SAXSdb — 2ns8

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

Tetracycline repressor protein

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 5	16 residue peptide Tip (Transcription inducing peptide) × 3	Consistent with protein count
2	Insufficient information	Heteromer	Protein 4	16 residue peptide Tip (Transcription inducing peptide) × 2	Consistent with protein count
3	Insufficient information	Heteromer	Protein 9	16 residue peptide Tip (Transcription inducing peptide) × 5	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TETR2_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–187； UniProt 1–187 Author chain B； PDBConstruct 1–187； UniProt 1–187 Author chain C； PDBConstruct 1–187； UniProt 1–187 Author chain D； PDBConstruct 1–187； UniProt 1–187

Tetracycline repressor protein

Escherichia coli

UniProt P0ACT4

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 5	16 residue peptide Tip (Transcription inducing peptide) × 3	Consistent with protein count
2	Insufficient information	Heteromer	Protein 4	16 residue peptide Tip (Transcription inducing peptide) × 2	Consistent with protein count
3	Insufficient information	Heteromer	Protein 9	16 residue peptide Tip (Transcription inducing peptide) × 5	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TETR4_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 188–208； UniProt 188–208 Author chain B； PDBConstruct 188–208； UniProt 188–208 Author chain C； PDBConstruct 188–208； UniProt 188–208 Author chain D； PDBConstruct 188–208； UniProt 188–208

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	2ns8
Deposition date deposition_date	2006-11-03
Structure title title	How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor
Keywords keywords	Transcription regulator, helix-turn-helix, bound repressor-inducing peptide, Transcription; TRANSCRIPTION
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2ns8__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2ns8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2ns8__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	23.12 Å
Rg (electron density)	22.12 Å
Total Rg	23.07 Å
Atom count	3466
Residues	431
Excluded volume	61367 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2ns8__assembly_1__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2ns8__assembly_2__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2ns8__assembly_3__model_1`	nonameric （9）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Tetracycline repressor protein
Molecular weight formula_weight	23531.7 kDa
Mutation mutation	C68S, C88N, C121T, C144S
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	6884

MSRLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEMLDRHHTHFSPLEGESWQDFLRNNAKSFRNALLSHRDGAKVHLGTRPTEKQYETLENQLAFLTQQGFSLENALYALSAVGHFTLGSVLEDQEHQVAKEERETPTTDSMPPLLRQAIELFDHQGAEPAFLHGLESLIRGFEVQLTALLQIV

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	16 residue peptide Tip (Transcription inducing peptide)
Molecular weight formula_weight	1668.8 kDa
Source method src_method	syn
Copy count entity_count	5

Polymer Polymer

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

XWTWNAYAFAAPSGGGS

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6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	2ns8A01
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	2ns8A02
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

Domain ID domain_id	2ns8B01
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	2ns8B02
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

Domain ID domain_id	2ns8C01
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	2ns8C02
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

Domain ID domain_id	2ns8D01
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	2ns8D02
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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Unit-cell length a length_a	77.890 Å
Unit-cell length b length_b	200.590 Å
Unit-cell length c length_c	65.280 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	20

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.550 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2110
R_work r_work	0.2060
R_free r_free	0.2700

How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor

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

Tetracycline repressor protein

State in the Current Structure

Other States of the Same Protein in the Database

Tetracycline repressor protein

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2ns8__assembly_1__model_1

2ns8__assembly_1__model_1 | I(q)

2ns8__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)

How an in vitro selected peptide mimics the antibiotic tetracycline to induce TET repressor

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

Tetracycline repressor protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Tetracycline repressor protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2ns8__assembly_1__model_1

2ns8__assembly_1__model_1 | I(q)

2ns8__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)