+Open data
-Basic information
Entry | Database: PDB / ID: 4unv | ||||||
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Title | Covalent dimer of lambda variable domains | ||||||
Components | IG LAMBDA CHAIN V-II REGION MGC | ||||||
Keywords | IMMUNE SYSTEM / BENCE-JONES / IMMUNOGLOBULIN / AMYLOID | ||||||
Function / homology | Function and homology information CD22 mediated BCR regulation / Fc epsilon receptor (FCERI) signaling / immunoglobulin complex / Classical antibody-mediated complement activation / Initial triggering of complement / FCGR activation / Role of phospholipids in phagocytosis / Role of LAT2/NTAL/LAB on calcium mobilization / Scavenging of heme from plasma / FCERI mediated Ca+2 mobilization ...CD22 mediated BCR regulation / Fc epsilon receptor (FCERI) signaling / immunoglobulin complex / Classical antibody-mediated complement activation / Initial triggering of complement / FCGR activation / Role of phospholipids in phagocytosis / Role of LAT2/NTAL/LAB on calcium mobilization / Scavenging of heme from plasma / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / antigen binding / Regulation of Complement cascade / Cell surface interactions at the vascular wall / FCERI mediated MAPK activation / FCGR3A-mediated phagocytosis / Regulation of actin dynamics for phagocytic cup formation / FCERI mediated NF-kB activation / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / adaptive immune response / Potential therapeutics for SARS / immune response / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Brumshtein, B. / Esswein, S. / Landau, M. / Ryan, C. / Whitelegge, J. / Sawaya, M. / Eisenberg, D.S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2014 Title: Formation of Amyloid Fibers by Monomeric Light-Chain Variable Domains. Authors: Brumshtein, B. / Esswein, S.R. / Landau, M. / Ryan, C.M. / Whitelegge, J.P. / Phillips, M.L. / Cascio, D. / Sawaya, M.R. / Eisenberg, D.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4unv.cif.gz | 36 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4unv.ent.gz | 24.3 KB | Display | PDB format |
PDBx/mmJSON format | 4unv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/un/4unv ftp://data.pdbj.org/pub/pdb/validation_reports/un/4unv | HTTPS FTP |
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-Related structure data
Related structure data | 4untC 4unuC 3mcgS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Antibody | Mass: 11553.544 Da / Num. of mol.: 1 / Fragment: LIGHT-CHAIN VARIABLE DOMAIN, RESIDUES 1-110 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: BLOOD / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P01709 | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.8 Å3/Da / Density % sol: 31 % / Description: NONE |
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Crystal grow | pH: 4.6 / Details: 0.1M CH3COONA PH4.6, 2M (NH4)2SO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 |
Detector | Type: RIGAKU CCD / Detector: CCD / Date: May 3, 2013 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→30 Å / Num. obs: 11350 / % possible obs: 98 % / Observed criterion σ(I): 3 / Redundancy: 7 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 39 |
Reflection shell | Resolution: 1.6→1.64 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 4.2 / % possible all: 86 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3MCG Resolution: 1.6→30.11 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.928 / SU B: 2.372 / SU ML: 0.084 / Cross valid method: THROUGHOUT / ESU R: 0.109 / ESU R Free: 0.12 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.659 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→30.11 Å
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Refine LS restraints |
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