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Yorodumi- PDB-1h3z: Solution structure of a PWWP domain from Schizosaccharomyces Pombe -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1h3z | ||||||
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| Title | Solution structure of a PWWP domain from Schizosaccharomyces Pombe | ||||||
Components | HYPOTHETICAL 62.8 KDA PROTEIN C215.07C | ||||||
Keywords | NUCLEAR PROTEIN / PWWP / CHROMATIN / BETA-BARREL | ||||||
| Function / homology | Function and homology informationNuA3 histone acetyltransferase complex / : / chromatin remodeling / nucleus Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / DISTANCE GEOMETRY SIMULATED ANNEALING | ||||||
Authors | Slater, L.M. / Allen, M.D. / Bycroft, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003Title: Structural Variation in Pwwp Domains Authors: Slater, L.M. / Allen, M.D. / Bycroft, M. | ||||||
| History |
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| Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1h3z.cif.gz | 766 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1h3z.ent.gz | 641.8 KB | Display | PDB format |
| PDBx/mmJSON format | 1h3z.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h3/1h3z ftp://data.pdbj.org/pub/pdb/validation_reports/h3/1h3z | HTTPS FTP |
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-Related structure data
| Similar structure data | |
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| Other databases |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein | Mass: 12210.151 Da / Num. of mol.: 1 / Fragment: PWWP DOMAIN, RESIDUES 118-225 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: SYNTHETIC GENE / Plasmid: PRSETA-GROEL / Production host: ![]() |
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| Compound details | THE PWWP DOMAIN IS NAMED AFTER A CONSERVED PRO-TRP-TRP-PRO MOTIF. IT IS PRESENT IN PROTEINS OF ...THE PWWP DOMAIN IS NAMED AFTER A CONSERVED PRO-TRP-TRP-PRO MOTIF. IT IS PRESENT IN PROTEINS OF NUCLEAR ORIGIN AND PLAYS A ROLE IN CEL GROWTH AND DIFFERENTI |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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| NMR experiment | Type: STANDARD |
| NMR details | Text: THE STRUCTURE WAS ASSIGNED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELLED PWWP. |
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Sample preparation
| Sample conditions | Ionic strength: 0.2 / pH: 6.5 / Temperature: 290 K |
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| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
| NMR software |
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| Refinement | Method: DISTANCE GEOMETRY SIMULATED ANNEALING / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE | ||||||||||||
| NMR ensemble | Conformer selection criteria: NO VIOLATION GREATER THAN 0.25A AND NO VIOLATIONS GREATER THAN 5 DEGREES Conformers calculated total number: 30 / Conformers submitted total number: 23 |
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