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- PDB-1co4: SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REG... -

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Basic information

Entry
Database: PDB / ID: 1co4
TitleSOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS
ComponentsPROTEIN (ACTIVATOR OF METALLOTHIONEIN 1)
KeywordsTRANSLATION/REGULATION PROTEIN / METALLOTHIONEIN / AMT / METAL REGULATION / TRANSLATION-REGULATION PROTEIN COMPLEX
Function / homology
Function and homology information


intracellular copper ion homeostasis / transcription initiation at RNA polymerase II promoter / transcription cis-regulatory region binding / copper ion binding / DNA-binding transcription factor activity / DNA binding / zinc ion binding / nucleus
Similarity search - Function
Activator Of Metallothionein 1; Chain A / Copper fist DNA-binding domain / Copper fist DNA-binding domain / Copper fist DNA-binding domain superfamily / Copper fist DNA binding domain / Copper-fist DNA-binding domain signature. / Copper-fist DNA-binding domain profile. / Copper-Fist / Copper-fist / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Metal-activated transcriptional activator protein AMT1
Similarity search - Component
MethodSOLUTION NMR / DYANA
AuthorsTurner, R.B. / Smith, D.L. / Zawrotny, M.E. / Summers, M.F. / Posewitz, M.C. / Winge, D.R.
CitationJournal: Nat.Struct.Biol. / Year: 1998
Title: Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors.
Authors: Turner, R.B. / Smith, D.L. / Zawrotny, M.E. / Summers, M.F. / Posewitz, M.C. / Winge, D.R.
History
DepositionJun 4, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0Jun 10, 1999Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (ACTIVATOR OF METALLOTHIONEIN 1)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,7522
Polymers4,6871
Non-polymers651
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / 100LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein/peptide PROTEIN (ACTIVATOR OF METALLOTHIONEIN 1) / AMT1


Mass: 4686.551 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-42 / Source method: obtained synthetically
Details: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THIS PROTEIN IS NATURALLY FOUND IN CANDIDA GLABRATA.
References: UniProt: P41772
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121HOHAHA

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Sample preparation

DetailsContents: 25MM NAOAC, 0.1MM ZNCL2, 90% WATER/10%D2O
Sample conditionsIonic strength: 25mM NACL / pH: 6.5 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

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

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Processing

NMR software
NameVersionDeveloperClassification
DYANAGUNTERT,WUTHRICHrefinement
NMRView2structure solution
RefinementMethod: DYANA / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 100 / Conformers submitted total number: 15

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