6z5l

Helical reconstruction of influenza A virus M1 in complex with nucleic acid.

Method: ELECTRON MICROSCOPY Dmax: 75.0 Å Quality: EXCELLENT

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

Matrix protein 1

Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)

UniProt P03485

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 homooligomer Homooligomer Protein × 80 PDB declaration: 80-meric(80) Consistent with protein copy count Chain A; UniProt 1–252 Mutation:R134K No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 10 cryo-EM vitrification conditions:Cryogen ETHANE;sample was applied 3 times each with 30s adsorption time Resolution 3.80 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.

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

View Construct and Data Evidence
UniProt name M1_I34A1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–252; UniProt 1–252

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 6z5l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6z5l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6z5l
Deposition date deposition_date2020-05-26
Structure title titleHelical reconstruction of influenza A virus M1 in complex with nucleic acid.
Keywords keywordsM1, Matrix protein, Influenza virus, Assembly, ribonucleoprotein complex, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier23.47
Radius of gyration Rg (electron density) rg_electron22.53
Forward intensity I(0) i014102900.00
Molecular weight molecular_weight27724.0 kDa
Excluded volume excluded_volume34577 ų
Envelope volume envelope_volume45017 ų
Hydration-shell volume shell_volume17670 ų
Envelope diameter envelope_diameter78.0
Shell Rg shell_rg27.78
Envelope Rg envelope_rg22.37
Shape Rg shape_rg22.51
Total Rg total_rg23.30
Total atoms total_atoms1936
Residues n_residues251
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 dmax75.0
Rg (real space) rg_real23.50
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.4100e+07
I(0) uncertainty (real space) i0_real_error1.7760e+05
Rg (reciprocal space) rg_reciprocal23.50
I(0) (reciprocal space) i0_reciprocal14100000.0000
Solution quality estimate total_estimate0.9023
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.272
Kurtosis Kurtosis kurtosis-0.672
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1412000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.928; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (2)

9. Files and Curves (10)