+Open data
-Basic information
Entry | Database: PDB / ID: 2msi | ||||||
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Title | TYPE III ANTIFREEZE PROTEIN ISOFORM HPLC 12 | ||||||
Components | TYPE III ANTIFREEZE PROTEIN ISOFORM HPLC 12 | ||||||
Keywords | ANTIFREEZE / ANTIFREEZE POLYPEPTIDE / MUTANT / ICE BINDING PROTEIN / THERMAL HYSTERESIS PROTEIN / GLYCOPROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Macrozoarces americanus (ocean pout) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Deluca, C.I. / Davies, P.L. / Ye, Q. / Jia, Z. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 Title: The effects of steric mutations on the structure of type III antifreeze protein and its interaction with ice. Authors: DeLuca, C.I. / Davies, P.L. / Ye, Q. / Jia, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2msi.cif.gz | 23.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2msi.ent.gz | 15.6 KB | Display | PDB format |
PDBx/mmJSON format | 2msi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2msi_validation.pdf.gz | 410.1 KB | Display | wwPDB validaton report |
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Full document | 2msi_full_validation.pdf.gz | 410.1 KB | Display | |
Data in XML | 2msi_validation.xml.gz | 4.5 KB | Display | |
Data in CIF | 2msi_validation.cif.gz | 5.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ms/2msi ftp://data.pdbj.org/pub/pdb/validation_reports/ms/2msi | HTTPS FTP |
-Related structure data
Related structure data | 3msiC 4msiC 5msiC 6msiC 7msiC 1msiS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 7056.444 Da / Num. of mol.: 1 / Mutation: A16M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Macrozoarces americanus (ocean pout) / Plasmid: PT7-7F/PGP1-2 / Production host: Escherichia coli (E. coli) / Strain (production host): JM 83 / References: UniProt: P19614 |
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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: 2.09 Å3/Da / Density % sol: 30 % | ||||||||||||||||||||||||||||||
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Crystal grow | Details: PROTEIN WAS CRYSTALLIZED IN 50-55% AMMONIUM SULFATE, 0.1 M SODIUM ACETATE PH 4-4.5 PH range: 4-4.5 | ||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 30 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / Details: Jia, Z.,(1995) Protein Sci., 4, 1236. / PH range low: 4.5 / PH range high: 4 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 11, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→8 Å / Num. obs: 4933 / % possible obs: 99.1 % / Observed criterion σ(I): 1 / Redundancy: 3.8 % / Rsym value: 0.077 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 1.9→1.97 Å / Rsym value: 0.306 / % possible all: 98.3 |
Reflection | *PLUS Num. measured all: 19230 / Rmerge(I) obs: 0.077 |
-Processing
Software |
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Refinement | Starting model: 1MSI Resolution: 1.9→25 Å / Cross valid method: FREE-R REFINEMENT / σ(F): 1
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Refinement step | Cycle: LAST / Resolution: 1.9→25 Å
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LS refinement shell | Resolution: 1.9→1.99 Å / Total num. of bins used: 8 / % reflection obs: 90.76 % | ||||||||||||||||||||
Xplor file |
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