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Open data
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Basic information
Entry | Database: PDB / ID: 1msi | ||||||
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Title | STRUCTURE OF ANTIFREEZE GLYCOPROTEIN QAE(HPLC 12) | ||||||
![]() | TYPE III ANTIFREEZE PROTEIN ISOFORM HPLC 12 | ||||||
![]() | ANTIFREEZE PROTEIN / MULTIGENE FAMILY / THERMAL HYSTERESIS | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Jia, Z. / Deluca, C.I. / Chao, H. / Davies, P.L. | ||||||
![]() | ![]() Title: Structural basis for the binding of a globular antifreeze protein to ice. Authors: Jia, Z. / DeLuca, C.I. / Chao, H. / Davies, P.L. #1: ![]() Title: Erratum. Structural Basis for the Binding of a Globular Antifreeze Protein to Ice Authors: Jia, Z. / Deluca, C.I. / Chao, H. / Davies, P.L. #2: ![]() Title: Crystallization and Preliminary X-Ray Crystallographic Studies on Type III Antifreeze Protein Authors: Jia, Z. / Deluca, C.I. / Davies, P.L. #3: ![]() Title: Use of Proline Mutants to Help Solve the NMR Solution Structure of Type III Antifreeze Protein Authors: Chao, H. / Davies, P.L. / Sykes, B.D. / Sonnichsen, F.D. #4: ![]() Title: Multiple Genes Provide the Basis for Antifreeze Protein Diversity and Dosage in the Ocean Pout, Macrozoarces Americanus Authors: Hew, C.L. / Wang, N.C. / Joshi, S. / Fletcher, G.L. / Scott, G.K. / Hayes, P.H. / Buettner, B. / Davies, P.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 30.5 KB | Display | ![]() |
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PDB format | ![]() | 21.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 409.7 KB | Display | ![]() |
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Full document | ![]() | 409.6 KB | Display | |
Data in XML | ![]() | 6.2 KB | Display | |
Data in CIF | ![]() | 7.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 7422.746 Da / Num. of mol.: 1 / Mutation: P64A, P65A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.92 Å3/Da / Density % sol: 30 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / PH range low: 4.5 / PH range high: 4 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 30, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.927 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→50 Å / Num. obs: 16529 / % possible obs: 96.6 % / Observed criterion σ(I): 1 / Redundancy: 2.8 % / Biso Wilson estimate: 15.46 Å2 / Rmerge(I) obs: 0.049 / Rsym value: 0.049 / Net I/σ(I): 24.1 |
Reflection shell | Resolution: 1.25→1.31 Å / Rmerge(I) obs: 0.557 / Mean I/σ(I) obs: 1.64 / Rsym value: 0.557 / % possible all: 98.1 |
Reflection | *PLUS Num. measured all: 46873 |
Reflection shell | *PLUS % possible obs: 98.1 % |
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Processing
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Refinement | Resolution: 1.25→8 Å / Cross valid method: FREE R / σ(F): 0
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Displacement parameters | Biso mean: 18.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.25→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.25→1.31 Å
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.3109 |