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Yorodumi- PDB-1cew: THE 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF CHICKEN EGG WHITE CY... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cew | ||||||
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Title | THE 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF CHICKEN EGG WHITE CYSTATIN AND ITS POSSIBLE MODE OF INTERACTION WITH CYSTEINE PROTEINASES | ||||||
Components | CYSTATIN | ||||||
Keywords | PROTEINASE INHIBITOR(CYSTEINE) | ||||||
Function / homology | Function and homology information cysteine-type endopeptidase inhibitor activity / vesicle / extracellular space / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Bode, W. / Musil, D. / Huber, R. | ||||||
Citation | Journal: EMBO J. / Year: 1988 Title: The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. Authors: Bode, W. / Engh, R. / Musil, D. / Thiele, U. / Huber, R. / Karshikov, A. / Brzin, J. / Kos, J. / Turk, V. #1: Journal: J.Mol.Biol. / Year: 1993 Title: Conformational Variability of Chicken Cystatin: Comparison of Structures Determined by X-Ray Diffraction and NMR-Spectroscopy Authors: Engh, R.A. / Dieckmann, T. / Bode, W. / Auerswald, E.A. / Turk, V. / Huber, R. / Oschkinat, H. #2: Journal: J.Mol.Biol. / Year: 1993 Title: The Structures of Native Phosphorylated Chicken Cystatin and of a Recombinant Unphosphorylated Variant in Solution Authors: Dieckmann, T. / Mitschang, L. / Hofmann, M. / Kos, J. / Turk, V. / Auerswald, E.A. / Jaenicke, R. / Oschkinat, H. #3: Journal: FEBS Lett. / Year: 1991 Title: The Cystatins: Protein Inhibitors of Cysteine Proteinases Authors: Turk, V. / Bode, W. #4: Journal: Biol.Chem.Hoppe-Seyler / Year: 1990 Title: Mechanism of Interaction of Cysteine Proteinases and Their Protein Inhibitors as Compared to the Serine Proteinase-Inhibitor Interaction Authors: Bode, W. / Engh, R. / Musil, D. / Laber, B. / Stubbs, M. / Huber, R. / Turk, V. #5: Journal: FEBS Lett. / Year: 1989 Title: Mechanism of Inhibition of Papain by Chicken Egg White Cystatin: Inhibition Constants of N-Terminally Truncated Forms and Cyanogen Bromide Fragments of the Inhibitor Authors: Machleidt, W. / Thiele, U. / Laber, B. / Assfalg-Machleidt, I. / Esterl, A. / Wiegand, G. / Kos, J. / Turk, V. / Bode, W. #6: Journal: FEBS Lett. / Year: 1989 Title: The Cysteine Proteinase Inhibitor Chicken Cystatin is a Phophoprotein Authors: Laber, B. / Krieglstein, K. / Henschen, A. / Kos, J. / Turk, V. / Huber, R. / Bode, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cew.cif.gz | 33.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cew.ent.gz | 26.1 KB | Display | PDB format |
PDBx/mmJSON format | 1cew.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ce/1cew ftp://data.pdbj.org/pub/pdb/validation_reports/ce/1cew | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: GLU I 88 - MET I 89 OMEGA =121.89 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
-Components
#1: Protein | Mass: 12204.868 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Organ: EGG / References: UniProt: P01038 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.17 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 8.2 / Method: unknown | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 6715 / % possible obs: 75 % / Rmerge(I) obs: 0.105 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.2 Å / % possible obs: 30 % |
-Processing
Software | Name: EREF / Classification: refinement | ||||||||||||
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Refinement | Rfactor Rwork: 0.198 / Highest resolution: 2 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Software | *PLUS Name: EREF / Classification: refinement | ||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 6 Å / Num. reflection obs: 6181 / Rfactor obs: 0.198 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS Biso mean: 20 Å2 | ||||||||||||
Refine LS restraints | *PLUS
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