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1tl6

Solution structure of T4 bacteriphage AsiA monomer

Method: SOLUTION NMR Dmax: 42.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

10 kDa anti-sigma factor

Enterobacteria phage T4

UniProt P32267

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 1–90 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 150 mM NaCl；Pressure 1 NMR sample composition：0.7 mM AsiA, phosphate buffered saline,2 mM CHAPS | 97% H2O, 3% D2O 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 1TL6 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1JR5 Solution Structure of the Anti-Sigma Factor AsiA Homodimer Deposited 2001-08-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–90（90 aa）
Chain B 1–90（90 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；298 K；Ionic strength (raw mmCIF value) 50 mM d4-acetate, 50 mM KCl；Pressure ambient
NMR measurement conditions pH 6.3；298 K；Ionic strength (raw mmCIF value) 50 mM d4-acetate, 50 mM KCl；Pressure ambient
NMR measurement conditions pH 6.3；298 K；Ionic strength (raw mmCIF value) 50 mM d4-acetate, 50 mM KCl；Pressure ambient
NMR sample composition 1.5 mM AsiA U-13C, 15N; 50 mM d4-acetate, 50 mM KCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1.5 mM AsiA U-15N; 50 mM d4-acetate, 50 mM KCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM U-13C, 15N and 1.0 mM unlabeled; 50 mM d4-acetate, 50 mM KCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
1TKV Solution Structure of T4 AsiA Dimer Deposited 2004-06-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–90（90 aa）
Chain B 1–90（90 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.2；298 K；Ionic strength (raw mmCIF value) 50 mM NaCl；Pressure 1
NMR sample composition 10 mM sodium phosphate, 50 mM NaCl, 2 mM CHAPS, 50 mM sodium azide | 97% H2O, 3% D2O
Resolution not provided
1TLH T4 AsiA bound to sigma70 region 4 Deposited 2004-06-09 Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–90（90 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；312 K；Ionic strength (raw mmCIF value) 150 mM NaCl；Pressure 1
NMR sample composition 0.7 mM protein, phosphate buffered saline, 50 mM sodium azide, 1 mM benzamidine hydrochloride | 97% H2O, 3% D2O
Resolution not provided
6K4Y CryoEM structure of sigma appropriation complex Deposited 2019-05-27 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 8 PDB declaration: decameric
Chain I 1–90（90 aa）
Not recorded MG MAGNESIUM ION × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.79 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASIA_BPT4
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–90； UniProt 1–90

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 1tl6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1tl6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1tl6
Deposition date deposition_date2004-06-09
Structure title titleSolution structure of T4 bacteriphage AsiA monomer
Keywords keywordsAsia, T4 bacteriophage, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.15 Å
Radius of gyration Rg (electron density) rg_electron13.49 Å
Forward intensity I(0) i0713414000.00
Molecular weight molecular_weight229320.0 kDa
Excluded volume excluded_volume288300 ų
Envelope volume envelope_volume25819 ų
Hydration-shell volume shell_volume14454 ų
Envelope diameter envelope_diameter46.6 Å
Shell Rg shell_rg21.00 Å
Envelope Rg envelope_rg15.05 Å
Shape Rg shape_rg13.46 Å
Total Rg total_rg13.72 Å
Total atoms total_atoms32406
Residues n_residues1958
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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax42.1 Å
Rg (real space) rg_real14.02 Å
Rg uncertainty (real space) rg_real_error0.27 Å
I(0) (real space) i0_real7.1340e+08
I(0) uncertainty (real space) i0_real_error7.5910e+06
Rg (reciprocal space) rg_reciprocal14.03 Å
I(0) (reciprocal space) i0_reciprocal713400000.0000
Solution quality estimate total_estimate0.8831
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary16.0 Å
Skewness Skewness skewness-0.121
Kurtosis Kurtosis kurtosis-0.568
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha100800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.973
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1tl6a_
Class classa — All alpha proteins
Fold Fold folda.150 — Anti-sigma factor AsiA
Superfamily Superfamily superfamilya.150.1 — Anti-sigma factor AsiA
Family Family familya.150.1.1 — Anti-sigma factor AsiA

CATH v4.4 (1 domains)

Domain ID domain_id1tl6A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1810 — Anti-sigma factor AsiA
Homologous superfamily homologous superfamily10 — Anti-Sigma Factor A
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8. Citations (1)

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9. Files and Curves (10)