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Yorodumi- PDB-2gv1: NMR solution structure of the Acylphosphatase from Eschaerichia Coli -
+Open data
-Basic information
Entry | Database: PDB / ID: 2gv1 | ||||||
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Title | NMR solution structure of the Acylphosphatase from Eschaerichia Coli | ||||||
Components | Probable acylphosphatase | ||||||
Keywords | HYDROLASE / globular alpha-helix/beta-sheet protein | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Pagano, K. / Corazza, A. / Viglino, P. / Esposito, G. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2006 Title: NMR solution structure of the acylphosphatase from Escherichia coli. Authors: Pagano, K. / Ramazzotti, M. / Viglino, P. / Esposito, G. / Degl'innocenti, D. / Taddei, N. / Corazza, A. #1: Journal: Proteins / Year: 2006 Title: Structure, Conformational Stability, and Enzymatic Properties of Acylphosphatase from the Hyperthermophile Sulfolobus Solfataricus Authors: Corazza, A. / Rosano, C. / Pagano, K. / Alverdi, V. / Esposito, G. / Capanni, C. / Bemporad, F. / Plakoutsi, G. / Stefani, M. / Chiti, F. / Zuccotti, S. / Bolognesi, M. / Viglino, P. #2: Journal: Structure / Year: 1997 Title: Crystal structure of common type acylphosphatase from bovine testis Authors: Thunnissen, M.M. / Taddei, N. / Liguri, G. / Ramponi, G. / Nordlund, P. #3: Journal: J.Mol.Biol. / Year: 1992 Title: Three-dimensional structure of acylphosphatase. Refinement and structure analysis. Authors: Pastore, A. / Saudek, V. / Ramponi, G. / Williams, R.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2gv1.cif.gz | 557.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2gv1.ent.gz | 487.2 KB | Display | PDB format |
PDBx/mmJSON format | 2gv1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gv/2gv1 ftp://data.pdbj.org/pub/pdb/validation_reports/gv/2gv1 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar 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: 10314.760 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: yccX / Production host: Escherichia coli (E. coli) / References: UniProt: P0AB65, acylphosphatase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy and standard 2D homonuclear techniques |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 65 mM / pH: 4.95 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: the structures are based on a total of 1029 restraints, 970 are NOE-derived distance restraints and 59 dihedral angle restraints | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 380 / Conformers submitted total number: 20 |