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- PDB-1fmy: HIGH RESOLUTION SOLUTION STRUCTURE OF THE PROTEIN PART OF CU7 MET... -

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Basic information

Entry
Database: PDB / ID: 1fmy
TitleHIGH RESOLUTION SOLUTION STRUCTURE OF THE PROTEIN PART OF CU7 METALLOTHIONEIN
ComponentsMETALLOTHIONEIN
KeywordsMETAL BINDING PROTEIN / metallothionein / copper / Saccharomyces cerevisiae
Function / homology
Function and homology information


detoxification of cadmium ion / detoxification of copper ion / response to copper ion / superoxide dismutase activity / cadmium ion binding / antioxidant activity / removal of superoxide radicals / copper ion binding / cytosol
Similarity search - Function
Ag-metallothionein / Metallothionein domain superfamily, yeast / Metallothionein domain, yeast / Copper metallothionein superfamily / Yeast metallothionein / Metallothionein domain superfamily / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Copper metallothionein 1-1 / Copper metallothionein 1-1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodSOLUTION NMR / distance geometry simulated annealing torsion angle dynamics
Model type detailsminimized average
AuthorsBertini, I. / Hartmann, H.J. / Klein, T. / Liu, G. / Luchinat, C. / Weser, U.
CitationJournal: Eur.J.Biochem. / Year: 2000
Title: High resolution solution structure of the protein part of Cu7 metallothionein.
Authors: Bertini, I. / Hartmann, H.J. / Klein, T. / Liu, G. / Luchinat, C. / Weser, U.
History
DepositionAug 18, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 13, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: METALLOTHIONEIN


Theoretical massNumber of molelcules
Total (without water)4,2761
Polymers4,2761
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)1 / 30mean structure
RepresentativeModel #1minimized average structure

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Components

#1: Protein/peptide METALLOTHIONEIN /


Mass: 4275.656 Da / Num. of mol.: 1 / Fragment: RESIDUES 9 TO 48 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: X-2180-1AA / References: UniProt: P07215, UniProt: P0CX80*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1212D TOCSY
2312D NOESY
2412D TOCSY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques.

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Sample preparation

DetailsContents: 5mM unenrich metallothionein; 18mM phosphate buffer; 90% H2O, 10% D2O;pH=6.5; 0.03% beta-mercaptoethanol
Solvent system: 90% H2O/10% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
10.02 6.5 normal 283 K
20.02 6.5 normal 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE8001
Bruker AVANCEBrukerAVANCE6002

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3.1Brukerdata analysis
XwinNMR3.1Brukerprocessing
DYANA1.5Guntert, P. ,et. alstructure solution
Amber5Pearlman, D. A., et. alrefinement
XEASY3.1Eccles, C., et.al.data analysis
RefinementMethod: distance geometry simulated annealing torsion angle dynamics
Software ordinal: 1
Details: A total of 1192 NOES, of which 1048 are meaningful, were used to determine the solution structure.
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformer selection criteria: mean structure / Conformers calculated total number: 30 / Conformers submitted total number: 1

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