← Back to search
1rjt

NMR Structure of CXC Chemokine CXCL11/ITAC

Method: SOLUTION NMR Dmax: 36.7 Å Quality: REASONABLE
▼

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

Small inducible cytokine B11

OrganismNot specified

UniProt O14625

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 22–94 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4.5；318 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR measurement conditions：pH 5；303 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR measurement conditions：pH 5；313 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition：2 mM CXCL11, partial N15 | 20 mM deuterated sodium acetate, 1 mM sodium azide, 1 mM DSS, 90% H2O, 10% 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 1RJT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8HNK CXCR3-DNGi complex activated by CXCL11 Deposited 2022-12-08 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric
Chain L 1–94（94 aa）
Not recorded CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.01 Å
9P0M Composite map of CXCL11-CXCR3-Gi-scFv16 Deposited 2025-06-07 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric
Chain B 22–94（73 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.95 Å

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

View Construct and Data Evidence
UniProt name SCYBB_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–73； UniProt 22–94

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 1rjt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rjt
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1rjt
Deposition date deposition_date2003-11-20
Structure title titleNMR Structure of CXC Chemokine CXCL11/ITAC
Keywords keywordschemokine, CYTOKINE; CYTOKINE
Experimental Method methodSOLUTION NMR
▼

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

Radius of gyration Rg (Guinier) rg_guinier13.71 Å
Radius of gyration Rg (electron density) rg_electron13.78 Å
Forward intensity I(0) i094967500.00
Molecular weight molecular_weight83181.0 kDa
Excluded volume excluded_volume105930 ų
Envelope volume envelope_volume30806 ų
Hydration-shell volume shell_volume15272 ų
Envelope diameter envelope_diameter66.5 Å
Shell Rg shell_rg23.40 Å
Envelope Rg envelope_rg18.51 Å
Shape Rg shape_rg13.80 Å
Total Rg total_rg14.26 Å
Total atoms total_atoms12090
Residues n_residues730
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
▼

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

Maximum dimension Dmax dmax36.7 Å
Rg (real space) rg_real12.97 Å
Rg uncertainty (real space) rg_real_error0.05 Å
I(0) (real space) i0_real9.0630e+07
I(0) uncertainty (real space) i0_real_error6.6430e+05
Rg (reciprocal space) rg_reciprocal13.81 Å
I(0) (reciprocal space) i0_reciprocal94970000.0000
Solution quality estimate total_estimate0.6849
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary13.9 Å
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha5.3770
Highest regularization parameter α highest_alpha204900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.999; Stabil: 0.970; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1rjta_
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_id1rjtA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40 —
▶

8. Citations (1)

▶

9. Files and Curves (10)