+Open data
-Basic information
Entry | Database: PDB / ID: 1bfv | ||||||
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Title | MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI | ||||||
Components | (FV4155) x 2 | ||||||
Keywords | IMMUNOGLOBULIN / FV FRAGMENT / STEROID HORMONE / FINE SPECIFICITY | ||||||
Function / homology | Function and homology information immunoglobulin complex / immunoglobulin mediated immune response / antigen binding / adaptive immune response / blood microparticle / immune response / extracellular space Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Trinh, C.H. / Phillips, S.E.V. | ||||||
Citation | Journal: Structure / Year: 1997 Title: Antibody fragment Fv4155 bound to two closely related steroid hormones: the structural basis of fine specificity. Authors: Trinh, C.H. / Hemmington, S.D. / Verhoeyen, M.E. / Phillips, S.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bfv.cif.gz | 60.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bfv.ent.gz | 46.5 KB | Display | PDB format |
PDBx/mmJSON format | 1bfv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bfv_validation.pdf.gz | 760.4 KB | Display | wwPDB validaton report |
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Full document | 1bfv_full_validation.pdf.gz | 768.9 KB | Display | |
Data in XML | 1bfv_validation.xml.gz | 14.5 KB | Display | |
Data in CIF | 1bfv_validation.cif.gz | 20.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bf/1bfv ftp://data.pdbj.org/pub/pdb/validation_reports/bf/1bfv | HTTPS FTP |
-Related structure data
Related structure data | 1cfvC 2bfvC 1nbvS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Antibody | Mass: 12437.998 Da / Num. of mol.: 1 / Fragment: MONOCLONAL ANTIBODY FV FRAGMENT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P01631 | ||||
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#2: Antibody | Mass: 13191.760 Da / Num. of mol.: 1 / Fragment: MONOCLONAL ANTIBODY FV FRAGMENT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P18529*PLUS | ||||
#3: Chemical | #4: Chemical | ChemComp-STG / | #5: 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: 2.37 Å3/Da / Density % sol: 48.1 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: PROTEIN WAS CRYSTALLIZED FROM 18% (W/V) PEG 8000, 200MM ZN ACETATE AND 100MM NA CACODYLATE, PH 7.5 | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Feb 1, 1996 / Details: MSC DOUBLE FOCUSING MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 14834 / % possible obs: 99.8 % / Observed criterion σ(I): 3 / Redundancy: 8.8 % / Rsym value: 0.074 / Net I/σ(I): 9.53 |
Reflection shell | Resolution: 2.1→2.17 Å / Redundancy: 8.9 % / Mean I/σ(I) obs: 3.1 / Rsym value: 0.243 / % possible all: 99.5 |
Reflection | *PLUS Num. measured all: 129898 / Rmerge(I) obs: 0.074 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1NBV Resolution: 2.1→10 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: VAL L 56 HAS DIHEDRAL ANGLES WHICH LIE OUTSIDE THEIR EXPECTED RANGE IN THE GAMMA QUADRANT OF THE RAMACHANDRAN PLOT.
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Displacement parameters | Biso mean: 21.89 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→10 Å
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Refine LS restraints |
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Software | *PLUS Name: 'PROLSQ (CCP4)' / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.187 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |