+Open data
-Basic information
Entry | Database: PDB / ID: 2jto | ||||||
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Title | Solution Structure of Tick Carboxypeptidase Inhibitor | ||||||
Components | Carboxypeptidase inhibitor | ||||||
Keywords | HYDROLASE INHIBITOR / PROTEIN / Blood coagulation / Fibrinolysis / Metalloenzyme inhibitor / Metalloprotease inhibitor / Secreted | ||||||
Function / homology | Function and homology information acquisition of nutrients from host / metalloendopeptidase inhibitor activity / enzyme inhibitor activity / fibrinolysis / blood coagulation / extracellular region Similarity search - Function | ||||||
Biological species | Rhipicephalus bursa (arthropod) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Pantoja-Uceda, D. / Blanco, F.J. | ||||||
Citation | Journal: Biochemistry / Year: 2008 Title: The NMR structure and dynamics of the two-domain tick carboxypeptidase inhibitor reveal flexibility in its free form and stiffness upon binding to human carboxypeptidase B. Authors: Pantoja-Uceda, D. / Arolas, J.L. / Garcia, P. / Lopez-Hernandez, E. / Padro, D. / Aviles, F.X. / Blanco, F.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jto.cif.gz | 407 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jto.ent.gz | 355.2 KB | Display | PDB format |
PDBx/mmJSON format | 2jto.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jt/2jto ftp://data.pdbj.org/pub/pdb/validation_reports/jt/2jto | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7945.104 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rhipicephalus bursa (arthropod) / Production host: Escherichia coli (E. coli) / References: UniProt: Q5EPH2 |
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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: 78.4 / pH: 5.6 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: stucture calculation with torsion angel dynamics, the 20 conformers with the lowest final CYANA target were subjected to restrained energy minimization energy in vacuo with the program AMBER7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 20 |