1g84

THE SOLUTION STRUCTURE OF THE C EPSILON2 DOMAIN FROM IGE

Method: SOLUTION NMR Dmax: 41.1 Å Quality: REASONABLE

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

IMMUNOGLOBULIN E

Homo sapiens

UniProt P01854

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 106–210 Fragment:C EPSILON2 Mutation:C16S, C104S No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 100mM;Pressure 1 NMR sample composition:2mM Ce2 U-15N,13C | 90% H2O/10% D2O NMR sample composition:1.4mM Ce2 U-15N | 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.

33 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHE_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–105; UniProt 106–210

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 1g84

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g84
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1g84
Deposition date deposition_date2000-11-16
Structure title titleTHE SOLUTION STRUCTURE OF THE C EPSILON2 DOMAIN FROM IGE
Keywords keywordsallergy, IgE, immunoglobulin domain, Ce2, antibody, Fc., IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.23
Radius of gyration Rg (electron density) rg_electron15.12
Forward intensity I(0) i0442929000.00
Molecular weight molecular_weight171710.0 kDa
Excluded volume excluded_volume212130 ų
Envelope volume envelope_volume27550 ų
Hydration-shell volume shell_volume13690 ų
Envelope diameter envelope_diameter67.7
Shell Rg shell_rg23.17
Envelope Rg envelope_rg18.82
Shape Rg shape_rg15.13
Total Rg total_rg15.27
Total atoms total_atoms23805
Residues n_residues1575
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 dmax41.1
Rg (real space) rg_real14.36
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real4.2270e+08
I(0) uncertainty (real space) i0_real_error3.4120e+06
Rg (reciprocal space) rg_reciprocal15.43
I(0) (reciprocal space) i0_reciprocal442900000.0000
Solution quality estimate total_estimate0.6810
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary14.6
Skewness Skewness skewness0.376
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha4.4470
Highest regularization parameter α highest_alpha290100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.979; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.000

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_idd1g84a_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (1 domains)

Domain ID domain_id1g84A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)