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Yorodumi- PDB-1dcj: SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dcj | ||||||
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Title | SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION | ||||||
Components | YHHP PROTEIN | ||||||
Keywords | STRUCTURAL GENOMICS / UNKNOWN FUNCTION / ALPHA-BETA SANDWICH | ||||||
Function / homology | Function and homology information sulfur carrier activity / tRNA wobble position uridine thiolation / Mo-molybdopterin cofactor biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / HYBRID DISTANCE GEOMETRY-SIMULATED ANNEALING | ||||||
Authors | Katoh, E. / Hatta, T. / Shindo, H. / Mizuno, T. / Yamazaki, T. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division. Authors: Katoh, E. / Hatta, T. / Shindo, H. / Ishii, Y. / Yamada, H. / Mizuno, T. / Yamazaki, T. #1: Journal: J.Bacteriol. / Year: 1998 Title: The yhhP Gene Encoding a Small Ubiquitous Protein is Fundamental for Normal Cell Growth of Escherichia Coli Authors: Yamashino, T. / Isomura, M. / Ueguchi, C. / Mizuno, T. #2: Journal: To be Published Title: Characterization of the yhhP Gene Whose Deficiency Results in a Non-Divided Filamentous Cell Morphology in Escherichia coli Authors: Ishii, Y. / Yamada, H. / Yamazaki, T. / Katoh, E. / Mizuno, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dcj.cif.gz | 487.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dcj.ent.gz | 426.5 KB | Display | PDB format |
PDBx/mmJSON format | 1dcj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dc/1dcj ftp://data.pdbj.org/pub/pdb/validation_reports/dc/1dcj | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9105.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET21 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A890 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 750 MHz |
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-Processing
NMR software |
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Refinement | Method: HYBRID DISTANCE GEOMETRY-SIMULATED ANNEALING / Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON A TOTAL OF 1655 RESTRAINTS, 1390 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 211 DIHEDRAL ANGLE RESTRAINTS, 54 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |