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Open data
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Basic information
Entry | Database: PDB / ID: 1b7j | ||||||
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Title | TYPE III ANTIFREEZE PROTEIN ISOFORM HPLC 12 V20A | ||||||
![]() | PROTEIN (ANTIFREEZE PROTEIN TYPE III) | ||||||
![]() | ANTIFREEZE PROTEIN / MUTANT / ICE BINDING PROTEIN / THERMAL HYSTERESIS PROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Graether, S.P. / Deluca, C.I. / Baardsnes, J. / Hill, G.A. / Davies, P.L. / Jia, Z. | ||||||
![]() | ![]() Title: Quantitative and qualitative analysis of type III antifreeze protein structure and function. Authors: Graether, S.P. / DeLuca, C.I. / Baardsnes, J. / Hill, G.A. / Davies, P.L. / Jia, Z. #1: ![]() 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. #2: ![]() Title: Structural Basis for the Binding of a Globular Antifreeze Protein to Ice Authors: Jia, Z. / Deluca, C.I. / Chao, H. / Davies, P.L. #3: ![]() Title: Crystallization and Preliminary X-Ray Crystallographic Studies on Type III Antifreeze Protein Authors: Jia, Z. / Deluca, C.I. / Davies, P.L. #4: ![]() 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. #5: ![]() 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 | ![]() | 24.2 KB | Display | ![]() |
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PDB format | ![]() | 15.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1b7iC ![]() 1b7kC ![]() 1eklC ![]() 1jabC ![]() 1msjC ![]() 2ameC ![]() 2jiaC ![]() 2msjC ![]() 2spgC ![]() 3ameC ![]() 4ameC ![]() 6ameC ![]() 7ameC ![]() 8ameC ![]() 8msiC ![]() 9ameC ![]() 9msiC ![]() 1msiS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 6951.180 Da / Num. of mol.: 1 / Mutation: V20A, 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: 2.14 Å3/Da / Density % sol: 42.41 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.5 / Details: pH 5.5 | ||||||||||||||||||||||||||||||
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: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→25 Å / Num. obs: 7106 / % possible obs: 93.3 % / Observed criterion σ(I): 1 / Redundancy: 5 % / Rsym value: 0.065 / Net I/σ(I): 18.1 |
Reflection shell | Resolution: 1.65→1.71 Å / Redundancy: 4.1 % / Mean I/σ(I) obs: 2.6 / Rsym value: 0.442 / % possible all: 89.6 |
Reflection | *PLUS Num. measured all: 27744 / Rmerge(I) obs: 0.065 |
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Processing
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Refinement | Method to determine structure: OTHER Starting model: 1MSI Resolution: 1.65→8 Å / Rfactor Rfree error: 0.011 / Cross valid method: FREE R / σ(F): 0
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Displacement parameters | Biso mean: 19.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.65→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.65→1.72 Å / Rfactor Rfree error: 0.061
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Xplor file | Serial no: 1 / Param file: PARAM19X.PRO / Topol file: TOPH19X.PRO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS % reflection Rfree: 5 % / Rfactor obs: 0.188 / Rfactor Rfree: 0.208 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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