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Yorodumi- PDB-1uez: Solution structure of the first PDZ domain of human KIAA1526 protein -
+Open data
-Basic information
Entry | Database: PDB / ID: 1uez | ||||||
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Title | Solution structure of the first PDZ domain of human KIAA1526 protein | ||||||
Components | KIAA1526 Protein | ||||||
Keywords | PROTEIN BINDING / PDZ domain / structural genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information paranodal junction maintenance / periciliary membrane compartment / stereocilia ankle link / USH2 complex / inner ear receptor cell differentiation / stereocilia ankle link complex / sensory perception of light stimulus / cerebellar Purkinje cell layer formation / photoreceptor connecting cilium / inner ear receptor cell stereocilium organization ...paranodal junction maintenance / periciliary membrane compartment / stereocilia ankle link / USH2 complex / inner ear receptor cell differentiation / stereocilia ankle link complex / sensory perception of light stimulus / cerebellar Purkinje cell layer formation / photoreceptor connecting cilium / inner ear receptor cell stereocilium organization / stereocilium tip / detection of mechanical stimulus involved in sensory perception of sound / stereocilium / retina homeostasis / auditory receptor cell stereocilium organization / Sensory processing of sound by outer hair cells of the cochlea / Sensory processing of sound by inner hair cells of the cochlea / photoreceptor inner segment / ciliary basal body / establishment of localization in cell / actin filament / sensory perception of sound / establishment of protein localization / cilium / growth cone / synapse / positive regulation of gene expression / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Li, H. / Kigawa, T. / Muto, Y. / Koshiba, S. / Inoue, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the first PDZ domain of human KIAA1526 protein Authors: Li, H. / Kigawa, T. / Muto, Y. / Koshiba, S. / Inoue, M. / Yokoyama, S. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uez.cif.gz | 580.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uez.ent.gz | 483.8 KB | Display | PDB format |
PDBx/mmJSON format | 1uez.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1uez_validation.pdf.gz | 341.7 KB | Display | wwPDB validaton report |
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Full document | 1uez_full_validation.pdf.gz | 496.6 KB | Display | |
Data in XML | 1uez_validation.xml.gz | 41 KB | Display | |
Data in CIF | 1uez_validation.cif.gz | 61.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ue/1uez ftp://data.pdbj.org/pub/pdb/validation_reports/ue/1uez | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10401.824 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 / Gene: KAZUSA cDNA fj04743 / Plasmid: P021030-45 / References: UniProt: Q9P202 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.6mM PDZ domain U-15N, 13C; 20mM d-Tris HCl(7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer 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 |