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Yorodumi- PDB-1ihq: GLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT S... -
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-Basic information
Entry | Database: PDB / ID: 1ihq | ||||||
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Title | GLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT SHORT ALPHA TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1B | ||||||
Components | CHIMERIC PEPTIDE GlyTM1bZip: TROPOMYOSIN ALPHA CHAIN, BRAIN-3 and GENERAL CONTROL PROTEIN GCN4 | ||||||
Keywords | DE NOVO PROTEIN / TROPOMYOSIN / EXON 1B / ACTIN-BINDING / THIN-FILAMENT-REGULATION / NON-MUSCLE / ALPHA-HELIX / COILED-COIL / DIMER / GCN4 / CHIMERIC-PEPTIDE-MODEL / TW0-CHAINED / Structural Genomics / PSI / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG | ||||||
Function / homology | Function and homology information Striated Muscle Contraction / Smooth Muscle Contraction / positive regulation of heart rate by epinephrine / regulation of ATP-dependent activity / : / bleb / negative regulation of vascular associated smooth muscle cell migration / muscle filament sliding / protein localization to nuclear periphery / Activation of the AP-1 family of transcription factors ...Striated Muscle Contraction / Smooth Muscle Contraction / positive regulation of heart rate by epinephrine / regulation of ATP-dependent activity / : / bleb / negative regulation of vascular associated smooth muscle cell migration / muscle filament sliding / protein localization to nuclear periphery / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / actin filament capping / ruffle organization / nitrogen catabolite activation of transcription from RNA polymerase II promoter / positive regulation of ATP-dependent activity / sarcomere organization / ventricular cardiac muscle tissue morphogenesis / myofibril / negative regulation of vascular associated smooth muscle cell proliferation / TFIID-class transcription factor complex binding / amino acid biosynthetic process / positive regulation of cell adhesion / positive regulation of transcription initiation by RNA polymerase II / positive regulation of RNA polymerase II transcription preinitiation complex assembly / stress fiber / cardiac muscle contraction / positive regulation of stress fiber assembly / cellular response to amino acid starvation / cytoskeletal protein binding / negative regulation of cell migration / muscle contraction / actin filament organization / actin filament / wound healing / ruffle membrane / cellular response to reactive oxygen species / RNA polymerase II transcription regulator complex / : / disordered domain specific binding / actin filament binding / actin cytoskeleton / actin binding / regulation of cell shape / DNA-binding transcription activator activity, RNA polymerase II-specific / in utero embryonic development / transcription regulator complex / RNA polymerase II-specific DNA-binding transcription factor binding / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / intracellular signal transduction / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / protein heterodimerization activity / chromatin binding / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / protein-containing complex / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / 1156 CONFORMATIONALLY-RESTRICTING NOE CONSTRAINTS (OUT OF A TOTAL OF 1746 NOE DERIVED DISTANCES) 112 LOOSE DIHEDRAL ANGLE CONSTRAINTS, FORTY-EIGHT BACKBONE INTRA-HELICAL HYDROGEN BOND CONSTRAINTS WERE UTILILIZED. | ||||||
Authors | Greenfield, N.J. / Yuang, Y.J. / Palm, T. / Swapna, G.V. / Monleon, D. / Montelione, G.T. / Hitchcock-Degregori, S.E. / Northeast Structural Genomics Consortium (NESG) | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein. Authors: Greenfield, N.J. / Huang, Y.J. / Palm, T. / Swapna, G.V. / Monleon, D. / Montelione, G.T. / Hitchcock-DeGregori, S.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ihq.cif.gz | 242.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ihq.ent.gz | 210.1 KB | Display | PDB format |
PDBx/mmJSON format | 1ihq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ih/1ihq ftp://data.pdbj.org/pub/pdb/validation_reports/ih/1ihq | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4331.915 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: The chimera consists of an initial GLY, residues 2-20 of TROPOMYOSIN ALPHA CHAIN, BRAIN-3 and residues 21-38 of GENERAL CONTROL PROTEIN GCN4. Source: (gene. exp.) Rattus norvegicus, Saccharomyces cerevisiae Genus: Rattus, Saccharomyces / Species: , / Strain: , / Plasmid: pPROEX HTa / Production host: Escherichia coli (E. coli) / Strain (production host): DH5 / References: UniProt: P18344, UniProt: P03069 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: TRIPLE RESONANCE |
NMR details | Text: The structure was determine using triple-resonance NMR spectroscopy. Inter-chain interactions were determined using X-filtered NOESY experiments |
-Sample preparation
Details | Contents: 1-2 mM Solvent system: 100 mM NaCl, 10 mM phosphate, 10% Deuterium Oxide, pH 6.4 |
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Sample conditions | Ionic strength: 0.12 N / pH: 6.4 / Pressure: atmospheric atm / Temperature: 281 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian INOVA 500 / Manufacturer: Varian / Model: INOVA 500 / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: 1156 CONFORMATIONALLY-RESTRICTING NOE CONSTRAINTS (OUT OF A TOTAL OF 1746 NOE DERIVED DISTANCES) 112 LOOSE DIHEDRAL ANGLE CONSTRAINTS, FORTY-EIGHT BACKBONE INTRA-HELICAL HYDROGEN BOND CONSTRAINTS WERE UTILILIZED. Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JOURNAL CITATION ABOVE. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry, structures with the least restraint violations,target function Conformers calculated total number: 200 / Conformers submitted total number: 10 |