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Yorodumi- PDB-1mzk: NMR structure of kinase-interacting FHA domain of kinase associat... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mzk | ||||||
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Title | NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis | ||||||
Components | KINASE ASSOCIATED PROTEIN PHOSPHATASE | ||||||
Keywords | HYDROLASE / BETA SANDWICH | ||||||
Function / homology | Function and homology information [pyruvate kinase]-phosphatase activity / myosin phosphatase activity / protein-serine/threonine phosphatase / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing in cartesian space, residual dipolar couplings | ||||||
Authors | Lee, G. / Ding, Z. / Walker, J.C. / Van Doren, S.R. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2003 Title: NMR Structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase. Authors: Lee, G. / Ding, Z. / Walker, J.C. / Van Doren, S.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mzk.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1mzk.ent.gz | 892.8 KB | Display | PDB format |
PDBx/mmJSON format | 1mzk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mzk_validation.pdf.gz | 346.6 KB | Display | wwPDB validaton report |
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Full document | 1mzk_full_validation.pdf.gz | 684.9 KB | Display | |
Data in XML | 1mzk_validation.xml.gz | 117.3 KB | Display | |
Data in CIF | 1mzk_validation.cif.gz | 154.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mz/1mzk ftp://data.pdbj.org/pub/pdb/validation_reports/mz/1mzk | HTTPS FTP |
-Related structure data
Similar structure data |
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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: 14885.836 Da / Num. of mol.: 1 / Fragment: KINASE INTERACTION DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Strain: Columbia / Gene: KAPP / Plasmid: pGEX6P-1 / Production host: Escherichia coli (E. coli) / Strain (production host): DH5alpha References: UniProt: P46014, protein-serine/threonine phosphatase |
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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. Residues preceding 180 originated from linker of GST tag. Residues beyond 298 are unstructured. Note that in all the models ...Text: The structure was determined using triple-resonance NMR spectroscopy. Residues preceding 180 originated from linker of GST tag. Residues beyond 298 are unstructured. Note that in all the models the residues A175-A176 and A299-A313 are disordered and missing from the model |
-Sample preparation
Details |
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Sample conditions |
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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 |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing in cartesian space, residual dipolar couplings Software ordinal: 1 Details: the structures are based on 1313 interresidue NOE-derived distance constraints, 176 dihedral angle restraints, 54 distance restraints from hydrogen bonds,as well as 131 1Dnh, 55 1Dcaha, 37 ...Details: the structures are based on 1313 interresidue NOE-derived distance constraints, 176 dihedral angle restraints, 54 distance restraints from hydrogen bonds,as well as 131 1Dnh, 55 1Dcaha, 37 1Dnco, 58 1Dcaco residual dipolar coupling restraints. The covalent bond angle deviations, listed in remark 500, result from refinement using residual dipolar couplings and have occurred in some structures with high energy. The residues with torsion angle deviations are relatively mobile and poorly defined in the model. | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 30 |