+Open data
-Basic information
Entry | Database: PDB / ID: 1ol0 | ||||||
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Title | Crystal structure of a camelised human VH | ||||||
Components | IMMUNOGLOBULIN G | ||||||
Keywords | IMMUNOGLOBULIN / CAMELISED VARIABLE HEAVY DOMAIN | ||||||
Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta Function and homology information | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Dottorini, T. / Vaughan, C.K. / Walsh, M.A. / Losurdo, P. / Sollazzo, M. | ||||||
Citation | Journal: Biochemistry / Year: 2004 Title: Crystal Structure of a Human Vh: Requirements for Maintaining a Monomeric Fragment Authors: Dottorini, T. / Vaughan, C.K. / Walsh, M.A. / Losurdo, P. / Sollazzo, M. #1: Journal: J.Biol.Chem. / Year: 2000 Title: Inhibition of the Hepatitis C Virus Ns3/4A Protease. The Crystal Structures of Two Protease-Inhibitor Complexes Authors: Dimarco, S. / Rizzi, M. / Volpari, C. / Walsh, M.A. / Narjes, F. / Colarusso, S. / Defrancesco, R. / Matassa, V.G. / Sollazzo, M. #2: Journal: Protein Eng. / Year: 1997 Title: Affinity Selection of a Camelized V(H) Domain Antibody Inhibitor of Hepatitis C Virus Ns3 Protease Authors: Martin, F. / Volpari, C. / Steinkuhler, C. / Dimasibrunetti, M. / Biasiol, G. / Altamura, S. / Cortese, R. / Defrancesco, R. / Sollazzo, M. #3: Journal: J.Mol.Biol. / Year: 1996 Title: Rearrangement of the Former Vl Interface in the Solution Structure of a Camelised, Single Antibody Vh Domain Authors: Riechmann, L. | ||||||
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 | 1ol0.cif.gz | 71.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ol0.ent.gz | 53.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ol0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ol0_validation.pdf.gz | 452.8 KB | Display | wwPDB validaton report |
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Full document | 1ol0_full_validation.pdf.gz | 454.2 KB | Display | |
Data in XML | 1ol0_validation.xml.gz | 16.5 KB | Display | |
Data in CIF | 1ol0_validation.cif.gz | 24.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ol/1ol0 ftp://data.pdbj.org/pub/pdb/validation_reports/ol/1ol0 | HTTPS FTP |
-Related structure data
Related structure data | 1hcvS 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: (Code: given Matrix: (-0.999943, -0.009568, -0.00477), Vector: |
-Components
#1: Antibody | Mass: 13254.387 Da / Num. of mol.: 2 / Fragment: VARIABLE HEAVY DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): B834 #2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-GOL / #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: 3.1 Å3/Da / Density % sol: 59.5 % | ||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: CRYSTALS GREW FROM 4 MICROLITRE HANGING DROPS FORMED BY MIXING 2 MICROLITERS OF PROTEIN AT A CONCENTRATION OF 5MG/ML WITH 2 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 15-20% (W/V) PEG ...Details: CRYSTALS GREW FROM 4 MICROLITRE HANGING DROPS FORMED BY MIXING 2 MICROLITERS OF PROTEIN AT A CONCENTRATION OF 5MG/ML WITH 2 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 15-20% (W/V) PEG 8000, 0.4 M AMMONIUM SULPHATE AND 0.1M HEPES AT PH 7.5. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / 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: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Oct 15, 2000 / Details: TOROIDAL |
Radiation | Monochromator: DIAMON 100/GE 220 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. obs: 29910 / % possible obs: 94.9 % / Observed criterion σ(I): -3 / Redundancy: 2.3 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 17.2 |
Reflection shell | Resolution: 1.8→1.83 Å / Redundancy: 2 % / Rmerge(I) obs: 0.227 / Mean I/σ(I) obs: 1.5 / % possible all: 71.5 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 25.2 Å / Num. measured all: 69437 / Rmerge(I) obs: 0.051 |
Reflection shell | *PLUS Lowest resolution: 1.84 Å / % possible obs: 71.5 % / Rmerge(I) obs: 0.227 / Mean I/σ(I) obs: 1.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1HCV Resolution: 1.8→25.24 Å / SU B: 1.401 / SU ML: 0.044 / Cross valid method: THROUGHOUT EXCEPT IN LAST RO / ESU R: 0.095
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Displacement parameters | Biso mean: 17.342 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→25.24 Å
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Refinement | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 25.2 Å / % reflection Rfree: 5 % / Rfactor Rfree: 0.1802 / Rfactor Rwork: 0.1558 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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