+Open data
-Basic information
Entry | Database: PDB / ID: 1mjd | ||||||
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Title | Structure of N-terminal domain of human doublecortin | ||||||
Components | DOUBLECORTIN | ||||||
Keywords | SIGNALING PROTEIN / DCX domain / ubiquitin-like fold / microtubule associated protein | ||||||
Function / homology | Function and homology information axoneme assembly / Neurofascin interactions / microtubule associated complex / central nervous system development / neuron migration / retina development in camera-type eye / nervous system development / microtubule binding / microtubule / cytoskeleton ...axoneme assembly / Neurofascin interactions / microtubule associated complex / central nervous system development / neuron migration / retina development in camera-type eye / nervous system development / microtubule binding / microtubule / cytoskeleton / intracellular signal transduction / neuron projection / protein kinase binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / automatic NOESY cross-peaks assignment, torsion angle dynamics, simulated annealing | ||||||
Authors | Kim, M.H. / Cierpicki, T. / Derewenda, U. / Krowarsch, D. / Feng, Y. / Devedjiev, Y. / Dauter, Z. / Walsh, C.A. / Otlewski, J. / Bushweller, J.H. / Derewenda, Z.S. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2003 Title: The DCX-domain Tandems of Doublecortin and Doublecortin-like Kinase Authors: Kim, M.H. / Cierpicki, T. / Derewenda, U. / Krowarsch, D. / Feng, Y. / Devedjiev, Y. / Dauter, Z. / Walsh, C.A. / Otlewski, J. / Bushweller, J.H. / Derewenda, Z.S. #1: Journal: J.Biomol.NMR / Year: 2003 Title: Letter to the Editor: Assignment of 1H, 13C and 15N Resonances of the N-terminal Microtubule-Binding Domain of Human Doublecortin Authors: Cierpicki, T. / Kim, M.H. / Otlewski, J. / Derewenda, Z.S. / Bushweller, J.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mjd.cif.gz | 701.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mjd.ent.gz | 585.8 KB | Display | PDB format |
PDBx/mmJSON format | 1mjd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mjd_validation.pdf.gz | 344.7 KB | Display | wwPDB validaton report |
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Full document | 1mjd_full_validation.pdf.gz | 492.1 KB | Display | |
Data in XML | 1mjd_validation.xml.gz | 39.2 KB | Display | |
Data in CIF | 1mjd_validation.cif.gz | 64.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mj/1mjd ftp://data.pdbj.org/pub/pdb/validation_reports/mj/1mjd | HTTPS FTP |
-Related structure data
Related structure data | 1mfwC 1mg4C C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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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: 12972.494 Da / Num. of mol.: 1 / Fragment: N-terminal domain, Residues (45-150) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DCX / Plasmid: GSTUni1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: O43602 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy |
-Sample preparation
Details | Contents: 1mM doublecortin 45-150 U-15N, 13C; 50mM phosphate buffer; 5mMM DTT Solvent system: 90% H2O, 10% H2O |
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Sample conditions | pH: 6 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: automatic NOESY cross-peaks assignment, torsion angle dynamics, simulated annealing Software ordinal: 1 Details: NOESY cross-peaks were assigned using combination of manual and automatic assignment employing NOAH/DYANA program. The final set of structures was refined in CNS. | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |