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Open data
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Basic information
Entry | Database: PDB / ID: 2llw | ||||||
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Title | Solution structure of the yeast Sti1 DP2 domain | ||||||
![]() | Heat shock protein STI1 | ||||||
![]() | CHAPERONE / DP domain / Alpha helix | ||||||
Function / homology | ![]() RND1 GTPase cycle / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / ATPase inhibitor activity / protein targeting to mitochondrion / Hsp70 protein binding / Hsp90 protein binding / protein localization / protein folding / mRNA binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | minimized average structure, model 1 | ||||||
Model type details | minimized average | ||||||
![]() | Schmid, A.B. / Lagleder, S. / Graewert, M.A. / Roehl, A. / Hagn, F. / Wandinger, S.K. / Cox, M.B. / Demmer, O. / Richter, K. / Groll, M. ...Schmid, A.B. / Lagleder, S. / Graewert, M.A. / Roehl, A. / Hagn, F. / Wandinger, S.K. / Cox, M.B. / Demmer, O. / Richter, K. / Groll, M. / Kessler, H. / Buchner, J. | ||||||
![]() | ![]() Title: The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. Authors: Schmid, A.B. / Lagleder, S. / Grawert, M.A. / Rohl, A. / Hagn, F. / Wandinger, S.K. / Cox, M.B. / Demmer, O. / Richter, K. / Groll, M. / Kessler, H. / Buchner, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 456.2 KB | Display | ![]() |
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PDB format | ![]() | 384.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 406 KB | Display | ![]() |
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Full document | ![]() | 527.8 KB | Display | |
Data in XML | ![]() | 25.6 KB | Display | |
Data in CIF | ![]() | 41.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2llvC ![]() 3upvC ![]() 3uq3C C: citing same article ( |
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Similar structure data | |
Other databases |
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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: 7926.000 Da / Num. of mol.: 1 / Fragment: STI1 2 domain residues 519-589 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: OR26.17, STI1, YOR027W / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 0.35 / pH: 7.5 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | |||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 21 |