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- PDB-2igf: CRYSTAL STRUCTURES OF AN ANTIBODY TO A PEPTIDE AND ITS COMPLEX WI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2igf | ||||||
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Title | CRYSTAL STRUCTURES OF AN ANTIBODY TO A PEPTIDE AND ITS COMPLEX WITH PEPTIDE ANTIGEN AT 2.8 ANGSTROMS | ||||||
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![]() | IMMUNOGLOBULIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Stanfield, R.L. / Wilson, I.A. | ||||||
![]() | ![]() Title: Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 A. Authors: Stanfield, R.L. / Fieser, T.M. / Lerner, R.A. / Wilson, I.A. #1: ![]() Title: Preliminary Crystallographic Data and Primary Sequence for Anti-Peptide Fab' B13I2 and its Complex with the C-Helix Peptide from Myohemerythrin Authors: Stura, E.A. / Stanfield, R.L. / Fieser, T.M. / Balderas, R.S. / Smith, L.R. / Lerner, R.A. / 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 | ![]() | 96.6 KB | Display | ![]() |
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PDB format | ![]() | 75.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 411 KB | Display | ![]() |
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Full document | ![]() | 429 KB | Display | |
Data in XML | ![]() | 12.4 KB | Display | |
Data in CIF | ![]() | 18 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUES 8, 95, 141 OF THE *L* CHAIN AND 149, 151 OF THE *H* CHAIN ARE CIS PROLINES. 2: NAG 600 IS LINKED TO ASN L 26. |
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Components
#1: Antibody | Mass: 24148.803 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Antibody | Mass: 23807.738 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#3: Protein/peptide | Mass: 2211.666 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P02247 |
#4: Sugar | ChemComp-NAG / |
Sequence details | THE FAB' FRAGMENT IS NUMBERED BY THE CONVENTION OF E.KABAT (E.A.KABAT,T.T.WU,M.REID-MILLER,H.M. ...THE FAB' FRAGMENT IS NUMBERED BY THE CONVENTION |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.49 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.75 / Method: vapor diffusion, sitting dropDetails: taken from Stura, E.A. et al(1989). J. Biol. Chem., 264, 15721-15725. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.8 Å / Num. obs: 26851 / Observed criterion σ(I): 2 / Num. measured all: 77906 / Rmerge(I) obs: 0.142 |
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Processing
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Refinement | Resolution: 2.8→8 Å / Rfactor Rwork: 0.22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 8 Å / Rfactor all: 0.22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.98 |