SAXSdb — 9m8n

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

Transient receptor potential cation channel subfamily A member 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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–1119 Chain B； UniProt 1–1119 Chain C； UniProt 1–1119 Chain D； UniProt 1–1119	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.81 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 9M8N	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3J9P Structure of the TRPA1 ion channel determined by electron cryo-microscopy Deposited 2015-02-14	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–1119（1118 aa） Fragment：SEE REMARK 999 Chain B 2–1119（1118 aa） Fragment：SEE REMARK 999 Chain C 2–1119（1118 aa） Fragment：SEE REMARK 999 Chain D 2–1119（1118 aa） Fragment：SEE REMARK 999	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM HEPES, 150 mM NaCl, 1 mM DTT, 1 mM IP6；pH 8；20 mM HEPES, 150 mM NaCl, 1 mM DTT, 1 mM IP6 cryo-EM vitrification conditions Blot for 7 seconds before plunging.；120 K；Cryogen ETHANE；Blot for 7 seconds before plunging into liquid ethane (FEI VITROBOT MARK I).	Resolution 4.24 Å
6HC8 Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPA1 (313-339) Deposited 2018-08-14	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 313–339（27 aa）	Not recorded	ZN ZINC ION × 2 OGA N-OXALYLGLYCINE × 2 SO4 SULFATE ION × 2 GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1 M Hepes pH = 7.5, 1.6 M ammonium sulfate, 6% PEG400	Resolution 1.90 Å R-free 0.189
6PQO Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist JT010 Deposited 2019-07-09	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–1119（1118 aa） Chain B 2–1119（1118 aa） Chain C 2–1119（1118 aa） Chain D 2–1119（1118 aa）	Not recorded	JT0 2-chloro-N-[4-(4-methoxyphenyl)-1,3-thiazol-2-yl]-N-(3-methoxypropyl)acetamide × 4 LBN 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine × 8 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 16	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.88 Å
6PQP Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist BITC Deposited 2019-07-09	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–1119（1118 aa） Chain B 2–1119（1118 aa） Chain C 2–1119（1118 aa） Chain D 2–1119（1118 aa）	Not recorded	9BE N-benzylthioformamide × 4 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 20 LBN 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.06 Å
6PQQ Cryo-EM structure of human TRPA1 C621S mutant in the apo state Deposited 2019-07-09	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–1119（1118 aa） Chain B 2–1119（1118 aa） Chain C 2–1119（1118 aa） Chain D 2–1119（1118 aa）	Mutation：C621S Mutation：C621S Mutation：C621S Mutation：C621S	LBN 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine × 8 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.81 Å
6V9V Structure of TRPA1 modified by Bodipy-iodoacetamide with bound calcium, LMNG Deposited 2019-12-16	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1119（1119 aa） Chain B 1–1119（1119 aa） Chain C 1–1119（1119 aa） Chain D 1–1119（1119 aa）	Mutation：D966E Mutation：D966E Mutation：D966E Mutation：D966E	QT4 ~{N}-[[2,2-bis(fluoranyl)-10,12-dimethyl-1,3-diaza-2$l^{4}-boratricyclo[7.3.0.0^{3,7}]dodeca-4,6,9,11-tetraen-4-yl]methyl]ethanamide × 4 CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
6V9W Structure of TRPA1 (ligand-free) with bound calcium, LMNG Deposited 2019-12-16	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1119（1119 aa） Chain B 1–1119（1119 aa） Chain C 1–1119（1119 aa） Chain D 1–1119（1119 aa）	Mutation：D966E Mutation：D966E Mutation：D966E Mutation：D966E	CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
6V9X Structure of TRPA1 modified by iodoacetamide, PMAL-C8 Deposited 2019-12-16	Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1119（1119 aa） Chain B 1–1119（1119 aa） Chain C 1–1119（1119 aa） Chain D 1–1119（1119 aa）	Mutation：D966E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D966E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D966E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：D966E Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
6V9Y Structure of TRPA1 bound with A-967079, PMAL-C8 Deposited 2019-12-16	Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1119（1119 aa） Chain B 1–1119（1119 aa） Chain C 1–1119（1119 aa） Chain D 1–1119（1119 aa）	Mutation：D966E Mutation：D966E Mutation：D966E Mutation：D966E	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
6WJ5 Structure of human TRPA1 in complex with inhibitor GDC-0334 Deposited 2020-04-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 448–1078（631 aa） Chain B 448–1078（631 aa） Chain C 448–1078（631 aa） Chain D 448–1078（631 aa）	Not recorded	LXY (4R,5S)-4-fluoro-1-[(4-fluorophenyl)sulfonyl]-5-methyl-N-({5-(trifluoromethyl)-2-[2-(trifluoromethyl)pyrimidin-5-yl]pyridin-4-yl}methyl)-L-prolinamide × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8.2 cryo-EM vitrification conditions Cryogen ETHANE；2 x 4s blot time	Resolution 3.60 Å
6X2J Structure of human TRPA1 in complex with agonist GNE551 Deposited 2020-05-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 448–1078（631 aa） Chain B 448–1078（631 aa） Chain C 448–1078（631 aa） Chain D 448–1078（631 aa）	Not recorded	ULJ 5-amino-1-[(4-bromo-2-fluorophenyl)methyl]-N-(2,5-dimethoxyphenyl)-1H-1,2,3-triazole-4-carboxamide × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8.2 cryo-EM vitrification conditions Cryogen ETHANE；Triple blot. Put blot in vitroblot Apply 3.5ul to grid, wait 30sec, blot manually Apply 3.5ul to grid, wait 30sec, blot manually, apply final 3.5ul, final blot by vitrobot (3.5s)	Resolution 3.00 Å
7JUP Structure of human TRPA1 in complex with antagonist compound 21 Deposited 2020-08-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 448–1078（631 aa） Chain B 448–1078（631 aa） Chain C 448–1078（631 aa） Chain D 448–1078（631 aa）	Not recorded	VKM 1-({3-[(3R,5R)-5-(4-fluorophenyl)oxolan-3-yl]-1,2,4-oxadiazol-5-yl}methyl)-7-methyl-1,7-dihydro-6H-purin-6-one × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8.2 cryo-EM vitrification conditions Cryogen ETHANE；Triple blot. Put blot in vitroblot Apply 3.5ul to grid, wait 30sec, blot manually Apply 3.5ul to grid, wait 30sec, blot manually, apply final 3.5ul, final blot by vitrobot (3.5s)	Resolution 3.05 Å
7OR0 Cryo-EM structure of the human TRPA1 ion channel in complex with the antagonist 3-60, conformation 2 Deposited 2021-06-04	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1119（1119 aa） Chain B 1–1119（1119 aa） Chain C 1–1119（1119 aa） Chain D 1–1119（1119 aa）	Not recorded	0IG ~{N}-[4-[4-[(azanylidene-$l^{4}-azanylidene)amino]phenyl]-1,3-thiazol-2-yl]-2-[1,3-dimethyl-2,6-bis(oxidanylidene)purin-7-yl]ethanamide × 4 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 8 CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 IHP INOSITOL HEXAKISPHOSPHATE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.64 Å
7OR1 Cryo-EM structure of the human TRPA1 ion channel in complex with the antagonist 3-60, conformation 1 Deposited 2021-06-04	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1119（1119 aa） Chain B 1–1119（1119 aa） Chain C 1–1119（1119 aa） Chain D 1–1119（1119 aa）	Not recorded	0IG ~{N}-[4-[4-[(azanylidene-$l^{4}-azanylidene)amino]phenyl]-1,3-thiazol-2-yl]-2-[1,3-dimethyl-2,6-bis(oxidanylidene)purin-7-yl]ethanamide × 4 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 8 CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 IHP INOSITOL HEXAKISPHOSPHATE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.64 Å
9M8S Cryo-EM structure of the human TRPA1 ion channel in ligand-free state. Deposited 2025-03-12	Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1119（1119 aa） Chain B 1–1119（1119 aa） Chain C 1–1119（1119 aa） Chain D 1–1119（1119 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9MOE Preclinical and clinical evaluation of a novel TRPA1 antagonist LY3526318 Deposited 2024-12-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–1119（1118 aa） Chain B 2–1119（1118 aa） Chain D 2–1119（1118 aa） Chain E 2–1119（1118 aa）	Not recorded	A1BNO (2S)-2-{3-methyl-1-[(3-methyl-1,2,4-oxadiazol-5-yl)methyl]-2,6-dioxo-1,2,3,6-tetrahydro-7H-purin-7-yl}-N-{6-[2-(trifluoromethyl)pyrimidin-5-yl]pyridin-2-yl}propanamide × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8；20 mM HEPES, pH 8, 150 mM NaCl, 0.5 mM TCEP and 0.01% LMNG cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TRPA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–1119； UniProt 1–1119 Author chain B； PDBConstruct 1–1119； UniProt 1–1119 Author chain C； PDBConstruct 1–1119； UniProt 1–1119 Author chain D； PDBConstruct 1–1119； UniProt 1–1119

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	9m8n
Deposition date deposition_date	2025-03-12
最后修订 last_revision	2025-10-29
Structure title title	Cryo-EM structure of the human TRPA1 ion channel in complex with crotalphine.
Keywords keywords	TRANSPORT PROTEIN, MEMBRANE PROTEIN; MEMBRANE PROTEIN
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	45.27 Å
Radius of gyration Rg (electron density) rg_electron	44.83 Å
Forward intensity I(0) i0	782838000.00
Molecular weight molecular_weight	250350.0 kDa
Excluded volume excluded_volume	321440 Å³
Envelope volume envelope_volume	460400 Å³
Hydration-shell volume shell_volume	83351 Å³
Envelope diameter envelope_diameter	144.8 Å
Shell Rg shell_rg	51.84 Å
Envelope Rg envelope_rg	43.41 Å
Shape Rg shape_rg	44.86 Å
Total Rg total_rg	45.04 Å
Total atoms total_atoms	17620
Residues n_residues	2208
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	139.1 Å
Rg (real space) rg_real	45.08 Å
Rg uncertainty (real space) rg_real_error	0.84 Å
I(0) (real space) i0_real	7.8280e+08
I(0) uncertainty (real space) i0_real_error	1.1210e+07
Rg (reciprocal space) rg_reciprocal	45.26 Å
I(0) (reciprocal space) i0_reciprocal	783000000.0000
Solution quality estimate total_estimate	0.8686
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	51.6 Å
Skewness Skewness skewness	0.219
Kurtosis Kurtosis kurtosis	-0.423
Angular range angular_range	— – 0.1750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	70060000.0000
Real-space data points n_real_points	36
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.524

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Description description	Transient receptor potential cation channel subfamily A member 1
Molecular weight formula_weight	127660.6 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	17620

MKRSLRKMWRPGEKKEPQGVVYEDVPDDTEDFKESLKVVFEGSAYGLQNFNKQKKLKRCDDMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYSGSVDIVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRWDECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHSTEDKSCRDYYIEYNFKYLQCPLEFTKKTPTQDVIYEPLTALNAMVQNNRIELLNHPVCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIKPGMAFNSTGIINETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQKRNYFMDISNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFENCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSSPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIAEVQKHASLKRIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHIFCFLFCTGEIRQEIPNADKSLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISETEDDDSHCSFQDRFKKEQMEQRNSRWNTVLRAVKAKTHHLEP

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	Homo sapiens

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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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	3.81 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	203880

fit	/app/data/saxs_computation/m8/9m8n/9m8n.fit
pddf	/app/data/pr_computation/m8/9m8n/9m8n.pr.out
profile	/app/data/saxs_computation/m8/9m8n/9m8n.dat

Cryo-EM structure of the human TRPA1 ion channel in complex with crotalphine.

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

Transient receptor potential cation channel subfamily A member 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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)