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Yorodumi- PDB-5huz: Solution structure of coiled coil domain of myosin binding subuni... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5huz | ||||||||||||
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Title | Solution structure of coiled coil domain of myosin binding subunit of myosin light chain phosphatase | ||||||||||||
Components | Protein phosphatase 1 regulatory subunit 12A | ||||||||||||
Keywords | SIGNALING PROTEIN / VASCULAR SMOOTH MUSCLE CELL | ||||||||||||
Function / homology | Function and homology information : / : / phosphatase regulator activity / PTW/PP1 phosphatase complex / contractile muscle fiber / regulation of nucleocytoplasmic transport / negative regulation of catalytic activity / RHO GTPases Activate ROCKs / RHO GTPases activate CIT / enzyme inhibitor activity ...: / : / phosphatase regulator activity / PTW/PP1 phosphatase complex / contractile muscle fiber / regulation of nucleocytoplasmic transport / negative regulation of catalytic activity / RHO GTPases Activate ROCKs / RHO GTPases activate CIT / enzyme inhibitor activity / centrosome cycle / A band / RHO GTPases activate PAKs / regulation of cell adhesion / stress fiber / RHO GTPases activate PKNs / 14-3-3 protein binding / protein dephosphorylation / kinetochore / Z disc / cellular response to xenobiotic stimulus / Regulation of PLK1 Activity at G2/M Transition / actin cytoskeleton / mitotic cell cycle / focal adhesion / centrosome / nucleolus / protein kinase binding / signal transduction / positive regulation of transcription by RNA polymerase II / nucleoplasm / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | SOLUTION NMR / torsion angle dynamics, molecular dynamics | ||||||||||||
Authors | Sharma, A.K. / Birrane, G. / Anklin, C. / Rigby, A.C. / Pollak, M. / Alper, S.L. | ||||||||||||
Citation | #1: Journal: Protein Pept Lett. / Year: 2014 Title: NMR assignment and secondary structure of coiled coil domain of C-terminal myosin binding subunit of myosin phosphatase Authors: Sharma, A.K. / Rigby, A.C. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5huz.cif.gz | 682.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5huz.ent.gz | 582.9 KB | Display | PDB format |
PDBx/mmJSON format | 5huz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5huz_validation.pdf.gz | 561.7 KB | Display | wwPDB validaton report |
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Full document | 5huz_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 5huz_validation.xml.gz | 100.4 KB | Display | |
Data in CIF | 5huz_validation.cif.gz | 91 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hu/5huz ftp://data.pdbj.org/pub/pdb/validation_reports/hu/5huz | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 5788.542 Da / Num. of mol.: 2 / Fragment: residues 931-978 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: Bacteria / Gene: PPP1R12A, MBS, MYPT1 / Plasmid: pET28a / Organ (production host): HOMO SAPIENS / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: O14974 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 1.0 mM [U-99% 13C; U-99% 15N] coiled coil mbs-1, 1.0 mM [U-99% 15N] coiled coil mbs-2, 1.0 mM coiled coil mbs-3, 90% H2O/10% D2O Details: 8% D2O, 1.0 MM [U-99% 13C; U-99% 15N] PROTEIN, 1 % DSS, 25 MM POTASSIUM PHOSPHATE, 0.05 % SODIUM AZIDE, 10 MM SODIUM CHLORIDE, 92% H2O/8% D2O Label: 13C,15N_sample, 15N_sample, unlabeled_sample / Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 10 mM / Ionic strength err: 0.1 / Label: conditions_1 / pH: 7 / PH err: 0.05 / Pressure: 1 atm / Pressure err: 0.01 / Temperature: 303 K / Temperature err: 0.2 |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: target function | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 20 / Conformers submitted total number: 20 |