210.4
Rg (real space) rg_real65.83
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real2.9690e+09
I(0) uncertainty (real space) i0_real_error5.1300e+07
Rg (reciprocal space) rg_reciprocal66.44
I(0) (reciprocal space) i0_reciprocal2972000000.0000
Solution quality estimate total_estimate0.8326
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary87.7
Skewness Skewness skewness0.075
Kurtosis Kurtosis kurtosis-0.606
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha130300000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; 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)