SAXSdb — 3c6d

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

Polyprotein

OrganismNot specified

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 heterocomplex Heteromer Protein × 360 PDB declaration: 360-meric（360） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Not recorded	prM × 180 （P14337）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Not recorded	prM × 3 （P14337）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å
3	Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Not recorded	prM × 15 （P14337）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å
4	Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric（36） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Not recorded	prM × 18 （P14337）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å
5	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Not recorded	prM × 3 （P14337）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å

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 3C6D	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 600 PDB declaration: 600-MERIC	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 50 PDB declaration: 50-meric	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different oligomeric state Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different oligomeric state Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 720 PDB declaration: 720-meric	Chain A 281–675（395 aa） Fragment：UNP residues 281-675 Chain B 281–675（395 aa） Fragment：UNP residues 281-675 Chain C 281–675（395 aa） Fragment：UNP residues 281-675	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 281–675（395 aa） Fragment：UNP residues 281-675 Chain B 281–675（395 aa） Fragment：UNP residues 281-675 Chain C 281–675（395 aa） Fragment：UNP residues 281-675	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 60 PDB declaration: 60-meric	Chain A 281–675（395 aa） Fragment：UNP residues 281-675 Chain B 281–675（395 aa） Fragment：UNP residues 281-675 Chain C 281–675（395 aa） Fragment：UNP residues 281-675	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Heteromer；Protein × 72 PDB declaration: 72-meric	Chain A 281–675（395 aa） Fragment：UNP residues 281-675 Chain B 281–675（395 aa） Fragment：UNP residues 281-675 Chain C 281–675（395 aa） Fragment：UNP residues 281-675	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 281–675（395 aa） Fragment：UNP residues 281-675 Chain B 281–675（395 aa） Fragment：UNP residues 281-675 Chain C 281–675（395 aa） Fragment：UNP residues 281-675	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
6ZQU Cryo-EM structure of mature Dengue virus 2 at 3.1 angstrom resolution Deposited 2020-07-10	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-meric	Chain B 206–280（75 aa） Chain D 206–280（75 aa） Chain F 206–280（75 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 360	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；PBS buffer cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.10 Å

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

View Construct and Data Evidence

UniProt name	O11875_9FLAV
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–395； UniProt 281–675 Author chain B； PDBConstruct 1–395； UniProt 281–675 Author chain C； PDBConstruct 1–395； UniProt 281–675

prM

OrganismNot specified

UniProt P14337

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 heterocomplex Heteromer Protein × 360 PDB declaration: 360-meric（360） Consistent with protein copy count	Chain D； UniProt 115–195 Chain E； UniProt 115–195 Chain F； UniProt 115–195	Not recorded	Polyprotein × 180 （O11875）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain D； UniProt 115–195 Chain E； UniProt 115–195 Chain F； UniProt 115–195	Not recorded	Polyprotein × 3 （O11875）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å
3	Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain D； UniProt 115–195 Chain E； UniProt 115–195 Chain F； UniProt 115–195	Not recorded	Polyprotein × 15 （O11875）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å
4	Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric（36） Consistent with protein copy count	Chain D； UniProt 115–195 Chain E； UniProt 115–195 Chain F； UniProt 115–195	Not recorded	Polyprotein × 18 （O11875）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å
5	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain D； UniProt 115–195 Chain E； UniProt 115–195 Chain F； UniProt 115–195	Not recorded	Polyprotein × 3 （O11875）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 12.50 Å

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 3C6D	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9T4P Dengue 2 Virus NS2B-NS3 protease fusion protein with crystal epitope mutation K174Q Deposited 2025-10-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1394–1440（47 aa） Chain A 1476–1660（185 aa）	Mutation：K174Q Mutation：K174Q	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293.15 K；LFS Eco well C09 0.1M HEPES pH 7, 0.2M Lithium chloride, 20% w/v PEG 6000, 10% v/v Ethylene glycol	Resolution 1.95 Å R-free 0.294

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	POLG_DEN28
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–81； UniProt 115–195 Author chain E； PDBConstruct 1–81； UniProt 115–195 Author chain F； PDBConstruct 1–81； UniProt 115–195

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	3c6d
Deposition date deposition_date	2008-02-04
Structure title title	The pseudo-atomic structure of dengue immature virus
Keywords keywords	;icosahedral virion, Helicase, Hydrolase, Nucleotide-binding, RNA replication, Transmembrane, ATP-binding, Capsid protein, Cleavage on pair of basic residues, Endoplasmic reticulum, Envelope protein, Glycoprotein, Metal-binding, Multifunctional enzyme, Nucleotidyltransferase, Nucleus, Phosphoprotein, Protease, Ribonucleoprotein, RNA-binding, RNA-directed RNA polymerase, Secreted, Serine protease, Transcription, Transcription regulation, Transferase, Viral nucleoprotein, icosahedral virus, VIRUS ;; VIRUS
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	55.35 Å
Radius of gyration Rg (electron density) rg_electron	55.68 Å
Forward intensity I(0) i0	369306000.00
Molecular weight molecular_weight	157790.0 kDa
Excluded volume excluded_volume	192350 Å³
Envelope volume envelope_volume	219360 Å³
Hydration-shell volume shell_volume	37274 Å³
Envelope diameter envelope_diameter	176.0 Å
Shell Rg shell_rg	51.37 Å
Envelope Rg envelope_rg	50.84 Å
Shape Rg shape_rg	55.78 Å
Total Rg total_rg	55.56 Å
Total atoms total_atoms	—
Residues n_residues	—
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	179.9 Å
Rg (real space) rg_real	55.28 Å
Rg uncertainty (real space) rg_real_error	1.59 Å
I(0) (real space) i0_real	3.6930e+08
I(0) uncertainty (real space) i0_real_error	7.6690e+06
Rg (reciprocal space) rg_reciprocal	55.37 Å
I(0) (reciprocal space) i0_reciprocal	369300000.0000
Solution quality estimate total_estimate	0.8616
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	83.5 Å
Skewness Skewness skewness	-0.002
Kurtosis Kurtosis kurtosis	-0.803
Angular range angular_range	— – 0.1400 Å⁻¹
Current regularization parameter α current_alpha	0.0002
Highest regularization parameter α highest_alpha	9039000.0000
Real-space data points n_real_points	29
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.783

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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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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Resolution resolution	12.50 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	2741

Description description	Polyprotein
Molecular weight formula_weight	43904.4 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	1413

Description description	prM
Molecular weight formula_weight	9261.5 kDa
Source method src_method	nat
Copy count entity_count	3

The pseudo-atomic structure of dengue immature virus

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

Polyprotein

State in the Current Structure

Other States of the Same Protein in the Database

prM

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/c6/3c6d/3c6d.fit
pddf	/app/data/pr_computation/c6/3c6d/3c6d.pr.out
profile	/app/data/saxs_computation/c6/3c6d/3c6d.dat