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- PDB-1tl5: Solution structure of apoHAH1 -

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Basic information

Entry
Database: PDB / ID: 1tl5
TitleSolution structure of apoHAH1
ComponentsCopper transport protein ATOX1
KeywordsMETAL TRANSPORT / copper protein / copper chaperone / Menkes / Wilson / Structural Proteomics in Europe / SPINE / Structural Genomics
Function / homology
Function and homology information


metallochaperone activity / Ion influx/efflux at host-pathogen interface / copper-dependent protein binding / copper chaperone activity / copper ion transport / Detoxification of Reactive Oxygen Species / cuprous ion binding / intracellular copper ion homeostasis / response to oxidative stress / copper ion binding / cytosol
Similarity search - Function
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 transport protein ATOX1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics, simulated annealing, restrained energy minimization
AuthorsAnastassopoulou, I. / Banci, L. / Bertini, I. / Cantini, F. / Katsari, E. / Rosato, A. / Structural Proteomics in Europe (SPINE)
CitationJournal: Biochemistry / Year: 2004
Title: Solution Structure of the Apo and Copper(I)-Loaded Human Metallochaperone HAH1.
Authors: Anastassopoulou, I. / Banci, L. / Bertini, I. / Cantini, F. / Katsari, E. / Rosato, A.
History
DepositionJun 9, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 26, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 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: Copper transport protein ATOX1


Theoretical massNumber of molelcules
Total (without water)7,4131
Polymers7,4131
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)30 / 400target function
Representative

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Components

#1: Protein Copper transport protein ATOX1 / Metal transport protein ATX1


Mass: 7412.646 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ATOX1, HAH1 / Plasmid: pET20b+ / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: O00244

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
112CBCANH
122CBCA(CO)NH
132HNCO
142HN(CA)CO
152(H)CCH-TOCSY
1623D 13C-separated NOESY
1713D 15N-separated NOESY
1832D NOESY
1932D TOCSY
1102HNHA

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Sample preparation

Details
Solution-IDContentsSolvent system
11.0 mM apoHAH1 U-15N; 5mM DTT; 100 mM phosphate buffer90% H2O/10% D2O
22 mM apoHAH1 U-95% 13C,U-98% 15N; 5 mM DTT; 100 mM phosphate buffer90% H2O/10% D2O
32 mM unlabelled apoHAH1 ; 5 mM DTT; 100 mM phosphate buffer90% H2O/10% D2O
Sample conditionsIonic strength: 100 mM phosphate buffer / pH: 7 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE5001
Bruker AVANCEBrukerAVANCE6002
Bruker AVANCEBrukerAVANCE7003

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Processing

NMR software
NameVersionClassification
XwinNMRcollection
XEASY1.3data analysis
DIANA1.5structure solution
CYANA1structure solution
Amber5refinement
RefinementMethod: torsion angle dynamics, simulated annealing, restrained energy minimization
Software ordinal: 1
Details: the structures were based on a total of 1219 meaningful distance constraints, 99 dihedral angle restraints.
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 400 / Conformers submitted total number: 30

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