1lei

The kB DNA sequence from the HLV-LTR functions as an allosteric regulator of HIV transcription

Method: X-RAY DIFFRACTION Dmax: 102.4 Å Quality: GOOD

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

NUCLEAR FACTOR NF-KAPPA-B P65 SUBUNIT

Mus musculus

UniProt Q04207

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 Heteromer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 20–291 Fragment:p65 RHR 5'-D(*CP*TP*CP*AP*GP*GP*GP*AP*AP*AP*GP*TP*AP*CP*AP*GP*A)-3' × 1 5'-D(*TP*CP*TP*GP*5ITP*AP*CP*5ITP*5ITP*5ITP*CP*CP*CP*TP*GP*AP*G)-3' × 1 NUCLEAR FACTOR NF-KAPPA-B P50 SUBUNIT × 1 (P25799) X-RAY DIFFRACTION X-ray crystallization conditions:SMALL TUBES;pH 6.5;291 K;PEG 3350, CaCl2, sodium spermine, pH 6.5, SMALL TUBES, temperature 291K Resolution 2.70 Å R-free 0.284

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.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF65_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 3–274; UniProt 20–291

NUCLEAR FACTOR NF-KAPPA-B P50 SUBUNIT

Mus musculus

UniProt P25799

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 Heteromer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 39–350 Fragment:p50 RHR 5'-D(*CP*TP*CP*AP*GP*GP*GP*AP*AP*AP*GP*TP*AP*CP*AP*GP*A)-3' × 1 5'-D(*TP*CP*TP*GP*5ITP*AP*CP*5ITP*5ITP*5ITP*CP*CP*CP*TP*GP*AP*G)-3' × 1 NUCLEAR FACTOR NF-KAPPA-B P65 SUBUNIT × 1 (Q04207) X-RAY DIFFRACTION X-ray crystallization conditions:SMALL TUBES;pH 6.5;291 K;PEG 3350, CaCl2, sodium spermine, pH 6.5, SMALL TUBES, temperature 291K Resolution 2.70 Å R-free 0.284

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.

20 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KBF1_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 2–313; UniProt 39–350

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 1lei

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1lei
Deposition date deposition_date2002-04-09
Structure title titleThe kB DNA sequence from the HLV-LTR functions as an allosteric regulator of HIV transcription
Keywords keywordstranscription factor, NF-kB-DNA complex, TRANSCRIPTION-DNA COMPLEX; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.14
Radius of gyration Rg (electron density) rg_electron30.85
Forward intensity I(0) i0116176000.00
Molecular weight molecular_weight76677.0 kDa
Excluded volume excluded_volume92089 ų
Envelope volume envelope_volume121700 ų
Hydration-shell volume shell_volume34279 ų
Envelope diameter envelope_diameter109.2
Shell Rg shell_rg36.17
Envelope Rg envelope_rg31.09
Shape Rg shape_rg30.96
Total Rg total_rg30.97
Total atoms total_atoms5321
Residues n_residues615
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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 dmax102.4
Rg (real space) rg_real30.21
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real1.1620e+08
I(0) uncertainty (real space) i0_real_error2.1560e+06
Rg (reciprocal space) rg_reciprocal30.18
I(0) (reciprocal space) i0_reciprocal116200000.0000
Solution quality estimate total_estimate0.8798
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.8
Skewness Skewness skewness0.419
Kurtosis Kurtosis kurtosis-0.230
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13410000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd1leia1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.1 — NF-kappa-B/REL/DORSAL transcription factors, C-terminal domain
Domain ID domain_idd1leia2
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.5 — p53-like transcription factors
Family Family familyb.2.5.3 — Rel/Dorsal transcription factors, DNA-binding domain
Domain ID domain_idd1leia3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1leib1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.1 — NF-kappa-B/REL/DORSAL transcription factors, C-terminal domain
Domain ID domain_idd1leib2
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.5 — p53-like transcription factors
Family Family familyb.2.5.3 — Rel/Dorsal transcription factors, DNA-binding domain

CATH v4.4 (4 domains)

Domain ID domain_id1leiA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily340 — Rel homology domain (RHD), DNA-binding domain
Domain ID domain_id1leiA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1leiB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily340 — Rel homology domain (RHD), DNA-binding domain
Domain ID domain_id1leiB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)