8u9l

Crystal Structure of RelA-cRel chimera complex with DNA

Method: X-RAY DIFFRACTION Dmax: 195.5 Å Quality: GOOD

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

Transcription factor p65,Proto-oncogene c-Rel chimera

Mus musculus

UniProt P15307

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 88–176 Chain B; UniProt 88–176 Not recorded ;DNA (5'-D(P*TP*TP*GP*AP*TP*GP*GP*GP*AP*AP*TP*TP*TP*CP*CP*GP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*CP*GP*GP*AP*AP*AP*TP*TP*CP*CP*CP*AP*TP*CP*AP*A)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.2M Sodium/Potassium phosphate 0.1M Bis Tris propane pH 6.5 20% PEG 3350 10mM DTT 0.5% BOG Resolution 3.09 Å R-free 0.329
2 Insufficient information Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain G; UniProt 88–176 Chain H; UniProt 88–176 Not recorded ;DNA (5'-D(P*TP*TP*GP*AP*TP*GP*GP*GP*AP*AP*TP*TP*TP*CP*CP*GP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*CP*GP*GP*AP*AP*AP*TP*TP*CP*CP*CP*AP*TP*CP*AP*A)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.2M Sodium/Potassium phosphate 0.1M Bis Tris propane pH 6.5 20% PEG 3350 10mM DTT 0.5% BOG Resolution 3.09 Å R-free 0.329
3 Insufficient information Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain K; UniProt 88–176 Chain L; UniProt 88–176 Not recorded ;DNA (5'-D(P*TP*TP*GP*AP*TP*GP*GP*GP*AP*AP*TP*TP*TP*CP*CP*GP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*CP*GP*GP*AP*AP*AP*TP*TP*CP*CP*CP*AP*TP*CP*AP*A)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.2M Sodium/Potassium phosphate 0.1M Bis Tris propane pH 6.5 20% PEG 3350 10mM DTT 0.5% BOG Resolution 3.09 Å R-free 0.329
4 Insufficient information Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain O; UniProt 88–176 Chain P; UniProt 88–176 Not recorded ;DNA (5'-D(P*TP*TP*GP*AP*TP*GP*GP*GP*AP*AP*TP*TP*TP*CP*CP*GP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*CP*GP*GP*AP*AP*AP*TP*TP*CP*CP*CP*AP*TP*CP*AP*A)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.2M Sodium/Potassium phosphate 0.1M Bis Tris propane pH 6.5 20% PEG 3350 10mM DTT 0.5% BOG Resolution 3.09 Å R-free 0.329

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name REL_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 82–170; UniProt 88–176 Author chain B; PDBConstruct 82–170; UniProt 88–176 Author chain G; PDBConstruct 82–170; UniProt 88–176 Author chain H; PDBConstruct 82–170; UniProt 88–176 Author chain K; PDBConstruct 82–170; UniProt 88–176 Author chain L; PDBConstruct 82–170; UniProt 88–176 Author chain O; PDBConstruct 82–170; UniProt 88–176 Author chain P; PDBConstruct 82–170; UniProt 88–176

Transcription factor p65,Proto-oncogene c-Rel chimera

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 Insufficient information Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 19–98 Chain A; UniProt 191–291 Chain B; UniProt 19–98 Chain B; UniProt 191–291 Not recorded ;DNA (5'-D(P*TP*TP*GP*AP*TP*GP*GP*GP*AP*AP*TP*TP*TP*CP*CP*GP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*CP*GP*GP*AP*AP*AP*TP*TP*CP*CP*CP*AP*TP*CP*AP*A)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.2M Sodium/Potassium phosphate 0.1M Bis Tris propane pH 6.5 20% PEG 3350 10mM DTT 0.5% BOG Resolution 3.09 Å R-free 0.329
2 Insufficient information Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain G; UniProt 19–98 Chain G; UniProt 191–291 Chain H; UniProt 19–98 Chain H; UniProt 191–291 Not recorded ;DNA (5'-D(P*TP*TP*GP*AP*TP*GP*GP*GP*AP*AP*TP*TP*TP*CP*CP*GP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*CP*GP*GP*AP*AP*AP*TP*TP*CP*CP*CP*AP*TP*CP*AP*A)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.2M Sodium/Potassium phosphate 0.1M Bis Tris propane pH 6.5 20% PEG 3350 10mM DTT 0.5% BOG Resolution 3.09 Å R-free 0.329
3 Insufficient information Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain K; UniProt 19–98 Chain K; UniProt 191–291 Chain L; UniProt 19–98 Chain L; UniProt 191–291 Not recorded ;DNA (5'-D(P*TP*TP*GP*AP*TP*GP*GP*GP*AP*AP*TP*TP*TP*CP*CP*GP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*CP*GP*GP*AP*AP*AP*TP*TP*CP*CP*CP*AP*TP*CP*AP*A)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.2M Sodium/Potassium phosphate 0.1M Bis Tris propane pH 6.5 20% PEG 3350 10mM DTT 0.5% BOG Resolution 3.09 Å R-free 0.329
4 Insufficient information Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain O; UniProt 19–98 Chain O; UniProt 191–291 Chain P; UniProt 19–98 Chain P; UniProt 191–291 Not recorded ;DNA (5'-D(P*TP*TP*GP*AP*TP*GP*GP*GP*AP*AP*TP*TP*TP*CP*CP*GP*AP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*TP*CP*GP*GP*AP*AP*AP*TP*TP*CP*CP*CP*AP*TP*CP*AP*A)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.2M Sodium/Potassium phosphate 0.1M Bis Tris propane pH 6.5 20% PEG 3350 10mM DTT 0.5% BOG Resolution 3.09 Å R-free 0.329

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 22 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 2–81; UniProt 19–98 Author chain A; PDBConstruct 177–277; UniProt 191–291 Author chain B; PDBConstruct 2–81; UniProt 19–98 Author chain B; PDBConstruct 177–277; UniProt 191–291 Author chain G; PDBConstruct 2–81; UniProt 19–98 Author chain G; PDBConstruct 177–277; UniProt 191–291 Author chain H; PDBConstruct 2–81; UniProt 19–98 Author chain H; PDBConstruct 177–277; UniProt 191–291 Author chain K; PDBConstruct 2–81; UniProt 19–98 Author chain K; PDBConstruct 177–277; UniProt 191–291 Author chain L; PDBConstruct 2–81; UniProt 19–98 Author chain L; PDBConstruct 177–277; UniProt 191–291 Author chain O; PDBConstruct 2–81; UniProt 19–98 Author chain O; PDBConstruct 177–277; UniProt 191–291 Author chain P; PDBConstruct 2–81; UniProt 19–98 Author chain P; PDBConstruct 177–277; UniProt 191–291

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 8u9l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u9l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u9l
Deposition date deposition_date2023-09-19
Structure title titleCrystal Structure of RelA-cRel chimera complex with DNA
Keywords keywordsVertebrate Evolution, transcription factor, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.25
Radius of gyration Rg (electron density) rg_electron56.88
Forward intensity I(0) i01617260000.00
Molecular weight molecular_weight299410.0 kDa
Excluded volume excluded_volume359230 ų
Envelope volume envelope_volume572000 ų
Hydration-shell volume shell_volume85601 ų
Envelope diameter envelope_diameter209.9
Shell Rg shell_rg57.56
Envelope Rg envelope_rg54.99
Shape Rg shape_rg56.94
Total Rg total_rg56.72
Total atoms total_atoms20864
Residues n_residues2360
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 dmax195.5
Rg (real space) rg_real56.32
Rg uncertainty (real space) rg_real_error1.84
I(0) (real space) i0_real1.6170e+09
I(0) uncertainty (real space) i0_real_error2.9760e+07
Rg (reciprocal space) rg_reciprocal56.16
I(0) (reciprocal space) i0_reciprocal1617000000.0000
Solution quality estimate total_estimate0.8829
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary62.9
Skewness Skewness skewness0.309
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha72490000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.873

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)