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Open data
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Basic information
Entry | Database: PDB / ID: 3hsf | |||||||||
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Title | HEAT SHOCK TRANSCRIPTION FACTOR (HSF) | |||||||||
![]() | HEAT SHOCK TRANSCRIPTION FACTOR | |||||||||
![]() | TRANSCRIPTION REGULATION | |||||||||
Function / homology | ![]() 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 | ![]() | |||||||||
Method | SOLUTION NMR | |||||||||
![]() | Damberger, F.F. / Pelton, J.G. / Liu, C. / Cho, H. / Harrison, C.J. / Nelson, H.C.M. / Wemmer, D.E. | |||||||||
![]() | ![]() Title: Refined solution structure and dynamics of the DNA-binding domain of the heat shock factor from Kluyveromyces lactis. Authors: Damberger, F.F. / Pelton, J.G. / Liu, C. / Cho, H. / Harrison, C.J. / Nelson, H.C. / Wemmer, D.E. #1: ![]() Title: Crystal Structure of the DNA Binding Domain of the Heat Shock Transcription Factor Authors: Harrison, C.J. / Bohm, A.A. / Nelson, H.C.M. #2: ![]() Title: Solution Structure of the DNA-Binding Domain of the Heat Shock Transcription Factor Determined by Multidimensional Heteronuclear Magnetic Resonance Spectroscopy Authors: Damberger, F.F. / Pelton, J.G. / Harrison, C.J. / Nelson, H.C.M. / Wemmer, D.E. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 877.2 KB | Display | ![]() |
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PDB format | ![]() | 736.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 350.1 KB | Display | ![]() |
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Full document | ![]() | 558.8 KB | Display | |
Data in XML | ![]() | 43.9 KB | Display | |
Data in CIF | ![]() | 72.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 10950.279 Da / Num. of mol.: 1 / Mutation: INS(E89-RHA) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other |
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Processing
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NMR software | Name: ![]() | ||||||||
NMR ensemble | Conformers submitted total number: 30 |