8oq9

Crystal structure of the titin domain Fn3-56

Method: X-RAY DIFFRACTION Dmax: 70.0 Å Quality: EXCELLENT

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

Titin

Homo sapiens

UniProt Q8WZ42

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 21497–21598 Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;10mM Tris-HCl pH 7.5 50mM NaCl 0.5mM DTT 0.1M MES 10mM ZnCl2 20% (w/v) PEG6000 Resolution 1.65 Å R-free 0.192
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 21497–21598 Not recorded ZN ZINC ION × 3 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;10mM Tris-HCl pH 7.5 50mM NaCl 0.5mM DTT 0.1M MES 10mM ZnCl2 20% (w/v) PEG6000 Resolution 1.65 Å R-free 0.192
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 21497–21598 Not recorded ZN ZINC ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;10mM Tris-HCl pH 7.5 50mM NaCl 0.5mM DTT 0.1M MES 10mM ZnCl2 20% (w/v) PEG6000 Resolution 1.65 Å R-free 0.192

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.

54 other PDB entries and 121 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TITIN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–105; UniProt 21497–21598 Author chain B; PDBConstruct 4–105; UniProt 21497–21598 Author chain C; PDBConstruct 4–105; UniProt 21497–21598

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 8oq9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8oq9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8oq9
Deposition date deposition_date2023-04-11
Structure title titleCrystal structure of the titin domain Fn3-56
Keywords keywordsTitin Fibronectin type III A-band STRUCTURAL PROTEIN, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.55
Radius of gyration Rg (electron density) rg_electron20.97
Forward intensity I(0) i020597900.00
Molecular weight molecular_weight32513.0 kDa
Excluded volume excluded_volume39871 ų
Envelope volume envelope_volume48443 ų
Hydration-shell volume shell_volume20005 ų
Envelope diameter envelope_diameter73.2
Shell Rg shell_rg26.86
Envelope Rg envelope_rg21.33
Shape Rg shape_rg20.97
Total Rg total_rg21.73
Total atoms total_atoms4431
Residues n_residues305
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 dmax70.0
Rg (real space) rg_real21.50
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real2.0600e+07
I(0) uncertainty (real space) i0_real_error2.5510e+05
Rg (reciprocal space) rg_reciprocal21.51
I(0) (reciprocal space) i0_reciprocal20600000.0000
Solution quality estimate total_estimate0.9006
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.485
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3511000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)