[English] 日本語
Yorodumi- PDB-1c89: NMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1c89 | ||||||
---|---|---|---|---|---|---|---|
Title | NMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 SA STRUCTURES | ||||||
Components | ANTIFREEZE PROTEIN TYPE III | ||||||
Keywords | ANTIFREEZE PROTEIN / ANTIFREEZE / THERMAL HYSTERESIS PROTEIN / ICE BINDING PROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Pachycara brachycephalum (Antarctic eelpout) | ||||||
Method | SOLUTION NMR / SA | ||||||
Authors | Miura, K. / Tsuda, S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: NMR analysis of type III antifreeze protein intramolecular dimer. Structural basis for enhanced activity. Authors: Miura, K. / Ohgiya, S. / Hoshino, T. / Nemoto, N. / Suetake, T. / Miura, A. / Spyracopoulos, L. / Kondo, H. / Tsuda, S. #1: Journal: J.Biochem.(Tokyo) / Year: 1999 Title: Determination of the Solution Structure of the N-Domain Plus Linker of Antarctic Eel Pout Antifreeze Protein Rd3 Authors: Miura, K. / Ohgiya, S. / Hoshino, T. / Nemoto, N. / Odaira, M. / Nitta, K. / Tsuda, S. #2: Journal: Nature / Year: 1996 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: Journal: Structure / Year: 1996 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. #4: Journal: Biochim.Biophys.Acta / Year: 1995 Title: Antifreeze Peptide Heterogeneity in an Antarctic Eel Pout Includes an Unusually Large Major Variant Comprised of Two 7 kDa Type III Afps Linked in Tandem Authors: Wang, X. / Devries, A.L. / Cheng, C.H. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1c89.cif.gz | 1.6 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1c89.ent.gz | 1.3 MB | Display | PDB format |
PDBx/mmJSON format | 1c89.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1c89_validation.pdf.gz | 343.9 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1c89_full_validation.pdf.gz | 738.1 KB | Display | |
Data in XML | 1c89_validation.xml.gz | 144.7 KB | Display | |
Data in CIF | 1c89_validation.cif.gz | 189.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c8/1c89 ftp://data.pdbj.org/pub/pdb/validation_reports/c8/1c89 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 14490.035 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pachycara brachycephalum (Antarctic eelpout) Tissue: BLOOD PLASMA / Description: SYNTHETIC GENE / Variant: RD3 / Plasmid: PKK223-3UC / Production host: Escherichia coli (E. coli) / Strain (production host): JM105 / References: UniProt: P35753 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C/15N-LABELED RD3 |
-Sample preparation
Details | Contents: 90% H2O/10% D2O |
---|---|
Sample conditions | pH: 6.7 / Pressure: 1 atm / Temperature: 277 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 500 MHz |
---|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: SA / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: AVERAGE / Conformers calculated total number: 40 / Conformers submitted total number: 40 |