2i9t

Structure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter

Method: X-RAY DIFFRACTION Dmax: 104.3 Å Quality: GOOD

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

Transcription factor p65

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 19–291 Fragment:residues 19-291 5'-D(*AP*GP*TP*GP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*CP*TP*G)-3' × 1 5'-D(*CP*AP*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*CP*AP*CP*T)-3' × 1 Nuclear factor NF-kappa-B p105 subunit × 1 (P25799) X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;293 K;8% PEG 5K monomethylether, 200mM sodium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 5.60 Resolution 2.80 Å R-free 0.288

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 7–279; UniProt 19–291

Nuclear factor NF-kappa-B p105 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:residues 39-350 5'-D(*AP*GP*TP*GP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*CP*TP*G)-3' × 1 5'-D(*CP*AP*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*CP*AP*CP*T)-3' × 1 Transcription factor p65 × 1 (Q04207) X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;293 K;8% PEG 5K monomethylether, 200mM sodium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 5.60 Resolution 2.80 Å R-free 0.288

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 NFKB1_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 2i9t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2i9t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2i9t
Deposition date deposition_date2006-09-06
Structure title titleStructure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter
Keywords keywordsPROTEIN-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_guinier30.43
Radius of gyration Rg (electron density) rg_electron30.98
Forward intensity I(0) i0108837000.00
Molecular weight molecular_weight74509.0 kDa
Excluded volume excluded_volume89764 ų
Envelope volume envelope_volume119780 ų
Hydration-shell volume shell_volume33820 ų
Envelope diameter envelope_diameter110.0
Shell Rg shell_rg36.04
Envelope Rg envelope_rg31.16
Shape Rg shape_rg31.05
Total Rg total_rg31.21
Total atoms total_atoms5205
Residues n_residues621
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 dmax104.3
Rg (real space) rg_real30.49
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.0880e+08
I(0) uncertainty (real space) i0_real_error1.6890e+06
Rg (reciprocal space) rg_reciprocal30.47
I(0) (reciprocal space) i0_reciprocal108800000.0000
Solution quality estimate total_estimate0.8774
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.1
Skewness Skewness skewness0.414
Kurtosis Kurtosis kurtosis-0.247
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12210000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.953

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_idd2i9ta1
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_idd2i9ta2
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_idd2i9ta3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2i9tb1
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_idd2i9tb2
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_id2i9tA01
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_id2i9tA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2i9tB01
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_id2i9tB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)