SAXSdb — 4ac0

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

TETRACYCLINE REPRESSOR PROTEIN CLASS B FROM TRANSPOSON TN1 0

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 2–203	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

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 4AC0	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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 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	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 ligand/ion 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 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 ligand/ion 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 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	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 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	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 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	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
6SY4 TetR in complex with the TetR-binding RNA-aptamer K1 Deposited 2019-09-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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 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 1–207（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 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 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
9DT4 Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), apo form Deposited 2024-09-30	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 1–207（207 aa） Chain B 1–207（207 aa）	Not recorded	No recorded non-water small molecule	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
9DT5 Crystal structure of the engineered sulfonylurea repressor CsR (L4.2-20), bound to chlorsulfuron Deposited 2024-09-30	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 1–207（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 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 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 1–202； UniProt 2–203

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	4ac0
Deposition date deposition_date	2011-12-12
Structure title title	TETR(B) IN COMPLEX WITH MINOCYCLINE AND MAGNESIUM
Keywords keywords	TRANSCRIPTION; TRANSCRIPTION
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	20.56 Å
Radius of gyration Rg (electron density) rg_electron	19.80 Å
Forward intensity I(0) i0	9790180.00
Molecular weight molecular_weight	22735.0 kDa
Excluded volume excluded_volume	28345 Å³
Envelope volume envelope_volume	35615 Å³
Hydration-shell volume shell_volume	16015 Å³
Envelope diameter envelope_diameter	70.8 Å
Shell Rg shell_rg	25.03 Å
Envelope Rg envelope_rg	20.39 Å
Shape Rg shape_rg	19.77 Å
Total Rg total_rg	20.73 Å
Total atoms total_atoms	1597
Residues n_residues	197
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	69.2 Å
Rg (real space) rg_real	20.60 Å
Rg uncertainty (real space) rg_real_error	0.51 Å
I(0) (real space) i0_real	9.7900e+06
I(0) uncertainty (real space) i0_real_error	1.3350e+05
Rg (reciprocal space) rg_reciprocal	20.59 Å
I(0) (reciprocal space) i0_reciprocal	9790000.0000
Solution quality estimate total_estimate	0.8002
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.0 Å
Skewness Skewness skewness	0.364
Kurtosis Kurtosis kurtosis	-0.447
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2293000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.823; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.930; Smooth: 0.000

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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	TETRACYCLINE REPRESSOR PROTEIN CLASS B FROM TRANSPOSON TN1 0
Molecular weight formula_weight	22894.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1623

SRLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEMLDRHHTHFCPLEGESWQDFLRNNAKSFRCALLSHRDGAKVHLGTRPTEKQYETLENQLAFLCQQGFSLENALYALSAVGHFTLGCVLEDQEHQVAKEERETPTTDSMPPLLRQAIELFDHQGAEPAFLFGLELIICGLEKQLKC

来源 Source

来源生物 organism	ESCHERICHIA COLI
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	(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
Molecular weight formula_weight	457.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	24

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d4ac0a1
Class class	a — All alpha proteins
Fold Fold fold	a.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamily	a.4.1 — Homeodomain-like
Family Family family	a.4.1.0 — automated matches

Domain ID domain_id	d4ac0a2
Class class	a — All alpha proteins
Fold Fold fold	a.121 — Tetracyclin repressor-like, C-terminal domain
Superfamily Superfamily superfamily	a.121.1 — Tetracyclin repressor-like, C-terminal domain
Family Family family	a.121.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	4ac0A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	60 — Homeodomain-like

Domain ID domain_id	4ac0A02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	357 — Tetracycline Repressor; domain 2
Homologous superfamily homologous superfamily	10 — Tetracycline Repressor, domain 2

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8. Citations (1)

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Unit-cell length a length_a	71.880 Å
Unit-cell length b length_b	71.880 Å
Unit-cell length c length_c	93.430 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	8

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.450 Å
Low-resolution limit resolution_low	56.970 Å
R factor r_factor	0.2370
R_work r_work	0.2344
R_free r_free	0.2938

fit	/app/data/saxs_computation/ac/4ac0/4ac0.fit
pddf	/app/data/pr_computation/ac/4ac0/4ac0.pr.out
profile	/app/data/saxs_computation/ac/4ac0/4ac0.dat

TETR(B) IN COMPLEX WITH MINOCYCLINE AND MAGNESIUM

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

TETRACYCLINE REPRESSOR PROTEIN CLASS B FROM TRANSPOSON TN1 0

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