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Yorodumi- PDB-4hih: Anti-Streptococcus pneumoniae 23F Fab 023.102 with bound rhamnose. -
+Open data
-Basic information
Entry | Database: PDB / ID: 4hih | ||||||
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Title | Anti-Streptococcus pneumoniae 23F Fab 023.102 with bound rhamnose. | ||||||
Components |
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Keywords | IMMUNE SYSTEM / Immunoglobin / Antibody / Streptococcus pneumoniae 23F | ||||||
Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / alpha-L-rhamnopyranose Function and homology information | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Bryson, S. / Risnes, L. / Damgupta, S. / Thomson, C.A. / Schrader, J.W. / Pai, E.F. | ||||||
Citation | Journal: J. Immunol. / Year: 2016 Title: Structures of Preferred Human IgV Genes-Based Protective Antibodies Identify How Conserved Residues Contact Diverse Antigens and Assign Source of Specificity to CDR3 Loop Variation. Authors: Bryson, S. / Thomson, C.A. / Risnes, L.F. / Dasgupta, S. / Smith, K. / Schrader, J.W. / Pai, E.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4hih.cif.gz | 173.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4hih.ent.gz | 136.7 KB | Display | PDB format |
PDBx/mmJSON format | 4hih.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4hih_validation.pdf.gz | 480.6 KB | Display | wwPDB validaton report |
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Full document | 4hih_full_validation.pdf.gz | 498.9 KB | Display | |
Data in XML | 4hih_validation.xml.gz | 34.4 KB | Display | |
Data in CIF | 4hih_validation.cif.gz | 48.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hi/4hih ftp://data.pdbj.org/pub/pdb/validation_reports/hi/4hih | HTTPS FTP |
-Related structure data
Related structure data | 4hh9C 4hhaC 4hieSC 4hiiC 4hijC 4pttC 4ptuC 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: 23929.469 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pARC / Production host: Escherichia coli (E. coli) / Strain (production host): XL1-Blue #2: Antibody | Mass: 25116.055 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pARC / Production host: Escherichia coli (E. coli) / Strain (production host): XL1-Blue #3: Sugar | #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: 2.69 Å3/Da / Density % sol: 54.24 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4 Details: 0.05M Na Citrate, pH 3-4, 18% PEG 3350, 0.2M Li Acetate , VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Feb 18, 2010 / Details: Rigaku Osmic VariMax |
Radiation | Monochromator: Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→17 Å / Num. all: 70705 / Num. obs: 69510 / % possible obs: 98.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 1.81 % / Rmerge(I) obs: 0.0527 / Net I/σ(I): 17.86 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 1.43 % / Rmerge(I) obs: 0.286 / Mean I/σ(I) obs: 2.94 / Num. unique all: 4326 / % possible all: 86.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4HIE Resolution: 2→17 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→17 Å
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Refine LS restraints |
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