8rn0

Influenza polymerase A/H7N9-4M encapsidase plus 627(R) / human ANP32A (from "Influenza polymerase A/H7N9-4M replication complex" | Local refinement)

Method: ELECTRON MICROSCOPY Dmax: 141.9 Å Quality: GOOD

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

Polymerase basic protein 2

Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))

UniProt X5F427

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–759 Chain F; UniProt 1–759 Mutation:G74R Polymerase acidic protein × 1 (M9TI86) RNA-directed RNA polymerase catalytic subunit × 1 (S5ME50) 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 3.13 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.

19 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name X5F427_9INFA
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–759; UniProt 1–759 Author chain F; PDBConstruct 1–759; UniProt 1–759

Polymerase acidic protein

Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))

UniProt M9TI86

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–716 Mutation:E349K; R490I Polymerase basic protein 2 × 2 (X5F427) RNA-directed RNA polymerase catalytic subunit × 1 (S5ME50) 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 3.13 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.

21 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name M9TI86_9INFA
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–716; UniProt 1–716

RNA-directed RNA polymerase catalytic subunit

Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))

UniProt S5ME50

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–757 Mutation:K577G Polymerase basic protein 2 × 2 (X5F427) Polymerase acidic protein × 1 (M9TI86) 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 3.13 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S5ME50_9INFA
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–757; UniProt 1–757

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 1–249 Not recorded Polymerase basic protein 2 × 2 (X5F427) Polymerase acidic protein × 1 (M9TI86) RNA-directed RNA polymerase catalytic subunit × 1 (S5ME50) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.13 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 8rn0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rn0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rn0
Deposition date deposition_date2024-01-09
最后修订 last_revision2024-09-11
Structure title titleInfluenza polymerase A/H7N9-4M encapsidase plus 627(R) / human ANP32A (from "Influenza polymerase A/H7N9-4M replication complex" | 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_guinier43.33
Radius of gyration Rg (electron density) rg_electron42.70
Forward intensity I(0) i0965384000.00
Molecular weight molecular_weight255150.0 kDa
Excluded volume excluded_volume319140 ų
Envelope volume envelope_volume443930 ų
Hydration-shell volume shell_volume83966 ų
Envelope diameter envelope_diameter143.0
Shell Rg shell_rg50.05
Envelope Rg envelope_rg42.02
Shape Rg shape_rg42.69
Total Rg total_rg43.06
Total atoms total_atoms35794
Residues n_residues2239
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 dmax141.9
Rg (real space) rg_real43.17
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real9.6540e+08
I(0) uncertainty (real space) i0_real_error1.8040e+07
Rg (reciprocal space) rg_reciprocal43.33
I(0) (reciprocal space) i0_reciprocal965600000.0000
Solution quality estimate total_estimate0.8803
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.2
Skewness Skewness skewness0.237
Kurtosis Kurtosis kurtosis-0.374
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha124800000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.891

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)