2mx4

NMR structure of Phosphorylated 4E-BP2

Method: SOLUTION NMR Dmax: 39.3 Å Quality: GOOD

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

Eukaryotic translation initiation factor 4E-binding protein 2

Homo sapiens

UniProt Q13542

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 18–62 Fragment:residues 18-62 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;20 K;Ionic strength (raw mmCIF value) 0.150;Pressure ambient NMR sample composition:1 mM [U-99% 13C; U-99% 15N] Phosphorylated 4E-BP2, 2 mM DTT, 100 mM sodium chloride, 30 mM sodium phosphate, 1 mM EDTA, 1 mM Benzamidine, 90% H2O/10% D2O | 90% H2O/10% 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 4EBP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–45; UniProt 18–62

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 2mx4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2mx4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2mx4
Deposition date deposition_date2014-12-10
Structure title titleNMR structure of Phosphorylated 4E-BP2
Keywords keywordsphosphorylation, intrinsic disorder, Translation, protein Binding; Translation,protein Binding
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier10.74
Radius of gyration Rg (electron density) rg_electron10.49
Forward intensity I(0) i0166013000.00
Molecular weight molecular_weight101750.0 kDa
Excluded volume excluded_volume124820 ų
Envelope volume envelope_volume13926 ų
Hydration-shell volume shell_volume9590 ų
Envelope diameter envelope_diameter41.8
Shell Rg shell_rg18.03
Envelope Rg envelope_rg13.31
Shape Rg shape_rg10.45
Total Rg total_rg10.85
Total atoms total_atoms13980
Residues n_residues860
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 dmax39.3
Rg (real space) rg_real10.72
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.6600e+08
I(0) uncertainty (real space) i0_real_error1.7780e+06
Rg (reciprocal space) rg_reciprocal10.72
I(0) (reciprocal space) i0_reciprocal166000000.0000
Solution quality estimate total_estimate0.8298
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary13.9
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.077
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.623; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)