9cyx

Cryo-EM structure of MRV full core

Method: ELECTRON MICROSCOPY Dmax: 238.3 Å Quality: GOOD

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

Lambda 1

OrganismNot specified

UniProt F1ARN3

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–1275 Chain H; UniProt 1–1275 Chain I; UniProt 1–1275 Not recorded Outer capsid protein lambda-2 × 1 (P11079) Inner capsid protein sigma-2 × 2 (P03525) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F1ARN3_9REOV
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–1275; UniProt 1–1275 Author chain H; PDBConstruct 1–1275; UniProt 1–1275 Author chain I; PDBConstruct 1–1275; UniProt 1–1275

Outer capsid protein lambda-2

OrganismNot specified

UniProt P11079

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 2–1289 Not recorded Lambda 1 × 3 (F1ARN3) Inner capsid protein sigma-2 × 2 (P03525) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LMBD2_REOVD
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–1288; UniProt 2–1289

Inner capsid protein sigma-2

OrganismNot specified

UniProt P03525

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain Q; UniProt 2–418 Chain R; UniProt 2–418 Not recorded Lambda 1 × 3 (F1ARN3) Outer capsid protein lambda-2 × 1 (P11079) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

2 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIGM2_REOVD
Isoform
PDB entities 3
Chains and sequence ranges Author chain Q; PDBConstruct 1–417; UniProt 2–418 Author chain R; PDBConstruct 1–417; UniProt 2–418

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 9cyx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cyx
Deposition date deposition_date2024-08-02
Structure title titleCryo-EM structure of MRV full core
Keywords keywordsMammalian reovirus, outer shell, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.60
Radius of gyration Rg (electron density) rg_electron70.94
Forward intensity I(0) i03329190000.00
Molecular weight molecular_weight490220.0 kDa
Excluded volume excluded_volume613830 ų
Envelope volume envelope_volume951430 ų
Hydration-shell volume shell_volume114510 ų
Envelope diameter envelope_diameter255.6
Shell Rg shell_rg68.05
Envelope Rg envelope_rg70.50
Shape Rg shape_rg70.99
Total Rg total_rg70.71
Total atoms total_atoms34537
Residues n_residues4377
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 dmax238.3
Rg (real space) rg_real70.78
Rg uncertainty (real space) rg_real_error3.63
I(0) (real space) i0_real3.3290e+09
I(0) uncertainty (real space) i0_real_error8.7620e+07
Rg (reciprocal space) rg_reciprocal69.83
I(0) (reciprocal space) i0_reciprocal3323000000.0000
Solution quality estimate total_estimate0.8475
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.0
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.543
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha169700000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.379

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)