2lww

NMR structure of RelA-TAD/CBP-TAZ1 complex

Method: SOLUTION NMR Dmax: 61.3 Å Quality: GOOD

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

CREB-binding protein

Mus musculus

UniProt P45481

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 340–439 Fragment:TAZ-type 1 zinc finger residues 340-439 Nuclear transcription factor RelA × 1 (Q548Y4) ZN ZINC ION × 3 SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 40;Pressure ambient NMR sample composition:0.8-1.1 mM [U-13C; U-15N] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.8-1.1 mM [U-13C] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM [U-2H] DTT, 20 mM [U-2H] TRIS, 40 mM sodium chloride, 99.8 % [U-2H] D2O, 100% D2O | 100% D2O NMR sample composition:0.7-0.9 mM [U-13C] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM [U-2H] DTT, 20 mM [U-2H] TRIS, 40 mM sodium chloride, 99.8 % [U-2H] D2O, 100% D2O | 100% D2O NMR sample composition:0.7-0.9 mM [U-13C; U-15N] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.8-1.1 mM [U-15N] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.7-0.9 mM [U-15N] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% 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.

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

View Construct and Data Evidence
UniProt name CBP_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–100; UniProt 340–439

Nuclear transcription factor RelA

Mus musculus

UniProt Q548Y4

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 425–490 Fragment:UNP residues 425-490 CREB-binding protein × 1 (P45481) ZN ZINC ION × 3 SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 40;Pressure ambient NMR sample composition:0.8-1.1 mM [U-13C; U-15N] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.8-1.1 mM [U-13C] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM [U-2H] DTT, 20 mM [U-2H] TRIS, 40 mM sodium chloride, 99.8 % [U-2H] D2O, 100% D2O | 100% D2O NMR sample composition:0.7-0.9 mM [U-13C] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM [U-2H] DTT, 20 mM [U-2H] TRIS, 40 mM sodium chloride, 99.8 % [U-2H] D2O, 100% D2O | 100% D2O NMR sample composition:0.7-0.9 mM [U-13C; U-15N] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.8-1.1 mM [U-15N] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.7-0.9 mM [U-15N] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% 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.

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

View Construct and Data Evidence
UniProt name Q548Y4_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–70; UniProt 425–490

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 2lww

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2lww
Deposition date deposition_date2012-08-07
Structure title titleNMR structure of RelA-TAD/CBP-TAZ1 complex
Keywords keywordsNF-kappaB, p65, Transcription; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.17
Radius of gyration Rg (electron density) rg_electron16.54
Forward intensity I(0) i02392770000.00
Molecular weight molecular_weight374760.0 kDa
Excluded volume excluded_volume453140 ų
Envelope volume envelope_volume68360 ų
Hydration-shell volume shell_volume25349 ų
Envelope diameter envelope_diameter70.4
Shell Rg shell_rg29.93
Envelope Rg envelope_rg23.23
Shape Rg shape_rg16.55
Total Rg total_rg16.73
Total atoms total_atoms51120
Residues n_residues3400
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 dmax61.3
Rg (real space) rg_real17.14
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real2.3930e+09
I(0) uncertainty (real space) i0_real_error3.2830e+07
Rg (reciprocal space) rg_reciprocal17.14
I(0) (reciprocal space) i0_reciprocal2393000000.0000
Solution quality estimate total_estimate0.7509
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.377
Kurtosis Kurtosis kurtosis0.113
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1509000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.595; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2lwwa_
Class classg — Small proteins
Fold Fold foldg.53 — TAZ domain
Superfamily Superfamily superfamilyg.53.1 — TAZ domain
Family Family familyg.53.1.1 — TAZ domain

CATH v4.4 (1 domains)

Domain ID domain_id2lwwA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1020 — CREB-binding Protein; Chain A
Homologous superfamily homologous superfamily10 — TAZ domain

8. Citations (1)

9. Files and Curves (10)