8peq

Complex of diubiquitin-derived artificial binding protein (Affilin) variant Af2 with its target oncofetal fibronectin (fragment 7B8)

Method: X-RAY DIFFRACTION Dmax: 128.1 Å Quality: GOOD

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

Fibronectin

Homo sapiens

UniProt P02751

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1174–1447 Not recorded Affilin variant Af2 × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.3;298 K;500 mM lithium sulfate, 15% PEG 8000 (w/v) Resolution 2.32 Å R-free 0.251
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1174–1447 Not recorded Affilin variant Af2 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.3;298 K;500 mM lithium sulfate, 15% PEG 8000 (w/v) Resolution 2.32 Å R-free 0.251
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1174–1447 Not recorded Affilin variant Af2 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.3;298 K;500 mM lithium sulfate, 15% PEG 8000 (w/v) Resolution 2.32 Å R-free 0.251

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 101 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FINC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–275; UniProt 1174–1447 Author chain B; PDBConstruct 2–275; UniProt 1174–1447 Author chain C; PDBConstruct 2–275; UniProt 1174–1447

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 8peq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8peq
Deposition date deposition_date2023-06-14
Structure title titleComplex of diubiquitin-derived artificial binding protein (Affilin) variant Af2 with its target oncofetal fibronectin (fragment 7B8)
Keywords keywords;extra domain B, EDB, oncofetal fibronectin, ubiquitin, diubiqutin, Affilin, beta strand register shift, strand slippage, scaffold, artificial binding protein, plasticity, directed evolution, DE NOVO PROTEIN ;; DE NOVO PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.70
Radius of gyration Rg (electron density) rg_electron39.13
Forward intensity I(0) i0303471000.00
Molecular weight molecular_weight141100.0 kDa
Excluded volume excluded_volume176610 ų
Envelope volume envelope_volume245590 ų
Hydration-shell volume shell_volume54130 ų
Envelope diameter envelope_diameter139.0
Shell Rg shell_rg43.20
Envelope Rg envelope_rg39.09
Shape Rg shape_rg39.10
Total Rg total_rg39.47
Total atoms total_atoms9950
Residues n_residues1278
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 dmax128.1
Rg (real space) rg_real39.59
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real3.0350e+08
I(0) uncertainty (real space) i0_real_error5.6950e+06
Rg (reciprocal space) rg_reciprocal39.66
I(0) (reciprocal space) i0_reciprocal303500000.0000
Solution quality estimate total_estimate0.8953
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.0
Skewness Skewness skewness0.241
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19880000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.876

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)