SAXSdb — 3ths

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

Glycine N-methyltransferase

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 2–293 Chain B； UniProt 2–293 Chain C； UniProt 2–293 Chain D； UniProt 2–293	Non-standard monomer：Yes (specific site not provided by mmCIF)	BME BETA-MERCAPTOETHANOL × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；20% PEG 3350, 0.2 M Na-fluoride or Ca-acetate, 100 mM Tris-HCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.50 Å R-free 0.280

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 3THS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BHJ CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT) Deposited 1998-06-09	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.8；pH 6.8	Resolution 2.50 Å R-free 0.318
1D2C METHYLTRANSFERASE Deposited 1999-09-23	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 2–293（292 aa） Chain B 2–293（292 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.6；277 K；PEG 3400, pH 5.6, VAPOR DIFFUSION, temperature 4.0K	Resolution 2.50 Å R-free 0.233
1D2C METHYLTRANSFERASE Deposited 1999-09-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–293（292 aa） Chain B 2–293（292 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.6；277 K；PEG 3400, pH 5.6, VAPOR DIFFUSION, temperature 4.0K	Resolution 2.50 Å R-free 0.233
1D2G CRYSTAL STRUCTURE OF R175K MUTANT GLYCINE N-METHYLTRANSFERASE FROM RAT LIVER Deposited 1999-10-08	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 2–293（292 aa） Fragment：WHOLE ENZYME Chain B 2–293（292 aa） Fragment：WHOLE ENZYME	Mutation：R175K Mutation：R175K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；PEG-4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.50 Å R-free 0.266
1D2G CRYSTAL STRUCTURE OF R175K MUTANT GLYCINE N-METHYLTRANSFERASE FROM RAT LIVER Deposited 1999-10-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–293（292 aa） Fragment：WHOLE ENZYME Chain B 2–293（292 aa） Fragment：WHOLE ENZYME	Mutation：R175K Mutation：R175K	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；PEG-4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.50 Å R-free 0.266
1D2H CRYSTAL STRUCTURE OF R175K MUTANT GLYCINE N-METHYLTRANSFERASE COMPLEXED WITH S-ADENOSYLHOMOCYSTEINE Deposited 1999-10-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–293（292 aa） Fragment：WHOLE ENZYME Chain B 2–293（292 aa） Fragment：WHOLE ENZYME Chain C 2–293（292 aa） Fragment：WHOLE ENZYME Chain D 2–293（292 aa） Fragment：WHOLE ENZYME	Mutation：R175K Mutation：R175K Mutation：R175K Mutation：R175K	SAH S-ADENOSYL-L-HOMOCYSTEINE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；PEG-4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 3.00 Å R-free 0.247
1KIA Crystal structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate Deposited 2001-12-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa） Chain C 1–292（292 aa） Chain D 1–292（292 aa）	Not recorded	ACT ACETATE ION × 4 SAM S-ADENOSYLMETHIONINE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；PEG 6000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.80 Å R-free 0.286
1NBH Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace Deposited 2002-12-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa） Chain C 1–292（292 aa） Chain D 1–292（292 aa）	Not recorded	ACT ACETATE ION × 4 SAM S-ADENOSYLMETHIONINE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；296 K；PEG 3400, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.80 Å R-free 0.278
1NBI Structure of R175K mutated glycine N-methyltransferase complexed with S-adenosylmethionine, R175K:SAM. Deposited 2002-12-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa） Chain C 1–292（292 aa） Chain D 1–292（292 aa）	Mutation：R175K Mutation：R175K Mutation：R175K Mutation：R175K	SAM S-ADENOSYLMETHIONINE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；296 K；PEG 3400, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 3.00 Å R-free 0.295
1XVA METHYLTRANSFERASE Deposited 1996-07-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa）	Not recorded	ACT ACETATE ION × 4 SAM S-ADENOSYLMETHIONINE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；pH 5.6	Resolution 2.20 Å R-free 0.262
2IDJ Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form Deposited 2006-09-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa） Chain C 1–292（292 aa） Chain D 1–292（292 aa）	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；20% PEG 3350, 0.1 M Ca acetate, 0.025 M Tris, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.35 Å R-free 0.272
2IDK Crystal Structure of Rat Glycine N-Methyltransferase Complexed With Folate Deposited 2006-09-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–292（292 aa） Chain B 1–292（292 aa） Chain C 1–292（292 aa） Chain D 1–292（292 aa）	Not recorded	C2F 5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；20% PEG 3350, 0.1 M Ca acetate, 0.025 M Tris, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.55 Å R-free 0.298
3THR Crystal structure of rat native liver Glycine N-methyltransferase complexed with 5-methyltetrahydrofolate monoglutamate Deposited 2011-08-19	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–293（292 aa） Chain B 2–293（292 aa） Chain C 2–293（292 aa） Chain D 2–293（292 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	C2F 5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID × 4 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；20% PEG 3350, 0.2 M Na-fluoride or Ca-acetate, 100 mM Tris-HCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K	Resolution 2.00 Å R-free 0.241

11 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GNMT_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–293； UniProt 2–293 Author chain B； PDBConstruct 2–293； UniProt 2–293 Author chain C； PDBConstruct 2–293； UniProt 2–293 Author chain D； PDBConstruct 2–293； UniProt 2–293

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	3ths
Deposition date deposition_date	2011-08-19
Structure title title	Crystal structure of rat native liver Glycine N-methyltransferase complexed with 5-methyltetrahydrofolate pentaglutamate
Keywords keywords	Glycine N-methyltransferase, GNMT, Folate, Folate binding, Transferase, TRANSFERASE-TRANSFERASE INHIBITOR complex; TRANSFERASE/TRANSFERASE INHIBITOR
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	35.54 Å
Radius of gyration Rg (electron density) rg_electron	35.00 Å
Forward intensity I(0) i0	483945000.00
Molecular weight molecular_weight	118770.0 kDa
Excluded volume excluded_volume	114660 Å³
Envelope volume envelope_volume	204220 Å³
Hydration-shell volume shell_volume	47574 Å³
Envelope diameter envelope_diameter	111.3 Å
Shell Rg shell_rg	42.62 Å
Envelope Rg envelope_rg	34.37 Å
Shape Rg shape_rg	34.99 Å
Total Rg total_rg	35.37 Å
Total atoms total_atoms	8999
Residues n_residues	1135
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	111.9 Å
Rg (real space) rg_real	35.44 Å
Rg uncertainty (real space) rg_real_error	0.65 Å
I(0) (real space) i0_real	4.8390e+08
I(0) uncertainty (real space) i0_real_error	7.5400e+06
Rg (reciprocal space) rg_reciprocal	35.51 Å
I(0) (reciprocal space) i0_reciprocal	484000000.0000
Solution quality estimate total_estimate	0.6911
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	47.2 Å
Skewness Skewness skewness	0.160
Kurtosis Kurtosis kurtosis	-0.659
Angular range angular_range	— – 0.2250 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	160200000.0000
Real-space data points n_real_points	46
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 1.000; Smooth: 0.950

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Glycine N-methyltransferase
Molecular weight formula_weight	32486.9 kDa
EC 编号 ec_number	2.1.1.20
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	9091

XVDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG

Entity 2 Entity 2 polymer

Description description	5-methyltetrahydrofolate pentaglutamate
Molecular weight formula_weight	975.9 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F

XEEEEE

Entity 3 Entity 3 non-polymer

Description description	BETA-MERCAPTOETHANOL
Molecular weight formula_weight	78.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	TRIS(HYDROXYETHYL)AMINOMETHANE
Molecular weight formula_weight	163.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	88

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3thsa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamily	c.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family family	c.66.1.5 — Glycine N-methyltransferase

Domain ID domain_id	d3thsb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamily	c.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family family	c.66.1.5 — Glycine N-methyltransferase

Domain ID domain_id	d3thsc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamily	c.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family family	c.66.1.5 — Glycine N-methyltransferase

Domain ID domain_id	d3thsd_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamily	c.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family family	c.66.1.5 — Glycine N-methyltransferase

CATH v4.4 (8 domains)

Domain ID domain_id	3thsA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	46 — Glycine N-methyltransferase; chain A, domain 1
Homologous superfamily homologous superfamily	10 — Glycine N-methyltransferase, chain A, domain 1

Domain ID domain_id	3thsA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	150 — Vaccinia Virus protein VP39

Domain ID domain_id	3thsB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	46 — Glycine N-methyltransferase; chain A, domain 1
Homologous superfamily homologous superfamily	10 — Glycine N-methyltransferase, chain A, domain 1

Domain ID domain_id	3thsB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	150 — Vaccinia Virus protein VP39

Domain ID domain_id	3thsC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	46 — Glycine N-methyltransferase; chain A, domain 1
Homologous superfamily homologous superfamily	10 — Glycine N-methyltransferase, chain A, domain 1

Domain ID domain_id	3thsC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	150 — Vaccinia Virus protein VP39

Domain ID domain_id	3thsD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	46 — Glycine N-methyltransferase; chain A, domain 1
Homologous superfamily homologous superfamily	10 — Glycine N-methyltransferase, chain A, domain 1

Domain ID domain_id	3thsD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	150 — Vaccinia Virus protein VP39

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8. Citations (1)

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Unit-cell length a length_a	193.036 Å
Unit-cell length b length_b	61.047 Å
Unit-cell length c length_c	146.352 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	128.92 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	48.220 Å
R factor r_factor	0.2303
R_work r_work	0.2278
R_free r_free	0.2798

fit	/app/data/saxs_computation/th/3ths/3ths.fit
pddf	/app/data/pr_computation/th/3ths/3ths.pr.out
profile	/app/data/saxs_computation/th/3ths/3ths.dat

Crystal structure of rat native liver Glycine N-methyltransferase complexed with 5-methyltetrahydrofolate pentaglutamate

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

Glycine N-methyltransferase

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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)