7s59

Crystal structure of the tick evasin EVA-P974 complexed to a chimera made of human chemokines CCL7 and CCL8

Method: X-RAY DIFFRACTION Dmax: 69.0 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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain 1; UniProt 30–114 Not recorded chimera protein of C-C motif chemokine 7 and C-C motif chemokine 8,C-C motif chemokine 7 × 1 (P80075,P80098) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.1 M TRIS 8.5 pH (Buffer) 2 M (NH4)2SO4 (Precipitant) Resolution 2.39 Å R-free 0.268
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain 3; UniProt 30–114 Not recorded chimera protein of C-C motif chemokine 7 and C-C motif chemokine 8,C-C motif chemokine 7 × 1 (P80075,P80098) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.1 M TRIS 8.5 pH (Buffer) 2 M (NH4)2SO4 (Precipitant) Resolution 2.39 Å R-free 0.268

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 1; PDBConstruct 1–85; UniProt 30–114 Author chain 3; PDBConstruct 1–85; UniProt 30–114

chimera protein of C-C motif chemokine 7 and C-C motif chemokine 8,C-C motif chemokine 7

Homo sapiens

UniProt P80075

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain 2; UniProt 24–38 Not recorded Evasin P974 × 1 (A0A023FDY8) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.1 M TRIS 8.5 pH (Buffer) 2 M (NH4)2SO4 (Precipitant) Resolution 2.39 Å R-free 0.268
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain 4; UniProt 24–38 Not recorded Evasin P974 × 1 (A0A023FDY8) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.1 M TRIS 8.5 pH (Buffer) 2 M (NH4)2SO4 (Precipitant) Resolution 2.39 Å R-free 0.268

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCL8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–15; UniProt 24–38 Author chain 4; PDBConstruct 1–15; UniProt 24–38

chimera protein of C-C motif chemokine 7 and C-C motif chemokine 8,C-C motif chemokine 7

Homo sapiens

UniProt P80098

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain 2; UniProt 39–99 Not recorded Evasin P974 × 1 (A0A023FDY8) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.1 M TRIS 8.5 pH (Buffer) 2 M (NH4)2SO4 (Precipitant) Resolution 2.39 Å R-free 0.268
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain 4; UniProt 39–99 Not recorded Evasin P974 × 1 (A0A023FDY8) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.1 M TRIS 8.5 pH (Buffer) 2 M (NH4)2SO4 (Precipitant) Resolution 2.39 Å R-free 0.268

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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCL7_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 16–76; UniProt 39–99 Author chain 4; PDBConstruct 16–76; UniProt 39–99

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 7s59

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s59
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7s59
Deposition date deposition_date2021-09-10
Structure title titleCrystal structure of the tick evasin EVA-P974 complexed to a chimera made of human chemokines CCL7 and CCL8
Keywords keywordsInflammation, Evasin, Chemokine binder, Evasin-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_guinier22.83
Radius of gyration Rg (electron density) rg_electron21.91
Forward intensity I(0) i020584600.00
Molecular weight molecular_weight32904.0 kDa
Excluded volume excluded_volume40414 ų
Envelope volume envelope_volume52238 ų
Hydration-shell volume shell_volume20058 ų
Envelope diameter envelope_diameter70.2
Shell Rg shell_rg28.26
Envelope Rg envelope_rg21.46
Shape Rg shape_rg21.94
Total Rg total_rg22.65
Total atoms total_atoms2293
Residues n_residues306
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 dmax69.0
Rg (real space) rg_real22.74
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real2.0580e+07
I(0) uncertainty (real space) i0_real_error2.5510e+05
Rg (reciprocal space) rg_reciprocal22.76
I(0) (reciprocal space) i0_reciprocal20580000.0000
Solution quality estimate total_estimate0.9183
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.105
Kurtosis Kurtosis kurtosis-0.653
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2876000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.980; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)