4rik

Amyloid forming segment, AVVTGVTAV, from the NAC domain of Parkinson's disease protein alpha-synuclein, residues 69-77

Method: X-RAY DIFFRACTION Dmax: 37.1 Å Quality: REASONABLE

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

Alpha-synuclein

OrganismNot specified

UniProt P37840

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 69–77 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;273 K;0.9M Ammonium Phosphate, 0.1M Sodium Acetate, pH 4.6, vapor diffusion, hanging drop, temperature 273K Resolution 1.85 Å R-free 0.221

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.

226 other PDB entries and 234 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYUA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–9; UniProt 69–77

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 4rik

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4rik
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4rik
Deposition date deposition_date2014-10-06
Structure title titleAmyloid forming segment, AVVTGVTAV, from the NAC domain of Parkinson's disease protein alpha-synuclein, residues 69-77
Keywords keywords;Amyloid, alpha-synuclein, Parkinson's Disease, Toxic Core, NAC, Lipid Binding Protein ;; LIPID BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier9.49
Radius of gyration Rg (electron density) rg_electron9.17
Forward intensity I(0) i027750.60
Molecular weight molecular_weight816.0 kDa
Excluded volume excluded_volume1062 ų
Envelope volume envelope_volume1414 ų
Hydration-shell volume shell_volume1977 ų
Envelope diameter envelope_diameter32.4
Shell Rg shell_rg11.48
Envelope Rg envelope_rg9.67
Shape Rg shape_rg9.10
Total Rg total_rg10.49
Total atoms total_atoms57
Residues n_residues9
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 dmax37.1
Rg (real space) rg_real9.80
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real2.7750e+04
I(0) uncertainty (real space) i0_real_error2.8700e+02
Rg (reciprocal space) rg_reciprocal9.79
I(0) (reciprocal space) i0_reciprocal27750.0000
Solution quality estimate total_estimate0.6916
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary8.0
Skewness Skewness skewness0.685
Kurtosis Kurtosis kurtosis-0.113
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2267.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.329; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.030; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)