SAXSdb — 1el0

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

I-309

OrganismNot specified

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 23–96	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5；303 K；Ionic strength (raw mmCIF value) 20 mM；Pressure ambient NMR measurement conditions：pH 5；303 K；Ionic strength (raw mmCIF value) 20 mM；Pressure ambient NMR sample composition：2 mM I-309, 20 mM sodium acetate buffer, DSS \| 90% H2O/10% D2O NMR sample composition：2 mM I-309, 20 mM sodium acetate buffer, DSS \| 99% D2O	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 1EL0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4OIJ X-ray crystal structure of racemic non-glycosylated chemokine Ser-CCL1 Deposited 2014-01-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 23–96（74 aa） Fragment：UNP residues 23-96 Chain B 23–96（74 aa） Fragment：UNP residues 23-96	Not recorded	SO4 SULFATE ION × 17	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 3.5；292 K；2 M Ammonium Sulfate, 0.1 M citric acid, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.00 Å R-free 0.283
4OIK (Quasi-)Racemic X-ray crystal structure of glycosylated chemokine Ser-CCL1. Deposited 2014-01-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 23–96（74 aa） Fragment：UNP residues 23-96 Chain B 23–96（74 aa） Fragment：UNP residues 23-96	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 15	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 3.5；292 K；2 M Ammonium Sulfate, 0.1 M citric acid, pH 3.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.10 Å R-free 0.276
8U1U Structure of a class A GPCR/agonist complex Deposited 2023-09-02	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 24–96（73 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

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

View Construct and Data Evidence

UniProt name	CCL1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–74； UniProt 23–96

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1el0
Deposition date deposition_date	2000-03-11
Structure title title	SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309
Keywords keywords	chemokine fold, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	13.16 Å
Radius of gyration Rg (electron density) rg_electron	13.10 Å
Forward intensity I(0) i0	981266000.00
Molecular weight molecular_weight	257620.0 kDa
Excluded volume excluded_volume	320580 Å³
Envelope volume envelope_volume	42681 Å³
Hydration-shell volume shell_volume	18785 Å³
Envelope diameter envelope_diameter	62.6 Å
Shell Rg shell_rg	25.57 Å
Envelope Rg envelope_rg	20.04 Å
Shape Rg shape_rg	13.04 Å
Total Rg total_rg	13.59 Å
Total atoms total_atoms	36300
Residues n_residues	2220
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	34.9 Å
Rg (real space) rg_real	12.46 Å
Rg uncertainty (real space) rg_real_error	0.04 Å
I(0) (real space) i0_real	9.3730e+08
I(0) uncertainty (real space) i0_real_error	6.6680e+06
Rg (reciprocal space) rg_reciprocal	13.21 Å
I(0) (reciprocal space) i0_reciprocal	981300000.0000
Solution quality estimate total_estimate	0.6826
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	15.4 Å
Skewness Skewness skewness	0.190
Kurtosis Kurtosis kurtosis	-0.341
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	4.2310
Highest regularization parameter α highest_alpha	180700.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.002; Oscil: 0.986; Stabil: 0.975; Sysdev: 0.000; Positv: 1.000; Valcen: 0.989; 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_id	d1el0a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

CATH v4.4 (1 domains)

Domain ID domain_id	1el0A00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	I-309
Molecular weight formula_weight	8594.2 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	36300

fit	/app/data/saxs_computation/el/1el0/1el0.fit
pddf	/app/data/pr_computation/el/1el0/1el0.pr.out
profile	/app/data/saxs_computation/el/1el0/1el0.dat

SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309

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

I-309

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)