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- PDB-1kde: NORTH-ATLANTIC OCEAN POUT ANTIFREEZE PROTEIN TYPE III ISOFORM HPL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1kde | ||||||
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Title | NORTH-ATLANTIC OCEAN POUT ANTIFREEZE PROTEIN TYPE III ISOFORM HPLC12 MUTANT, NMR, 22 STRUCTURES | ||||||
![]() | ANTIFREEZE PROTEIN TYPE III ISOFORM HPLC12 MUTANT | ||||||
![]() | ANTIFREEZE PROTEIN / ICE BINDING PROTEIN / THERMAL HYSTERESIS PROTEIN / GLYCOPROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DG_SUB_EMBED, DGSA, REFINE | ||||||
![]() | Sonnichsen, F.D. / Deluca, C.I. / Davies, P.L. / Sykes, B.D. | ||||||
![]() | ![]() Title: Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction. Authors: Sonnichsen, F.D. / DeLuca, C.I. / Davies, P.L. / Sykes, B.D. #1: ![]() Title: Structure-Function Relationship in the Globular Type III Antifreeze Protein: Identification of a Cluster of Surface Residues Required for Binding to Ice Authors: Chao, H. / Sonnichsen, F.D. / Deluca, C.I. / Sykes, B.D. / Davies, P.L. #2: ![]() Title: The Nonhelical Structure of Antifreeze Protein Type III Authors: Sonnichsen, F.D. / Sykes, B.D. / Chao, H. / 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 | ![]() | 422.4 KB | Display | ![]() |
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PDB format | ![]() | 353.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 7525.890 Da / Num. of mol.: 1 / Mutation: INS(M0), P64A, P65A, INS(K66, D67, E68, L69) Source method: isolated from a genetically manipulated source Details: QAE-COMPONENT / Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 7.6 / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 600 MHz |
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Processing
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NMR software |
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Refinement | Method: DG_SUB_EMBED, DGSA, REFINE / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: X-PLOR ENERGIES / Conformers calculated total number: 50 / Conformers submitted total number: 22 |