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Yorodumi- PDB-2c1p: Fab-fragment of enantioselective antibody complexed with finrozole -
+Open data
-Basic information
Entry | Database: PDB / ID: 2c1p | ||||||
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Title | Fab-fragment of enantioselective antibody complexed with finrozole | ||||||
Components |
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Keywords | IMMUNE SYSTEM / FAB FRAGMENT / ENANTIOSELECTIVE / FINROZOLE / ANTIBODY / ENANTIOSELECTIVE ANTIBODY / IMMUNOGLOBULIN DOMAIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | MUS MUSCULUS (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Parkkinen, T. / Nevanen, T.K. / Koivula, A. / Rouvinen, J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2006 Title: Crystal Structures of an Enantioselective Fab-Fragment in Free and Complex Forms. Authors: Parkkinen, T. / Nevanen, T.K. / Koivula, A. / Rouvinen, J. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2c1p.cif.gz | 185.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2c1p.ent.gz | 146.8 KB | Display | PDB format |
PDBx/mmJSON format | 2c1p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2c1p_validation.pdf.gz | 963.7 KB | Display | wwPDB validaton report |
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Full document | 2c1p_full_validation.pdf.gz | 981.2 KB | Display | |
Data in XML | 2c1p_validation.xml.gz | 38.1 KB | Display | |
Data in CIF | 2c1p_validation.cif.gz | 54.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c1/2c1p ftp://data.pdbj.org/pub/pdb/validation_reports/c1/2c1p | HTTPS FTP |
-Related structure data
Related structure data | 2c1oC 1f8tS 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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2 |
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Unit cell |
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-Components
#1: Antibody | Mass: 24027.752 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) / Strain (production host): RV308 / References: UniProt: Q58EU8*PLUS #2: Antibody | Mass: 23366.123 Da / Num. of mol.: 2 / Fragment: FAB-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): RV308 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 48 % |
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Crystal grow | pH: 8.5 / Details: 22% PEG3350,0.1 M TRIS,10 EXCESS LIGAND, pH 8.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X13 / Wavelength: 0.8122 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 3, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8122 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→25 Å / Num. obs: 171606 / % possible obs: 78.3 % / Observed criterion σ(I): 7.1 / Redundancy: 3.9 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 7.1 |
Reflection shell | Resolution: 2.05→2.12 Å / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 4 / % possible all: 68.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1F8T Resolution: 2→25 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Bsol: 44.3408 Å2 / ksol: 0.348283 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2→25 Å
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Refine LS restraints |
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Xplor file |
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