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- PDB-1mnl: HIGH-RESOLUTION SOLUTION STRUCTURE OF A SWEET PROTEIN SINGLE-CHAI... -

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Entry
Database: PDB / ID: 1mnl
TitleHIGH-RESOLUTION SOLUTION STRUCTURE OF A SWEET PROTEIN SINGLE-CHAIN MONELLIN (SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND DYNAMICAL SIMULATED ANNEALING CALCULATIONS, 21 STRUCTURES
ComponentsMONELLIN
KeywordsSWEET PROTEIN / SWEET RECEPTOR BINDING / ALPHA/BETA MOTIF
Function / homology
Function and homology information


Monellin, A chain / Monellin, A chain superfamily / Monellin / Monellin / Nuclear Transport Factor 2; Chain: A, - #10 / Cystatin superfamily / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta
Similarity search - Domain/homology
Biological speciesDioscoreophyllum cumminsii (serendipity berry)
MethodSOLUTION NMR / HYBRID GEOMETRY, DYNAMICAL SIMULATED ANNEALING CALCULATIONS
AuthorsLee, S.-Y. / Lee, J.-H. / Chang, H.-J. / Jo, J.-M. / Jung, J.-W. / Lee, W.
CitationJournal: Biochemistry / Year: 1999
Title: Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations.
Authors: Lee, S.Y. / Lee, J.H. / Chang, H.J. / Cho, J.M. / Jung, J.W. / Lee, W.
History
DepositionAug 6, 1998Processing site: BNL
Revision 1.0Jun 8, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MONELLIN


Theoretical massNumber of molelcules
Total (without water)11,0841
Polymers11,0841
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)21 / 500.5A, 5 DEGREES
RepresentativeModel #21

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Components

#1: Protein MONELLIN / / SCM


Mass: 11083.628 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Dioscoreophyllum cumminsii (serendipity berry)
Production host: Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P02881

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111TOCSY
121NOESY
131DQF-COSY
1411H-15N HSQC
1511H-15N HMQC-J
1611H-15N NOESY-HSQC
1711H-15N HOHAHA-HMQC
NMR detailsText: 2D-TOCSY, NOESY, DQF-COSY, 1H-15N HSQC, 1H-15N HMQC-J 3D-1H-15N NOESY-HSQC, 1H-15N HOHAHA-HMQC

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Sample preparation

Sample conditionspH: 7.0 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX600 / Manufacturer: Bruker / Model: DMX600 / Field strength: 600 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.8model building
X-PLOR3.8refinement
X-PLOR3.8phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.81BRUNGERrefinement
X-PLOR3.81structure solution
RefinementMethod: HYBRID GEOMETRY, DYNAMICAL SIMULATED ANNEALING CALCULATIONS
Software ordinal: 1
NMR ensembleConformer selection criteria: 0.5A, 5 DEGREES / Conformers calculated total number: 50 / Conformers submitted total number: 21

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