+Open data
-Basic information
Entry | Database: PDB / ID: 1bpv | ||||||
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Title | TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES | ||||||
Components | TITIN | ||||||
Keywords | CONNECTIN / TITIN / FIBRONECTIN TYPE III | ||||||
Function / homology | Function and homology information sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / detection of muscle stretch / muscle alpha-actinin binding / cardiac muscle tissue morphogenesis / regulation of catalytic activity / Striated Muscle Contraction ...sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / detection of muscle stretch / muscle alpha-actinin binding / cardiac muscle tissue morphogenesis / regulation of catalytic activity / Striated Muscle Contraction / mitotic chromosome condensation / cardiac muscle hypertrophy / M band / actinin binding / I band / cardiac muscle cell development / regulation of protein kinase activity / structural constituent of muscle / sarcomere organization / skeletal muscle thin filament assembly / striated muscle thin filament / striated muscle contraction / protein kinase A signaling / cardiac muscle contraction / muscle contraction / condensed nuclear chromosome / positive regulation of protein secretion / Z disc / response to calcium ion / : / actin filament binding / Platelet degranulation / protein tyrosine kinase activity / protease binding / calmodulin binding / non-specific serine/threonine protein kinase / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / extracellular exosome / extracellular region / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Muhle-Goll, C. / Pastore, A. / Nilges, M. | ||||||
Citation | Journal: Structure / Year: 1998 Title: The three-dimensional structure of a type I module from titin: a prototype of intracellular fibronectin type III domains. Authors: Goll, C.M. / Pastore, A. / Nilges, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bpv.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1bpv.ent.gz | 1.5 MB | Display | PDB format |
PDBx/mmJSON format | 1bpv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bp/1bpv ftp://data.pdbj.org/pub/pdb/validation_reports/bp/1bpv | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12476.979 Da / Num. of mol.: 1 / Fragment: 71 TH DOMAIN FROM THE A-BAND / Mutation: I9V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Tissue: MUSCLESkeletal muscle / Organ: HEART / Organelle: SARCOMERE / Plasmid: PET8C / Gene (production host): TITIN GENE / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 PLYSS / References: UniProt: Q10466, UniProt: Q8WZ42*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: REPRESENTATIVE MODEL NUMBER: 1 THE STRUCTURE WAS DETERMINED USING A 3D N15-EDITED NOESY-HSQC AND HOMONUCLEAR 2D NOESY EXPERIMENTS. |
-Sample preparation
Details | Contents: 10 MM ACETATE BUFFER |
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Sample conditions | Ionic strength: 50 mM NACL / pH: 5.6 / Temperature: 310 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX600 / Manufacturer: Bruker / Model: AMX600 / Field strength: 600 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: STRUCTURE CALCULATIONS WERE PERFORMED WITH THE SUPPORT OF THE ARIA (AMBIGUOUS RESTRAINTS FOR ITERATIVE ASSIGNMENT) PROTOCOL (NILGES ET AL., J. MOL. BIOL. 269, 408-422). 100 STRUCTURES WERE ...Details: STRUCTURE CALCULATIONS WERE PERFORMED WITH THE SUPPORT OF THE ARIA (AMBIGUOUS RESTRAINTS FOR ITERATIVE ASSIGNMENT) PROTOCOL (NILGES ET AL., J. MOL. BIOL. 269, 408-422). 100 STRUCTURES WERE CALCULATED OF WHICH THE BEST 50 STRUCTURES WERE SELECTED. | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 1 / Conformers submitted total number: 50 |