+Open data
-Basic information
Entry | Database: PDB / ID: 1n4x | ||||||
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Title | Structure of scFv 1696 at acidic pH | ||||||
Components |
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Keywords | IMMUNE SYSTEM / immunoglobulin | ||||||
Function / homology | Function and homology information immunoglobulin complex / antigen binding / adaptive immune response / immune response / extracellular space Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Lescar, J. / Brynda, J. / Fabry, M. / Horejsi, M. / Rezacova, P. / Sedlacek, J. / Bentley, G.A. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2003 Title: Structure of a single-chain Fv fragment of an antibody that inhibits the HIV-1 and HIV-2 proteases. Authors: Lescar, J. / Brynda, J. / Fabry, M. / Horejsi, M. / Rezacova, P. / Sedlacek, J. / Bentley, G.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1n4x.cif.gz | 111.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1n4x.ent.gz | 88.7 KB | Display | PDB format |
PDBx/mmJSON format | 1n4x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n4/1n4x ftp://data.pdbj.org/pub/pdb/validation_reports/n4/1n4x | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Antibody | Mass: 12452.980 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / References: UniProt: Q99M37, UniProt: P01631*PLUS #2: Antibody | Mass: 13552.892 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / References: UniProt: Q921A6 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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-Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 34.69 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 291 K / pH: 7.3 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID2 / Wavelength: 0.99 Å |
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Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Jan 6, 1998 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99 Å / Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 20 Å / Num. obs: 45422 / % possible obs: 91 % / Redundancy: 4.89 % / Rmerge(I) obs: 0.09 |
Reflection shell | *PLUS % possible obs: 84.2 % / Redundancy: 3.34 % / Num. unique obs: 5930 / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 6.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→20 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 20 Å | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |