9bdr

Cryo-EM structure of cardiac amyloid fibril from a variant ATTRV122delta, double filament morphology 1

Method: ELECTRON MICROSCOPY Dmax: 134.6 Å Quality: GOOD

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

Transthyretin

OrganismNot specified

UniProt P02766

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 21–147 Chain B; UniProt 21–147 Chain C; UniProt 21–147 Chain D; UniProt 21–147 Chain E; UniProt 21–147 Chain F; UniProt 21–147 Chain G; UniProt 21–147 Chain H; UniProt 21–147 Chain I; UniProt 21–147 Chain J; UniProt 21–147 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7;Fibrils were purified in ice-chilled water cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.82 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.

460 other PDB entries and 501 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TTHY_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–126; UniProt 21–147 Author chain B; PDBConstruct 1–126; UniProt 21–147 Author chain C; PDBConstruct 1–126; UniProt 21–147 Author chain D; PDBConstruct 1–126; UniProt 21–147 Author chain E; PDBConstruct 1–126; UniProt 21–147 Author chain F; PDBConstruct 1–126; UniProt 21–147 Author chain G; PDBConstruct 1–126; UniProt 21–147 Author chain H; PDBConstruct 1–126; UniProt 21–147 Author chain I; PDBConstruct 1–126; UniProt 21–147 Author chain J; PDBConstruct 1–126; UniProt 21–147

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 9bdr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bdr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9bdr
Deposition date deposition_date2024-04-12
Structure title titleCryo-EM structure of cardiac amyloid fibril from a variant ATTRV122delta, double filament morphology 1
Keywords keywordsATTR, transthyretin amyloidosis, V122delta, ex vivo, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.06
Radius of gyration Rg (electron density) rg_electron39.56
Forward intensity I(0) i0136704000.00
Molecular weight molecular_weight99273.0 kDa
Excluded volume excluded_volume126090 ų
Envelope volume envelope_volume159510 ų
Hydration-shell volume shell_volume36528 ų
Envelope diameter envelope_diameter140.7
Shell Rg shell_rg40.79
Envelope Rg envelope_rg39.69
Shape Rg shape_rg39.54
Total Rg total_rg39.70
Total atoms total_atoms7030
Residues n_residues895
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 dmax134.6
Rg (real space) rg_real39.67
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real1.3670e+08
I(0) uncertainty (real space) i0_real_error2.5310e+06
Rg (reciprocal space) rg_reciprocal39.30
I(0) (reciprocal space) i0_reciprocal136700000.0000
Solution quality estimate total_estimate0.8009
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.7
Skewness Skewness skewness0.579
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14120000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.724; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.601; Smooth: 0.633

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)