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- PDB-1tet: CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tet | ||||||
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Title | CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX AT 2.3 ANGSTROMS | ||||||
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![]() | IMMUNOGLOBULIN | ||||||
Function / homology | ![]() toxin activity / killing of cells of another organism / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Shoham, M. | ||||||
![]() | ![]() Title: Crystal structure of an anticholera toxin peptide complex at 2.3 A. Authors: Shoham, M. #1: ![]() Title: Crystal Parameters and Molecular Replacement of an Anticholera Toxin Peptide Complex Authors: Shoham, M. / Proctor, P. / Hughes, D. / Baldwin, E.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.7 KB | Display | ![]() |
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PDB format | ![]() | 76.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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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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 |
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Components
#1: Antibody | Mass: 23872.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Antibody | Mass: 22805.709 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#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: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.26 % | ||||||||||||
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Crystal grow | *PLUS pH: 4 / Method: unknown | ||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / % possible obs: 84 % / Rmerge(I) obs: 0.1 |
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Processing
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Refinement | Resolution: 2.3→5 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.3→5 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 |