SAXSdb — 1bl0

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

PROTEIN (MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN)

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric（3） Consistent with all polymer counts	Chain A； UniProt 1–129	Not recorded	;DNA (5'-D(GPGPGPGPAPTPTPTPAPGPCPAPAPAPAPCPGPTPGPGPCPAP* TPC)-3') ; × 1 ;DNA (5'-D(CPCPGPAPTPGPCPCPAPCPGPTPTPTPTPGPCPTPAPAPAPTP CP*C)-3') ; × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；12% PEG8000,100MM NA-CACODYLATE(PH8.0), 100MM CA-ACETATE, VAPOR DIFFUSION, HANGING DROP	Resolution 2.30 Å R-free 0.303

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 1BL0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1XS9 A MODEL OF THE TERNARY COMPLEX FORMED BETWEEN MARA, THE ALPHA-CTD OF RNA POLYMERASE AND DNA Deposited 2004-10-18	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain A 1–129（129 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.7 NMR sample composition AS DESCRIBED IN PAPER	Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MARA_ECOLI
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 1–129； UniProt 1–129

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	1bl0
Deposition date deposition_date	1998-07-22
Structure title title	MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN (MARA)/DNA COMPLEX
Keywords keywords	TRANSCRIPTIONAL ACTIVATOR; A BIPARTITE HELIX-TURN-HELIX PROTEIN, TRANSCRIPTION-DNA COMPLEX; TRANSCRIPTION/DNA
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	21.89 Å
Radius of gyration Rg (electron density) rg_electron	20.81 Å
Forward intensity I(0) i0	24696500.00
Molecular weight molecular_weight	28558.0 kDa
Excluded volume excluded_volume	31560 Å³
Envelope volume envelope_volume	40436 Å³
Hydration-shell volume shell_volume	17460 Å³
Envelope diameter envelope_diameter	87.5 Å
Shell Rg shell_rg	25.88 Å
Envelope Rg envelope_rg	21.25 Å
Shape Rg shape_rg	20.71 Å
Total Rg total_rg	21.55 Å
Total atoms total_atoms	1952
Residues n_residues	164
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	83.7 Å
Rg (real space) rg_real	22.09 Å
Rg uncertainty (real space) rg_real_error	0.80 Å
I(0) (real space) i0_real	2.4700e+07
I(0) uncertainty (real space) i0_real_error	3.1340e+05
Rg (reciprocal space) rg_reciprocal	22.06 Å
I(0) (reciprocal space) i0_reciprocal	24700000.0000
Solution quality estimate total_estimate	0.7814
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.5 Å
Skewness Skewness skewness	0.593
Kurtosis Kurtosis kurtosis	0.079
Angular range angular_range	— – 0.3650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3068000.0000
Real-space data points n_real_points	68
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.573; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.500; Smooth: 0.935

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	;DNA (5'-D(GPGPGPGPAPTPTPTPAPGPCPAPAPAPAPCPGPTPGPGPCPAP* TP*C)-3') ;
Molecular weight formula_weight	7458.8 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	B
Atom count atom_count	2096

GGGGATTTAGCAAAACGTGGCATC

Entity 2 Entity 2 polymer

Description description	;DNA (5'-D(CPCPGPAPTPGPCPCPAPCPGPTPTPTPTPGPCPTPAPAPAPTP* CP*C)-3') ;
Molecular weight formula_weight	7280.7 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	C

CCGATGCCACGTTTTGCTAAATCC

Entity 3 Entity 3 polymer

Description description	PROTEIN (MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN)
Molecular weight formula_weight	15441.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

MTMSRRNTDAITIHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLTRTFKNYFDVPPHKYRMTNMQGESRFLHPLNHYNS

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 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	144

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1bl0a1
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.4.1.8 — AraC type transcriptional activator

Domain ID domain_id	d1bl0a2
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.4.1.8 — AraC type transcriptional activator

CATH v4.4 (2 domains)

Domain ID domain_id	1bl0A01
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	1bl0A02
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

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8. Citations (1)

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Unit-cell length a length_a	47.100 Å
Unit-cell length b length_b	47.100 Å
Unit-cell length c length_c	298.200 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	2.300 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2250
R_work r_work	0.2250
R_free r_free	0.3030

fit	/app/data/saxs_computation/bl/1bl0/1bl0.fit
pddf	/app/data/pr_computation/bl/1bl0/1bl0.pr.out
profile	/app/data/saxs_computation/bl/1bl0/1bl0.dat

MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN (MARA)/DNA COMPLEX

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

PROTEIN (MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN)

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)