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Open data
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Basic information
Entry | Database: PDB / ID: 1azw | ||||||
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Title | PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI | ||||||
![]() | PROLINE IMINOPEPTIDASE | ||||||
![]() | AMINOPEPTIDASE / PROLINE IMINOPEPTIDASE / SERINE PROTEASE / XANTHOMONAS CAMPESTRIS | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Medrano, F.J. / Alonso, J. / Garcia, J.L. / Romero, A. / Bode, W. / Gomis-Ruth, F.X. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 135.5 KB | Display | ![]() |
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PDB format | ![]() | 108.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 381.6 KB | Display | ![]() |
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Full document | ![]() | 394.4 KB | Display | |
Data in XML | ![]() | 14.2 KB | Display | |
Data in CIF | ![]() | 22.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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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: |
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Components
#1: Protein | Mass: 35520.746 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #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: ![]() |
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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: ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |