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- PDB-1fho: Solution Structure of the PH Domain from the C. Elegans Muscle Pr... -
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Basic information
Entry | Database: PDB / ID: 1fho | ||||||
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Title | Solution Structure of the PH Domain from the C. Elegans Muscle Protein UNC-89 | ||||||
![]() | UNC-89 | ||||||
![]() | SIGNALING PROTEIN / Pleckstrin Homology domain / electrostatics / muscle / signal transduction | ||||||
Function / homology | ![]() nematode pharyngeal gland morphogenesis / Cross-presentation of soluble exogenous antigens (endosomes) / : / Platelet sensitization by LDL / regulation of skeletal muscle contraction by calcium ion signaling / Integrin cell surface interactions / Platelet degranulation / positive regulation of locomotion / guanyl-nucleotide exchange factor activity => GO:0005085 / MATH domain binding ...nematode pharyngeal gland morphogenesis / Cross-presentation of soluble exogenous antigens (endosomes) / : / Platelet sensitization by LDL / regulation of skeletal muscle contraction by calcium ion signaling / Integrin cell surface interactions / Platelet degranulation / positive regulation of locomotion / guanyl-nucleotide exchange factor activity => GO:0005085 / MATH domain binding / small GTPase binding => GO:0031267 / striated muscle myosin thick filament assembly / Neutrophil degranulation / protein localization => GO:0008104 / positive regulation of sarcomere organization / positive regulation of protein localization to endoplasmic reticulum / myosin filament assembly / positive regulation of striated muscle contraction / skeletal muscle myosin thick filament assembly / M band / A band / sarcomere organization / plasma membrane => GO:0005886 / phosphatase binding / protein kinase activity / positive regulation of gene expression / ATP binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / Automated NOE assignment,Torsion angle dynamics, Cartesian simulated annealing. | ||||||
![]() | Blomberg, N. / Baraldi, E. / Sattler, M. / Saraste, M. / Nilges, M. | ||||||
![]() | ![]() Title: Structure of a PH domain from the C. elegans muscle protein UNC-89 suggests a novel function. Authors: Blomberg, N. / Baraldi, E. / Sattler, M. / Saraste, M. / Nilges, M. #1: ![]() Title: 1H, 15N, and 13C Resonance Assignment of the PH Domain from C. elegans UNC-89 Authors: Blomberg, N. / Sattler, M. / Nilges, M. #2: ![]() Title: Classification of Protein Sequences by Homology Modelling and Quantitative Analysis of Electrostatic Similarity Authors: Blomberg, N. / Gabdoulline, R.R. / Nilges, M. / Wade, R.C. #3: ![]() Title: Functional Diversity of PH Domains: an Exhaustive Modelling Study Authors: Blomberg, N. / Nilges, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1022.7 KB | Display | ![]() |
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PDB format | ![]() | 858.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 356.5 KB | Display | ![]() |
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Full document | ![]() | 581.8 KB | Display | |
Data in XML | ![]() | 60.6 KB | Display | |
Data in CIF | ![]() | 92.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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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: 14103.741 Da / Num. of mol.: 1 / Fragment: PLECKSTRIN HOMOLOGY (PH) DOMAIN 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: Structure determined using triple resonance NMR techniques. |
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Sample preparation
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: Automated NOE assignment,Torsion angle dynamics, Cartesian simulated annealing. Software ordinal: 1 Details: The structure was calculated automated NOE assignment and structure calculation using ARIA/CNS. Manual NOE assignments were added between cycles of automated assignment. The final structures ...Details: The structure was calculated automated NOE assignment and structure calculation using ARIA/CNS. Manual NOE assignments were added between cycles of automated assignment. The final structures were refined in a shell of explicit solvent. Data consisted of: 1230 unique NOE restaints; 44 phi restraints (3JHNHA scalar couplings, direct refinement against couplings); 41 1JHN residual dipolar couplings. Final ensemble was refined in explicit water. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 25 |