+Open data
-Basic information
Entry | Database: PDB / ID: 2m7k | ||||||
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Title | NMR solution structure of N-terminal domain of (Y81F)-EhCaBP1 | ||||||
Components | Calcium-binding protein | ||||||
Keywords | METAL BINDING PROTEIN | ||||||
Function / homology | Function and homology information regulation of actin filament bundle assembly / positive regulation of macropinocytosis / regulation of protein kinase activity / pseudopodium / phagocytic cup / actin monomer binding / phagocytosis / positive regulation of phagocytosis / actin filament binding / calcium ion binding ...regulation of actin filament bundle assembly / positive regulation of macropinocytosis / regulation of protein kinase activity / pseudopodium / phagocytic cup / actin monomer binding / phagocytosis / positive regulation of phagocytosis / actin filament binding / calcium ion binding / endoplasmic reticulum / cytoplasm Similarity search - Function | ||||||
Biological species | Entamoeba histolytica (eukaryote) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Chary, K.V. / Rout, A.K. / Patel, S. / Bhattacharya, A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2013 Title: Functional Manipulation of a Calcium-binding Protein from Entamoeba histolytica Guided by Paramagnetic NMR. Authors: Rout, A.K. / Patel, S. / Somlata / Shukla, M. / Saraswathi, D. / Bhattacharya, A. / Chary, K.V. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m7k.cif.gz | 234.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m7k.ent.gz | 197.1 KB | Display | PDB format |
PDBx/mmJSON format | 2m7k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m7/2m7k ftp://data.pdbj.org/pub/pdb/validation_reports/m7/2m7k | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7380.256 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Entamoeba histolytica (eukaryote) / Production host: Escherichia coli (E. coli) / References: UniProt: P38505 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.05 / pH: 7.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||
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: 10 |