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1plx

NMR structure of Methionine-Enkephalin in fast tumbling Bicelles/DMPG

Method: SOLUTION NMR Dmax: 11.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Met-enkephalin 1

OrganismNot specified

UniProt P01210

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 100–104 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4.8；295 K；Ionic strength (raw mmCIF value) 9mM；Pressure ambient NMR sample composition：5.1uM Menk; (DMPC+DMPG)/DHPC: 0.5:1 (molar ratio); DMPC/DMPG: 9:1 (molar ratio); Lipid/peptide: 25:1 (molar ratio); 10% w/v of lipids in water; 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.

Other PDB Difference from Current Entry 1PLX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1PLW NMR structure of Methionine-Enkephalin in fast tumbling DMPC/DHPC bicelles Deposited 2003-06-09 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 100–104（5 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.5；295 K；Ionic strength (raw mmCIF value) 9mM；Pressure ambient
NMR sample composition 5.4uM Menk; DMPC/DHPC: 0.5:1 (molar ratio); Lipid/peptide: 25:1 (molar ratio); 10% w/v of lipids in water; 90%H2O, 10%D2O | 90% H2O/10% D2O
Resolution not provided
2LWC Met-enkephalin in DPMC SUV Deposited 2012-07-27 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 100–104（5 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；303 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 0.5 mM menk, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
8JGG CryoEM structure of Gi-coupled MRGPRX1 with peptide agonist BAM8-22 Deposited 2023-05-20 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain L 220–230（11 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PENK_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–5； UniProt 100–104

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 1plx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1plx
Deposition date deposition_date2003-06-09
Structure title titleNMR structure of Methionine-Enkephalin in fast tumbling Bicelles/DMPG
Keywords keywordsNEUROPEPTIDE; NEUROPEPTIDE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier3.37 Å
Radius of gyration Rg (electron density) rg_electron4.25 Å
Forward intensity I(0) i026265600.00
Molecular weight molecular_weight45893.0 kDa
Excluded volume excluded_volume57675 ų
Envelope volume envelope_volume968 ų
Hydration-shell volume shell_volume2196 ų
Envelope diameter envelope_diameter14.8 Å
Shell Rg shell_rg8.70 Å
Envelope Rg envelope_rg4.92 Å
Shape Rg shape_rg4.20 Å
Total Rg total_rg4.50 Å
Total atoms total_atoms6000
Residues n_residues400
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 dmax11.8 Å
Rg (real space) rg_real3.67 Å
Rg uncertainty (real space) rg_real_error0.02 Å
I(0) (real space) i0_real2.6900e+07
I(0) uncertainty (real space) i0_real_error1.2060e+05
Rg (reciprocal space) rg_reciprocal3.24 Å
I(0) (reciprocal space) i0_reciprocal26270000.0000
Solution quality estimate total_estimate0.7001
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary3.9 Å
Skewness Skewness skewness0.299
Kurtosis Kurtosis kurtosis-0.609
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha2.2980
Highest regularization parameter α highest_alpha62.9900
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 0.925; Sysdev: 0.000; Positv: 1.000; Valcen: 0.710; Smooth: 0.733
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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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8. Citations (1)

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9. Files and Curves (10)