9ryc

Structure of human 1918 influenza A polymerase heterotrimer in complex with WSN NEP.

Method: ELECTRON MICROSCOPY Dmax: 151.2 Å Quality: GOOD

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

Polymerase acidic protein

Influenza A virus (A/Brevig Mission/1/1918(H1N1))

UniProt Q3HM39

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–716 Not recorded RNA-directed RNA polymerase catalytic subunit × 1 (Q3HM40) Polymerase basic protein 2 × 1 (Q3HM41) Nuclear export protein × 1 (Q77IX1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.93 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PA_I18A0
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–716; UniProt 1–716

RNA-directed RNA polymerase catalytic subunit

Influenza A virus (A/Brevig Mission/1/1918(H1N1))

UniProt Q3HM40

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–757 Not recorded Polymerase acidic protein × 1 (Q3HM39) Polymerase basic protein 2 × 1 (Q3HM41) Nuclear export protein × 1 (Q77IX1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.93 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RDRP_I18A0
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–757; UniProt 1–757

Polymerase basic protein 2

Influenza A virus (A/Brevig Mission/1/1918(H1N1))

UniProt Q3HM41

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–759 Not recorded Polymerase acidic protein × 1 (Q3HM39) RNA-directed RNA polymerase catalytic subunit × 1 (Q3HM40) Nuclear export protein × 1 (Q77IX1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.93 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PB2_I18A0
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–759; UniProt 1–759

Nuclear export protein

Influenza A virus (A/Brevig Mission/1/1918(H1N1))

UniProt Q77IX1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–121 Not recorded Polymerase acidic protein × 1 (Q3HM39) RNA-directed RNA polymerase catalytic subunit × 1 (Q3HM40) Polymerase basic protein 2 × 1 (Q3HM41) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.93 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 NEP_I18A0
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 10–130; UniProt 1–121

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 9ryc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ryc
Deposition date deposition_date2025-07-15
Structure title titleStructure of human 1918 influenza A polymerase heterotrimer in complex with WSN NEP.
Keywords keywordsinfluenza virus, nuclear export, NEP, NS2, 1918 polymerase, spanish Flu, viral polymerase, cryo-EM, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.91
Radius of gyration Rg (electron density) rg_electron40.54
Forward intensity I(0) i0644425000.00
Molecular weight molecular_weight206760.0 kDa
Excluded volume excluded_volume258610 ų
Envelope volume envelope_volume346640 ų
Hydration-shell volume shell_volume70999 ų
Envelope diameter envelope_diameter160.0
Shell Rg shell_rg46.47
Envelope Rg envelope_rg40.13
Shape Rg shape_rg40.56
Total Rg total_rg40.79
Total atoms total_atoms28022
Residues n_residues1797
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 dmax151.2
Rg (real space) rg_real40.92
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real6.4440e+08
I(0) uncertainty (real space) i0_real_error9.3690e+06
Rg (reciprocal space) rg_reciprocal40.91
I(0) (reciprocal space) i0_reciprocal644400000.0000
Solution quality estimate total_estimate0.8233
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.4
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis0.231
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha123400000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.590; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)