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1gur

GURMARIN, A SWEET TASTE-SUPPRESSING POLYPEPTIDE, NMR, 10 STRUCTURES

Method: SOLUTION NMR Dmax: 139.6 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

GURMARIN

Gymnema sylvestre

UniProt P25810

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 2–35 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1GUR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C4E GURMARIN FROM GYMNEMA SYLVESTRE Deposited 1999-07-27 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–35（35 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 2.9；298 K；Pressure ATMOSPHERIC
Resolution not provided
5OLL Crystal structure of gurmarin, a sweet taste suppressing polypeptide Deposited 2017-07-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 1–35（35 aa）
Not recorded NI NICKEL (II) ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；100 mM MES, 5 mM MgCl2, 5 mM CaCl2, 50 mM CdCl2, 50 mM NiCl2 and 12% (w/v) PEG 3350
Resolution 1.45 Å R-free 0.191

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GUR_GYMSY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–35； UniProt 2–35

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 1gur

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1gur
Deposition date deposition_date1996-03-12
Structure title titleGURMARIN, A SWEET TASTE-SUPPRESSING POLYPEPTIDE, NMR, 10 STRUCTURES
Keywords keywordsSWEET-TASTE, SUPPRESSING PROTEIN, SWEET TASTE-SUPPRESSING PROTEIN; SWEET TASTE-SUPPRESSING 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_guinier52.69 Å
Radius of gyration Rg (electron density) rg_electron54.76 Å
Forward intensity I(0) i029406900.00
Molecular weight molecular_weight42139.0 kDa
Excluded volume excluded_volume52392 ų
Envelope volume envelope_volume130110 ų
Hydration-shell volume shell_volume25486 ų
Envelope diameter envelope_diameter199.7 Å
Shell Rg shell_rg42.39 Å
Envelope Rg envelope_rg53.62 Å
Shape Rg shape_rg54.80 Å
Total Rg total_rg53.66 Å
Total atoms total_atoms5660
Residues n_residues340
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 dmax139.6 Å
Rg (real space) rg_real47.72 Å
Rg uncertainty (real space) rg_real_error0.57 Å
I(0) (real space) i0_real2.7990e+07
I(0) uncertainty (real space) i0_real_error4.6820e+05
Rg (reciprocal space) rg_reciprocal51.97 Å
I(0) (reciprocal space) i0_reciprocal29340000.0000
Solution quality estimate total_estimate0.6699
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.8 Å
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.464
Angular range angular_range— – 0.1500 Å−1
Current regularization parameter α current_alpha0.5422
Highest regularization parameter α highest_alpha2722000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.933; Stabil: 0.978; Sysdev: 0.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.001
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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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1gura_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.4 — Gurmarin-like
Family Family familyg.3.4.1 — Gurmarin, a sweet taste-suppressing polypeptide
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8. Citations (3)

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9. Files and Curves (10)