SAXSdb — 7zyh

▼

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

Cleavage and polyadenylation specificity factor subunit 4

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 118–178	Not recorded	;Isoform 4 of Pre-mRNA 3'-end-processing factor FIP1 ; × 2 （Q6UN15-4） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；292.15 K；1.626 M (NH4)SO4, 0.1 M Bis-Tris pH 6.5	Resolution 2.20 Å R-free 0.264
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 118–178	Not recorded	;Isoform 4 of Pre-mRNA 3'-end-processing factor FIP1 ; × 2 （Q6UN15-4） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；292.15 K；1.626 M (NH4)SO4, 0.1 M Bis-Tris pH 6.5	Resolution 2.20 Å R-free 0.264
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain G； UniProt 118–178	Not recorded	;Isoform 4 of Pre-mRNA 3'-end-processing factor FIP1 ; × 2 （Q6UN15-4） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；292.15 K；1.626 M (NH4)SO4, 0.1 M Bis-Tris pH 6.5	Resolution 2.20 Å R-free 0.264
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain J； UniProt 118–178	Not recorded	;Isoform 4 of Pre-mRNA 3'-end-processing factor FIP1 ; × 2 （Q6UN15-4） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；292.15 K；1.626 M (NH4)SO4, 0.1 M Bis-Tris pH 6.5	Resolution 2.20 Å R-free 0.264

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 7ZYH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2D9N Solution structure of CCCH type zinc-finger domain 2 in Cleavage and polyadenylation specificity factor Deposited 2005-12-12	Different construct 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 61–126（66 aa） Fragment：CCCH-type zinc finger motif	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100mM；Pressure ambient NMR sample composition 20mM d-Tris-HCl(pH7.0), 100mM NaCl, 1mM d-DTT, 0.02% NaN3, 50uM ZnCl2+1mM IDA, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2RHK Crystal structure of influenza A NS1A protein in complex with F2F3 fragment of human cellular factor CPSF30, Northeast Structural Genomics Targets OR8C and HR6309A Deposited 2007-10-09	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 C 61–121（61 aa） Fragment：F2F3 Zinc-binding domains (UNP residues 61-121) Chain D 61–121（61 aa） Fragment：F2F3 Zinc-binding domains (UNP residues 61-121)	Mutation：P94S Mutation：P94S	NO3 NITRATE ION × 5 ZN ZINC ION × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；293 K；0.5 M KNO3, 10% sucroes, 0.1M sodium acitate, pH 5.5, EVAPORATION, temperature 293K, pH 5.50	Resolution 1.95 Å R-free 0.234
2RHK Crystal structure of influenza A NS1A protein in complex with F2F3 fragment of human cellular factor CPSF30, Northeast Structural Genomics Targets OR8C and HR6309A Deposited 2007-10-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 61–121（61 aa） Fragment：F2F3 Zinc-binding domains (UNP residues 61-121) Chain D 61–121（61 aa） Fragment：F2F3 Zinc-binding domains (UNP residues 61-121)	Mutation：P94S Mutation：P94S	NO3 NITRATE ION × 9 ZN ZINC ION × 6 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；293 K；0.5 M KNO3, 10% sucroes, 0.1M sodium acitate, pH 5.5, EVAPORATION, temperature 293K, pH 5.50	Resolution 1.95 Å R-free 0.234
2RHK Crystal structure of influenza A NS1A protein in complex with F2F3 fragment of human cellular factor CPSF30, Northeast Structural Genomics Targets OR8C and HR6309A Deposited 2007-10-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 61–121（61 aa） Fragment：F2F3 Zinc-binding domains (UNP residues 61-121) Chain D 61–121（61 aa） Fragment：F2F3 Zinc-binding domains (UNP residues 61-121)	Mutation：P94S Mutation：P94S	NO3 NITRATE ION × 5 ZN ZINC ION × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；293 K；0.5 M KNO3, 10% sucroes, 0.1M sodium acitate, pH 5.5, EVAPORATION, temperature 293K, pH 5.50	Resolution 1.95 Å R-free 0.234
2RHK Crystal structure of influenza A NS1A protein in complex with F2F3 fragment of human cellular factor CPSF30, Northeast Structural Genomics Targets OR8C and HR6309A Deposited 2007-10-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 61–121（61 aa） Fragment：F2F3 Zinc-binding domains (UNP residues 61-121)	Mutation：P94S	NO3 NITRATE ION × 4 ZN ZINC ION × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；293 K；0.5 M KNO3, 10% sucroes, 0.1M sodium acitate, pH 5.5, EVAPORATION, temperature 293K, pH 5.50	Resolution 1.95 Å R-free 0.234
6DNH Cryo-EM structure of human CPSF-160-WDR33-CPSF-30-PAS RNA complex at 3.4 A resolution Deposited 2018-06-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–244（244 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9；25 mM Tris-HCl, pH 7.9, 380 mM NaCl, 5 mM DTT cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
6FUW Cryo-EM structure of the human CPSF160-WDR33-CPSF30 complex bound to the PAS AAUAAA motif at 3.1 Angstrom resolution Deposited 2018-02-28	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–178（178 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；15 seconds wait time prior to blotting	Resolution 3.07 Å
6URG Cryo-EM structure of human CPSF160-WDR33-CPSF30-CPSF100 PIM complex Deposited 2019-10-23	Different construct 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 C 1–244（244 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5 mM DTT cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
6URO Cryo-EM structure of human CPSF160-WDR33-CPSF30-PAS RNA-CstF77 complex Deposited 2019-10-23	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 5 PDB declaration: hexameric	Chain C 1–244（244 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5 mM DTT cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
8E3I CRYO-EM STRUCTURE OF the human MPSF IN COMPLEX WITH THE AUUAAA poly(A) signal Deposited 2022-08-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–244（244 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM Tris (pH 8.0), 150 mM NaCl, and 5 mM DTT cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.53 Å
8E3Q CRYO-EM STRUCTURE OF the human MPSF Deposited 2022-08-17	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–244（244 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8；25 mM Tris (pH 8.0), 150 mM NaCl, and 5 mM DTT cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.68 Å
8R8R Cryo-EM structure of the human mPSF with PAPOA C-terminus peptide (PAPOAc) Deposited 2023-11-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 4 PDB declaration: pentameric	Chain C 2–244（243 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.9 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.79 Å
9OXE CRYO-EM STRUCTURE OF the human mPSF IN COMPLEX WITH THE AGUAAA poly(A) signal Deposited 2025-06-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–244（244 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.53 Å
9OXS CRYO-EM STRUCTURE OF the human mPSF IN COMPLEX WITH THE AAUAAU poly(A) signal Deposited 2025-06-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–244（244 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CPSF4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–64； UniProt 118–178 Author chain D； PDBConstruct 4–64； UniProt 118–178 Author chain G； PDBConstruct 4–64； UniProt 118–178 Author chain J； PDBConstruct 4–64； UniProt 118–178

;Isoform 4 of Pre-mRNA 3'-end-processing factor FIP1 ;

Homo sapiens

UniProt Q6UN15-4

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 130–195 Chain C； UniProt 130–195	Not recorded	Cleavage and polyadenylation specificity factor subunit 4 × 1 （O95639） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；292.15 K；1.626 M (NH4)SO4, 0.1 M Bis-Tris pH 6.5	Resolution 2.20 Å R-free 0.264
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain E； UniProt 130–195 Chain F； UniProt 130–195	Not recorded	Cleavage and polyadenylation specificity factor subunit 4 × 1 （O95639） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；292.15 K；1.626 M (NH4)SO4, 0.1 M Bis-Tris pH 6.5	Resolution 2.20 Å R-free 0.264
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain H； UniProt 130–195 Chain I； UniProt 130–195	Not recorded	Cleavage and polyadenylation specificity factor subunit 4 × 1 （O95639） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；292.15 K；1.626 M (NH4)SO4, 0.1 M Bis-Tris pH 6.5	Resolution 2.20 Å R-free 0.264
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain K； UniProt 130–195 Chain L； UniProt 130–195	Not recorded	Cleavage and polyadenylation specificity factor subunit 4 × 1 （O95639） ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；292.15 K；1.626 M (NH4)SO4, 0.1 M Bis-Tris pH 6.5	Resolution 2.20 Å R-free 0.264

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	FIP1-4_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 4–69； UniProt 130–195 Author chain C； PDBConstruct 4–69； UniProt 130–195 Author chain E； PDBConstruct 4–69； UniProt 130–195 Author chain F； PDBConstruct 4–69； UniProt 130–195 Author chain H； PDBConstruct 4–69； UniProt 130–195 Author chain I； PDBConstruct 4–69； UniProt 130–195 Author chain K； PDBConstruct 4–69； UniProt 130–195 Author chain L； PDBConstruct 4–69； UniProt 130–195

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	7zyh
Deposition date deposition_date	2022-05-24
Structure title title	Crystal structure of human CPSF30 in complex with hFip1
Keywords keywords	;Complex, 3' end processing, CPSF, GENE REGULATION ;; GENE REGULATION
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	27.95 Å
Radius of gyration Rg (electron density) rg_electron	27.18 Å
Forward intensity I(0) i0	77069800.00
Molecular weight molecular_weight	66174.0 kDa
Excluded volume excluded_volume	81690 Å³
Envelope volume envelope_volume	109410 Å³
Hydration-shell volume shell_volume	33568 Å³
Envelope diameter envelope_diameter	88.4 Å
Shell Rg shell_rg	34.61 Å
Envelope Rg envelope_rg	27.08 Å
Shape Rg shape_rg	27.16 Å
Total Rg total_rg	28.05 Å
Total atoms total_atoms	8977
Residues n_residues	552
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

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	83.8 Å
Rg (real space) rg_real	27.74 Å
Rg uncertainty (real space) rg_real_error	0.39 Å
I(0) (real space) i0_real	7.7070e+07
I(0) uncertainty (real space) i0_real_error	1.0240e+06
Rg (reciprocal space) rg_reciprocal	27.81 Å
I(0) (reciprocal space) i0_reciprocal	77070000.0000
Solution quality estimate total_estimate	0.9068
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	38.2 Å
Skewness Skewness skewness	0.076
Kurtosis Kurtosis kurtosis	-0.477
Angular range angular_range	— – 0.2850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8319000.0000
Real-space data points n_real_points	58
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.966

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Cleavage and polyadenylation specificity factor subunit 4
Molecular weight formula_weight	7482.7 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D,G,J
Atom count atom_count	9075

SNAESKIKDCPWYDRGFCKHGPLCRHRHTRRVICVNYLVGFCPEGPSCKFMHPRFELPMGTTEQ

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 polymer

Description description	;Isoform 4 of Pre-mRNA 3'-end-processing factor FIP1 ;
Molecular weight formula_weight	7865.8 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,C,E,F,H,I,K,L

SNAGSINGVPLLEVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIRMGLEVIPVTSTTNK

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	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	98

▶

8. Citations (1)

▶

Unit-cell length a length_a	60.127 Å
Unit-cell length b length_b	115.125 Å
Unit-cell length c length_c	66.444 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	116.78 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

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

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	48.650 Å
R factor r_factor	0.2498
R_work r_work	0.2472
R_free r_free	0.2644

fit	/app/data/saxs_computation/zy/7zyh/7zyh.fit
pddf	/app/data/pr_computation/zy/7zyh/7zyh.pr.out
profile	/app/data/saxs_computation/zy/7zyh/7zyh.dat

Crystal structure of human CPSF30 in complex with hFip1

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

Cleavage and polyadenylation specificity factor subunit 4

State in the Current Structure

Other States of the Same Protein in the Database

;Isoform 4 of Pre-mRNA 3'-end-processing factor FIP1 ;

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 (4)

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 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)