SAXSdb — 3kat

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

NACHT, LRR and PYD domains-containing protein 1

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1371–1467	Fragment：CARD domain 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；291 K；Protein solution: 100mM NaCl, 5mM DTT, 0.02% NaN3, 10mM Tris-HCl (pH 7.5) . Reservoir solution: 18% PEG3350 and 150 mM sodium formate., VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.10 Å R-free 0.260
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1371–1467	Fragment：CARD domain 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；291 K；Protein solution: 100mM NaCl, 5mM DTT, 0.02% NaN3, 10mM Tris-HCl (pH 7.5) . Reservoir solution: 18% PEG3350 and 150 mM sodium formate., VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.10 Å R-free 0.260

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 3KAT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1PN5 NMR structure of the NALP1 Pyrin domain (PYD) Deposited 2003-06-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–93（93 aa） Fragment：Pyrin domain (PYD)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；293 K；Pressure 1 NMR sample composition 1mM NALP1 PYD U-15N,13C; 50mM Na / PO4 - Buffer; 50mM NaCl; 1mM CHAPS; 20mM DTT (D10); 0.02% NaN3; 0.1mM EDTA; protease inhibitor cocktail (Complete, Roche); 95% H2O, 5% D2O \| 95% H2O/5% D2O	Resolution not provided
4IFP X-ray Crystal Structure of Human NLRP1 CARD Domain Deposited 2012-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1335–1418（84 aa） Fragment：NLRP1-CARD	Not recorded	MLI MALONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；298 K；1.4 M Malonate, 100 mM HEPES 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.99 Å R-free 0.208
4IFP X-ray Crystal Structure of Human NLRP1 CARD Domain Deposited 2012-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1335–1418（84 aa） Fragment：NLRP1-CARD	Not recorded	MLI MALONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；298 K；1.4 M Malonate, 100 mM HEPES 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.99 Å R-free 0.208
4IFP X-ray Crystal Structure of Human NLRP1 CARD Domain Deposited 2012-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1335–1418（84 aa） Fragment：NLRP1-CARD	Not recorded	MLI MALONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；298 K；1.4 M Malonate, 100 mM HEPES 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.99 Å R-free 0.208
4IM6 LRR domain from human NLRP1 Deposited 2013-01-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 791–990（200 aa） Fragment：LRR domain (UNP Residues 791-990)	Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1 M Tris pH 8.0, 0.02 M MgCl2, 25 % (w/v) PAA 5100, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.65 Å R-free 0.183
4IM6 LRR domain from human NLRP1 Deposited 2013-01-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 791–990（200 aa） Fragment：LRR domain (UNP Residues 791-990)	Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1 M Tris pH 8.0, 0.02 M MgCl2, 25 % (w/v) PAA 5100, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.65 Å R-free 0.183
5Y3S Crystal structure of human NLRP1 leucine rich repeat domain Deposited 2017-07-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 790–990（201 aa） Fragment：UNP residues 790-990	Not recorded	PO4 PHOSPHATE ION × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；298 K；1.6M Sodium Potassium Phosphate, 100mM HEPES, pH 6.4	Resolution 2.45 Å R-free 0.259
5Y3S Crystal structure of human NLRP1 leucine rich repeat domain Deposited 2017-07-30	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 790–990（201 aa） Fragment：UNP residues 790-990	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；298 K；1.6M Sodium Potassium Phosphate, 100mM HEPES, pH 6.4	Resolution 2.45 Å R-free 0.259
5Y3S Crystal structure of human NLRP1 leucine rich repeat domain Deposited 2017-07-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 790–990（201 aa） Fragment：UNP residues 790-990	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；298 K；1.6M Sodium Potassium Phosphate, 100mM HEPES, pH 6.4	Resolution 2.45 Å R-free 0.259
5Y3S Crystal structure of human NLRP1 leucine rich repeat domain Deposited 2017-07-30	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 790–990（201 aa） Fragment：UNP residues 790-990	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；298 K；1.6M Sodium Potassium Phosphate, 100mM HEPES, pH 6.4	Resolution 2.45 Å R-free 0.259
6K7V Structure of NLRP1 CARD filament Deposited 2019-06-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1379–1466（88 aa） Chain B 1379–1466（88 aa） Chain C 1379–1466（88 aa） Chain D 1379–1466（88 aa） Chain E 1379–1466（88 aa） Chain F 1379–1466（88 aa） Chain G 1379–1466（88 aa） Chain H 1379–1466（88 aa） Chain I 1379–1466（88 aa） Chain J 1379–1466（88 aa） Chain K 1379–1466（88 aa） Chain L 1379–1466（88 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å R-free 0.285
6X6A Cryo-EM structure of NLRP1-DPP9 complex Deposited 2020-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–1212（1212 aa） Chain C 1213–1473（261 aa） Chain E 1–1212（1212 aa） Chain F 1213–1473（261 aa） Chain G 1213–1473（261 aa） Chain I 1213–1473（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM Tris pH 7.5, 150 mM NaCl, 1 mM TCEP cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
6X6C Cryo-EM structure of NLRP1-DPP9-VbP complex Deposited 2020-05-27	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 × 4 PDB declaration: tetrameric	Chain E 1–1473（1473 aa） Chain F 1–1473（1473 aa）	Not recorded	GK2 [(2~{R})-1-[(2~{R})-2-azanyl-3-methyl-butanoyl]pyrrolidin-2-yl]boronic acid × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM Tris pH 7.5, 150 mM NaCl, 1 mM TCEP cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
6XKK Cryo-EM structure of the NLRP1-CARD filament Deposited 2020-06-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 44 PDB declaration: 44-meric	Chain A 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain B 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain C 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain D 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain E 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain F 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain G 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain H 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain I 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain J 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain K 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain L 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain M 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain N 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain O 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain P 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain Q 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain R 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain S 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain T 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain U 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain V 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain a 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain b 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain c 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain d 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain e 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain f 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain g 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain h 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain i 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain j 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain k 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain l 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain m 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain n 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain o 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain p 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain q 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain r 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain s 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain t 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain u 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399) Chain v 1305–1399（95 aa） Fragment：CARD domain (UNP residues 1305-1399)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.72 Å
7WGE Human NLRP1 complexed with thioredoxin Deposited 2021-12-28	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 95–994（900 aa）	Not recorded	AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8ZGD The Crystal Structure of the NLRP1_LRR domain from Biortus. Deposited 2024-05-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 791–990（200 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；20mM MgCl2, 0.1M Tris pH 8.0, 19% polyacrylic acid 5100	Resolution 2.05 Å R-free 0.221
9BJ9 Human CRL-2 ZYG11B binding to human NLRP1 Gly/N degron Deposited 2024-04-25	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 P 131–139（9 aa） Fragment：residues 131-139 (Uniprot numbering)	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å

11 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NALP1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 11–107； UniProt 1371–1467

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	3kat
Deposition date deposition_date	2009-10-19
Structure title title	Crystal Structure of the CARD domain of the human NLRP1 protein, Northeast Structural Genomics Consortium Target HR3486E
Keywords keywords	;Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, Alternative splicing, ATP-binding, Cytoplasm, Leucine-rich repeat, Nucleotide-binding, Nucleus, Polymorphism, APOPTOSIS ;; APOPTOSIS
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	13.63 Å
Radius of gyration Rg (electron density) rg_electron	12.05 Å
Forward intensity I(0) i0	2228650.00
Molecular weight molecular_weight	10131.0 kDa
Excluded volume excluded_volume	12610 Å³
Envelope volume envelope_volume	13649 Å³
Hydration-shell volume shell_volume	9793 Å³
Envelope diameter envelope_diameter	42.2 Å
Shell Rg shell_rg	17.58 Å
Envelope Rg envelope_rg	12.32 Å
Shape Rg shape_rg	12.04 Å
Total Rg total_rg	13.37 Å
Total atoms total_atoms	707
Residues n_residues	82
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	42.6 Å
Rg (real space) rg_real	13.54 Å
Rg uncertainty (real space) rg_real_error	0.22 Å
I(0) (real space) i0_real	2.2290e+06
I(0) uncertainty (real space) i0_real_error	2.1580e+04
Rg (reciprocal space) rg_reciprocal	13.54 Å
I(0) (reciprocal space) i0_reciprocal	2229000.0000
Solution quality estimate total_estimate	0.8084
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.3 Å
Skewness Skewness skewness	0.114
Kurtosis Kurtosis kurtosis	-0.261
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	476300.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; 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) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	3katA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

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8. Citations (1)

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Unit-cell length a length_a	40.708 Å
Unit-cell length b length_b	40.708 Å
Unit-cell length c length_c	160.413 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 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	3.100 Å
Low-resolution limit resolution_low	19.970 Å
R factor r_factor	—
R_work r_work	0.2020
R_free r_free	0.2600

Description description	NACHT, LRR and PYD domains-containing protein 1
Molecular weight formula_weight	12733.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	707

Crystal Structure of the CARD domain of the human NLRP1 protein, Northeast Structural Genomics Consortium Target HR3486E

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

NACHT, LRR and PYD domains-containing protein 1

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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 BL21(DE3)

fit	/app/data/saxs_computation/ka/3kat/3kat.fit
pddf	/app/data/pr_computation/ka/3kat/3kat.pr.out
profile	/app/data/saxs_computation/ka/3kat/3kat.dat