+Open data
-Basic information
Entry | Database: PDB / ID: 1ip9 | ||||||
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Title | SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P | ||||||
Components | BEM1 PROTEIN | ||||||
Keywords | SIGNALING PROTEIN / ubiquitin alpha/beta roll | ||||||
Function / homology | Function and homology information RHO GTPases Activate NADPH Oxidases / conjugation with cellular fusion / cell morphogenesis involved in conjugation with cellular fusion / PAR polarity complex / site of polarized growth / cellular bud site selection / incipient cellular bud site / cellular bud tip / maintenance of protein location / cellular bud neck ...RHO GTPases Activate NADPH Oxidases / conjugation with cellular fusion / cell morphogenesis involved in conjugation with cellular fusion / PAR polarity complex / site of polarized growth / cellular bud site selection / incipient cellular bud site / cellular bud tip / maintenance of protein location / cellular bud neck / regulation of Rho protein signal transduction / mating projection tip / phosphatidylinositol-3-phosphate binding / protein-macromolecule adaptor activity / cell cortex / molecular adaptor activity / cytoskeleton / mitochondrion / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / dynamical simulated annealing | ||||||
Authors | Terasawa, H. / Noda, Y. / Ito, T. / Hatanaka, H. / Ichikawa, S. / Ogura, K. / Sumimoto, H. / Inagaki, F. | ||||||
Citation | Journal: EMBO J. / Year: 2001 Title: Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif. Authors: Terasawa, H. / Noda, Y. / Ito, T. / Hatanaka, H. / Ichikawa, S. / Ogura, K. / Sumimoto, H. / Inagaki, F. #1: Journal: Embo J. / Year: 2001 Title: Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions Authors: Ito, T. / Matsui, Y. / Ago, T. / Ota, K. / Sumimoto, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ip9.cif.gz | 586.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ip9.ent.gz | 502.9 KB | Display | PDB format |
PDBx/mmJSON format | 1ip9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ip/1ip9 ftp://data.pdbj.org/pub/pdb/validation_reports/ip/1ip9 | HTTPS FTP |
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-Related 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: 9519.925 Da / Num. of mol.: 1 / Fragment: PB1 DOMAIN(RESIDUES 472-551) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Plasmid: PPROEX-HTA / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: P29366 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details | Contents: 2mM Bem PB1 U-15N, 13C; 50mM potassium phosphate pH 6.3; 150mM sodium chloride; 1mM sodium azide; 90% H2O, 10% D2O Solvent system: 90% H2O, 10% D2O, 100% D2O |
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Sample conditions | Ionic strength: 50mM potassium phosphate, 150mM sodium chloride pH: 6.3 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-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: dynamical simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 1334 restraints, 1269 are NOE-derived distance constraints, 65 dihedral angle restraints. | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |