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Yorodumi- PDB-2yr3: Solution structure of the fourth Ig-like domain from myosin light... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2yr3 | ||||||
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Title | Solution structure of the fourth Ig-like domain from myosin light chain kinase, smooth muscle | ||||||
Components | Myosin light chain kinase, smooth muscle | ||||||
Keywords | TRANSFERASE / Ig domain / Myosin light chain kinase / smooth muscle / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information aorta smooth muscle tissue morphogenesis / tonic smooth muscle contraction / myosin-light-chain kinase / myosin light chain kinase activity / cellular hypotonic response / bleb assembly / positive regulation of calcium ion transport / positive regulation of wound healing / RHO GTPases activate PAKs / cleavage furrow ...aorta smooth muscle tissue morphogenesis / tonic smooth muscle contraction / myosin-light-chain kinase / myosin light chain kinase activity / cellular hypotonic response / bleb assembly / positive regulation of calcium ion transport / positive regulation of wound healing / RHO GTPases activate PAKs / cleavage furrow / smooth muscle contraction / Smooth Muscle Contraction / stress fiber / actin cytoskeleton / lamellipodium / actin binding / calmodulin binding / positive regulation of cell migration / protein phosphorylation / ATP binding / metal ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Qin, X.R. / Kurosaki, C. / Yoshida, M. / Hayahsi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the fourth Ig-like domain from myosin light chain kinase, smooth muscle Authors: Qin, X.R. / Kurosaki, C. / Yoshida, M. / Hayashi, F. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2yr3.cif.gz | 552.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2yr3.ent.gz | 462.1 KB | Display | PDB format |
PDBx/mmJSON format | 2yr3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2yr3_validation.pdf.gz | 341.2 KB | Display | wwPDB validaton report |
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Full document | 2yr3_full_validation.pdf.gz | 473.9 KB | Display | |
Data in XML | 2yr3_validation.xml.gz | 30.6 KB | Display | |
Data in CIF | 2yr3_validation.cif.gz | 48.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yr/2yr3 ftp://data.pdbj.org/pub/pdb/validation_reports/yr/2yr3 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Antibody | Mass: 10457.673 Da / Num. of mol.: 1 / Fragment: Ig domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: cell-free protein synthesis / Gene: MYLK / Plasmid: P061030-13 / References: UniProt: Q15746, myosin-light-chain kinase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.13mM 13C, 15N-labeled protein; 20mM d-Tris-HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: JEOL ECA / Manufacturer: JEOL / Model: ECA / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |