+Open data
-Basic information
Entry | Database: PDB / ID: 2mbw | |||||||||
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Title | RECOMBINANT SPERM WHALE MYOGLOBIN (MET) | |||||||||
Components | MYOGLOBIN | |||||||||
Keywords | OXYGEN TRANSPORT / HEME / RESPIRATORY PROTEIN | |||||||||
Function / homology | Function and homology information Oxidoreductases; Acting on other nitrogenous compounds as donors / nitrite reductase activity / sarcoplasm / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / removal of superoxide radicals / oxygen carrier activity / peroxidase activity / oxygen binding / heme binding / extracellular exosome / metal ion binding Similarity search - Function | |||||||||
Biological species | Physeter catodon (sperm whale) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.5 Å | |||||||||
Authors | Brucker, E.A. / Phillips Jr., G.N. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 1996 Title: High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin. Authors: Brucker, E.A. / Olson, J.S. / Phillips Jr., G.N. / Dou, Y. / Ikeda-Saito, M. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1987 Title: High-Level Expression of Sperm Whale Myoglobin in Escherichia Coli Authors: Springer, B.A. / Sligar, S.G. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mbw.cif.gz | 46.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mbw.ent.gz | 31.7 KB | Display | PDB format |
PDBx/mmJSON format | 2mbw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mbw_validation.pdf.gz | 816.9 KB | Display | wwPDB validaton report |
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Full document | 2mbw_full_validation.pdf.gz | 817.8 KB | Display | |
Data in XML | 2mbw_validation.xml.gz | 10.1 KB | Display | |
Data in CIF | 2mbw_validation.cif.gz | 13.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mb/2mbw ftp://data.pdbj.org/pub/pdb/validation_reports/mb/2mbw | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 17365.164 Da / Num. of mol.: 1 / Mutation: INITIATOR MET, D122N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Physeter catodon (sperm whale) / Production host: Escherichia coli (E. coli) / References: UniProt: P02185 |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-HEM / |
#4: Water | ChemComp-HOH / |
Nonpolymer details | HOH 155 IS COVALENTLY |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.18 Å3/Da / Density % sol: 61.26 % | |||||||||||||||
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Crystal grow | pH: 9 / Details: pH 9. | |||||||||||||||
Crystal grow | *PLUS Temperature: 17 ℃ / Method: batch method | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→18.2 Å / Num. obs: 32143 / % possible obs: 91.8 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.025 |
-Processing
Software |
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Refinement | Resolution: 1.5→5 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.5→5 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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