2nlw

Solution structure of the RRM domain of human eukaryotic initiation factor 3b

Method: SOLUTION NMR Dmax: 60.6 Å Quality: GOOD

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

Eukaryotic translation initiation factor 3 subunit 9

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 170–274 Fragment:RNA Recognition Motif No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 300mM;Pressure ambient NMR sample composition:0.8mM eIF3b-RRM unlabeled, 20mM HEPES, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.8mM eIF3b-RRM U-15N, 20mM HEPES, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:0.8mM eIF3b-RRM U-15N,13C, 20mM HEPES, 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.

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

View Construct and Data Evidence
UniProt name IF39_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–105; UniProt 170–274

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 2nlw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2nlw
Deposition date deposition_date2006-10-20
Structure title titleSolution structure of the RRM domain of human eukaryotic initiation factor 3b
Keywords keywordstranslation initiation, eukaryotic initiation factor 3 complex, RNA recognition motif, TRANSLATION; TRANSLATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.40
Radius of gyration Rg (electron density) rg_electron15.00
Forward intensity I(0) i0491338000.00
Molecular weight molecular_weight190950.0 kDa
Excluded volume excluded_volume240480 ų
Envelope volume envelope_volume44029 ų
Hydration-shell volume shell_volume19159 ų
Envelope diameter envelope_diameter64.0
Shell Rg shell_rg25.67
Envelope Rg envelope_rg20.19
Shape Rg shape_rg14.92
Total Rg total_rg15.60
Total atoms total_atoms26784
Residues n_residues1680
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 dmax60.6
Rg (real space) rg_real15.46
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real4.9130e+08
I(0) uncertainty (real space) i0_real_error6.2060e+06
Rg (reciprocal space) rg_reciprocal15.45
I(0) (reciprocal space) i0_reciprocal491300000.0000
Solution quality estimate total_estimate0.7695
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.6
Skewness Skewness skewness0.516
Kurtosis Kurtosis kurtosis0.244
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha288600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.431; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.707; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2nlwA01
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)