SAXSdb — 1i89

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

CHALCONE SYNTHASE 2

Medicago sativa

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–389 Chain B； UniProt 1–389	Mutation：G256L Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.86 Å R-free 0.259

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 1I89	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BI5 CHALCONE SYNTHASE FROM ALFALFA Deposited 1998-06-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.56 Å R-free 0.193
1BQ6 CHALCONE SYNTHASE FROM ALFALFA WITH COENZYME A Deposited 1998-08-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–389（388 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2 COA COENZYME A × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.56 Å R-free 0.212
1CGK CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH NARINGENIN Deposited 1999-03-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Not recorded	NAR NARINGENIN × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；THE DROPLE CONSISTED ON 25 MGR/ML (FINAL CONCENTRATION) PROTEIN MIXED WITH THE RESERVOIR WHICH CONTAINED 2.4 M AMMONIUM SULFATE, 100 MM PIPES BUFFER (PH 6.5) , IN THE PRESENCE (UP TO 5 MM) OR ABSENCE OF DTT REDUCING AGENT. CRYSTALS WERE STABILIZED IN 40% (V/V) PEG400, 100 MM PIPES 16 MM NARINGENIN PRIOR TO FREEZING AT 105 K, pH 6.50	Resolution 1.84 Å R-free 0.225
1CGZ CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH RESVERATROL Deposited 1999-03-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Not recorded	STL RESVERATROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.50	Resolution 1.70 Å R-free 0.217
1CHW CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH HEXANOYL-COA Deposited 1999-03-30	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：C164S Mutation：C164S	HXC HEXANOYL-COENZYME A × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；THE CRYSTALS WERE OBTAINED OVERNIGHT AT 4 C HANGING-DROP VAPOR DIFFUSION METHOD. THE DROPLET CONSISTED ON 25 MGR/ML (FINAL CONCENTRATION) PROTEIN MIXED WITH THE RESERVOIR WHICH CONTAINED 2.4 M AMMONIUM SULFATE, 100 MM PIPES BUFFER (PH 6.5), IN THE PRESENCE (UP TO 5 MM) OR ABSENCE OF DTT REDUCING AGENT. CRYSTALS WERE STABILIZED IN 40% (V/V) PEG400, 100 MM PIPES AND 20 MM HEXANOYL-COA PRIOR TO FREEZING AT 105 K.	Resolution 1.90 Å R-free 0.290
1CML CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH MALONYL-COA Deposited 1999-03-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Mutation：C164A	SO4 SULFATE ION × 2 MLC MALONYL-COENZYME A × 2 PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID) × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.50	Resolution 1.69 Å R-free 0.200
1D6F CHALCONE SYNTHASE C164A MUTANT Deposited 1999-10-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Mutation：C164A	SO4 SULFATE ION × 2 B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 1.69 Å R-free 0.201
1D6H CHALONE SYNTHASE (N336A MUTANT COMPLEXED WITH COA) Deposited 1999-10-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 3–389（387 aa）	Mutation：N336A Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2 COA COENZYME A × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.15 Å R-free 0.257
1D6I CHALCONE SYNTHASE (H303Q MUTANT) Deposited 1999-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–389（388 aa） Fragment：CHS Chain B 2–389（388 aa） Fragment：CHS	Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.00 Å R-free 0.269
1D6I CHALCONE SYNTHASE (H303Q MUTANT) Deposited 1999-10-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–389（388 aa） Fragment：CHS Chain B 2–389（388 aa） Fragment：CHS	Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.00 Å R-free 0.269
1I86 CHALCONE SYNTHASE, G256A MUTANT Deposited 2001-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Mutation：CHALCONE SYNTHASE (G256A) Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 100 mM PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.50 Å R-free 0.221
1I88 CHALCONE SYNTHASE (G256V) Deposited 2001-03-12	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：G256V Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G256V Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.45 Å R-free 0.221
1I8B Chalcone synthase (G256F) Deposited 2001-03-12	Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：G256F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G256F Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.251
1JWX Chalcone Synthase--F215S mutant Deposited 2001-09-05	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Mutation：F215S Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；ammonium sulfate, PIPES, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.63 Å R-free 0.225
1U0V An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization of Specificity of Type III Polyketide Synthases: 18xCHS structure Deposited 2004-07-14	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.227
1U0W An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization Specificity of Type III Polyketide Synthases: 18xCHS+resveratrol Structure Deposited 2004-07-14	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D	STL RESVERATROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, resveratrol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.264
1U0W An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization Specificity of Type III Polyketide Synthases: 18xCHS+resveratrol Structure Deposited 2004-07-14	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–389（389 aa） Chain D 1–389（389 aa）	Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D	STL RESVERATROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, resveratrol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.264

15 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CHS2_MEDSA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–389； UniProt 1–389 Author chain B； PDBConstruct 1–389； UniProt 1–389

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	1i89
Deposition date deposition_date	2001-03-12
Structure title title	Chalcone synthase (G256L)
Keywords keywords	chalcone synthase, polyketide synthase, TRANSFERASE; TRANSFERASE
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	36.49 Å
Radius of gyration Rg (electron density) rg_electron	36.24 Å
Forward intensity I(0) i0	108074000.00
Molecular weight molecular_weight	85321.0 kDa
Excluded volume excluded_volume	107620 Å³
Envelope volume envelope_volume	136470 Å³
Hydration-shell volume shell_volume	33073 Å³
Envelope diameter envelope_diameter	120.8 Å
Shell Rg shell_rg	39.99 Å
Envelope Rg envelope_rg	35.88 Å
Shape Rg shape_rg	36.23 Å
Total Rg total_rg	36.53 Å
Total atoms total_atoms	5986
Residues n_residues	774
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	122.3 Å
Rg (real space) rg_real	36.81 Å
Rg uncertainty (real space) rg_real_error	1.22 Å
I(0) (real space) i0_real	1.0810e+08
I(0) uncertainty (real space) i0_real_error	2.0040e+06
Rg (reciprocal space) rg_reciprocal	36.62 Å
I(0) (reciprocal space) i0_reciprocal	108100000.0000
Solution quality estimate total_estimate	0.7878
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	28.4 Å
Skewness Skewness skewness	0.405
Kurtosis Kurtosis kurtosis	-0.750
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23860000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.641; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.508; Smooth: 0.806

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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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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1i89a1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.2 — Chalcone synthase-like

Domain ID domain_id	d1i89a2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.2 — Chalcone synthase-like

Domain ID domain_id	d1i89b1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.2 — Chalcone synthase-like

Domain ID domain_id	d1i89b2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.2 — Chalcone synthase-like

CATH v4.4 (4 domains)

Domain ID domain_id	1i89A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

Domain ID domain_id	1i89A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

Domain ID domain_id	1i89B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

Domain ID domain_id	1i89B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

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8. Citations (1)

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Unit-cell length a length_a	98.103 Å
Unit-cell length b length_b	98.103 Å
Unit-cell length c length_c	131.132 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	1.860 Å
Low-resolution limit resolution_low	31.200 Å
R factor r_factor	—
R_work r_work	0.2150
R_free r_free	0.2590

Description description	CHALCONE SYNTHASE 2
Molecular weight formula_weight	42843.4 kDa
EC 编号 ec_number	2.3.1.74
Mutation mutation	G256L
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6433

Chalcone synthase (G256L)

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

CHALCONE SYNTHASE 2

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Medicago sativa
NCBI Class编号 ncbi_taxonomy_id	3879
宿主生物 host_organism	Escherichia coli BL21

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	447

fit	/app/data/saxs_computation/i8/1i89/1i89.fit
pddf	/app/data/pr_computation/i8/1i89/1i89.pr.out
profile	/app/data/saxs_computation/i8/1i89/1i89.dat