8rnc

Influenza B polymerase, replication complex, an asymmetric polymerase dimer bound to human ANP32A (from "Influenza B polymerase apo-trimer" | Local refinement)

Method: ELECTRON MICROSCOPY Dmax: 196.0 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–726 Chain D; UniProt 1–726 Chain X; UniProt 1–726 Not recorded RNA-directed RNA polymerase catalytic subunit × 3 (Q5V8Y6) Polymerase basic protein 2 × 2 (Q5V8X3) Acidic leucine-rich nuclear phosphoprotein 32 family member A × 1 (P39687) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 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 Author chain D; PDBConstruct 1–726; UniProt 1–726 Author chain X; 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 1–752 Chain E; UniProt 1–752 Chain Y; UniProt 1–752 Not recorded Polymerase acidic protein × 3 (Q5V8Z9) Polymerase basic protein 2 × 2 (Q5V8X3) Acidic leucine-rich nuclear phosphoprotein 32 family member A × 1 (P39687) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 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 Author chain E; PDBConstruct 1–752; UniProt 1–752 Author chain Y; 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 1–770 Chain F; UniProt 1–770 Not recorded Polymerase acidic protein × 3 (Q5V8Z9) RNA-directed RNA polymerase catalytic subunit × 3 (Q5V8Y6) Acidic leucine-rich nuclear phosphoprotein 32 family member A × 1 (P39687) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 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 Author chain F; PDBConstruct 1–770; UniProt 1–770

Acidic leucine-rich nuclear phosphoprotein 32 family member A

Homo sapiens

UniProt P39687

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain G; UniProt 1–249 Not recorded Polymerase acidic protein × 3 (Q5V8Z9) RNA-directed RNA polymerase catalytic subunit × 3 (Q5V8Y6) Polymerase basic protein 2 × 2 (Q5V8X3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 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.

8 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AN32A_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 27–275; UniProt 1–249

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 8rnc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8rnc
Deposition date deposition_date2024-01-09
最后修订 last_revision2024-09-11
Structure title titleInfluenza B polymerase, replication complex, an asymmetric polymerase dimer bound to human ANP32A (from "Influenza B polymerase apo-trimer" | 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_guinier57.81
Radius of gyration Rg (electron density) rg_electron57.68
Forward intensity I(0) i03607130000.00
Molecular weight molecular_weight508470.0 kDa
Excluded volume excluded_volume637990 ų
Envelope volume envelope_volume913810 ų
Hydration-shell volume shell_volume128810 ų
Envelope diameter envelope_diameter203.0
Shell Rg shell_rg62.61
Envelope Rg envelope_rg56.72
Shape Rg shape_rg57.68
Total Rg total_rg57.78
Total atoms total_atoms71539
Residues n_residues4477
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 dmax196.0
Rg (real space) rg_real57.81
Rg uncertainty (real space) rg_real_error1.76
I(0) (real space) i0_real3.6070e+09
I(0) uncertainty (real space) i0_real_error7.1020e+07
Rg (reciprocal space) rg_reciprocal57.78
I(0) (reciprocal space) i0_reciprocal3607000000.0000
Solution quality estimate total_estimate0.8623
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.3
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha408400000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.722

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)