2na9

Transmembrane Structure of the P441A Mutant of the Cytokine Receptor Common Subunit beta

Method: SOLUTION NMR Dmax: 74.0 Å Quality: REASONABLE

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

Cytokine receptor common subunit beta

Homo sapiens

UniProt P32927

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 432–473 Fragment:Helical transmembrane residues 432-473 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.4;313 K;Ionic strength (raw mmCIF value) 0.05;Pressure ambient NMR sample composition:0.5 mM [U-99% 13C; U-99% 15N; 80% 2H] protein, 93% H2O/7% D2O | 93% H2O/7% 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.

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

View Construct and Data Evidence
UniProt name IL3RB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–44; UniProt 432–473

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 2na9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2na9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2na9
Deposition date deposition_date2015-12-21
Structure title titleTransmembrane Structure of the P441A Mutant of the Cytokine Receptor Common Subunit beta
Keywords keywordstransmembrane helix, NBP residue, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier20.33
Radius of gyration Rg (electron density) rg_electron19.48
Forward intensity I(0) i0123952000.00
Molecular weight molecular_weight107480.0 kDa
Excluded volume excluded_volume140650 ų
Envelope volume envelope_volume27709 ų
Hydration-shell volume shell_volume10738 ų
Envelope diameter envelope_diameter79.7
Shell Rg shell_rg28.55
Envelope Rg envelope_rg24.89
Shape Rg shape_rg19.47
Total Rg total_rg19.84
Total atoms total_atoms15855
Residues n_residues924
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 dmax74.0
Rg (real space) rg_real20.87
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real1.2400e+08
I(0) uncertainty (real space) i0_real_error1.8070e+06
Rg (reciprocal space) rg_reciprocal20.77
I(0) (reciprocal space) i0_reciprocal123900000.0000
Solution quality estimate total_estimate0.5400
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks5
Primary peak position r_peak_primary6.3
Skewness Skewness skewness0.454
Kurtosis Kurtosis kurtosis-0.883
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12360.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.003; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.009; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)