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Open data
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Basic information
Entry | Database: PDB / ID: 1mjd | ||||||
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Title | Structure of N-terminal domain of human doublecortin | ||||||
![]() | DOUBLECORTIN | ||||||
![]() | SIGNALING PROTEIN / DCX domain / ubiquitin-like fold / microtubule associated protein | ||||||
Function / homology | ![]() axoneme assembly / Neurofascin interactions / microtubule associated complex / microtubule organizing center / central nervous system development / neuron migration / retina development in camera-type eye / nervous system development / microtubule binding / microtubule ...axoneme assembly / Neurofascin interactions / microtubule associated complex / microtubule organizing center / 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 | ![]() | ||||||
Method | SOLUTION NMR / automatic NOESY cross-peaks assignment, torsion angle dynamics, simulated annealing | ||||||
![]() | 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. | ||||||
![]() | ![]() 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: ![]() 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. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 701.5 KB | Display | ![]() |
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PDB format | ![]() | 585.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344.7 KB | Display | ![]() |
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Full document | ![]() | 492.1 KB | Display | |
Data in XML | ![]() | 39.2 KB | Display | |
Data in CIF | ![]() | 64.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1mfwC ![]() 1mg4C C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() |
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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 |
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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: 6.0 / 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 |
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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 |