SAXSdb — 1he1

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

EXOENZYME S

PSEUDOMONAS AERUGINOSA

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 95–229	Fragment：96-234, GTPASE-ACTIVATING PROTEIN (GAP-DOMAIN)	RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 （P15154） NI NICKEL (II) ION × 3 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；8% PEG 6000, 3MM NICL2, 100 MM TRIS/HCL PH8.5, pH 8.50	Resolution 2.00 Å R-free 0.224
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 95–229	Fragment：96-234, GTPASE-ACTIVATING PROTEIN (GAP-DOMAIN)	RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 （P15154） NI NICKEL (II) ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；8% PEG 6000, 3MM NICL2, 100 MM TRIS/HCL PH8.5, pH 8.50	Resolution 2.00 Å R-free 0.224

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 1HE1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1HE9 Crystal structure of the GAP domain of the Pseudomonas aeruginosa ExoS toxin Deposited 2000-11-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 102–235（134 aa） Fragment：96-234 GTPASE-ACTIVATING PROTEIN (GAP-DOMAIN)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；MGCL2, (NH4)2SO4, PEG 6000, NA-CACODYLATE PH5.5, pH 5.50	Resolution 2.40 Å R-free 0.265
2C23 14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide Deposited 2005-09-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain P 421–431（11 aa） Fragment：14-3-3 BINDING REGION, RESIDUES 421-431	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.05M MGCL2,0.1M HEPES PH7.5, 30% PEG MME 550, pH 8.00	Resolution 2.65 Å R-free 0.286
6GN0 Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form Deposited 2018-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 234–453（220 aa） Chain G 234–453（220 aa）	Mutation：E379A, E381A Mutation：E379A, E381A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；12% PEG 3350, 4% Tacsimate	Resolution 3.24 Å R-free 0.294
6GN0 Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form Deposited 2018-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 234–453（220 aa） Chain H 234–453（220 aa）	Mutation：E379A, E381A Mutation：E379A, E381A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；12% PEG 3350, 4% Tacsimate	Resolution 3.24 Å R-free 0.294
6Y7T Engineered conjugation of lysine-specific molecular tweezers with ExoS derived peptidic inhibitor enhance affinity towards target protein 14-3-3 through ditopic binding Deposited 2020-03-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: TRIMERIC	Chain D 420–430（11 aa）	Not recorded	NA SODIUM ION × 3 GOL GLYCEROL × 1 TWZ 2-[4-[2-[hydroxy-[[(1R,5S,9S,16R,20R,24S,28S,35R)-22-phosphonooxy-3-tridecacyclo[22.14.1.15,20.19,16.128,35.02,23.04,21.06,19.08,17.010,15.025,38.027,36.029,34]dotetraconta-2,4(21),6(19),7,10,12,14,17,22,25(38),26,29,31,33,36-pentadecaenyl]oxy]phosphoryl]oxyethyl]triazol-1-yl]acetic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Bis-Tris Propane 0.2M sodium acetate trihydrate 20% PEG1000 10% Glycerol pH 7 Grew at 4 degree Celsius after a few days	Resolution 2.50 Å R-free 0.268
6Y7T Engineered conjugation of lysine-specific molecular tweezers with ExoS derived peptidic inhibitor enhance affinity towards target protein 14-3-3 through ditopic binding Deposited 2020-03-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: TRIMERIC	Chain E 420–430（11 aa）	Not recorded	NA SODIUM ION × 2 GOL GLYCEROL × 1 TWZ 2-[4-[2-[hydroxy-[[(1R,5S,9S,16R,20R,24S,28S,35R)-22-phosphonooxy-3-tridecacyclo[22.14.1.15,20.19,16.128,35.02,23.04,21.06,19.08,17.010,15.025,38.027,36.029,34]dotetraconta-2,4(21),6(19),7,10,12,14,17,22,25(38),26,29,31,33,36-pentadecaenyl]oxy]phosphoryl]oxyethyl]triazol-1-yl]acetic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Bis-Tris Propane 0.2M sodium acetate trihydrate 20% PEG1000 10% Glycerol pH 7 Grew at 4 degree Celsius after a few days	Resolution 2.50 Å R-free 0.268

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q51451
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–135； UniProt 95–229 Author chain B； PDBConstruct 1–135； UniProt 95–229

RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1

HOMO SAPIENS

UniProt P15154

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–176	Fragment：2-184	EXOENZYME S × 1 （Q51451） NI NICKEL (II) ION × 3 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；8% PEG 6000, 3MM NICL2, 100 MM TRIS/HCL PH8.5, pH 8.50	Resolution 2.00 Å R-free 0.224
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1–176	Fragment：2-184	EXOENZYME S × 1 （Q51451） NI NICKEL (II) ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；8% PEG 6000, 3MM NICL2, 100 MM TRIS/HCL PH8.5, pH 8.50	Resolution 2.00 Å R-free 0.224

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 1HE1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1E96 Structure of the Rac/p67phox complex Deposited 2000-10-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–192（192 aa）	Mutation：YES	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 10.5；0.1 M CAPS PH 10.5, 0.2 M LI ACETATE, 0.8 M NAH2PO4, 1.2 M K2HPO4	Resolution 2.40 Å R-free 0.284
1HH4 Rac1-RhoGDI complex involved in NADPH oxidase activation Deposited 2000-12-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–192（192 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GER GERAN-8-YL GERAN × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；HANGING DROP AT 20C WITH RESERVOIR: 30% PEG 4000, 100 MM NA CITRATE PH=5.6, 5 MM MGCL2, 200 MM AMMONIUM ACETATE, pH 5.60	Resolution 2.70 Å R-free 0.280
1HH4 Rac1-RhoGDI complex involved in NADPH oxidase activation Deposited 2000-12-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–192（192 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GER GERAN-8-YL GERAN × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；HANGING DROP AT 20C WITH RESERVOIR: 30% PEG 4000, 100 MM NA CITRATE PH=5.6, 5 MM MGCL2, 200 MM AMMONIUM ACETATE, pH 5.60	Resolution 2.70 Å R-free 0.280

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

View Construct and Data Evidence

UniProt name	RAC1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–176； UniProt 1–176 Author chain D； PDBConstruct 1–176； UniProt 1–176

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	1he1
Deposition date deposition_date	2000-11-18
Structure title title	Crystal structure of the complex between the GAP domain of the Pseudomonas aeruginosa ExoS toxin and human Rac
Keywords keywords	;SIGNALING PROTEIN, SIGNALLING COMPLEX, EXOS, RAC, PSEUDOMONAS AERUGINOSA, GAP, TOXIN, VIRULENCE FACTOR, TRANSITION STATE, PROTEIN-PROTEIN COMPLEX, GTPASE, SIGNAL TRANSDUCTION ;; SIGNALING PROTEIN
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	29.43 Å
Radius of gyration Rg (electron density) rg_electron	29.02 Å
Forward intensity I(0) i0	78430700.00
Molecular weight molecular_weight	68839.0 kDa
Excluded volume excluded_volume	85914 Å³
Envelope volume envelope_volume	104830 Å³
Hydration-shell volume shell_volume	31158 Å³
Envelope diameter envelope_diameter	103.8 Å
Shell Rg shell_rg	34.80 Å
Envelope Rg envelope_rg	29.10 Å
Shape Rg shape_rg	29.03 Å
Total Rg total_rg	29.55 Å
Total atoms total_atoms	4812
Residues n_residues	622
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	99.1 Å
Rg (real space) rg_real	29.55 Å
Rg uncertainty (real space) rg_real_error	0.94 Å
I(0) (real space) i0_real	7.8430e+07
I(0) uncertainty (real space) i0_real_error	1.2010e+06
Rg (reciprocal space) rg_reciprocal	29.50 Å
I(0) (reciprocal space) i0_reciprocal	78430000.0000
Solution quality estimate total_estimate	0.8019
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.5 Å
Skewness Skewness skewness	0.444
Kurtosis Kurtosis kurtosis	-0.370
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	37560000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	EXOENZYME S
Molecular weight formula_weight	14261.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5525

ASSAVVFKQMVLQQALPMTLKGLDKASELATLTPEGLAREHSRLASGDGALRSLSTALAGIRAGSQVEESRIQAGRLLERSIGGIALQQWGTTGGAASQLVLDASPELRREITDQLHQVMSEVALLRQAVESEVS

来源 Source

来源生物 organism	PSEUDOMONAS AERUGINOSA
NCBI Class编号 ncbi_taxonomy_id	287
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1
Molecular weight formula_weight	19563.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

PQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAV

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 3 Entity 3 non-polymer

Description description	NICKEL (II) ION
Molecular weight formula_weight	58.7 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	GUANOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	443.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	ALUMINUM FLUORIDE
Molecular weight formula_weight	84.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	712

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1he1a1
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.11 — Bacterial GAP domain
Family Family family	a.24.11.1 — Bacterial GAP domain

Domain ID domain_id	d1he1a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1he1b1
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.11 — Bacterial GAP domain
Family Family family	a.24.11.1 — Bacterial GAP domain

Domain ID domain_id	d1he1b2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1he1c1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.8 — G proteins

Domain ID domain_id	d1he1c2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1he1d1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.8 — G proteins

Domain ID domain_id	d1he1d2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id	1he1A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	260 — Virulence factor YopE uncharacterised domain

Domain ID domain_id	1he1B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	260 — Virulence factor YopE uncharacterised domain

Domain ID domain_id	1he1C00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1he1D00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

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8. Citations (1)

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Unit-cell length a length_a	46.025 Å
Unit-cell length b length_b	125.087 Å
Unit-cell length c length_c	136.284 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	2.000 Å
Low-resolution limit resolution_low	29.920 Å
R factor r_factor	0.1750
R_work r_work	0.1750
R_free r_free	0.2240

fit	/app/data/saxs_computation/he/1he1/1he1.fit
pddf	/app/data/pr_computation/he/1he1/1he1.pr.out
profile	/app/data/saxs_computation/he/1he1/1he1.dat

Crystal structure of the complex between the GAP domain of the Pseudomonas aeruginosa ExoS toxin and human Rac

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

EXOENZYME S

State in the Current Structure

Other States of the Same Protein in the Database

RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)