SAXSdb — 9dt4

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

Sulfonylurea repressor CsR (L4.2-20)

Escherichia coli

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 1–207 Chain B； UniProt 1–207	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；0.2 M Sodium acetate 0.1 M TRIS hydrochloride pH 8.5 30% w/v Polyethylene glycol 4,000	Resolution 2.40 Å R-free 0.241

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 9DT4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2NS7 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–187（187 aa） Chain B 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；1.4M ammonium sulfate, 0.1M sodium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.40 Å R-free 0.277
2NS7 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–187（187 aa） Chain D 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；1.4M ammonium sulfate, 0.1M sodium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.40 Å R-free 0.277
2NS8 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–187（187 aa） Chain B 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；292 K；4M sodium formate, 0.1M Tris-HCl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.55 Å R-free 0.270
2NS8 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–187（187 aa） Chain D 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；292 K；4M sodium formate, 0.1M Tris-HCl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.55 Å R-free 0.270
2NS8 How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor Deposited 2006-11-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 1–187（187 aa） Chain B 1–187（187 aa） Chain C 1–187（187 aa） Chain D 1–187（187 aa）	Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S Mutation：C68S, C88N, C121T, C144S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；292 K；4M sodium formate, 0.1M Tris-HCl, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.55 Å R-free 0.270
2VKV TetR (BD) variant L17G with reverse phenotype Deposited 2008-01-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	TDC 5A,6-ANHYDROTETRACYCLINE × 2 MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.7；277 K；0.1 M TRIS-HCL (PH 8.7), 0.3 M MGCL2, 20 % PEG 4000, 3 % DIOXANE, AT 277 K	Resolution 1.74 Å R-free 0.225
2XGC Crystal structure of a designed heterodimeric variant T-A(I)B of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.15 Å R-free 0.271
2XGC Crystal structure of a designed heterodimeric variant T-A(I)B of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.15 Å R-free 0.271
2XGD Crystal structure of a designed homodimeric variant T-A(L)A(L) of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	CL CHLORIDE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.25 Å R-free 0.259
2XGE Crystal structure of a designed heterodimeric variant T-A(A)B of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Not recorded	EDO 1,2-ETHANEDIOL × 2 NA SODIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.14 Å R-free 0.260
2XGE Crystal structure of a designed heterodimeric variant T-A(A)B of the tetracycline repressor Deposited 2010-06-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–50（50 aa） Fragment：RESIDUES 1-50,51-208	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.14 Å R-free 0.260
3FK6 Crystal structure of TetR triple mutant (H64K, S135L, S138I) Deposited 2008-12-16	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：DNA-binding domain (residues 1-50) and the effector-binding domain (residues 51-208) Chain B 1–50（50 aa） Fragment：DNA-binding domain (residues 1-50) and the effector-binding domain (residues 51-208)	Mutation：H64K, S135L, S138I Mutation：H64K, S135L, S138I	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；1M dipotassium hydrogen phosphate, 200mM sodium chloride, 50mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.10 Å R-free 0.262
3FK7 Crystal structure of TetR triple mutant (H64K, S135L, S138I) in complex with 4-ddma-atc Deposited 2008-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–50（50 aa） Fragment：DNA-binding domain (residues 1-50) and the effector-binding domain (residues 51-208) Chain B 1–50（50 aa） Fragment：DNA-binding domain (residues 1-50) and the effector-binding domain (residues 51-208)	Mutation：H64K, S135L, S138I Mutation：H64K, S135L, S138I	MG MAGNESIUM ION × 2 4DM (4aS,12aS)-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-1,4,4a,5,12,12a-hexahydrotetracene-2-carboxamide × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；1M dipotassium hydrogen phosphate, 200mM sodium chloride, 50mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.06 Å R-free 0.261
3ZQF Structure of Tetracycline repressor in complex with antiinducer peptide-TAP1 Deposited 2011-06-09	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–187（187 aa） Fragment：RESIDUES 1-187,188-208	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；RESERVOIR: 3 M NACL, 0.1 M BIS-TRIS, PH 6.	Resolution 2.56 Å R-free 0.247
3ZQG Structure of Tetracycline repressor in complex with antiinducer peptide-TAP2 Deposited 2011-06-09	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–187（187 aa） Fragment：RESIDUES 1-187,188-208	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；RESERVOIR: 3 M NACL, 0.1 M BIS-TRIS, PH 6.5	Resolution 2.45 Å R-free 0.234
3ZQH Structure of Tetracycline repressor in complex with inducer peptide- TIP3 Deposited 2011-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–187（187 aa） Fragment：RESIDUES 1-187,188-208	Mutation：YES	EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；0.2 M NACL, 0.1 M TRIS PH 9.0, 25% PEG 3350.	Resolution 1.60 Å R-free 0.224
3ZQI Structure of Tetracycline repressor in complex with inducer peptide- TIP2 Deposited 2011-06-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–187（187 aa） Fragment：RESIDUES 1-187,188-208 Chain B 1–187（187 aa） Fragment：RESIDUES 1-187,188-208	Mutation：YES Mutation：YES	EDO 1,2-ETHANEDIOL × 5 MG MAGNESIUM ION × 1 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.2 M MAGNESIUM ACETATE, 0.1 M SODIUM CACODYLATE, PH 7.0, 20% PEG 8000.	Resolution 1.50 Å R-free 0.195
4AC0 TETR(B) IN COMPLEX WITH MINOCYCLINE AND MAGNESIUM Deposited 2011-12-12	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 2–203（202 aa）	Not recorded	MIY (4S,4AS,5AR,12AS)-4,7-BIS(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2- CARBOXAMIDE × 2 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 2.45 Å R-free 0.294
6SY4 TetR in complex with the TetR-binding RNA-aptamer K1 Deposited 2019-09-27	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain A 1–203（203 aa） Chain B 1–203（203 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；4% v/v Tacsimate pH 6.0, 12% w/v PEG 3350	Resolution 2.69 Å R-free 0.246
6SY6 TetR in complex with the TetR-binding RNA-aptamer K2 Deposited 2019-09-27	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 2 PDB declaration: trimeric	Chain A 1–203（203 aa） Chain B 1–203（203 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；15 % (v/v) pentaerythritol propoxylate (5/4 PO/OH), 0.2 M NaCl, pH 6.0, 0.1 M MES-NaOH	Resolution 2.90 Å R-free 0.288
9DT3 Crystal structure of the engineered sulfonylurea repressor EsR (L11-C6), bound to ethametsulfuron-methyl Deposited 2024-09-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–207（207 aa） Chain B 1–207（207 aa）	Not recorded	RXF methyl 2-[[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoylsulfamoyl]benzoate × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.05 M Magnesium chloride 0.1 M HEPES pH 7.5 30% v/v Polyethylene glycol monomethyl ether 550	Resolution 2.80 Å R-free 0.278
9DT3 Crystal structure of the engineered sulfonylurea repressor EsR (L11-C6), bound to ethametsulfuron-methyl Deposited 2024-09-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–207（207 aa） Chain D 1–207（207 aa）	Not recorded	RXF methyl 2-[[4-ethoxy-6-(methylamino)-1,3,5-triazin-2-yl]carbamoylsulfamoyl]benzoate × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.05 M Magnesium chloride 0.1 M HEPES pH 7.5 30% v/v Polyethylene glycol monomethyl ether 550	Resolution 2.80 Å R-free 0.278
9DT5 Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), bound to chlorsulfuron Deposited 2024-09-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–207（207 aa） Chain B 1–207（207 aa）	Not recorded	1CS 1-(2-CHLOROPHENYLSULFONYL)-3-(4-METHOXY-6-METHYL-L,3,5-TRIAZIN-2-YL)UREA × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.05 M Ammonium sulfate 0.05 M BIS-TRIS pH 6.5 30% w/v Polyethylene glycol 600	Resolution 2.00 Å R-free 0.228
9DT5 Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), bound to chlorsulfuron Deposited 2024-09-30	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–207（207 aa） Chain D 1–207（207 aa）	Not recorded	1CS 1-(2-CHLOROPHENYLSULFONYL)-3-(4-METHOXY-6-METHYL-L,3,5-TRIAZIN-2-YL)UREA × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.05 M Ammonium sulfate 0.05 M BIS-TRIS pH 6.5 30% w/v Polyethylene glycol 600	Resolution 2.00 Å R-free 0.228

17 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TETR2_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–207； UniProt 1–207 Author chain B； PDBConstruct 1–207； UniProt 1–207

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	9dt4
Deposition date deposition_date	2024-09-30
最后修订 last_revision	2025-10-08
Structure title title	Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), apo form
Keywords keywords	engineered, ligand, repressor, transcription, DNA BINDING PROTEIN; DNA BINDING 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	23.43 Å
Radius of gyration Rg (electron density) rg_electron	22.30 Å
Forward intensity I(0) i0	33788400.00
Molecular weight molecular_weight	45351.0 kDa
Excluded volume excluded_volume	57155 Å³
Envelope volume envelope_volume	69279 Å³
Hydration-shell volume shell_volume	25824 Å³
Envelope diameter envelope_diameter	78.9 Å
Shell Rg shell_rg	29.48 Å
Envelope Rg envelope_rg	22.46 Å
Shape Rg shape_rg	22.32 Å
Total Rg total_rg	23.16 Å
Total atoms total_atoms	3201
Residues n_residues	399
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	75.5 Å
Rg (real space) rg_real	23.32 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	3.3790e+07
I(0) uncertainty (real space) i0_real_error	4.6610e+05
Rg (reciprocal space) rg_reciprocal	23.35 Å
I(0) (reciprocal space) i0_reciprocal	33790000.0000
Solution quality estimate total_estimate	0.8962
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	29.0 Å
Skewness Skewness skewness	0.198
Kurtosis Kurtosis kurtosis	-0.424
Angular range angular_range	— – 0.3400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7948000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.997

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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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8. Citations (1)

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Unit-cell length a length_a	37.120 Å
Unit-cell length b length_b	56.840 Å
Unit-cell length c length_c	106.007 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.32 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	19.872 Å
R factor r_factor	—
R_work r_work	0.1785
R_free r_free	0.2412

Description description	Sulfonylurea repressor CsR (L4.2-20)
Molecular weight formula_weight	23509.8 kDa
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	3218

Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), apo form

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

Sulfonylurea repressor CsR (L4.2-20)

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

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	17

fit	/app/data/saxs_computation/dt/9dt4/9dt4.fit
pddf	/app/data/pr_computation/dt/9dt4/9dt4.pr.out
profile	/app/data/saxs_computation/dt/9dt4/9dt4.dat