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Yorodumi- PDB-1r63: STRUCTURAL ROLE OF A BURIED SALT BRIDGE IN THE 434 REPRESSOR DNA-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1r63 | ||||||
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Title | STRUCTURAL ROLE OF A BURIED SALT BRIDGE IN THE 434 REPRESSOR DNA-BINDING DOMAIN, NMR, 20 STRUCTURES | ||||||
Components | REPRESSOR PROTEIN FROM BACTERIOPHAGE 434 | ||||||
Keywords | GENE REGULATING PROTEIN / PHAGE 434 REPRESSOR / HELIX-TURN-HELIX / DNA-BINDING DOMAIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Phage 434 (virus) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY WITH DIANA, ENERGY MINIMIZATION WITH OPAL | ||||||
Authors | Pervushin, K.V. / Billeter, M. / Siegal, G. / Wuthrich, K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: Structural role of a buried salt bridge in the 434 repressor DNA-binding domain. Authors: Pervushin, K. / Billeter, M. / Siegal, G. / Wuthrich, K. #1: Journal: J.Mol.Biol. / Year: 1992 Title: Determination of the Nuclear Magnetic Resonance Solution Structure of the DNA-Binding Domain (Residues 1 to 69) of the 434 Repressor and Comparison with the X-Ray Crystal Structure Authors: Neri, D. / Billeter, M. / Wuthrich, K. #2: Journal: J.Mol.Biol. / Year: 1989 Title: Structure of the Amino-Terminal Domain of Phage 434 Repressor at 2.0 A Resolution Authors: Mondragon, A. / Subbiah, S. / Almo, S.C. / Drottar, M. / Harrison, S.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1r63.cif.gz | 427.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1r63.ent.gz | 364.6 KB | Display | PDB format |
PDBx/mmJSON format | 1r63.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1r63_validation.pdf.gz | 356.6 KB | Display | wwPDB validaton report |
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Full document | 1r63_full_validation.pdf.gz | 463.3 KB | Display | |
Data in XML | 1r63_validation.xml.gz | 18.1 KB | Display | |
Data in CIF | 1r63_validation.cif.gz | 32.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r6/1r63 ftp://data.pdbj.org/pub/pdb/validation_reports/r6/1r63 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 6900.871 Da / Num. of mol.: 1 / Fragment: DNA-BINDING DOMAIN, RESIDUES 1 - 63 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Phage 434 (virus) / Genus: Lambda-like viruses / Species: Enterobacteria phage lambda / Production host: Escherichia coli (E. coli) / References: UniProt: P16117 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 4.8 / Temperature: 286 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX600 / Manufacturer: Bruker / Model: AMX600 / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY WITH DIANA, ENERGY MINIMIZATION WITH OPAL Software ordinal: 1 | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: DIANA PENALTY FUNCTION / Conformers calculated total number: 20 / Conformers submitted total number: 20 |