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- PDB-1wik: Solution Structure of the PICOT homology 2 domain of the mouse PK... -

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Basic information

Entry
Database: PDB / ID: 1wik
TitleSolution Structure of the PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein
ComponentsThioredoxin-like protein 2
KeywordsELECTRON TRANSPORT / PICOT homology 2 domain / PICOT protein / thioredoxin like 2 / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI
Function / homology
Function and homology information


protein maturation by iron-sulfur cluster transfer / negative regulation of cardiac muscle hypertrophy / regulation of the force of heart contraction / [2Fe-2S] cluster assembly / iron-sulfur cluster binding / protein-disulfide reductase activity / protein kinase C binding / Z disc / cell cortex / intracellular iron ion homeostasis ...protein maturation by iron-sulfur cluster transfer / negative regulation of cardiac muscle hypertrophy / regulation of the force of heart contraction / [2Fe-2S] cluster assembly / iron-sulfur cluster binding / protein-disulfide reductase activity / protein kinase C binding / Z disc / cell cortex / intracellular iron ion homeostasis / dendrite / identical protein binding / metal ion binding / nucleus / cytosol
Similarity search - Function
Monothiol glutaredoxin-related / Glutaredoxin, PICOT-like / Glutaredoxin / Glutaredoxin / Glutaredoxin domain profile. / Thioredoxin / Thioredoxin domain profile. / Thioredoxin domain / Glutaredoxin / Glutaredoxin ...Monothiol glutaredoxin-related / Glutaredoxin, PICOT-like / Glutaredoxin / Glutaredoxin / Glutaredoxin domain profile. / Thioredoxin / Thioredoxin domain profile. / Thioredoxin domain / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsMiyamoto, K. / Tomizawa, T. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: To be Published
Title: Solution Structure of the PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein
Authors: Miyamoto, K. / Tomizawa, T. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S.
History
DepositionMay 28, 2004Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 28, 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 / struct_ref_seq_dif
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 / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Thioredoxin-like protein 2


Theoretical massNumber of molelcules
Total (without water)11,8401
Polymers11,8401
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)20 / 100structures with the least restraint violations, structures with the lowest energy, target function
RepresentativeModel #1lowest energy

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Components

#1: Protein Thioredoxin-like protein 2 / PKC-interacting cousin of thioredoxin / PKC-theta-interacting protein / PKCq-interacting protein


Mass: 11840.396 Da / Num. of mol.: 1 / Fragment: PICOT homology 2 domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 2410003E11 / Plasmid: P030421-03 / References: UniProt: Q9CQM9

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1213D 15N-separated NOESY

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Sample preparation

DetailsContents: 0.65mM PICOT homology 2 domain U-13C,15N; 20mM d-Tris-HCl(pH6.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10%D2O
Solvent system: 90% H2O, 10% D20
Sample conditionsIonic strength: 120mM / pH: 6.0 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3.5Brukercollection
NMRPipe20020425Delaglio, F.processing
NMRView5.0.4Johnson, B. A.data analysis
KUJIRA0.8996Kobayashi, N.data analysis
CYANA1.0.7Guentert, P.structure solution
CYANA1.0.7Guentert, P.refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations, structures with the lowest energy, target function
Conformers calculated total number: 100 / Conformers submitted total number: 20

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