9cyy

Cryo-EM structure of MRV virion

Method: ELECTRON MICROSCOPY Dmax: 289.6 Å Quality: EXCELLENT

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

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain 0; UniProt 1–418 Chain C; UniProt 1–418 Not recorded Outer capsid protein mu-1 × 6 (P11078) Outer capsid protein sigma-3 × 3 (P03527) Outer capsid protein lambda-2 × 1 (P11079) Lambda 1 × 15 (F1ARN3) Mu2 × 1 (Q6EDZ8) RNA-directed RNA polymerase × 1 (A0A0B5CSU4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 1
Chains and sequence ranges Author chain 0; PDBConstruct 1–418; UniProt 1–418 Author chain C; PDBConstruct 1–418; UniProt 1–418

Outer capsid protein mu-1

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 × 29 PDB declaration: 29-meric(29) 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 Inner capsid protein sigma-2 × 2 (P03525) Outer capsid protein sigma-3 × 3 (P03527) Outer capsid protein lambda-2 × 1 (P11079) Lambda 1 × 15 (F1ARN3) Mu2 × 1 (Q6EDZ8) RNA-directed RNA polymerase × 1 (A0A0B5CSU4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain G; UniProt 1–365 Chain I; UniProt 1–365 Chain L; UniProt 1–365 Not recorded Inner capsid protein sigma-2 × 2 (P03525) Outer capsid protein mu-1 × 6 (P11078) Outer capsid protein lambda-2 × 1 (P11079) Lambda 1 × 15 (F1ARN3) Mu2 × 1 (Q6EDZ8) RNA-directed RNA polymerase × 1 (A0A0B5CSU4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain J; UniProt 1–1289 Not recorded Inner capsid protein sigma-2 × 2 (P03525) Outer capsid protein mu-1 × 6 (P11078) Outer capsid protein sigma-3 × 3 (P03527) Lambda 1 × 15 (F1ARN3) Mu2 × 1 (Q6EDZ8) RNA-directed RNA polymerase × 1 (A0A0B5CSU4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 4
Chains and sequence ranges Author chain J; PDBConstruct 1–1289; UniProt 1–1289

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain K; UniProt 1–1275 Chain M; UniProt 1–1275 Chain Y; UniProt 1–1275 Chain Z; UniProt 1–1275 Chain a; UniProt 1–1275 Chain b; UniProt 1–1275 Chain c; UniProt 1–1275 Chain d; UniProt 1–1275 Chain e; UniProt 1–1275 Chain f; UniProt 1–1275 Chain g; UniProt 1–1275 Chain h; UniProt 1–1275 Chain i; UniProt 1–1275 Chain k; UniProt 1–1275 Chain m; UniProt 1–1275 Not recorded Inner capsid protein sigma-2 × 2 (P03525) Outer capsid protein mu-1 × 6 (P11078) Outer capsid protein sigma-3 × 3 (P03527) Outer capsid protein lambda-2 × 1 (P11079) Mu2 × 1 (Q6EDZ8) RNA-directed RNA polymerase × 1 (A0A0B5CSU4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 5
Chains and sequence ranges Author chain K; PDBConstruct 1–1275; UniProt 1–1275 Author chain M; PDBConstruct 1–1275; UniProt 1–1275 Author chain Y; PDBConstruct 1–1275; UniProt 1–1275 Author chain Z; PDBConstruct 1–1275; UniProt 1–1275 Author chain a; PDBConstruct 1–1275; UniProt 1–1275 Author chain b; PDBConstruct 1–1275; UniProt 1–1275 Author chain c; PDBConstruct 1–1275; UniProt 1–1275 Author chain d; PDBConstruct 1–1275; UniProt 1–1275 Author chain e; PDBConstruct 1–1275; UniProt 1–1275 Author chain f; PDBConstruct 1–1275; UniProt 1–1275 Author chain g; PDBConstruct 1–1275; UniProt 1–1275 Author chain h; PDBConstruct 1–1275; UniProt 1–1275 Author chain i; PDBConstruct 1–1275; UniProt 1–1275 Author chain k; PDBConstruct 1–1275; UniProt 1–1275 Author chain m; PDBConstruct 1–1275; UniProt 1–1275

Mu2

OrganismNot specified

UniProt Q6EDZ8

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain V; UniProt 1–736 Not recorded Inner capsid protein sigma-2 × 2 (P03525) Outer capsid protein mu-1 × 6 (P11078) Outer capsid protein sigma-3 × 3 (P03527) Outer capsid protein lambda-2 × 1 (P11079) Lambda 1 × 15 (F1ARN3) RNA-directed RNA polymerase × 1 (A0A0B5CSU4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 Q6EDZ8_9REOV
Isoform
PDB entities 6
Chains and sequence ranges Author chain V; PDBConstruct 1–736; UniProt 1–736

RNA-directed RNA polymerase

OrganismNot specified

UniProt A0A0B5CSU4

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 × 29 PDB declaration: 29-meric(29) Consistent with protein copy count Chain W; UniProt 1–1267 Not recorded Inner capsid protein sigma-2 × 2 (P03525) Outer capsid protein mu-1 × 6 (P11078) Outer capsid protein sigma-3 × 3 (P03527) Outer capsid protein lambda-2 × 1 (P11079) Lambda 1 × 15 (F1ARN3) Mu2 × 1 (Q6EDZ8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 A0A0B5CSU4_9REOV
Isoform
PDB entities 7
Chains and sequence ranges Author chain W; PDBConstruct 1–1267; UniProt 1–1267

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 9cyy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cyy
Deposition date deposition_date2024-08-03
最后修订 last_revision2024-12-18
Structure title titleCryo-EM structure of MRV virion
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_guinier
Radius of gyration Rg (electron density) rg_electron109.60
Forward intensity I(0) i057668900000.00
Molecular weight molecular_weight2069400.0 kDa
Excluded volume excluded_volume2594300 ų
Envelope volume envelope_volume4079300 ų
Hydration-shell volume shell_volume315370 ų
Envelope diameter envelope_diameter395.2
Shell Rg shell_rg96.30
Envelope Rg envelope_rg108.40
Shape Rg shape_rg109.70
Total Rg total_rg109.40
Total atoms total_atoms145604
Residues n_residues18547
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 dmax289.6
Rg (real space) rg_real105.60
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real5.5180e+10
I(0) uncertainty (real space) i0_real_error1.0660e+09
Rg (reciprocal space) rg_reciprocal108.10
I(0) (reciprocal space) i0_reciprocal57270000000.0000
Solution quality estimate total_estimate0.9029
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary124.1
Skewness Skewness skewness0.167
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.0700 −1
Current regularization parameter α current_alpha0.9891
Highest regularization parameter α highest_alpha1442000000.0000
Real-space data points n_real_points15
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.995; Stabil: 0.972; Sysdev: 1.000; Positv: 1.000; Valcen: 0.839; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)