8fj2

Crystal Structure of the Tick Evasin EVA-AAM1001(C8) Complexed to Human Chemokine CCL17

Method: X-RAY DIFFRACTION Dmax: 57.4 Å Quality: GOOD

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

Evasin P1243

Amblyomma americanum

UniProt A0A0C9S461

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 21–123 Not recorded C-C motif chemokine 17 × 1 (Q92583) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;4.3 M NaCl, 0.1 M HEPES pH 7.4 Resolution 2.07 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 21–123 Not recorded C-C motif chemokine 17 × 1 (Q92583) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;4.3 M NaCl, 0.1 M HEPES pH 7.4 Resolution 2.07 Å R-free 0.231

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E1243_AMBAM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–103; UniProt 21–123

C-C motif chemokine 17

Homo sapiens

UniProt Q92583

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 B; UniProt 24–94 Not recorded Evasin P1243 × 1 (A0A0C9S461) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;4.3 M NaCl, 0.1 M HEPES pH 7.4 Resolution 2.07 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 24–94 Not recorded Evasin P1243 × 1 (A0A0C9S461) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;4.3 M NaCl, 0.1 M HEPES pH 7.4 Resolution 2.07 Å R-free 0.231

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.

6 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCL17_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–71; UniProt 24–94

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 8fj2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fj2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8fj2
Deposition date deposition_date2022-12-19
Structure title titleCrystal Structure of the Tick Evasin EVA-AAM1001(C8) Complexed to Human Chemokine CCL17
Keywords keywordsEvasin, Chemokine-binding protein, ticks, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.86
Radius of gyration Rg (electron density) rg_electron16.40
Forward intensity I(0) i04746090.00
Molecular weight molecular_weight15119.0 kDa
Excluded volume excluded_volume18669 ų
Envelope volume envelope_volume22129 ų
Hydration-shell volume shell_volume12148 ų
Envelope diameter envelope_diameter57.5
Shell Rg shell_rg21.12
Envelope Rg envelope_rg16.75
Shape Rg shape_rg16.42
Total Rg total_rg17.20
Total atoms total_atoms2046
Residues n_residues142
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 dmax57.4
Rg (real space) rg_real16.93
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real4.7460e+06
I(0) uncertainty (real space) i0_real_error5.5150e+04
Rg (reciprocal space) rg_reciprocal16.92
I(0) (reciprocal space) i0_reciprocal4746000.0000
Solution quality estimate total_estimate0.7863
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.480
Kurtosis Kurtosis kurtosis-0.168
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha854600.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.770; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)