+Open data
-Basic information
Entry | Database: PDB / ID: 1auw | ||||||
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Title | H91N DELTA 2 CRYSTALLIN FROM DUCK | ||||||
Components | DELTA 2 CRYSTALLIN | ||||||
Keywords | EYE LENS PROTEIN / DELTA 2 CRYSTALLIN / ARGINOSUCCINATE LYASE | ||||||
Function / homology | Function and homology information argininosuccinate lyase / argininosuccinate lyase activity / arginine biosynthetic process via ornithine / structural constituent of eye lens / arginine biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | Anas platyrhynchos (mallard) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Abu-Abed, M. / Vallee, F. / Howell, P.L. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: Structural comparison of the enzymatically active and inactive forms of delta crystallin and the role of histidine 91. Authors: Abu-Abed, M. / Turner, M.A. / Vallee, F. / Simpson, A. / Slingsby, C. / Howell, P.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1auw.cif.gz | 347.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1auw.ent.gz | 285.7 KB | Display | PDB format |
PDBx/mmJSON format | 1auw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1auw_validation.pdf.gz | 443.4 KB | Display | wwPDB validaton report |
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Full document | 1auw_full_validation.pdf.gz | 467.1 KB | Display | |
Data in XML | 1auw_validation.xml.gz | 62.6 KB | Display | |
Data in CIF | 1auw_validation.cif.gz | 87.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/au/1auw ftp://data.pdbj.org/pub/pdb/validation_reports/au/1auw | HTTPS FTP |
-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:
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-Components
#1: Protein | Mass: 51737.242 Da / Num. of mol.: 4 / Mutation: H89N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Anas platyrhynchos (mallard) / Cell line: BL21 / Organ: EYE / Plasmid: BL21 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: P24058, argininosuccinate lyase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 9 |
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-Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 52 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 Details: PROTEIN WAS CRYSTALLIZED FROM 18-20% PEG MME 2K, 300 MM MGCL2,100 MM TRIS-HCL PH 8.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 80 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918 |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Jan 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→15 Å / Num. obs: 65641 / % possible obs: 95 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Rsym value: 0.103 |
Reflection shell | Resolution: 2.5→2.6 Å / Rsym value: 0.33 / % possible all: 92.6 |
Reflection | *PLUS Num. measured all: 239855 / Rmerge(I) obs: 0.103 |
Reflection shell | *PLUS % possible obs: 92.6 % / Rmerge(I) obs: 0.33 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: TURKEY DELTA 1 CRYSTALLINE Resolution: 2.5→8 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 2 Details: CIS PEPTIDES NOT INCLUDED IN DIHEDRAL ANGLES. X-PLOR 3.1 ALSO WAS USED.
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Displacement parameters | Biso mean: 31.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.178 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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