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Yorodumi- PDB-1fbs: HEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fbs | ||||||
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Title | HEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237A MUTATION | ||||||
Components | HEAT SHOCK FACTOR PROTEIN | ||||||
Keywords | TRANSCRIPTION / helical bulge / helical kink / helix-turn-helix | ||||||
Function / homology | Function and homology information protein-DNA complex / cellular response to heat / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / regulation of transcription by RNA polymerase II / DNA binding / nucleus Similarity search - Function | ||||||
Biological species | Kluyveromyces lactis (yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2 Å | ||||||
Authors | Hardy, J.A. / Nelson, H.C.M. | ||||||
Citation | Journal: Protein Sci. / Year: 2000 Title: Proline in alpha-helical kink is required for folding kinetics but not for kinked structure, function, or stability of heat shock transcription factor. Authors: Hardy, J.A. / Nelson, H.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fbs.cif.gz | 51.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fbs.ent.gz | 37.4 KB | Display | PDB format |
PDBx/mmJSON format | 1fbs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fbs_validation.pdf.gz | 369.8 KB | Display | wwPDB validaton report |
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Full document | 1fbs_full_validation.pdf.gz | 372.2 KB | Display | |
Data in XML | 1fbs_validation.xml.gz | 5.3 KB | Display | |
Data in CIF | 1fbs_validation.cif.gz | 8.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fb/1fbs ftp://data.pdbj.org/pub/pdb/validation_reports/fb/1fbs | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 10695.971 Da / Num. of mol.: 2 / Fragment: HSF DNA BINDING DOMAIN / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) Kluyveromyces lactis (yeast) / Plasmid: PET3B/PLYSS / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P22121 #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: 2.11 Å3/Da / Density % sol: 41.83 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 100 mM Citrate buffer pH 6.0, 26% Polyethylene glycol average molecular weight 4000, 200 mM Ammonium acetate , VAPOR DIFFUSION, HANGING DROP, temperature 4.0K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / PH range low: 6.2 / PH range high: 5.6 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 24, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. all: 16534 / Biso Wilson estimate: 5.1 Å2 / Rmerge(I) obs: 0.053 |
Reflection | *PLUS % possible obs: 90.8 % |
-Processing
Software |
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Refinement | Resolution: 2→19.73 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 1006742.77 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 44.95 Å2 / ksol: 0.404 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 11.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→19.73 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.13 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 10.4 % / Rfactor Rfree: 0.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 11.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.311 / % reflection Rfree: 11.7 % / Rfactor Rwork: 0.237 |