1ikl

NMR study of monomeric human interleukin-8 (minimized average structure)

Method: SOLUTION NMR Dmax: 44.9 Å Quality: EXCELLENT

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

HUMAN INTERLEUKIN-8 (MONOMERIC)

Homo sapiens

UniProt P10145

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 28–99 Mutation:DEL(1-3), H LEU 25 MODIFIED TO N-METHYL Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–72; UniProt 28–99

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 1ikl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ikl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ikl
Deposition date deposition_date1995-08-03
Structure title titleNMR study of monomeric human interleukin-8 (minimized average structure)
Keywords keywordsCYTOKINE (CHEMOTACTIC); CYTOKINE (CHEMOTACTIC)
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.04
Radius of gyration Rg (electron density) rg_electron12.42
Forward intensity I(0) i01504130.00
Molecular weight molecular_weight8118.0 kDa
Excluded volume excluded_volume10229 ų
Envelope volume envelope_volume12345 ų
Hydration-shell volume shell_volume8829 ų
Envelope diameter envelope_diameter43.2
Shell Rg shell_rg17.49
Envelope Rg envelope_rg12.93
Shape Rg shape_rg12.39
Total Rg total_rg13.90
Total atoms total_atoms1149
Residues n_residues68
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 dmax44.9
Rg (real space) rg_real13.97
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real1.5040e+06
I(0) uncertainty (real space) i0_real_error1.6340e+04
Rg (reciprocal space) rg_reciprocal13.97
I(0) (reciprocal space) i0_reciprocal1504000.0000
Solution quality estimate total_estimate0.9017
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.0
Skewness Skewness skewness0.117
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha183100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.973

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_idd1ikla_
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_id1iklA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40

8. Citations (2)

9. Files and Curves (10)