← Back to search
1tns

A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING DOMAIN OF MU TRANSPOSASE

Method: SOLUTION NMR Dmax: 49.6 Å Quality: GOOD
▼

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

MU-TRANSPOSASE

Enterobacteria phage Mu

UniProt P07636

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–76 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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 1TNS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BCM BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT Deposited 1995-05-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 248–574（327 aa）
Chain B 248–574（327 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å R-free 0.276
1BCO BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN Deposited 1995-05-26 Different construct Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 248–574（327 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.40 Å R-free 0.260
1TNT A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING DOMAIN OF MU TRANSPOSASE Deposited 1994-10-10 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–76（76 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
2EZH SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, MINIMIZED AVERAGE STRUCTURE Deposited 1997-07-25 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 174–247（74 aa） Fragment：IGAMMA SUBDOMAIN, RESIDUES 174 - 247
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；303 K
Resolution not provided
2EZI SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, 30 STRUCTURES Deposited 1997-07-25 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 174–247（74 aa） Fragment：IGAMMA SUBDOMAIN, RESIDUES 174 - 247
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；303 K
Resolution not provided
2EZK SOLUTION NMR STRUCTURE OF THE IBETA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF PHAGE MU TRANSPOSASE, REGULARIZED MEAN STRUCTURE Deposited 1997-10-04 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 77–174（98 aa） Fragment：IBETA SUBDOMAIN, RESIDUES 77 - 174
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；303 K
Resolution not provided
2EZL SOLUTION NMR STRUCTURE OF THE IBETA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF PHAGE MU TRANSPOSASE, 29 STRUCTURES Deposited 1997-10-04 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 77–174（98 aa） Fragment：IBETA SUBDOMAIN, RESIDUES 77 - 174
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；303 K
Resolution not provided
4FCY Crystal structure of the bacteriophage Mu transpososome Deposited 2012-05-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: decameric
Chain A 77–605（529 aa） Fragment：UNP residues 77-605
Chain B 77–605（529 aa） Fragment：UNP residues 77-605
Mutation：M521L, N525L Mutation：M521L, N525L No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；24-28% PEG400, 0.2 M magnesium chloride, 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 3.71 Å R-free 0.437
4FCY Crystal structure of the bacteriophage Mu transpososome Deposited 2012-05-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Homooligomer；Protein × 8 PDB declaration: eicosameric
Chain A 77–605（529 aa） Fragment：UNP residues 77-605
Chain B 77–605（529 aa） Fragment：UNP residues 77-605
Mutation：M521L, N525L Mutation：M521L, N525L No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；24-28% PEG400, 0.2 M magnesium chloride, 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 3.71 Å R-free 0.437

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRA_BPMU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–76； UniProt 1–76

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1tns

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1tns
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1tns
Deposition date deposition_date1994-10-10
Structure title titleA NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING DOMAIN OF MU TRANSPOSASE
Keywords keywordsDNA-BINDING PROTEIN, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR
▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.47 Å
Radius of gyration Rg (electron density) rg_electron13.33 Å
Forward intensity I(0) i01453470.00
Molecular weight molecular_weight8262.0 kDa
Excluded volume excluded_volume10495 ų
Envelope volume envelope_volume13152 ų
Hydration-shell volume shell_volume9052 ų
Envelope diameter envelope_diameter49.5 Å
Shell Rg shell_rg18.03 Å
Envelope Rg envelope_rg13.75 Å
Shape Rg shape_rg13.34 Å
Total Rg total_rg14.56 Å
Total atoms total_atoms1185
Residues n_residues76
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax49.6 Å
Rg (real space) rg_real14.44 Å
Rg uncertainty (real space) rg_real_error0.33 Å
I(0) (real space) i0_real1.4530e+06
I(0) uncertainty (real space) i0_real_error1.6250e+04
Rg (reciprocal space) rg_reciprocal14.45 Å
I(0) (reciprocal space) i0_reciprocal1453000.0000
Solution quality estimate total_estimate0.7846
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.0 Å
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.152
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha171700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.736; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1tnsa_
Class classa — All alpha proteins
Fold Fold folda.6 — Putative DNA-binding domain
Superfamily Superfamily superfamilya.6.1 — Putative DNA-binding domain
Family Family familya.6.1.7 — Excisionase-like

CATH v4.4 (1 domains)

Domain ID domain_id1tnsA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
▶

8. Citations (1)

▶

9. Files and Curves (10)