+Open data
-Basic information
Entry | Database: PDB / ID: 1z1v | ||||||
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Title | NMR structure of the Saccharomyces cerevisiae Ste50 SAM domain | ||||||
Components | STE50 protein | ||||||
Keywords | CELL CYCLE / all helix protein / SAM domain | ||||||
Function / homology | Function and homology information : / osmosensory signaling pathway via Sho1 osmosensor / signal transduction involved in filamentous growth / SAM domain binding / pheromone-dependent signal transduction involved in conjugation with cellular fusion / protein kinase regulator activity / regulation of cell cycle / cell cycle / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Kwan, J.J. / Warner, N. / Maini, J. / Pawson, T. / Donaldson, L.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2006 Title: Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction. Authors: Kwan, J.J. / Warner, N. / Maini, J. / Chan Tung, K.W. / Zakaria, H. / Pawson, T. / Donaldson, L.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1z1v.cif.gz | 32.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1z1v.ent.gz | 21.7 KB | Display | PDB format |
PDBx/mmJSON format | 1z1v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z1/1z1v ftp://data.pdbj.org/pub/pdb/validation_reports/z1/1z1v | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9309.657 Da / Num. of mol.: 1 / Fragment: ste50 SAM domain (residues 32-107) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Description: this protein fragment was cloned into the NdeI and BamHI sites of pET15b creating an aminoterminal hexahistidine tagged protein with an intervening thrombin protease cleavage site. After ...Description: this protein fragment was cloned into the NdeI and BamHI sites of pET15b creating an aminoterminal hexahistidine tagged protein with an intervening thrombin protease cleavage site. After thrombin treatment, the non-native residues GSH remained amino terminal to the native Ste50 sequence Gene: STE50 / Plasmid: pET15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P25344 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 3D heteronuclear techniques |
-Sample preparation
Details | Contents: 0.8 mM Ste50 SAM U-15N,13C, 20 mM sodium phosphate buffer, pH 7.8, 150 mM sodium chloride, 0.02 % sodium azide, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 150 mM NaCl / pH: 7.8 / Pressure: 1 atm / Temperature: 293 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Experimental observations: 615 intermolecular NOE distance restraints, 328 short range NOE distance restraints, 163 medium range NOE distance restraints, 149 long range NOE restraints, 42 ...Details: Experimental observations: 615 intermolecular NOE distance restraints, 328 short range NOE distance restraints, 163 medium range NOE distance restraints, 149 long range NOE restraints, 42 pairs of hydrogen bond distance restraints and 69 pairs of phi/psi dihedral angle restraints. An initial ensemble of 500 structures were calculated with CYANA 2.0. The top 25 structures with minimum restraint violations were refined in water using XPLOR-NIH and a protocol by C. Spronk. All 25 water refined structures had no NOE violations > 0.5 A and no dihedral violations > 5 degrees. For residues 35-100, the backbone RMSD of the ensemble is 0.75 +/- 0.14 A. Residues 28-32 and 101-107 are disordered. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |