1ea3

Influenza virus M1 protein

Method: X-RAY DIFFRACTION Dmax: 68.2 Å Quality: EXCELLENT

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

MATRIX PROTEIN M1

INFLUENZA A VIRUS

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–164 Fragment:N-TERMINAL DOMAIN RESIDUES 1-164 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;0.1M HEPES PH7.5, 5% V/V ISOPROPANOL,6-10% PEG4000, pH 7.00 Resolution 2.30 Å R-free 0.313
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–164 Fragment:N-TERMINAL DOMAIN RESIDUES 1-164 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;0.1M HEPES PH7.5, 5% V/V ISOPROPANOL,6-10% PEG4000, pH 7.00 Resolution 2.30 Å R-free 0.313

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 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VMT1_IAPUE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–164; UniProt 1–164 Author chain B; PDBConstruct 1–164; UniProt 1–164

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 1ea3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ea3
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1ea3
Deposition date deposition_date2000-11-03
Structure title titleInfluenza virus M1 protein
Keywords keywordsINFLUENZA VIRUS, MATRIX PROTEIN; INFLUENZA VIRUS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.66
Radius of gyration Rg (electron density) rg_electron20.62
Forward intensity I(0) i019745800.00
Molecular weight molecular_weight34474.0 kDa
Excluded volume excluded_volume43590 ų
Envelope volume envelope_volume51378 ų
Hydration-shell volume shell_volume21120 ų
Envelope diameter envelope_diameter69.4
Shell Rg shell_rg26.72
Envelope Rg envelope_rg20.60
Shape Rg shape_rg20.62
Total Rg total_rg21.45
Total atoms total_atoms2418
Residues n_residues314
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 dmax68.2
Rg (real space) rg_real21.58
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.9750e+07
I(0) uncertainty (real space) i0_real_error2.5600e+05
Rg (reciprocal space) rg_reciprocal21.60
I(0) (reciprocal space) i0_reciprocal19750000.0000
Solution quality estimate total_estimate0.9042
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4984000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ea3a_
Class classa — All alpha proteins
Fold Fold folda.95 — Influenza virus matrix protein M1
Superfamily Superfamily superfamilya.95.1 — Influenza virus matrix protein M1
Family Family familya.95.1.1 — Influenza virus matrix protein M1
Domain ID domain_idd1ea3b_
Class classa — All alpha proteins
Fold Fold folda.95 — Influenza virus matrix protein M1
Superfamily Superfamily superfamilya.95.1 — Influenza virus matrix protein M1
Family Family familya.95.1.1 — Influenza virus matrix protein M1

CATH v4.4 (4 domains)

Domain ID domain_id1ea3A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Influenza matrix M1, N-terminal subdomain 1
Domain ID domain_id1ea3A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily180 — Influenza matrix protein M1, N-terminal subdomain 2
Domain ID domain_id1ea3B01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Influenza matrix M1, N-terminal subdomain 1
Domain ID domain_id1ea3B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily180 — Influenza matrix protein M1, N-terminal subdomain 2

8. Citations (1)

9. Files and Curves (10)