8rms

Influenza polymerase A/H7N9-4M replicase minus 627(R) (from "Influenza polymerase A/H7N9-4M replication complex" | Local refinement)

Method: ELECTRON MICROSCOPY Dmax: 132.7 Å Quality: GOOD

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–716 Mutation:E349K; R490I RNA-directed RNA polymerase catalytic subunit × 1 (S5ME50) Polymerase basic protein 2 × 1 (X5F427) MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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 1
Chains and sequence ranges Author chain A; 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–757 Mutation:K577G Polymerase acidic protein × 1 (M9TI86) Polymerase basic protein 2 × 1 (X5F427) MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–757; UniProt 1–757

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–759 Mutation:G74R Polymerase acidic protein × 1 (M9TI86) RNA-directed RNA polymerase catalytic subunit × 1 (S5ME50) MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.21 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–759; UniProt 1–759

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 8rms

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8rms
Deposition date deposition_date2024-01-08
最后修订 last_revision2024-09-11
Structure title titleInfluenza polymerase A/H7N9-4M replicase minus 627(R) (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_guinier39.96
Radius of gyration Rg (electron density) rg_electron39.28
Forward intensity I(0) i0811367000.00
Molecular weight molecular_weight231010.0 kDa
Excluded volume excluded_volume288580 ų
Envelope volume envelope_volume387380 ų
Hydration-shell volume shell_volume78854 ų
Envelope diameter envelope_diameter140.4
Shell Rg shell_rg47.47
Envelope Rg envelope_rg38.63
Shape Rg shape_rg39.28
Total Rg total_rg39.71
Total atoms total_atoms32434
Residues n_residues2019
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 dmax132.7
Rg (real space) rg_real39.68
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real8.1140e+08
I(0) uncertainty (real space) i0_real_error1.4580e+07
Rg (reciprocal space) rg_reciprocal39.85
I(0) (reciprocal space) i0_reciprocal811500000.0000
Solution quality estimate total_estimate0.8708
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.1
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.311
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha274600000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.783; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)