8rn6

Pseudo-symmetrical influenza B polymerase apo-dimer, ENDO(E) moiety (from "Influenza B polymerase pseudo-symmetrical dimer" | Local refinement)

Method: ELECTRON MICROSCOPY Dmax: 117.0 Å Quality: GOOD

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

Polymerase acidic protein

Influenza B virus (B/Memphis/13/2003)

UniProt Q5V8Z9

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–726 Not recorded RNA-directed RNA polymerase catalytic subunit × 1 (Q5V8Y6) Polymerase basic protein 2 × 1 (Q5V8X3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.82 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.

34 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5V8Z9_9INFB
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–726; UniProt 1–726

RNA-directed RNA polymerase catalytic subunit

Influenza B virus (B/Memphis/13/2003)

UniProt Q5V8Y6

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–752 Not recorded Polymerase acidic protein × 1 (Q5V8Z9) Polymerase basic protein 2 × 1 (Q5V8X3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.82 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.

30 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5V8Y6_9INFB
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–752; UniProt 1–752

Polymerase basic protein 2

Influenza B virus (B/Memphis/13/2003)

UniProt Q5V8X3

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–770 Not recorded Polymerase acidic protein × 1 (Q5V8Z9) RNA-directed RNA polymerase catalytic subunit × 1 (Q5V8Y6) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.82 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.

31 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5V8X3_9INFB
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–770; UniProt 1–770

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 8rn6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rn6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rn6
Deposition date deposition_date2024-01-09
最后修订 last_revision2024-09-11
Structure title titlePseudo-symmetrical influenza B polymerase apo-dimer, ENDO(E) moiety (from "Influenza B polymerase pseudo-symmetrical dimer" | Local refinement)
Keywords keywordsViral polymerase, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.66
Radius of gyration Rg (electron density) rg_electron35.85
Forward intensity I(0) i0408845000.00
Molecular weight molecular_weight164560.0 kDa
Excluded volume excluded_volume206400 ų
Envelope volume envelope_volume273670 ų
Hydration-shell volume shell_volume61241 ų
Envelope diameter envelope_diameter127.0
Shell Rg shell_rg44.07
Envelope Rg envelope_rg35.33
Shape Rg shape_rg35.87
Total Rg total_rg36.33
Total atoms total_atoms23047
Residues n_residues1455
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 dmax117.0
Rg (real space) rg_real36.44
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real4.0880e+08
I(0) uncertainty (real space) i0_real_error5.9840e+06
Rg (reciprocal space) rg_reciprocal36.58
I(0) (reciprocal space) i0_reciprocal408900000.0000
Solution quality estimate total_estimate0.8852
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.0
Skewness Skewness skewness0.143
Kurtosis Kurtosis kurtosis-0.357
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha88320000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.920

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)