2y29

Structure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph III

Method: X-RAY DIFFRACTION Dmax: 30.9 Å Quality: GOOD

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

AMYLOID BETA A4 PROTEIN

OrganismNot specified

UniProt P05067

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 687–692 Fragment:SEGMENT KLVFFA, RESIDUES 687-692 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;AB16-21 FORM III CRYSTALS WERE OBTAINED AFTER THE SEGMENT WAS DISSOLVED IN WATER AT 5 MG/ML AND MIXED WITH 0.2M AMMONIUM ACETATE, 0.1 M TRIS BUFFER PH 8.5 AND 30% ISOPROPANOL. Resolution 2.30 Å R-free 0.260

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.

211 other PDB entries and 282 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–6; UniProt 687–692

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 2y29

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2y29
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2y29
Deposition date deposition_date2010-12-14
Structure title titleStructure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph III
Keywords keywordsPROTEIN FIBRIL, ALZHEIMER DISEASE; PROTEIN FIBRIL
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier8.21
Radius of gyration Rg (electron density) rg_electron7.00
Forward intensity I(0) i019180.90
Molecular weight molecular_weight724.9 kDa
Excluded volume excluded_volume1006 ų
Envelope volume envelope_volume1160 ų
Hydration-shell volume shell_volume2030 ų
Envelope diameter envelope_diameter25.9
Shell Rg shell_rg9.93
Envelope Rg envelope_rg7.56
Shape Rg shape_rg6.87
Total Rg total_rg9.12
Total atoms total_atoms52
Residues n_residues6
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 dmax30.9
Rg (real space) rg_real8.38
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.9180e+04
I(0) uncertainty (real space) i0_real_error2.1040e+02
Rg (reciprocal space) rg_reciprocal8.38
I(0) (reciprocal space) i0_reciprocal19180.0000
Solution quality estimate total_estimate0.7870
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary8.2
Skewness Skewness skewness0.650
Kurtosis Kurtosis kurtosis0.092
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2234.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.670; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.278; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)