4r0u

Tgvtava, an amyloid forming segment from alpha synuclein, residues 72-78

Method: X-RAY DIFFRACTION Dmax: 27.9 Å Quality: GOOD

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 72–78 Fragment:UNP RESIDUES 72-78 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2M magnesium formate, vapor diffusion, hanging drop, temperature 298K Resolution 1.38 Å R-free 0.217

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 1–7; UniProt 72–78

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 4r0u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4r0u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4r0u
Deposition date deposition_date2014-08-01
Structure title titleTgvtava, an amyloid forming segment from alpha synuclein, residues 72-78
Keywords keywordsamyloid-like protofibril, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier7.56
Radius of gyration Rg (electron density) rg_electron6.44
Forward intensity I(0) i020746.00
Molecular weight molecular_weight617.7 kDa
Excluded volume excluded_volume780 ų
Envelope volume envelope_volume912 ų
Hydration-shell volume shell_volume1749 ų
Envelope diameter envelope_diameter22.6
Shell Rg shell_rg9.40
Envelope Rg envelope_rg6.87
Shape Rg shape_rg6.39
Total Rg total_rg8.15
Total atoms total_atoms43
Residues n_residues7
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 dmax27.9
Rg (real space) rg_real7.69
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real2.0750e+04
I(0) uncertainty (real space) i0_real_error2.6960e+02
Rg (reciprocal space) rg_reciprocal7.68
I(0) (reciprocal space) i0_reciprocal20750.0000
Solution quality estimate total_estimate0.7965
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.718; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.266; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)