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- PDB-1c4e: GURMARIN FROM GYMNEMA SYLVESTRE -

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Basic information

Entry
Database: PDB / ID: 1c4e
TitleGURMARIN FROM GYMNEMA SYLVESTRE
ComponentsPROTEIN (GURMARIN)
KeywordsPLANT PROTEIN / GURMARIN / SWEET TASTE SUPPRESSION / CYSTINE KNOT / SWEET TASTE TRANSDUCTION
Function / homologyGurmarin/antifungal peptide / Gurmarin
Function and homology information
Biological speciesGymnema sylvestre (plant)
MethodSOLUTION NMR / DISTANCE GEOMETRY, DYNAMICAL SIMULATED ANNEALING
AuthorsFletcher, J.I. / Dingley, A.J. / King, G.F.
Citation
Journal: Eur.J.Biochem. / Year: 1999
Title: High-resolution solution structure of gurmarin, a sweet-taste-suppressing plant polypeptide.
Authors: Fletcher, J.I. / Dingley, A.J. / Smith, R. / Connor, M. / Christie, M.J. / King, G.F.
#1: Journal: J.Biomol.NMR / Year: 1995
Title: Three-Dimensional Structure of Gurmarin, a Sweet Taste-Suppressing Polypeptide
Authors: Arai, K. / Ishima, R. / Morikawa, S. / Miyasaka, A. / Imoto, T. / Yoshimura, S. / Aimoto, S. / Akasaka, K.
#2: Journal: J.Biochem.(Tokyo) / Year: 1992
Title: Amino Acid Sequence of Sweet-Taste-Suppressing Peptide (Gurmarin) from the Leaves of Gymnema Sylvestre
Authors: Kamei, K. / Takano, R. / Miyasaka, A. / Imoto, T. / Hara, S.
#3: Journal: COMP.BIOCHEM.PHYSIOL. A: PHYSIOL. / Year: 1991
Title: A Novel Peptide Isolated from the Leaves of Gymnema Sylvestre-I. Characterization and its Suppressive Effect on the Neural Responses to Sweet Taste Stimuli in the Rat
Authors: Imoto, T. / Miyasaka, A. / Ishima, R. / Akasaka, K.
History
DepositionJul 27, 1999Deposition site: RCSB / Processing site: RCSB
SupersessionAug 27, 1999ID: 2GUR
Revision 1.0Aug 27, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations
Category: pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf
Revision 2.0Dec 25, 2019Group: Database references / Derived calculations / Polymer sequence
Category: entity_poly / pdbx_struct_mod_residue ...entity_poly / pdbx_struct_mod_residue / struct_conn / struct_ref_seq_dif
Item: _entity_poly.pdbx_seq_one_letter_code_can / _pdbx_struct_mod_residue.parent_comp_id / _struct_conn.pdbx_leaving_atom_flag
Revision 2.1Dec 27, 2023Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (GURMARIN)


Theoretical massNumber of molelcules
Total (without water)4,2211
Polymers4,2211
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100LOWEST ENERGY
Representative

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Components

#1: Protein/peptide PROTEIN (GURMARIN)


Mass: 4220.952 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: CHEMICALLY SYNTHESIZED / Source: (natural) Gymnema sylvestre (plant) / Tissue: LEAVES / References: UniProt: P25810
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121DQFCOSY
131TOCSY
141ECOSY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR TECHNIQUES

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Sample preparation

Sample conditionspH: 2.9 / Pressure: ATMOSPHERIC atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX600 / Manufacturer: Bruker / Model: AMX600 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DYANA1.5GUENTERTrefinement
X-PLOR3.843BRUNGERrefinement
DYANAstructure solution
X-PLORstructure solution
RefinementMethod: DISTANCE GEOMETRY, DYNAMICAL SIMULATED ANNEALING / Software ordinal: 1 / Details: SEE PRIMARY REFERENCE ABOVE.
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 20

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