SAXSdb — 3il9

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

3-oxoacyl-[acyl-carrier-protein] synthase 3

Escherichia coli K-12

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 1–317 Chain B； UniProt 1–317	Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；288 K；12% PEG 3350, 5 mM calcium acetate, 0.1 M HEPES, pH 7.5, 2 mM TCEP and 1% DMSO, VAPOR DIFFUSION, HANGING DROP, temperature 288K	Resolution 1.85 Å R-free 0.213

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 3IL9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EBL THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI Deposited 2000-01-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–317（317 aa） Chain B 1–317（317 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.8-2.0 M ammonium sulphate, 2% PEG 400, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.80 Å R-free 0.225
1HN9 CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III Deposited 2000-12-07	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 1–317（317 aa） Chain B 1–317（317 aa）	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；PEK4000, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.00 Å R-free 0.218
1HND CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX Deposited 2000-12-07	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 1–317（317 aa）	Not recorded	COA COENZYME A × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.60 Å R-free 0.257
1HNH CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + DEGRADED FORM OF ACETYL-COA Deposited 2000-12-07	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 1–317（317 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	COA COENZYME A × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；PEK4000, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 1.90 Å R-free 0.274
1HNJ CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + MALONYL-COA Deposited 2000-12-07	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 1–317（317 aa）	Not recorded	PO4 PHOSPHATE ION × 2 MLC MALONYL-COENZYME A × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.46 Å R-free 0.193
1HNK CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM Deposited 2000-12-07	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–317（317 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å R-free 0.240
1MZS CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III WITH BOUND dichlorobenzyloxy-indole-carboxylic acid inhibitor Deposited 2002-10-09	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 1–317（317 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 1 669 1-(5-CARBOXYPENTYL)-5-(2,6-DICHLOROBENZYLOXY)-1H-INDOLE-2-CARBOXYLIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；278 K；20% PEG 8000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 278K	Resolution 2.10 Å R-free 0.230
1MZS CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III WITH BOUND dichlorobenzyloxy-indole-carboxylic acid inhibitor Deposited 2002-10-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–317（317 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 2 669 1-(5-CARBOXYPENTYL)-5-(2,6-DICHLOROBENZYLOXY)-1H-INDOLE-2-CARBOXYLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；278 K；20% PEG 8000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 278K	Resolution 2.10 Å R-free 0.230
2EFT Methanethiol-CYS 112 inhibition complex of E. coli ketoacyl synthase III (FABH) and Coenzyme A (high concentration (1.7mM) soak) Deposited 2007-02-24	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 1–317（317 aa） Chain B 1–317（317 aa）	Not recorded	SO4 SULFATE ION × 2 COA COENZYME A × 1 MEE METHANETHIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；1.7M AMMONIUM SULFATE, 2% PEG 400, 100MM NA HEPES, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.00 Å R-free 0.246
2GYO Methanethiol-Cys 112 Inhibition Complex of E. Coli Ketoacyl Synthase III (FabH) and Coenzyme A Deposited 2006-05-09	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 1–317（317 aa） Chain B 1–317（317 aa）	Not recorded	COA COENZYME A × 1 MEE METHANETHIOL × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；1.7M ammonium sulfate, 2% PEG400, 100 mM Na Hepes (pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.00 Å R-free 0.268
5BNM E. coli FabH with Small Molecule Inhibitor 1 Deposited 2015-05-26	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 1–317（317 aa） Chain B 1–317（317 aa）	Not recorded	SO4 SULFATE ION × 1 4VK N-{[3'-(hydroxymethyl)biphenyl-4-yl]methyl}benzenesulfonamide × 1 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；14% PEG 4000, 0.1 M magnesium chloride, 0.1 M Tris	Resolution 1.70 Å R-free 0.269
5BNR E. coli Fabh with small molecule inhibitor 2 Deposited 2015-05-26	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 1–317（317 aa）	Not recorded	4VL 1-{5-[2-fluoro-5-(hydroxymethyl)phenyl]pyridin-2-yl}piperidine-4-carboxylic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；14% PEG 4000, magnesium chloride, 0.1 M Tris	Resolution 1.89 Å R-free 0.245
5BNS E. coli Fabh with small molecule inhibitor 2 Deposited 2015-05-26	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 1–317（317 aa） Chain B 1–317（317 aa）	Not recorded	4VM 1-{5-[2-fluoro-5-(hydroxymethyl)phenyl]pyridin-2-yl}-N-(quinolin-6-ylmethyl)piperidine-4-carboxamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；14% PEG 4000, 0.1 M magnesium chloride, 0.1 m Tris	Resolution 2.20 Å R-free 0.287
6X7R E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) in complex with oxa(dethia)-coenzyme A Deposited 2020-05-30	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 1–317（317 aa）	Not recorded	UT7 oxa(dethia)-CoA × 2 MG MAGNESIUM ION × 2 DMS DIMETHYL SULFOXIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；75 mM magnesium chloride, 100 mM HEPES:NaOH, pH 7.5, 23% PEG3350, 1.5% DMSO	Resolution 1.35 Å R-free 0.176
8D1U E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) with an acetylated cysteine and in complex with oxa(dethia)-Coenzyme A Deposited 2022-05-27	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 1–317（317 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	UT7 oxa(dethia)-CoA × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；75 mM Magnesium Chloride, 20% PEG 6000, 3% PEG 400	Resolution 1.30 Å R-free 0.167
9KA2 Crystal structure of beta-ketoacyl-ACP synthase FabH from E. coli Deposited 2024-10-28	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–317（317 aa） Chain B 1–317（317 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M Tris Bicine, PH8.5, 10% w/v PEG 20000	Resolution 1.50 Å R-free 0.198
9KA5 Crystal structure of beta-ketoacyl-ACP synthase FabH C112Q from E. coli Deposited 2024-10-28	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–317（317 aa）	Mutation：C112Q	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M Tris Bicine, PH8.5, 10% w/v PEG 20000	Resolution 1.42 Å R-free 0.192
9KA6 Crystal structure of beta-ketoacyl-ACP synthase FabH C112Q in complex with acyl-ACP from E. coli Deposited 2024-10-28	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–317（317 aa） Chain B 1–317（317 aa）	Mutation：C112Q Mutation：C112Q	6VG ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] ethanethioate × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；1.0M sodium chloride,0.1M HEPES PH7.0	Resolution 1.47 Å R-free 0.178
9KA7 Crystal structure of beta-ketoacyl-ACP synthase FabH C112Q in complex with malonyl-ACP from E. coli Deposited 2024-10-28	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–317（317 aa） Chain B 1–317（317 aa）	Mutation：C112Q Mutation：C112Q	A1EE0 3-[2-[3-[[(2R)-4-bis(oxidanyl)phosphanyloxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-3-oxidanylidene-propanoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；1.0M sodium chloride,0.1M HEPES PH7.0	Resolution 2.30 Å R-free 0.207

18 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FABH_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 24–340； UniProt 1–317 Author chain B； PDBConstruct 24–340； UniProt 1–317

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	3il9
Deposition date deposition_date	2009-08-06
Structure title title	Structure of E. coli FabH
Keywords keywords	FabH, fatty acid biosynthesis, antibiotic, Acyltransferase, Lipid synthesis, Multifunctional enzyme, Transferase; TRANSFERASE
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	25.07 Å
Radius of gyration Rg (electron density) rg_electron	23.91 Å
Forward intensity I(0) i0	75533900.00
Molecular weight molecular_weight	67072.0 kDa
Excluded volume excluded_volume	83600 Å³
Envelope volume envelope_volume	95970 Å³
Hydration-shell volume shell_volume	32305 Å³
Envelope diameter envelope_diameter	81.9 Å
Shell Rg shell_rg	32.24 Å
Envelope Rg envelope_rg	24.25 Å
Shape Rg shape_rg	23.90 Å
Total Rg total_rg	24.80 Å
Total atoms total_atoms	4706
Residues n_residues	632
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	79.7 Å
Rg (real space) rg_real	24.98 Å
Rg uncertainty (real space) rg_real_error	0.40 Å
I(0) (real space) i0_real	7.5530e+07
I(0) uncertainty (real space) i0_real_error	9.8660e+05
Rg (reciprocal space) rg_reciprocal	25.01 Å
I(0) (reciprocal space) i0_reciprocal	75540000.0000
Solution quality estimate total_estimate	0.8948
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	30.4 Å
Skewness Skewness skewness	0.281
Kurtosis Kurtosis kurtosis	-0.322
Angular range angular_range	— – 0.3150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	22190000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.987

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3il9a1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.0 — automated matches

Domain ID domain_id	d3il9a2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.0 — automated matches

Domain ID domain_id	d3il9b1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.0 — automated matches

Domain ID domain_id	d3il9b2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	3il9A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

Domain ID domain_id	3il9A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

Domain ID domain_id	3il9B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

Domain ID domain_id	3il9B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

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8. Citations (1)

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Unit-cell length a length_a	64.079 Å
Unit-cell length b length_b	66.871 Å
Unit-cell length c length_c	161.503 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.850 Å
Low-resolution limit resolution_low	24.970 Å
R factor r_factor	0.1850
R_work r_work	0.1820
R_free r_free	0.2130

Description description	3-oxoacyl-[acyl-carrier-protein] synthase 3
Molecular weight formula_weight	36358.9 kDa
EC 编号 ec_number	2.3.1.180
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5086

Structure of E. coli FabH

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

3-oxoacyl-[acyl-carrier-protein] synthase 3

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Escherichia coli K-12
NCBI Class编号 ncbi_taxonomy_id	83333
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	380

fit	/app/data/saxs_computation/il/3il9/3il9.fit
pddf	/app/data/pr_computation/il/3il9/3il9.pr.out
profile	/app/data/saxs_computation/il/3il9/3il9.dat