+Open data
-Basic information
Entry | Database: PDB / ID: 1wfa | ||||||
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Title | WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C | ||||||
Components | ANTIFREEZE PROTEIN ISOFORM HPLC6 | ||||||
Keywords | ANTIFREEZE POLYPEPTIDE / ICE BINDING PROTEIN / THERMAL HYSTERESIS PROTEIN | ||||||
Function / homology | Antifreeze protein, type I / ice binding / extracellular space / identical protein binding / Ice-structuring protein A Function and homology information | ||||||
Biological species | Pseudopleuronectes americanus (winter flounder) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.7 Å | ||||||
Authors | Yang, D.S.C. / Sicheri, F. | ||||||
Citation | Journal: Nature / Year: 1995 Title: Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Authors: Sicheri, F. / Yang, D.S. #1: Journal: To be Published Title: Structure Determination of an Antifreeze Protein from Winter Flounder Authors: Sicheri, F. / Yang, D.S.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wfa.cif.gz | 23.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wfa.ent.gz | 16.4 KB | Display | PDB format |
PDBx/mmJSON format | 1wfa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1wfa_validation.pdf.gz | 352.9 KB | Display | wwPDB validaton report |
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Full document | 1wfa_full_validation.pdf.gz | 352.9 KB | Display | |
Data in XML | 1wfa_validation.xml.gz | 2.3 KB | Display | |
Data in CIF | 1wfa_validation.cif.gz | 3.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wf/1wfa ftp://data.pdbj.org/pub/pdb/validation_reports/wf/1wfa | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein/peptide | Mass: 3242.490 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudopleuronectes americanus (winter flounder) References: UniProt: P04002 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.46 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.3 / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.54 |
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Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jul 1, 1993 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Num. obs: 5505 / % possible obs: 81.7 % / Observed criterion σ(I): 1 / Redundancy: 3.1 % / Rmerge(I) obs: 0.044 |
Reflection | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 40 Å / Num. measured all: 16614 / Rmerge(I) obs: 0.044 |
-Processing
Software |
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Refinement | Resolution: 1.7→8 Å / σ(F): 1
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Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |