1ilf

NMR STRUCTURE OF APO CBFB

Method: SOLUTION NMR Dmax: 55.7 Å Quality: GOOD

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

CORE-BINDING FACTOR

Mus musculus

UniProt Q08024

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 1–141 Fragment:BETA-SUBUNIT No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.6;297 K;Ionic strength (raw mmCIF value) 150mM sodium chloride;Pressure 1 NMR sample composition:1.6mM CBFb U-15N, 13C | 25mM phosphate buffer, 3mM DTT, 100 % D2O NMR sample composition:1.6mM CBFb U-15N | 25mM phosphate buffer, 3mM DTT, 10 % D2O NMR sample composition:0.8mM CBFb | 25mM phosphate buffer,3mM DTT, 100 % 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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PEBB_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–141; UniProt 1–141

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 1ilf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ilf
Deposition date deposition_date2001-05-08
Structure title titleNMR STRUCTURE OF APO CBFB
Keywords keywordspartially open beta barrel, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.77
Radius of gyration Rg (electron density) rg_electron16.19
Forward intensity I(0) i02615470000.00
Molecular weight molecular_weight414690.0 kDa
Excluded volume excluded_volume510130 ų
Envelope volume envelope_volume37491 ų
Hydration-shell volume shell_volume17496 ų
Envelope diameter envelope_diameter61.4
Shell Rg shell_rg24.17
Envelope Rg envelope_rg18.42
Shape Rg shape_rg16.17
Total Rg total_rg16.37
Total atoms total_atoms57250
Residues n_residues3525
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 dmax55.7
Rg (real space) rg_real16.75
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real2.6150e+09
I(0) uncertainty (real space) i0_real_error3.0170e+07
Rg (reciprocal space) rg_reciprocal16.75
I(0) (reciprocal space) i0_reciprocal2615000000.0000
Solution quality estimate total_estimate0.7542
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.461
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha659400.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 0.394; Positv: 1.000; Valcen: 0.981; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ilfa_
Class classb — All beta proteins
Fold Fold foldb.54 — Core binding factor beta, CBF
Superfamily Superfamily superfamilyb.54.1 — Core binding factor beta, CBF
Family Family familyb.54.1.1 — Core binding factor beta, CBF

CATH v4.4 (1 domains)

Domain ID domain_id1ilfA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology250 — Polyomavirus Enhancer Binding Protein 2; Chain: A;
Homologous superfamily homologous superfamily10 — Core binding factor, beta subunit

8. Citations (1)

9. Files and Curves (10)