9cyt

Cryo-EM structure of MRV outer shell

Method: ELECTRON MICROSCOPY Dmax: 203.4 Å Quality: REASONABLE

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

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain J; UniProt 1–1289 Not recorded Outer capsid protein mu-1N × 6 (P11078) Outer capsid protein sigma-3 × 3 (P03527) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 1
Chains and sequence ranges Author chain J; PDBConstruct 1–1289; UniProt 1–1289

Outer capsid protein mu-1N

OrganismNot specified

UniProt P11078

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–708 Chain B; UniProt 1–708 Chain D; UniProt 1–708 Chain E; UniProt 1–708 Chain F; UniProt 1–708 Chain H; UniProt 1–708 Not recorded Outer capsid protein lambda-2 × 1 (P11079) Outer capsid protein sigma-3 × 3 (P03527) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MU1_REOVD
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–708; UniProt 1–708 Author chain B; PDBConstruct 1–708; UniProt 1–708 Author chain D; PDBConstruct 1–708; UniProt 1–708 Author chain E; PDBConstruct 1–708; UniProt 1–708 Author chain F; PDBConstruct 1–708; UniProt 1–708 Author chain H; PDBConstruct 1–708; UniProt 1–708

Outer capsid protein sigma-3

OrganismNot specified

UniProt P03527

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–365 Chain I; UniProt 1–365 Chain L; UniProt 1–365 Not recorded Outer capsid protein lambda-2 × 1 (P11079) Outer capsid protein mu-1N × 6 (P11078) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 SIGM3_REOVD
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–365; UniProt 1–365 Author chain I; PDBConstruct 1–365; UniProt 1–365 Author chain L; PDBConstruct 1–365; UniProt 1–365

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 9cyt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cyt
Deposition date deposition_date2024-08-02
最后修订 last_revision2024-12-18
Structure title titleCryo-EM structure of MRV outer shell
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_guinier59.02
Radius of gyration Rg (electron density) rg_electron58.93
Forward intensity I(0) i03274020000.00
Molecular weight molecular_weight483320.0 kDa
Excluded volume excluded_volume605630 ų
Envelope volume envelope_volume875170 ų
Hydration-shell volume shell_volume123150 ų
Envelope diameter envelope_diameter207.0
Shell Rg shell_rg60.72
Envelope Rg envelope_rg58.97
Shape Rg shape_rg58.99
Total Rg total_rg58.75
Total atoms total_atoms33991
Residues n_residues4390
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 dmax203.4
Rg (real space) rg_real59.08
Rg uncertainty (real space) rg_real_error1.92
I(0) (real space) i0_real3.2740e+09
I(0) uncertainty (real space) i0_real_error7.1230e+07
Rg (reciprocal space) rg_reciprocal58.96
I(0) (reciprocal space) i0_reciprocal3273000000.0000
Solution quality estimate total_estimate0.6336
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.8
Skewness Skewness skewness0.384
Kurtosis Kurtosis kurtosis-0.269
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha275500000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 0.009; Positv: 1.000; Valcen: 0.998; Smooth: 0.733

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)