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- PDB-1air: PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1air | ||||||
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Title | PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERS | ||||||
![]() | PECTATE LYASE C | ||||||
![]() | PECTATE CLEAVAGE / PECTINOLYITC ACTIVITY / TRANS-ELIMINATION | ||||||
Function / homology | ![]() pectate lyase / pectate lyase activity / pectin catabolic process / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lietzke, S.E. / Scavetta, R.D. / Yoder, M.D. / Jurnak, F.A. | ||||||
![]() | ![]() Title: The Refined Three-Dimensional Structure of Pectate Lyase E from Erwinia chrysanthemi at 2.2 A Resolution. Authors: Lietzke, S.E. / Scavetta, R.D. / Yoder, M.D. / Jurnak, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 97.4 KB | Display | ![]() |
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PDB format | ![]() | 75 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 377.3 KB | Display | ![]() |
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Full document | ![]() | 379.1 KB | Display | |
Data in XML | ![]() | 8.3 KB | Display | |
Data in CIF | ![]() | 12.8 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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Unit cell |
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Components
#1: Protein | Mass: 37733.605 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.76 Å3/Da / Density % sol: 67.29 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.2 Details: PROTEIN WAS CRYSTALLIZED FROM 1.9 M AMMONIUM SULFATE, 0.1M HEPES, PH 7.2 SYMMETRY OPERATIONS FOR NON-STANDARD SETTING: SYMMETRY= (X,Y,Z) SYMMETRY=(-X+1/2,-Y,Z+1/2) SYMMETRY= (-X,Y+1/2,-Z+1/2) ...Details: PROTEIN WAS CRYSTALLIZED FROM 1.9 M AMMONIUM SULFATE, 0.1M HEPES, PH 7.2 SYMMETRY OPERATIONS FOR NON-STANDARD SETTING: SYMMETRY= (X,Y,Z) SYMMETRY=(-X+1/2,-Y,Z+1/2) SYMMETRY= (-X,Y+1/2,-Z+1/2) SYMMETRY=(X+1/2,-Y+1/2,-Z) | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 8.5 / Method: vapor diffusion, sitting drop / Details: Kim, C-Y., (1989) J. Mol. Biol., 208, 365. | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ![]() |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Feb 1, 1990 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→10 Å / Num. obs: 25685 / % possible obs: 95.1 % / Redundancy: 2.8 % / Rmerge(I) obs: 0.175 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.175 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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