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- PDB-1cpz: COPPER CHAPERONE OF ENTEROCOCCUS HIRAE (APO-FORM) -

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Basic information

Entry
Database: PDB / ID: 1cpz
TitleCOPPER CHAPERONE OF ENTEROCOCCUS HIRAE (APO-FORM)
ComponentsCopper chaperone
KeywordsGENE REGULATION / COPPER CHAPERONE / METAL TRANSPORT
Function / homology
Function and homology information


copper ion binding / cytoplasm
Similarity search - Function
Heavy metal-associated domain, copper ion-binding / Heavy-metal-associated, conserved site / Heavy-metal-associated domain. / Heavy-metal-associated domain / Heavy metal-associated domain superfamily / Heavy-metal-associated domain profile. / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Copper chaperone / Copper chaperone CopZ
Similarity search - Component
Biological speciesEnterococcus hirae (bacteria)
MethodSOLUTION NMR / distance geometry
AuthorsWimmer, R. / Herrmann, T. / Solioz, M. / Wuethrich, K.
CitationJournal: J.Biol.Chem. / Year: 1999
Title: NMR structure and metal interactions of the CopZ copper chaperone.
Authors: Wimmer, R. / Herrmann, T. / Solioz, M. / Wuthrich, K.
History
DepositionMay 6, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0May 11, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4Dec 21, 2022Group: Database references / Source and taxonomy / Structure summary
Category: entity / entity_src_gen ...entity / entity_src_gen / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _entity.pdbx_description / _entity_src_gen.pdbx_beg_seq_num ..._entity.pdbx_description / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_seq_type / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.pdbx_db_accession / _struct_ref_seq.seq_align_beg / _struct_ref_seq_dif.db_mon_id / _struct_ref_seq_dif.details / _struct_ref_seq_dif.pdbx_seq_db_accession_code / _struct_ref_seq_dif.pdbx_seq_db_seq_num
Revision 1.5May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Copper chaperone


Theoretical massNumber of molelcules
Total (without water)7,4761
Polymers7,4761
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 50LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein Copper chaperone


Mass: 7475.661 Da / Num. of mol.: 1 / Mutation: N-TERMINUS CHANGED FROM MKQ TO AQ
Source method: isolated from a genetically manipulated source
Details: N-TERMINUS CHANGED FROM MKQ TO AQ / Source: (gene. exp.) Enterococcus hirae (bacteria) / Strain: WILD-TYPE
Description: E. HIRAE COPZ GENE CLONED IN E.COLI EXPRESSION VECTOR PQE6 WITH HELPER PLASMID PREP4
Cellular location: CYTOPLASM / Gene: copZ / Plasmid: PDZ69 / Species (production host): Escherichia coli / Gene (production host): COPZ / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / Keywords: N-TERMINUS CHANGED FROM MKQ TO AQ / References: UniProt: A0A1V8XBM5, UniProt: Q47840*PLUS
Sequence detailsMODIFIED EXPRESSION IN ESCHERICHIA COLI (REASON UNKNOWN)

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112QF-COSY
1213QF COSY
131E.COSY
1411H-1H-TOCSY
151NOESY
161J-HNHB
1713D-15N-RESOLVED 1H-1H-TOCSY
1813D 15N-RESOLVED NOESY
NMR detailsText: UNLABELED AND 15N-LABELED PROTEIN WAS USED. SAMPLES WERE PREPARED UNDER OXYGEN- FREE CONDITIONS AND SEALED.

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Sample preparation

DetailsContents: 10% D2O/90% H2O, 10UM NA2S2O4, 50MM NAPI
Sample conditionsIonic strength: 50 mM / pH: 7.0 / Temperature: 288.2 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRX500BrukerDRX5005001
Bruker DRX 600BrukerDRX 6006002
Bruker DRX 750BrukerDRX 7507503

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Processing

NMR software
NameDeveloperClassification
OPALpKORADI, GUENTERT, BILLETERrefinement
DYANAstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 50 / Conformers submitted total number: 20

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