+Open data
-Basic information
Entry | Database: PDB / ID: 1b00 | ||||||
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Title | PHOB RECEIVER DOMAIN FROM ESCHERICHIA COLI | ||||||
Components | PHOSPHATE REGULON TRANSCRIPTIONAL REGULATORY PROTEIN PHOB | ||||||
Keywords | GENE REGULATION / TRANSCRIPTION FACTOR / PHOSPHATE REGULATION / ACTIVATION OF THE PHO REGULON / ALPHA/BETA DOUBLY WOUND FOLD | ||||||
Function / homology | Function and homology information bacterial-type RNA polymerase holo enzyme binding / phosphate ion transport / phosphorelay response regulator activity / DNA-binding transcription activator activity / regulation of DNA-templated transcription initiation / protein-DNA complex / transcription cis-regulatory region binding / regulation of DNA-templated transcription / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.88 Å | ||||||
Authors | Sola, M. / Gomis-Ruth, F.X. / Serrano, L. / Gonzalez, A. / Coll, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: Three-dimensional crystal structure of the transcription factor PhoB receiver domain. Authors: Sola, M. / Gomis-Ruth, F.X. / Serrano, L. / Gonzalez, A. / Coll, M. #1: Journal: Acta Crystallogr.,Sect.D / Year: 1998 Title: Overexpression, Purification, Crystallization and Preliminary X-Ray Diffraction Analysis of the Receiver Domain of Phob Authors: Sola, M. / Rueth, F.-X.G. / Serrano, L. / Gonzalez, A. / Coll, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b00.cif.gz | 62.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b00.ent.gz | 46.4 KB | Display | PDB format |
PDBx/mmJSON format | 1b00.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1b00_validation.pdf.gz | 369.8 KB | Display | wwPDB validaton report |
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Full document | 1b00_full_validation.pdf.gz | 374.8 KB | Display | |
Data in XML | 1b00_validation.xml.gz | 6.5 KB | Display | |
Data in CIF | 1b00_validation.cif.gz | 10.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b0/1b00 ftp://data.pdbj.org/pub/pdb/validation_reports/b0/1b00 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.520534, 0.841544, 0.14439), Vector: |
-Components
#1: Protein | Mass: 14515.757 Da / Num. of mol.: 2 / Fragment: RECEIVER DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: XL1-BLUE / Cellular location: CYTOPLASM / Plasmid: PBAT-4 / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P08402, UniProt: P0AFJ5*PLUS #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 33 % |
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Crystal grow | pH: 8 / Details: pH 8.0 |
Crystal grow | *PLUS Temperature: 395 K / Method: vapor diffusion, hanging drop |
Components of the solutions | *PLUS Conc.: 6.2 mg/ml / Common name: protein |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.885 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jul 1, 1996 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.885 Å / Relative weight: 1 |
Reflection | Resolution: 1.88→40 Å / Num. obs: 17784 / % possible obs: 84.8 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.039 / Net I/σ(I): 41.8 |
Reflection shell | Resolution: 1.88→1.95 Å / Rmerge(I) obs: 0.11 / Mean I/σ(I) obs: 7.5 / % possible all: 73.4 |
Reflection shell | *PLUS % possible obs: 73.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.88→20 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 30.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.88→20 Å
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Refine LS restraints |
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Xplor file |
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