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- PDB-1frg: CRYSTAL STRUCTURE, SEQUENCE, AND EPITOPE MAPPING OF A PEPTIDE COM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1frg | ||||||
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Title | CRYSTAL STRUCTURE, SEQUENCE, AND EPITOPE MAPPING OF A PEPTIDE COMPLEX OF AN ANTI-INFLUENZA HA PEPTIDE ANTIBODY FAB 26(SLASH)9: FINE-TUNING ANTIBODY SPECIFICITY | ||||||
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Function / homology | ![]() immunoglobulin complex, circulating / immunoglobulin receptor binding / B cell differentiation / ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Churchill, M.E.A. / Wilson, I.A. | ||||||
![]() | ![]() Title: Crystal structure of a peptide complex of anti-influenza peptide antibody Fab 26/9. Comparison of two different antibodies bound to the same peptide antigen. Authors: Churchill, M.E. / Stura, E.A. / Pinilla, C. / Appel, J.R. / Houghten, R.A. / Kono, D.H. / Balderas, R.S. / Fieser, G.G. / Schulze-Gahmen, U. / Wilson, I.A. #1: ![]() Title: Detailed Analysis of the Free and Bound Conformations of an Antibody: X-Ray Structures of Fab 17(Slash)9 and Three Different Fab-Peptide Complexes Authors: Schulze-Gahmen, U. / Rini, J.M. / Wilson, I.A. #2: ![]() Title: Structural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition Authors: Rini, J.M. / Schulze-Gahmen, U. / Wilson, I.A. #3: ![]() Title: Preliminary Crystallographic Data, Primary Sequence, and Binding Data for the Anti-Peptide Fab and its Complex with a Synthetic Peptide from Influenza Hemagglutinin Authors: Schulze-Gahmen, U. / Rini, J.M. / Arevalo, J. / Stura, E.A. / Kenten, J.H. / Wilson, I.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 99 KB | Display | ![]() |
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PDB format | ![]() | 74.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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 L 8 / 2: CIS PROLINE - PRO L 101 / 3: CIS PROLINE - PRO L 147 / 4: CIS PROLINE - PRO H 371 / 5: CIS PROLINE - PRO H 373 / 6: CIS PROLINE - PRO H 413 |
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Components
#1: Antibody | Mass: 24028.650 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Antibody | Mass: 23756.715 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Protein/peptide | Mass: 902.969 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: E3W6A8*PLUS |
#4: Water | ChemComp-HOH / ![]() |
Nonpolymer details | ONE BOUND WATER IS INCLUDED IN THE PEPTIDE BINDING SITE OF THE FAB. |
Sequence details | THE LIGHT CHAIN IS NUMBERED AS CHAIN L 1 - 217. THE HEAVY CHAIN IS NUMBERED AS CHAIN H 218 - 437. ...THE LIGHT CHAIN IS NUMBERED AS CHAIN L 1 - 217. THE HEAVY CHAIN IS NUMBERED AS CHAIN H 218 - 437. THE PEPTIDE IS NUMBERED AS CHAIN P 1 - 9. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 57.35 % | |||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 22.5 ℃ / Method: vapor diffusion, sitting drop / PH range low: 9 / PH range high: 7 | |||||||||||||||||||||||||
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: 2.6 Å / Lowest resolution: 9999 Å / Num. obs: 15290 / % possible obs: 87 % / Num. measured all: 45397 / Rmerge(I) obs: 0.1 |
Reflection shell | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 2.8 Å / % possible obs: 43 % / Num. unique obs: 1237 / Num. measured obs: 2555 / Rmerge(I) obs: 0.48 |
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Processing
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Refinement | Resolution: 2.8→8 Å / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.19 / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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