+Open data
-Basic information
Entry | Database: PDB / ID: 2blj | ||||||
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Title | Structure of L29W MbCO | ||||||
Components | MYOGLOBIN | ||||||
Keywords | OXYGEN TRANSPORT / MYOGLOBIN / MUTANT / HEME | ||||||
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 / OTHER / Resolution: 1.8 Å | ||||||
Authors | Nienhaus, K. / Ostermann, A. / Nienhaus, G.U. / Parak, F.G. / Schmidt, M. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Ligand Migration and Protein Fluctuations in Myoglobin Mutant L29W Authors: Nienhaus, K. / Ostermann, A. / Nienhaus, G.U. / Parak, F.G. / Schmidt, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2blj.cif.gz | 45.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2blj.ent.gz | 33.4 KB | Display | PDB format |
PDBx/mmJSON format | 2blj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2blj_validation.pdf.gz | 467.7 KB | Display | wwPDB validaton report |
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Full document | 2blj_full_validation.pdf.gz | 468.8 KB | Display | |
Data in XML | 2blj_validation.xml.gz | 5 KB | Display | |
Data in CIF | 2blj_validation.cif.gz | 6.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bl/2blj ftp://data.pdbj.org/pub/pdb/validation_reports/bl/2blj | 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: 17307.020 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) PHYSETER CATODON (sperm whale) / Tissue: MUSCLE / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P02185 |
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#2: Chemical | ChemComp-HEM / |
#3: Chemical | ChemComp-CMO / |
Sequence details | SEQUENCE REVISION TO CHAIN A 122, ASP TO ASN. REFERENCE: ROMERO-HERRERA A.E., LEHMANN H. RESIDUE ...SEQUENCE REVISION TO CHAIN A 122, ASP TO ASN. REFERENCE: ROMERO-HERRERA A.E., LEHMANN H. RESIDUE 122 OF SPERM WHALE AND HORSE MYOGLOBIN. BIOCHIM. BIOPHYS. ACTA 336:318-323(1974). |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.24 Å3/Da / Density % sol: 62.04 % |
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Crystal grow | pH: 7.8 / Details: pH 7.80 |
-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ROTATING ANODE / Type: ENRAF-NONIUS FR591 / Wavelength: 1.5418 |
Detector | Type: BRUKER MULTIWIRE / Detector: AREA DETECTOR / Date: Sep 12, 2003 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 73405 / % possible obs: 80 % / Redundancy: 4.5 % / Biso Wilson estimate: 16.6 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 11 |
Reflection shell | Resolution: 1.8→1.88 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.24 / Mean I/σ(I) obs: 3 / % possible all: 61 |
-Processing
Software |
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Refinement | Method to determine structure: OTHER / Resolution: 1.8→50 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Bsol: 50.1287 Å2 / ksol: 0.359627 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.5 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→50 Å
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Refine LS restraints |
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Xplor file |
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