SAXSdb — 1qe6

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

INTERLEUKIN-8 VARIANT

Homo sapiens

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 28–99 Chain B； UniProt 28–99	Mutation：L5C, H33C	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.2；292 K；NACL, AMMONIUM SULFATE, PEG 8000, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 19K	Resolution 2.35 Å R-free 0.278
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 28–99 Chain D； UniProt 28–99	Mutation：L5C, H33C	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.2；292 K；NACL, AMMONIUM SULFATE, PEG 8000, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 19K	Resolution 2.35 Å R-free 0.278
3	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 28–99 Chain B； UniProt 28–99 Chain C； UniProt 28–99 Chain D； UniProt 28–99	Mutation：L5C, H33C	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.2；292 K；NACL, AMMONIUM SULFATE, PEG 8000, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 19K	Resolution 2.35 Å R-free 0.278

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 1QE6	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ICW INTERLEUKIN-8, MUTANT WITH GLU 38 REPLACED BY CYS AND CYS 50 REPLACED BY ALA Deposited 1996-09-18	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 28–99（72 aa） Chain B 28–99（72 aa）	Mutation：E38C, C50A Mutation：E38C, C50A	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.01 Å R-free 0.266
1IKL NMR study of monomeric human interleukin-8 (minimized average structure) Deposited 1995-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 28–99（72 aa）	Mutation：DEL(1-3), H LEU 25 MODIFIED TO N-METHYL Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1IKM NMR study of monomeric human interleukin-8 (30 structures) Deposited 1995-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 28–99（72 aa）	Mutation：DEL(1-3), THE AMIDE PROTON OF LEU 25 MODIFIED TO N-METHYL Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1IL8 THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION Deposited 1990-03-08	Different mutation/modification 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 28–99（72 aa） Chain B 28–99（72 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1ILP CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 Deposited 1998-12-16	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 28–99（72 aa） Chain B 28–99（72 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 0.15 M；Pressure 1	Resolution not provided
1ILQ CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 (MINIMIZED MEAN) Deposited 1998-12-17	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 28–99（72 aa） Chain B 28–99（72 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 0.15 M；Pressure 1	Resolution not provided
1ROD CHIMERIC PROTEIN OF INTERLEUKIN 8 AND HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN, NMR Deposited 1995-11-24	Different construct Different mutation/modification 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 28–80（53 aa） Fragment：INTERLEUKIN 8 RESIDUES 1 - 53, HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN RESIDUES 54 - 72 Chain B 28–80（53 aa） Fragment：INTERLEUKIN 8 RESIDUES 1 - 53, HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN RESIDUES 54 - 72	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2IL8 THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION Deposited 1990-03-08	Different mutation/modification 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 28–99（72 aa） Chain B 28–99（72 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
3IL8 CRYSTAL STRUCTURE OF INTERLEUKIN 8: SYMBIOSIS OF NMR AND CRYSTALLOGRAPHY Deposited 1990-12-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 28–99（72 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
4XDX The crystal structure of soluble human interleukin 8 expressed in Pichia pastoris Deposited 2014-12-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 30–99（70 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；291 K；0.17 M Ammonium acetate, 0.085 M Sodium citrate tribasic dihydrate pH 5.6, 20% w/v Polyethylene glycol 4,000, 15% v/v Glycerol	Resolution 0.95 Å R-free 0.136
5D14 The atomic resolution crystal structure of human IL-8 Deposited 2015-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 30–99（70 aa） Fragment：unp residues 30-99	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.6；291 K；0.17 M Ammonium acetate, 0.085 M Sodium citrate tribasic dihydrate pH 5.6, 20% w/v Polyethylene glycol 4,000, 15% v/v Glycerol. All crystals were grown at 18 deg C.	Resolution 1.00 Å R-free 0.135
5WDZ Structure of monomeric Interleukin-8 (1-66) Deposited 2017-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 28–93（66 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.3；313 K；Ionic strength (raw mmCIF value) 20；Pressure 1 NMR sample composition 20 mM [U-13C; U-15N] IL-8 1-66, 20 mM HEPES, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 20 mM [U-15N] IL-8, 20 mM HEPES, 70 mM sodium chloride, 13.5 mg/L Y21M bacteriophage, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 20 mM [U-15N] IL-8 1-66, 20 mM HEPES, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6LFM Cryo-EM structure of a class A GPCR Deposited 2019-12-03	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain D 28–99（72 aa） Chain E 28–99（72 aa）	Not recorded	CLR CHOLESTEROL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
6LFO Cryo-EM structure of a class A GPCR monomer Deposited 2019-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 28–92（65 aa）	Not recorded	CLR CHOLESTEROL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
6N2U IL-8 Structure from Bacterial Expression Source Deposited 2018-11-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–99（99 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2.4 M Ammonium Phosphate dibasic, 0.1 M Tris HCl pH 8.5	Resolution 1.25 Å R-free 0.223
6WZM LY3041658 Fab bound to CXCL8 Deposited 2020-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 28–93（66 aa） Chain F 28–93（66 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；20% PEG 3350, 200mM Magnesium Chloride	Resolution 2.28 Å R-free 0.229
6XMN Solution NMR CXCL8-CXCR1 N-domain complex structure Deposited 2020-06-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 28–93（66 aa） Fragment：residues 28-93	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 0.4 mM [U-13C; U-15N] CXCL8, 1.2 mM CXCR1, 50 mM sodium phosphate, 0.01 % sodium azide, 10 % [U-100% 2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.2 mM CXCL8, 0.5 mM [U-13C; U-15N] CXCR1, 50 mM sodium phosphate, 0.01 % sodium azide, 10 % [U-100% 2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
8IC0 Cryo-EM structure of CXCL8 bound C-X-C chemokine receptor 1 in complex with Gi heterotrimer Deposited 2023-02-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain F 28–99（72 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；50 mM HEPES pH8.0, 100 mM NaCl, 1 mM MgCl2, 0.5 mM TCEP, 0.001% LMNG, 0.0001% CHS, 1 uM IL8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.41 Å
8XWN Structure of CXCR2 bound to CXCL8 (Ligand-receptor focused map) Deposited 2024-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 21–99（79 aa） Chain E 21–99（79 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.29 Å
8XX6 Structure of CXCR2 bound to CXCL8 (CXCR2-CXCL8-Go Full map) Deposited 2024-01-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain D 21–99（79 aa） Chain E 21–99（79 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
8YNF Structure of Duffy Antigen Receptor for Chemokines (DARC)/ACKR1 in complex with the chemokine, CXCL8 Deposited 2024-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 21–99（79 aa） Chain E 21–99（79 aa） Chain G 21–99（79 aa） Chain H 21–99（79 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å

21 other PDB entries and 21 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 Author chain B； PDBConstruct 1–72； UniProt 28–99 Author chain C； PDBConstruct 1–72； UniProt 28–99 Author chain D； 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1qe6
Deposition date deposition_date	1999-07-13
Structure title title	INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)
Keywords keywords	INTERCRINE ALPHA FAMILY, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	24.16 Å
Radius of gyration Rg (electron density) rg_electron	23.49 Å
Forward intensity I(0) i0	19137300.00
Molecular weight molecular_weight	32650.0 kDa
Excluded volume excluded_volume	40768 Å³
Envelope volume envelope_volume	52577 Å³
Hydration-shell volume shell_volume	19588 Å³
Envelope diameter envelope_diameter	83.8 Å
Shell Rg shell_rg	29.09 Å
Envelope Rg envelope_rg	23.33 Å
Shape Rg shape_rg	23.45 Å
Total Rg total_rg	24.35 Å
Total atoms total_atoms	2273
Residues n_residues	278
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	80.2 Å
Rg (real space) rg_real	24.30 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	1.9140e+07
I(0) uncertainty (real space) i0_real_error	2.8810e+05
Rg (reciprocal space) rg_reciprocal	24.27 Å
I(0) (reciprocal space) i0_reciprocal	19140000.0000
Solution quality estimate total_estimate	0.8663
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	23.8 Å
Skewness Skewness skewness	0.449
Kurtosis Kurtosis kurtosis	-0.448
Angular range angular_range	— – 0.3300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3974000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.859; Smooth: 0.972

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	INTERLEUKIN-8 VARIANT
Molecular weight formula_weight	8356.8 kDa
Mutation mutation	L5C, H33C
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	2510

SAKECRCQCIKTYSKPFHPKFIKELRVIESGPCCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	231

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1qe6a_
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

Domain ID domain_id	d1qe6b_
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

Domain ID domain_id	d1qe6c_
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

Domain ID domain_id	d1qe6d_
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 (4 domains)

Domain ID domain_id	1qe6A00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1qe6B00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1qe6C00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1qe6D00
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 (3)

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Unit-cell length a length_a	37.540 Å
Unit-cell length b length_b	71.770 Å
Unit-cell length c length_c	57.860 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.46 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.350 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2080
R_work r_work	0.2080
R_free r_free	0.2780

fit	/app/data/saxs_computation/qe/1qe6/1qe6.fit
pddf	/app/data/pr_computation/qe/1qe6/1qe6.pr.out
profile	/app/data/saxs_computation/qe/1qe6/1qe6.dat

INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)

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

INTERLEUKIN-8 VARIANT

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

Refinement Refinement

Diffraction experiment Diffraction