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- PDB-1mch: PRINCIPLES AND PITFALLS IN DESIGNING SITE DIRECTED PEPTIDE LIGANDS -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mch | ||||||
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Title | PRINCIPLES AND PITFALLS IN DESIGNING SITE DIRECTED PEPTIDE LIGANDS | ||||||
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Function / homology | ![]() Immunoglobulin V-Type / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Domain/homology | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Edmundson, A.B. / Harris, D.L. / Fan, Z.-C. / Guddat, L.W. | ||||||
![]() | ![]() Title: Principles and pitfalls in designing site-directed peptide ligands. Authors: Edmundson, A.B. / Harris, D.L. / Fan, Z.C. / Guddat, L.W. / Schley, B.T. / Hanson, B.L. / Tribbick, G. / Geysen, H.M. #1: ![]() Title: The Binding of Opioid Peptides to the Mcg Light Chain Dimer: Flexible Keys and Adjustable Locks Authors: Edmundson, A.B. / Ely, K.R. / Herron, J.N. / Cheson, B.D. #2: ![]() Title: Binding of N-Formylated Chemotactic Peptides in Crystals of the Mcg Light Chain Dimer: Similarities with Neutrophil Receptors Authors: Edmundson, A.B. / Ely, K.R. #3: ![]() Title: A Search for Site-Filling Ligands in the Mcg Bence-Jones Dimer: Crystal Binding Studies of Fluorescent Compounds Authors: Edmundson, A.B. / Ely, K.R. / Herron, J.N. / Cheson, B.D. #4: ![]() Title: Binding of 2,4-Dinitrophenyl Compounds and Other Small Molecules to a Crystalline Lambdal-Type Bence-Jones Dimer Authors: Edmundson, A.B. / Ely, K.R. / Girling, R.L. / Abola, E.E. / Schiffer, M. / Westholm, F.A. / Fausch, M.D. / Deutsch, H.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80 KB | Display | ![]() |
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PDB format | ![]() | 63.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1mcbC ![]() 1mccC ![]() 1mcdC ![]() 1mceC ![]() 1mcfC ![]() 1mciC ![]() 1mcjC ![]() 1mckC ![]() 1mclC ![]() 1mcnC ![]() 1mcqC ![]() 1mcrC ![]() 1mcsC C: citing same article ( |
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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 A 61 / 2: CIS PROLINE - PRO A 145 3: PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION ASN B 33 - TYR B 34 149.590 4: CIS PROLINE - PRO B 145 / 5: CIS PROLINE - PRO B 158 6: PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION GLN P 1 - PHE P 2 149.409 RESIDUES PHE P 2 AND PRO P 4 ARE D IN FORM OF THE AMINO ACIDS. 7: PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION BAL P 5 - BAL P 6 227.181 RESIDUES BAL P 5 AND BAL P 6 ARE BETA FORMS OF ALANINE. |
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Components
#1: Antibody | Mass: 22819.080 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein/peptide | | Mass: 696.773 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Sequence details | THE LIGHT CHAIN WAS SEQUENCED BY FETT AND DEUTSCH (1974) BIOCHEMIST | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.34 % | ||||||||||||||||||||
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Crystal grow![]() | Details: THIS COMPLEX WAS PREPARED BY COCRYSTALLIZATION OF THE PEPTIDE AND DIMER. | ||||||||||||||||||||
Crystal grow | *PLUS pH: 6.2 / Method: batch method | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
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Processing
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Refinement | Resolution: 2.7→6 Å / σ(F): 1.5 /
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Refinement step | Cycle: LAST / Resolution: 2.7→6 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 6 Å / Num. reflection obs: 10054 / σ(F): 1.5 / Rfactor obs: 0.252 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |