SAXSdb — 1tac

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

TAT PROTEIN

Human immunodeficiency virus 1

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 2–86	Mutation：M1L, C22S, C25A, C27A, C30S, C31A, C34S, C37A	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5；298 K；Ionic strength (raw mmCIF value) 0.85 M；Pressure 10E+5 PA NMR sample composition：H2O/D2O (9:1)	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 1TAC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1TBC HIV-1 TAT, NMR, 10 STRUCTURES Deposited 1998-03-13	Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–86（85 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 0.85 M；Pressure 10E+5 PA NMR sample composition H2O/D2O (9:1)	Resolution not provided
1TIV STRUCTURAL STUDIES OF HIV-1 TAT PROTEIN Deposited 1995-02-14	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–86（86 aa）	Mutation：THR 40 LYS	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2BGN HIV-1 Tat protein derived N-terminal nonapeptide Trp2-Tat(1-9) bound to the active site of Dipeptidyl peptidase IV (CD26) Deposited 2005-01-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain W 1–9（9 aa） Fragment：HIV-1 TAT PROTEIN DERIVED N-TERMINAL NONAPEPTIDE, RESIDUES 1-9 Chain X 1–9（9 aa） Fragment：HIV-1 TAT PROTEIN DERIVED N-TERMINAL NONAPEPTIDE, RESIDUES 1-9	Mutation：YES Mutation：YES	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ZN ZINC ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.15 Å R-free 0.247
2BGN HIV-1 Tat protein derived N-terminal nonapeptide Trp2-Tat(1-9) bound to the active site of Dipeptidyl peptidase IV (CD26) Deposited 2005-01-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain Y 1–9（9 aa） Fragment：HIV-1 TAT PROTEIN DERIVED N-TERMINAL NONAPEPTIDE, RESIDUES 1-9 Chain Z 1–9（9 aa） Fragment：HIV-1 TAT PROTEIN DERIVED N-TERMINAL NONAPEPTIDE, RESIDUES 1-9	Mutation：YES Mutation：YES	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ZN ZINC ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.15 Å R-free 0.247
2BGR Crystal structure of HIV-1 Tat derived nonapeptides Tat(1-9) bound to the active site of Dipeptidyl peptidase IV (CD26) Deposited 2005-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain Y 1–9（9 aa） Chain Z 1–9（9 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.203
8CCW Crystal structure of human Sirt3 in complex with an acetylated HIV1 Tat-46-54 substrate peptide Deposited 2023-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 46–54（9 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；10 mg/ml human Sirt3-(118-399) in 20 mM Tris/HCl, pH 8.0, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP were incubated with 2 mM ac-Tat-46-54 for 60 min at 293.15 K. The complex was crystallized using the sitting-drop vapor-diffusion method at 293.15 K with 100 mM MES, pH 6.0, 30% (w/v) PEG 200, 5% (w/v) PEG 3000 as reservoir solution.	Resolution 1.65 Å R-free 0.209
8CCZ Crystal structure of human Sirt3 in complex with an inhibiting HIV1 Tat-37-59 peptide Deposited 2023-01-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 37–59（23 aa）	Mutation：C37A	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；10 mg/ml human Sirt3-(118-399) in 20 mM Tris/HCl, pH 8.0, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP were incubated with 2 mM Tat-37-59 in 10% (v/v) DMSO for 60 min at 293.15 K. The complex was crystallized using the sitting-drop vapor-diffusion method at 293.15 K with 100 mM CHES, pH 9.0, 20% (w/v) PEG 8000 as reservoir solution.	Resolution 1.95 Å R-free 0.276
8CCZ Crystal structure of human Sirt3 in complex with an inhibiting HIV1 Tat-37-59 peptide Deposited 2023-01-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–59（23 aa）	Mutation：C37A	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；10 mg/ml human Sirt3-(118-399) in 20 mM Tris/HCl, pH 8.0, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP were incubated with 2 mM Tat-37-59 in 10% (v/v) DMSO for 60 min at 293.15 K. The complex was crystallized using the sitting-drop vapor-diffusion method at 293.15 K with 100 mM CHES, pH 9.0, 20% (w/v) PEG 8000 as reservoir solution.	Resolution 1.95 Å R-free 0.276

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

View Construct and Data Evidence

UniProt name	TAT_HV1Z2
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–86； UniProt 2–86

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	1tac
Deposition date deposition_date	1998-03-13
Structure title title	HIV-1 TAT CYS-, NMR, 10 STRUCTURES
Keywords keywords	TRANSCRIPTION REGULATION, HIV-1, TRANSACTIVATION, RNA BINDING; TRANSCRIPTION REGULATION
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	12.94 Å
Radius of gyration Rg (electron density) rg_electron	12.89 Å
Forward intensity I(0) i0	150520000.00
Molecular weight molecular_weight	95527.0 kDa
Excluded volume excluded_volume	117090 Å³
Envelope volume envelope_volume	19268 Å³
Hydration-shell volume shell_volume	11832 Å³
Envelope diameter envelope_diameter	45.3 Å
Shell Rg shell_rg	19.52 Å
Envelope Rg envelope_rg	14.21 Å
Shape Rg shape_rg	12.86 Å
Total Rg total_rg	13.19 Å
Total atoms total_atoms	13450
Residues n_residues	860
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	43.4 Å
Rg (real space) rg_real	12.90 Å
Rg uncertainty (real space) rg_real_error	0.30 Å
I(0) (real space) i0_real	1.5050e+08
I(0) uncertainty (real space) i0_real_error	1.6510e+06
Rg (reciprocal space) rg_reciprocal	12.91 Å
I(0) (reciprocal space) i0_reciprocal	150500000.0000
Solution quality estimate total_estimate	0.8932
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	15.4 Å
Skewness Skewness skewness	0.208
Kurtosis Kurtosis kurtosis	-0.453
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	181000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.982

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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_id	d1taca_
Class class	j — Peptides
Fold Fold fold	j.40 — Transactivation protein TAT
Superfamily Superfamily superfamily	j.40.1 — Transactivation protein TAT
Family Family family	j.40.1.1 — Transactivation protein TAT

CATH v4.4 (1 domains)

Domain ID domain_id	1tacA00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	20 — HIV-1 Transactivator Protein
Homologous superfamily homologous superfamily	10 — Tat domain

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8. Citations (2)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	TAT PROTEIN
Molecular weight formula_weight	9562.7 kDa
Mutation mutation	M1L, C22S, C25A, C27A, C30S, C31A, C34S, C37A
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	13450

来源生物 organism	Human immunodeficiency virus 1
NCBI Class编号 ncbi_taxonomy_id	11676
宿主生物 host_organism	Escherichia coli BL21(DE3)

HIV-1 TAT CYS-, NMR, 10 STRUCTURES

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

TAT 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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/ta/1tac/1tac.fit
pddf	/app/data/pr_computation/ta/1tac/1tac.pr.out
profile	/app/data/saxs_computation/ta/1tac/1tac.dat