7s4n

Crystal structure of the tick evasin EVA-P974 complexed to human chemokine CCL17

Method: X-RAY DIFFRACTION Dmax: 71.6 Å Quality: EXCELLENT

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

Evasin P974

Amblyomma cajennense

UniProt A0A023FDY8

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 30–114 Not recorded C-C motif chemokine 17 × 1 (Q92583) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 3.5;291 K;0.1 M Na3 Cit 3.5 pH (Buffer) 3 M NaCl (Precipitant) Resolution 1.65 Å R-free 0.237
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 30–114 Not recorded C-C motif chemokine 17 × 1 (Q92583) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 3.5;291 K;0.1 M Na3 Cit 3.5 pH (Buffer) 3 M NaCl (Precipitant) Resolution 1.65 Å R-free 0.237

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.

3 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EV974_AMBCJ
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–85; UniProt 30–114 Author chain C; PDBConstruct 1–85; UniProt 30–114

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 P974 × 1 (A0A023FDY8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 3.5;291 K;0.1 M Na3 Cit 3.5 pH (Buffer) 3 M NaCl (Precipitant) Resolution 1.65 Å R-free 0.237
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 24–94 Not recorded Evasin P974 × 1 (A0A023FDY8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 3.5;291 K;0.1 M Na3 Cit 3.5 pH (Buffer) 3 M NaCl (Precipitant) Resolution 1.65 Å R-free 0.237

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 Author chain D; 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 7s4n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s4n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7s4n
Deposition date deposition_date2021-09-09
Structure title titleCrystal structure of the tick evasin EVA-P974 complexed to human chemokine CCL17
Keywords keywordsInflammation, Evasin, Chemokine, Evasion-chemokine complex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.10
Radius of gyration Rg (electron density) rg_electron22.51
Forward intensity I(0) i018887800.00
Molecular weight molecular_weight31316.0 kDa
Excluded volume excluded_volume38451 ų
Envelope volume envelope_volume50317 ų
Hydration-shell volume shell_volume19606 ų
Envelope diameter envelope_diameter71.6
Shell Rg shell_rg27.96
Envelope Rg envelope_rg22.08
Shape Rg shape_rg22.51
Total Rg total_rg23.22
Total atoms total_atoms2187
Residues n_residues296
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 dmax71.6
Rg (real space) rg_real23.09
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.8890e+07
I(0) uncertainty (real space) i0_real_error2.4420e+05
Rg (reciprocal space) rg_reciprocal23.09
I(0) (reciprocal space) i0_reciprocal18890000.0000
Solution quality estimate total_estimate0.9145
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.607
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2422000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)