+Open data
-Basic information
Entry | Database: PDB / ID: 1azw | ||||||
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Title | PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI | ||||||
Components | PROLINE IMINOPEPTIDASEProlyl aminopeptidase | ||||||
Keywords | AMINOPEPTIDASE / PROLINE IMINOPEPTIDASE / SERINE PROTEASE / XANTHOMONAS CAMPESTRIS | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Xanthomonas citri (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.7 Å | ||||||
Authors | Medrano, F.J. / Alonso, J. / Garcia, J.L. / Romero, A. / Bode, W. / Gomis-Ruth, F.X. | ||||||
Citation | Journal: EMBO J. / Year: 1998 Title: Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family. Authors: Medrano, F.J. / Alonso, J. / Garcia, J.L. / Romero, A. / Bode, W. / Gomis-Ruth, F.X. #1: Journal: FEBS Lett. / Year: 1997 Title: Crystallization and Preliminary X-Ray Diffraction Analysis of Proline Iminopeptidase from Xanthomonas Campestris Pv. Citri Authors: Medrano, F.J. / Alonso, J. / Garcia, J.L. / Bode, W. / Gomis-Ruth, F.X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1azw.cif.gz | 135.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1azw.ent.gz | 108.2 KB | Display | PDB format |
PDBx/mmJSON format | 1azw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/az/1azw ftp://data.pdbj.org/pub/pdb/validation_reports/az/1azw | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.735159, -0.677868, -0.006), Vector: |
-Components
#1: Protein | Mass: 35520.746 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xanthomonas citri (bacteria) / Production host: Escherichia coli (E. coli) / Strain (production host): HB101 / References: UniProt: P52279, prolyl aminopeptidase #2: Water | ChemComp-HOH / | Compound details | SER 110 IS ARRANGED IN A SHARP GAMMA-TURN AND EXHIBITS AN ENERGETICALLY UNFAVORABLE CONFORMATION, ...SER 110 IS ARRANGED IN A SHARP GAMMA-TURN AND EXHIBITS AN ENERGETICA | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 3.6 Å3/Da / Density % sol: 65 % | ||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / Method: vapor diffusion, sitting dropDetails: drop solution was mixed with an equal volume of reservoir solution | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 260 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1996 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.7 Å / Num. obs: 29854 / % possible obs: 93.9 % / Observed criterion σ(I): 2 / Redundancy: 3.1 % / Rmerge(I) obs: 0.096 |
Reflection | *PLUS Num. measured all: 154900 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.7→7 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.7→7 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |