+Open data
-Basic information
Entry | Database: PDB / ID: 1udd | ||||||
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Title | TenA homologue protein from P.horikoshii OT3 | ||||||
Components | transcriptional regulator | ||||||
Keywords | LIPID BINDING PROTEIN / Helix-bundle | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Pyrococcus horikoshii (archaea) | ||||||
Method | X-RAY DIFFRACTION / MAD / Resolution: 2.15 Å | ||||||
Authors | Itou, H. / Yao, M. / Watanabe, N. / Tanaka, I. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2004 Title: Structure analysis of PH1161 protein, a transcriptional activator TenA homologue from the hyperthermophilic archaeon Pyrococcus horikoshii. Authors: Itou, H. / Yao, M. / Watanabe, N. / Tanaka, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1udd.cif.gz | 180.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1udd.ent.gz | 147.5 KB | Display | PDB format |
PDBx/mmJSON format | 1udd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1udd_validation.pdf.gz | 459.8 KB | Display | wwPDB validaton report |
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Full document | 1udd_full_validation.pdf.gz | 479.2 KB | Display | |
Data in XML | 1udd_validation.xml.gz | 33 KB | Display | |
Data in CIF | 1udd_validation.cif.gz | 45.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ud/1udd ftp://data.pdbj.org/pub/pdb/validation_reports/ud/1udd | 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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Unit cell |
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-Components
#1: Protein | Mass: 26620.748 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus horikoshii (archaea) / Strain: OT3 / Plasmid: PET26b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O58873 #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: 2.62 Å3/Da / Density % sol: 53.13 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: PEG1000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Sep 13, 2002 / Details: mirrors |
Radiation | Monochromator: Ni filter / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→40 Å / Num. all: 58766 / Num. obs: 58735 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rsym value: 0.082 / Net I/σ(I): 7 |
Reflection shell | Resolution: 2.15→2.27 Å / Redundancy: 3.7 % / Mean I/σ(I) obs: 3 / Num. unique all: 8595 / Rsym value: 0.284 / % possible all: 99.7 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.15→10 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.15→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.23 Å
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