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1jei

LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN EMERIN

Method: SOLUTION NMR Dmax: 44.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

EMERIN

OrganismNot specified

UniProt P50402

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 2–54 Fragment：LEM DOMAIN (RESIDUES 2-54) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.3；298 K；Ionic strength (raw mmCIF value) 20mM NMR sample composition：LEM domain of emerin 1mM | NaH2PO4/Na2HPO4 20mM, pH 6.3, 90% H2O/10% D2O or 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.

Other PDB Difference from Current Entry 1JEI Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2ODC LEM-domain of the nuclear envelope protein emerin Deposited 2006-12-22 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain I 2–47（46 aa） Fragment：residues 2-47
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 50 mM POTASSIUM PHOSPHATE
Resolution not provided
2ODG Complex of barrier-to-autointegration factor and LEM-domain of emerin Deposited 2006-12-22 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 2–47（46 aa） Fragment：RESIDUES 2-47
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 50 mM POTASSIUM PHOSPHATE 200 mM NACL
Resolution not provided
6GHD Structural analysis of the ternary complex between lamin A/C, BAF and emerin identifies an interface disrupted in autosomal recessive progeroid diseases Deposited 2018-05-07 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain G 2–45（44 aa）
Not recorded SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；25% PEG3.350, 20mM Tris-BispH5.5, 30mM NaCl, 0.2M NH4SO4
Resolution 2.10 Å R-free 0.247
6GHD Structural analysis of the ternary complex between lamin A/C, BAF and emerin identifies an interface disrupted in autosomal recessive progeroid diseases Deposited 2018-05-07 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain H 2–45（44 aa）
Not recorded SO4 SULFATE ION × 3 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；25% PEG3.350, 20mM Tris-BispH5.5, 30mM NaCl, 0.2M NH4SO4
Resolution 2.10 Å R-free 0.247
7NDY Di-phosphorylated Barrier-to-Autointegration Factor (BAF) in complex with LEM domain of Emerin Deposited 2021-02-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain G 2–187（186 aa）
Not recorded EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Hepes Sodium salt 0.1 M pH 7.5 PEG 600 25% W/V
Resolution 1.44 Å R-free 0.225

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

View Construct and Data Evidence
UniProt name EMD_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–53； UniProt 2–54

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 1jei

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jei
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jei
Deposition date deposition_date2001-06-18
Structure title titleLEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN EMERIN
Keywords keywordsemerin nucleus membrane domain dystrophy, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.41 Å
Radius of gyration Rg (electron density) rg_electron11.91 Å
Forward intensity I(0) i060724800.00
Molecular weight molecular_weight62300.0 kDa
Excluded volume excluded_volume77276 ų
Envelope volume envelope_volume17079 ų
Hydration-shell volume shell_volume10555 ų
Envelope diameter envelope_diameter49.2 Å
Shell Rg shell_rg19.58 Å
Envelope Rg envelope_rg15.51 Å
Shape Rg shape_rg11.86 Å
Total Rg total_rg12.44 Å
Total atoms total_atoms8770
Residues n_residues530
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax44.7 Å
Rg (real space) rg_real12.52 Å
Rg uncertainty (real space) rg_real_error0.34 Å
I(0) (real space) i0_real6.0720e+07
I(0) uncertainty (real space) i0_real_error6.1470e+05
Rg (reciprocal space) rg_reciprocal12.52 Å
I(0) (reciprocal space) i0_reciprocal60720000.0000
Solution quality estimate total_estimate0.5492
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary13.6 Å
Skewness Skewness skewness0.589
Kurtosis Kurtosis kurtosis0.276
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97270.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.498; Stabil: 0.998; Sysdev: 0.256; Positv: 1.000; Valcen: 0.880; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1jeia_
Class classa — All alpha proteins
Fold Fold folda.140 — LEM/SAP HeH motif
Superfamily Superfamily superfamilya.140.1 — LEM domain
Family Family familya.140.1.1 — LEM domain

CATH v4.4 (1 domains)

Domain ID domain_id1jeiA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology720 — Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1
Homologous superfamily homologous superfamily40 —
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8. Citations (2)

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9. Files and Curves (10)