[English] 日本語
Yorodumi- PDB-1tet: CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tet | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS | ||||||
Components |
| ||||||
Keywords | IMMUNOGLOBULIN | ||||||
Function / homology | Function and homology information toxin activity / killing of cells of another organism / extracellular region Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Shoham, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1993 Title: Crystal structure of an anticholera toxin peptide complex at 2.3 A. Authors: Shoham, M. #1: Journal: Proteins / Year: 1991 Title: Crystal Parameters and Molecular Replacement of an Anticholera Toxin Peptide Complex Authors: Shoham, M. / Proctor, P. / Hughes, D. / Baldwin, E.T. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1tet.cif.gz | 101.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1tet.ent.gz | 76.9 KB | Display | PDB format |
PDBx/mmJSON format | 1tet.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tet_validation.pdf.gz | 405.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1tet_full_validation.pdf.gz | 421.4 KB | Display | |
Data in XML | 1tet_validation.xml.gz | 12.3 KB | Display | |
Data in CIF | 1tet_validation.cif.gz | 18.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/te/1tet ftp://data.pdbj.org/pub/pdb/validation_reports/te/1tet | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO L 8 / 2: CIS PROLINE - PRO L 95 / 3: CIS PROLINE - PRO L 141 / 4: CIS PROLINE - PRO H 147 / 5: CIS PROLINE - PRO H 149 6: SER H 186 - PRO H 187 OMEGA = 145.25 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 7: CIS PROLINE - PRO H 189 |
-Components
#1: Antibody | Mass: 23872.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / References: PIR: PC4203 |
---|---|
#2: Antibody | Mass: 22805.709 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / References: GenBank: 2072131 |
#3: Protein/peptide | Mass: 1625.800 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P32890 |
#4: Chemical | ChemComp-CIT / |
#5: Water | ChemComp-HOH / |
Sequence details | THE NUMBERING OF TE33 RESIDUES IS ESSENTIALLY ACCORDING TO C.CHOTHIA AND A.M.LESK, J.MOL.BIOL. V. ...THE NUMBERING OF TE33 RESIDUES IS ESSENTIALL |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.26 % | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 4 / Method: unknown | ||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / % possible obs: 84 % / Rmerge(I) obs: 0.1 |
---|
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.3→5 Å / σ(F): 2 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→5 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 5 Å / Num. reflection obs: 13714 / σ(F): 2 / Rfactor obs: 0.148 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.58 |