+Open data
-Basic information
Entry | Database: PDB / ID: 3fct | ||||||
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Title | MATURE METAL CHELATASE CATALYTIC ANTIBODY WITH HAPTEN | ||||||
Components | (PROTEIN (METAL CHELATASE CATALYTIC ...) x 2 | ||||||
Keywords | IMMUNE SYSTEM / METAL CHELATASE / CATALYTIC ANTIBODY / FAB FRAGMENT | ||||||
Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / : / N-METHYLMESOPORPHYRIN Function and homology information | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Romesberg, F.E. / Santarsiero, B.D. / Barnes, D. / Yin, J. / Spiller, B. / Schultz, P.G. / Stevens, R.C. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: Structural and kinetic evidence for strain in biological catalysis. Authors: Romesberg, F.E. / Santarsiero, B.D. / Spiller, B. / Yin, J. / Barnes, D. / Schultz, P.G. / Stevens, R.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3fct.cif.gz | 191.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3fct.ent.gz | 151.1 KB | Display | PDB format |
PDBx/mmJSON format | 3fct.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3fct_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 3fct_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 3fct_validation.xml.gz | 44.1 KB | Display | |
Data in CIF | 3fct_validation.cif.gz | 62.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fc/3fct ftp://data.pdbj.org/pub/pdb/validation_reports/fc/3fct | HTTPS FTP |
-Related structure data
Related structure data | 1hklS 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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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
-Antibody , 2 types, 4 molecules ACBD
#1: Antibody | Mass: 23432.014 Da / Num. of mol.: 2 / Fragment: FAB FRAGMENT Source method: isolated from a genetically manipulated source Details: CHIMERIC FAB FRAGMENT / Source: (gene. exp.) Homo sapiens (human) / Strain: SWISS WEBSTER / Cell: B LYMPHOCYTE / Cell line: 7G12 HYBRIDOMA / Cellular location: PERIPLASM / Organ: SPLEEN / Production host: Escherichia coli (E. coli) #2: Antibody | Mass: 23097.074 Da / Num. of mol.: 2 / Fragment: FAB FRAGMENT Source method: isolated from a genetically manipulated source Details: CHIMERIC FAB FRAGMENT / Source: (gene. exp.) Homo sapiens (human) / Strain: SWISS WEBSTER / Cell: B LYMPHOCYTE / Cell line: 7G12 HYBRIDOMA / Cellular location: PERIPLASM / Organ: SPLEEN / Production host: Escherichia coli (E. coli) |
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-Non-polymers , 6 types, 558 molecules
#3: Chemical | ChemComp-CD / | ||||
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#4: Chemical | ChemComp-CA / | ||||
#5: Chemical | ChemComp-MG / | ||||
#6: Chemical | ChemComp-NA / #7: Chemical | #8: 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: 2.6 Å3/Da / Density % sol: 45 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PROTEIN WAS CRYSTALLIZED FROM 27% PEG 2000-MME, 200 MM AMMONIUM SULFATE, 100 MM TRIS, PH 7.0, 10MM CADMIUM SULFATE, WITH 10-FOLD EXCESS OF DIASTEREOMERIC N- METHYLMESOPORPHYRIN AT 20C ...Details: PROTEIN WAS CRYSTALLIZED FROM 27% PEG 2000-MME, 200 MM AMMONIUM SULFATE, 100 MM TRIS, PH 7.0, 10MM CADMIUM SULFATE, WITH 10-FOLD EXCESS OF DIASTEREOMERIC N- METHYLMESOPORPHYRIN AT 20C (HANGING DROP)., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 1.1 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 15, 1996 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / % possible obs: 85.9 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rmerge(I) obs: 0.081 / Net I/σ(I): 18.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1HKL Resolution: 2.4→50 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Solvent computation | Solvent model: CNS / Bsol: 45.64 Å2 / ksol: 0.313 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→50 Å
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Refine LS restraints |
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Xplor file |
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