+Open data
-Basic information
Entry | Database: PDB / ID: 2o13 | ||||||
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Title | Solution structure of the C-terminal LIM domain of MLP/CRP3 | ||||||
Components | Muscle LIM protein | ||||||
Keywords | METAL BINDING PROTEIN / LIM domain / zinc binding / CRP / MLP | ||||||
Function / homology | Function and homology information positive regulation of actin filament severing / negative regulation of actin filament severing / muscle tissue development / T-tubule organization / protein kinase C signaling / protein localization to organelle / telethonin binding / cardiac myofibril assembly / detection of muscle stretch / regulation of the force of heart contraction ...positive regulation of actin filament severing / negative regulation of actin filament severing / muscle tissue development / T-tubule organization / protein kinase C signaling / protein localization to organelle / telethonin binding / cardiac myofibril assembly / detection of muscle stretch / regulation of the force of heart contraction / negative regulation of myoblast differentiation / cardiac muscle tissue development / cardiac muscle hypertrophy / actinin binding / structural constituent of muscle / sarcomere organization / muscle cell cellular homeostasis / positive regulation of myoblast differentiation / regulation of protein localization to plasma membrane / cardiac muscle contraction / skeletal muscle tissue development / Z disc / intracellular calcium ion homeostasis / insulin receptor signaling pathway / glucose homeostasis / actin binding / cytoskeleton / inflammatory response / positive regulation of transcription by RNA polymerase II / nucleoplasm / identical protein binding / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Schallus, T. / Muhle-Goll, C. / Edlich, C. | ||||||
Citation | Journal: To be Published Title: Structure of the muscular LIM protein MLP and its interaction with Actinin Authors: Schallus, T. / Stier, G. / Feher, K. / Muhle-Goll, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2o13.cif.gz | 385.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2o13.ent.gz | 324.2 KB | Display | PDB format |
PDBx/mmJSON format | 2o13.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o1/2o13 ftp://data.pdbj.org/pub/pdb/validation_reports/o1/2o13 | 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: 6423.557 Da / Num. of mol.: 1 / Fragment: LIM zinc-binding domain 2, residues 119-176 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CSRP3, CLP, MLP / Plasmid: pET24 / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21 DE3 pLysS / References: UniProt: P50461 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.2mM C-terminal LIM domain, 20mM phosphate buffer K, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 150mM KCl / pH: 6.8 / Pressure: ambient / Temperature: 295 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
-Processing
NMR software | Name: CNS / Developer: Brunger, Adams, Clore, Gros, Nilges and Read / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: zinc coordination fixed by explicit bonds and angles |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |