2krb

Solution structure of EIF3B-RRM bound to EIF3J peptide

Method: SOLUTION NMR Dmax: 41.8 Å Quality: GOOD

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

Eukaryotic translation initiation factor 3 subunit B

Homo sapiens

UniProt P55884

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 184–264 Fragment:RRM domain, UNP residues 184-264 Eukaryotic translation initiation factor 3 subunit J × 1 (O75822) SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure AMBIENT NMR sample composition:0.7 mM [U-100% 13C; U-100% 15N] eIF3b-RRM, 0.85 mM eIF3j peptide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM eIF3b-RRM, 0.85 mM [U-100% 13C; U-100% 15N] eIF3j peptide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM [U-100% 13C; U-100% 15N] eIF3b-RRM, 0.85 mM eIF3j peptide, 100% D2O | 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EIF3B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–81; UniProt 184–264

Eukaryotic translation initiation factor 3 subunit J

Homo sapiens

UniProt O75822

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 45–55 Fragment:UNP residues 45-55 Eukaryotic translation initiation factor 3 subunit B × 1 (P55884) SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure AMBIENT NMR sample composition:0.7 mM [U-100% 13C; U-100% 15N] eIF3b-RRM, 0.85 mM eIF3j peptide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM eIF3b-RRM, 0.85 mM [U-100% 13C; U-100% 15N] eIF3j peptide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.7 mM [U-100% 13C; U-100% 15N] eIF3b-RRM, 0.85 mM eIF3j peptide, 100% D2O | 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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EIF3J_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–11; UniProt 45–55

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 2krb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2krb
Deposition date deposition_date2009-12-16
Structure title titleSolution structure of EIF3B-RRM bound to EIF3J peptide
Keywords keywordseIF3, Translation initiation, eukaryotic initiation factor, eIF3b, eIF3j, TRANSLATION; TRANSLATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.39
Radius of gyration Rg (electron density) rg_electron12.82
Forward intensity I(0) i0157518000.00
Molecular weight molecular_weight105060.0 kDa
Excluded volume excluded_volume131230 ų
Envelope volume envelope_volume19927 ų
Hydration-shell volume shell_volume12232 ų
Envelope diameter envelope_diameter45.4
Shell Rg shell_rg19.67
Envelope Rg envelope_rg14.19
Shape Rg shape_rg12.78
Total Rg total_rg13.19
Total atoms total_atoms14600
Residues n_residues920
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 dmax41.8
Rg (real space) rg_real13.30
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.5750e+08
I(0) uncertainty (real space) i0_real_error1.7900e+06
Rg (reciprocal space) rg_reciprocal13.31
I(0) (reciprocal space) i0_reciprocal157500000.0000
Solution quality estimate total_estimate0.8957
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.5
Skewness Skewness skewness0.032
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha164600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2krbA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)