+
Open data
-
Basic information
Entry | Database: PDB / ID: 1ggc | ||||||
---|---|---|---|---|---|---|---|
Title | MAJOR ANTIGEN-INDUCED DOMAIN REARRANGEMENTS IN AN ANTIBODY | ||||||
![]() |
| ||||||
![]() | IMMUNOGLOBULIN | ||||||
Function / homology | ![]() positive regulation of B cell activation / humoral immune response mediated by circulating immunoglobulin / early endosome to late endosome transport / phagocytosis, recognition / positive regulation of type IIa hypersensitivity / regulation of proteolysis / positive regulation of type I hypersensitivity / antibody-dependent cellular cytotoxicity / phagocytosis, engulfment / endosome to lysosome transport ...positive regulation of B cell activation / humoral immune response mediated by circulating immunoglobulin / early endosome to late endosome transport / phagocytosis, recognition / positive regulation of type IIa hypersensitivity / regulation of proteolysis / positive regulation of type I hypersensitivity / antibody-dependent cellular cytotoxicity / phagocytosis, engulfment / endosome to lysosome transport / positive regulation of endocytosis / antigen processing and presentation / immunoglobulin mediated immune response / positive regulation of phagocytosis / immunoglobulin complex, circulating / immunoglobulin receptor binding / multivesicular body / complement activation, classical pathway / antigen binding / response to bacterium / positive regulation of immune response / antibacterial humoral response / blood microparticle / extracellular exosome / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Takimoto-Kamimura, M. / Wilson, I.A. | ||||||
![]() | ![]() Title: Major antigen-induced domain rearrangements in an antibody. Authors: Stanfield, R.L. / Takimoto-Kamimura, M. / Rini, J.M. / Profy, A.T. / Wilson, I.A. #1: ![]() Title: Crystal Structure of a Human Immunodeficiency Virus Type 1 Neutralizing Antibody, 50.1, In Complex with its V3 Loop Peptide Antigen Authors: Rini, J.M. / Stanfield, R.L. / Stura, E.A. / Salinas, P.A. / Profy, A.T. / Wilson, I.A. #2: ![]() Title: Crystallization, Sequence, and Preliminary Crystallographic Data for an Antipeptide Fab 50.1 And Peptide Complexes with the Principal Neutralizing Determinant of HIV-1 Gp120 Authors: Stura, E.A. / Stanfield, R.L. / Fieser, G.G. / Silver, S. / Roguska, M. / Hincapie, L.M. / Simmerman, H.K.B. / Profy, A.T. / Wilson, I.A. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 94.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 72.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 377.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 396.8 KB | Display | |
Data in XML | ![]() | 11.8 KB | Display | |
Data in CIF | ![]() | 17.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO L 8 2: GLN L 42 - PRO L 43 OMEGA =146.05 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: CIS PROLINE - PRO L 77 / 4: CIS PROLINE - PRO L 95 / 5: CIS PROLINE - PRO L 141 / 6: CIS PROLINE - PRO H 149 / 7: CIS PROLINE - PRO H 151 / 8: CIS PROLINE - PRO H 200 |
-
Components
#1: Antibody | Mass: 23647.979 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
---|---|
#2: Antibody | Mass: 23129.889 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.86 % | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 7 / Method: vapor diffusionDetails: referred to 'Stura, E.A.', (1992) 'Proteins.Struct.,Funct., Genet.', 14, 499-508 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.6 Å / % possible obs: 75 % / Rmerge(I) obs: 0.096 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork: 0.19 / Rfactor obs: 0.19 / Highest resolution: 2.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Rfactor obs: 0.19 / Lowest resolution: 10 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d |