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Yorodumi- PDB-2plh: STRUCTURE OF ALPHA-1-PUROTHIONIN AT ROOM TEMPERATURE AND 2.8 ANGS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2plh | ||||||
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Title | STRUCTURE OF ALPHA-1-PUROTHIONIN AT ROOM TEMPERATURE AND 2.8 ANGSTROMS RESOLUTION | ||||||
Components | ALPHA-1-PUROTHIONIN | ||||||
Keywords | TOXIN / MEMBRANE ACTIVE / DISULFIDE RICH | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Triticum aestivum (bread wheat) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Teeter, M.M. / Stec, B. / Rao, U. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1995 Title: Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 1: alpha1-purothionin revisited. Authors: Rao, U. / Stec, B. / Teeter, M.M. #1: Journal: Proteins / Year: 1990 Title: Crystal Structure of a Protein-Toxin Alpha1-Purothionin at 2.5 Angstroms and a Comparison with Predicted Models Authors: Teeter, M.M. / Ma, X.-Q. / Rao, U. / Whitlow, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2plh.cif.gz | 20.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2plh.ent.gz | 15.2 KB | Display | PDB format |
PDBx/mmJSON format | 2plh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2plh_validation.pdf.gz | 438.9 KB | Display | wwPDB validaton report |
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Full document | 2plh_full_validation.pdf.gz | 440.8 KB | Display | |
Data in XML | 2plh_validation.xml.gz | 3.9 KB | Display | |
Data in CIF | 2plh_validation.cif.gz | 5.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pl/2plh ftp://data.pdbj.org/pub/pdb/validation_reports/pl/2plh | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein/peptide , 1 types, 1 molecules A
#1: Protein/peptide | Mass: 4835.840 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: SOLUTE MOLECULES NOT ADDED TO THE / Source: (natural) Triticum aestivum (bread wheat) / Tissue: GRAIN / References: UniProt: P01544 |
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-Non-polymers , 5 types, 116 molecules
#2: Chemical | #3: Chemical | ChemComp-PO4 / | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52.5 % Description: AREA DETECTOR AND DIFFRACTOMETER DATA SETS WERE MERGED | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: CRAD, P21 / Date: Jan 1, 1989 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→10 Å / Num. obs: 2106 / % possible obs: 61.5 % / Observed criterion σ(I): 2 / Redundancy: 2 % / Rmerge(I) obs: 0.123 |
Reflection | *PLUS Rmerge(I) obs: 0.123 |
-Processing
Software |
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Refinement | Resolution: 2.5→10 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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