+Open data
-Basic information
Entry | Database: PDB / ID: 2kdg | ||||||
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Title | Solution Structure of the 1st Ig domain of Myotilin | ||||||
Components | MyotilinMYOT | ||||||
Keywords | STRUCTURAL PROTEIN / Myotilin / Immonoglobulin domain / actin-binding / Cell membrane / Cytoplasm / Cytoskeleton / Disease mutation / Immunoglobulin domain / Limb-girdle muscular dystrophy / Membrane / Muscle protein / Polymorphism | ||||||
Function / homology | Function and homology information axon guidance receptor activity / dendrite self-avoidance / cell-cell adhesion mediator activity / structural constituent of muscle / alpha-actinin binding / homophilic cell adhesion via plasma membrane adhesion molecules / muscle contraction / synapse organization / sarcolemma / Z disc ...axon guidance receptor activity / dendrite self-avoidance / cell-cell adhesion mediator activity / structural constituent of muscle / alpha-actinin binding / homophilic cell adhesion via plasma membrane adhesion molecules / muscle contraction / synapse organization / sarcolemma / Z disc / actin cytoskeleton / actin binding / axon / neuronal cell body / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Heikkinen, O. / Kilpelainen, I. / Permi, P. / Koskela, H. / Ylanne, J. / Carpen, O. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2009 Title: Solution structure of the first immunoglobulin domain of human myotilin Authors: Heikkinen, O. / Permi, P. / Koskela, H. / Carpen, O. / Ylanne, J. / Kilpelainen, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kdg.cif.gz | 750.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kdg.ent.gz | 635.8 KB | Display | PDB format |
PDBx/mmJSON format | 2kdg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kd/2kdg ftp://data.pdbj.org/pub/pdb/validation_reports/kd/2kdg | HTTPS FTP |
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-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: Protein | Mass: 10971.523 Da / Num. of mol.: 1 Fragment: The first immunoglobulin domain (Residues 249-344) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MYOT, TTID / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q9UBF9 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: Dihedral angle restraints were extracted from alpha and beta carbon chemical shifts using TALOS program |
-Sample preparation
Details | Contents: 0.5mM [U-13C; U-15N] Myotilin 249-344-1, 20mM potassium phosphate-2, 140mM sodium chloride-3, 1mM DTT-4, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 140 / pH: 6.7 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 / Details: Born implicit solvent model | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy Conformers calculated total number: 40 / Conformers submitted total number: 25 / Representative conformer: 1 |