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Yorodumi- PDB-2kxg: The solution structure of the squash aspartic acid proteinase inh... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2kxg | ||||||
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Title | The solution structure of the squash aspartic acid proteinase inhibitor (SQAPI) | ||||||
Components | Aspartic protease inhibitor | ||||||
Keywords | HYDROLASE INHIBITOR / SQAPI / protein / aspartic protease inhibitor | ||||||
Function / homology | Aspartic acid proteinase inhibitor / Cystatin domain / Nuclear Transport Factor 2; Chain: A, - #10 / cysteine-type endopeptidase inhibitor activity / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta / Aspartic protease inhibitor Function and homology information | ||||||
Biological species | Cucurbita maxima (winter squash) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing, simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Headey, S.J. / Macaskill, U.K. / Wright, M. / Claridge, J.K. / Edwards, P.J.B. / Farley, P.C. / Christeller, J.T. / Laing, W.A. / Pascal, S.M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2010 Title: Solution structure of the squash aspartic acid proteinase inhibitor (SQAPI) and mutational analysis of pepsin inhibition. Authors: Headey, S.J. / Macaskill, U.K. / Wright, M.A. / Claridge, J.K. / Edwards, P.J.B. / Farley, P.C. / Christeller, J.T. / Laing, W.A. / Pascal, S.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kxg.cif.gz | 292.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kxg.ent.gz | 243.7 KB | Display | PDB format |
PDBx/mmJSON format | 2kxg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kx/2kxg ftp://data.pdbj.org/pub/pdb/validation_reports/kx/2kxg | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10420.930 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 8-102 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cucurbita maxima (winter squash) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / Variant (production host): pLysS / References: UniProt: Q6DLC9 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.6mM [U-98% 13C; U-98% 15N] SQAPI-1, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.6 mM / Component: SQAPI-1 / Isotopic labeling: [U-98% 13C; U-98% 15N] |
Sample conditions | pH: 3 / Pressure: ambient / Temperature: 323 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing, simulated annealing Software ordinal: 1 Details: beginning with extended conformer, beginning with folded structure using Cartesian dynamics, final refinement using Cartesian dynamics in a layer of TIP3 water molecules | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 / Representative conformer: 1 |