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2eot

SOLUTION STRUCTURE OF EOTAXIN, AN ENSEMBLE OF 32 NMR SOLUTION STRUCTURES

Method: SOLUTION NMR Dmax: 33.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

EOTAXIN

Homo sapiens

UniProt P51671

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 24–97 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5；303 K；Ionic strength (raw mmCIF value) 20mM SODIUM ACETATE；Pressure 1 NMR sample composition：90% H2O/10% H2O OR 100% D2O BUFFER, ALSO CONTAINED 1MM DSS AND 1MM SODIUM AZIDE Resolution not provided

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.

Other PDB Difference from Current Entry 2EOT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1EOT SOLUTION NMR STRUCTURE OF EOTAXIN, MINIMIZED AVERAGE STRUCTURE Deposited 1998-06-17 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 24–97（74 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；303 K；Ionic strength (raw mmCIF value) 20mM SODIUM ACETATE；Pressure 1
NMR sample composition 90% H2O/10% H2O OR 100% D2O. BUFFER ALSO CONTAINED 1MM DSS AND 1MM SODIUM AZIDE.
Resolution not provided
2MPM Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: the N-terminal Region of CCR3 Bound to CCL11/Eotaxin-1 Deposited 2014-05-26 Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 24–97（74 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；313 K；Ionic strength (raw mmCIF value) 20；Pressure AMBIENT
NMR sample composition 0.2-0.4 MM [U-100% 13C, U-100% 15N] CCL11/EOTAXIN-1, 0.2-0.4 MM CCR3 SU1617 SULFOPEPTIDE, 95% V/V H2O, 5% V/V [U-100% 2H] D2O, 20 MM [U-100% 2H] SODIUM ACETATE-D6, 0.02% V/V SODIUM AZIDE, 20 UM DSS, 95% H2O/5% D2O
Resolution not provided
7SCS Crystal Structure of the Tick Evasin EVA-AAM1001 Complexed to Human Chemokine CCL11 Deposited 2021-09-29 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 24–97（74 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M BIS-TRIS 6.5 pH (Buffer) , 2 M (NH4)2SO4 (Precipitant)
Resolution 1.51 Å R-free 0.206

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

View Construct and Data Evidence
UniProt name CCL11_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–74； UniProt 24–97

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 2eot

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2eot
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2eot
Deposition date deposition_date1998-06-29
Structure title titleSOLUTION STRUCTURE OF EOTAXIN, AN ENSEMBLE OF 32 NMR SOLUTION STRUCTURES
Keywords keywordsCYTOKINE, CHEMOKINE, PROTEIN SYNTHESIS, EOTAXIN, SOLUTION STRUCTURE, CCR3, EOSINOPHIL; CYTOKINE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.13 Å
Radius of gyration Rg (electron density) rg_electron13.18 Å
Forward intensity I(0) i0943954000.00
Molecular weight molecular_weight268030.0 kDa
Excluded volume excluded_volume340040 ų
Envelope volume envelope_volume40922 ų
Hydration-shell volume shell_volume18523 ų
Envelope diameter envelope_diameter66.4 Å
Shell Rg shell_rg24.92 Å
Envelope Rg envelope_rg19.32 Å
Shape Rg shape_rg13.15 Å
Total Rg total_rg13.56 Å
Total atoms total_atoms38560
Residues n_residues2368
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax33.8 Å
Rg (real space) rg_real12.44 Å
Rg uncertainty (real space) rg_real_error0.04 Å
I(0) (real space) i0_real9.0190e+08
I(0) uncertainty (real space) i0_real_error6.3600e+06
Rg (reciprocal space) rg_reciprocal13.17 Å
I(0) (reciprocal space) i0_reciprocal944000000.0000
Solution quality estimate total_estimate0.6882
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.4 Å
Skewness Skewness skewness0.136
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha4.1590
Highest regularization parameter α highest_alpha118200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 1.000; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2eota_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.9 — IL8-like
Superfamily Superfamily superfamilyd.9.1 — Interleukin 8-like chemokines
Family Family familyd.9.1.1 — Interleukin 8-like chemokines

CATH v4.4 (1 domains)

Domain ID domain_id2eotA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40 —
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8. Citations (1)

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9. Files and Curves (10)