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- PDB-1ujd: Solution Structure of RSGI RUH-003, a PDZ domain of hypothetical ... -

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Basic information

Entry
Database: PDB / ID: 1ujd
TitleSolution Structure of RSGI RUH-003, a PDZ domain of hypothetical KIAA0559 protein from human cDNA
ComponentsKIAA0559 protein
KeywordsSTRUCTURAL GENOMICS / UNKNOWN FUNCTION / PDZ domain / human cdna / RIKEN Structural Genomics/Proteomics Initiative / RSGI
Function / homology
Function and homology information


presynaptic active zone assembly / presynapse to nucleus signaling pathway / structural constituent of presynaptic active zone / cytoskeleton of presynaptic active zone / profilin binding / protein localization to synapse / regulation of exocytosis / calcium-dependent phospholipid binding / insulin secretion / synaptic vesicle exocytosis ...presynaptic active zone assembly / presynapse to nucleus signaling pathway / structural constituent of presynaptic active zone / cytoskeleton of presynaptic active zone / profilin binding / protein localization to synapse / regulation of exocytosis / calcium-dependent phospholipid binding / insulin secretion / synaptic vesicle exocytosis / cAMP-mediated signaling / GABA-ergic synapse / cytoskeleton organization / postsynaptic density / cytoskeleton / axon / glutamatergic synapse / synapse / calcium ion binding / extracellular exosome
Similarity search - Function
Zinc finger, piccolo-type / Protein piccolo / Piccolo, FYVE-related domain 1 / Piccolo Zn-finger / C2 domain / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain profile. / PDZ domain / Pdz3 Domain ...Zinc finger, piccolo-type / Protein piccolo / Piccolo, FYVE-related domain 1 / Piccolo Zn-finger / C2 domain / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain profile. / PDZ domain / Pdz3 Domain / C2 domain superfamily / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Zinc finger, FYVE/PHD-type / Zinc finger, RING/FYVE/PHD-type / Roll / Mainly Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing, torsion angle dynamics
AuthorsOhashi, W. / Hirota, H. / Yamazaki, T. / Muto, Y. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: To be published
Title: Solution Structure of RSGI RUH-003, a PDZ domain of hypothetical KIAA0559 protein from human cDNA
Authors: Ohashi, W. / Hirota, H. / Yamazaki, T. / Muto, Y. / Yokoyama, S.
History
DepositionJul 31, 2003Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 31, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 27, 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
Revision 1.4Dec 27, 2023Group: 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: KIAA0559 protein


Theoretical massNumber of molelcules
Total (without water)12,2801
Polymers12,2801
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 / 100The submitted conformer models are those with the lowest number of target function
RepresentativeModel #1lowest target function

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Components

#1: Protein KIAA0559 protein


Mass: 12279.770 Da / Num. of mol.: 1 / Fragment: PDZ domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / References: UniProt: Q9Y6V0

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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
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy

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Sample preparation

DetailsContents: 1.5mM RSGI RUH-003 U-13C,15N; 20mM Tris-HCl, 100mM NaCl, 1mM DTT U-2H, 0.02% NaN3; 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 100mM NaCl / pH: 7.0 / 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: 800 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3.1Brukercollection
NMRPipe2.1Delaglioprocessing
NMRView5.0.4Johnsondata analysis
CYANA1.0.7Guentertstructure solution
CYANA1.0.7Guentertrefinement
RefinementMethod: simulated annealing, torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest target function
NMR ensembleConformer selection criteria: The submitted conformer models are those with the lowest number of target function
Conformers calculated total number: 100 / Conformers submitted total number: 20

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