7elh

In situ structure of transcriptional enzyme complex and capsid shell protein of mammalian reovirus at initiation state

Method: ELECTRON MICROSCOPY Dmax: 261.8 Å Quality: EXCELLENT

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

Minor core protein 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–RNA Heteromer Protein × 17 RNA 9 PDB declaration: 26-meric(26) Consistent with all polymer counts Chain A; UniProt 1–736 Not recorded RNA-directed RNA polymerase × 1 (A0A0B5CSU4) transcript RNA × 1 Lambda 1 × 10 (F1ARN3) Lambda 1 × 5 (F1ARN3) RNA (60-MER) × 8 PO4 PHOSPHATE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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 1
Chains and sequence ranges Author chain A; 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–RNA Heteromer Protein × 17 RNA 9 PDB declaration: 26-meric(26) Consistent with all polymer counts Chain B; UniProt 1–1267 Not recorded Minor core protein mu2 × 1 (Q6EDZ8) transcript RNA × 1 Lambda 1 × 10 (F1ARN3) Lambda 1 × 5 (F1ARN3) RNA (60-MER) × 8 PO4 PHOSPHATE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1267; UniProt 1–1267

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–RNA Heteromer Protein × 17 RNA 9 PDB declaration: 26-meric(26) Consistent with all polymer counts Chain D; UniProt 181–1275 Chain E; UniProt 181–1275 Chain F; UniProt 181–1275 Chain G; UniProt 181–1275 Chain H; UniProt 181–1275 Chain I; UniProt 181–1275 Chain J; UniProt 181–1275 Chain K; UniProt 181–1275 Chain L; UniProt 181–1275 Chain M; UniProt 181–1275 Chain e; UniProt 1–180 Chain g; UniProt 1–180 Chain i; UniProt 1–180 Chain k; UniProt 1–180 Chain m; UniProt 1–180 Not recorded Minor core protein mu2 × 1 (Q6EDZ8) RNA-directed RNA polymerase × 1 (A0A0B5CSU4) transcript RNA × 1 RNA (60-MER) × 8 PO4 PHOSPHATE ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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 4, 5
Chains and sequence ranges Author chain D; PDBConstruct 1–1095; UniProt 181–1275 Author chain E; PDBConstruct 1–1095; UniProt 181–1275 Author chain F; PDBConstruct 1–1095; UniProt 181–1275 Author chain G; PDBConstruct 1–1095; UniProt 181–1275 Author chain H; PDBConstruct 1–1095; UniProt 181–1275 Author chain I; PDBConstruct 1–1095; UniProt 181–1275 Author chain J; PDBConstruct 1–1095; UniProt 181–1275 Author chain K; PDBConstruct 1–1095; UniProt 181–1275 Author chain L; PDBConstruct 1–1095; UniProt 181–1275 Author chain M; PDBConstruct 1–1095; UniProt 181–1275 Author chain e; PDBConstruct 1–180; UniProt 1–180 Author chain g; PDBConstruct 1–180; UniProt 1–180 Author chain i; PDBConstruct 1–180; UniProt 1–180 Author chain k; PDBConstruct 1–180; UniProt 1–180 Author chain m; PDBConstruct 1–180; UniProt 1–180

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 7elh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7elh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7elh
Deposition date deposition_date2021-04-11
Structure title titleIn situ structure of transcriptional enzyme complex and capsid shell protein of mammalian reovirus at initiation state
Keywords keywordsasymmetric, mu2, lambda3, lambda1, VIRUS, VIRAL PROTEIN-TRANSFERASE-RNA complex; VIRAL PROTEIN/TRANSFERASE/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier97.76
Radius of gyration Rg (electron density) rg_electron98.73
Forward intensity I(0) i037670700000.00
Molecular weight molecular_weight1596600.0 kDa
Excluded volume excluded_volume1971400 ų
Envelope volume envelope_volume3145400 ų
Hydration-shell volume shell_volume269160 ų
Envelope diameter envelope_diameter327.9
Shell Rg shell_rg88.15
Envelope Rg envelope_rg97.09
Shape Rg shape_rg98.84
Total Rg total_rg98.27
Total atoms total_atoms114995
Residues n_residues13688
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 dmax261.8
Rg (real space) rg_real94.10
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real3.6030e+10
I(0) uncertainty (real space) i0_real_error6.7120e+08
Rg (reciprocal space) rg_reciprocal96.23
I(0) (reciprocal space) i0_reciprocal37470000000.0000
Solution quality estimate total_estimate0.9134
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary114.6
Skewness Skewness skewness0.212
Kurtosis Kurtosis kurtosis-0.671
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha1.0600
Highest regularization parameter α highest_alpha1550000000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.999; Stabil: 0.962; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; 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)