+Open data
-Basic information
Entry | Database: PDB / ID: 1c27 | ||||||
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Title | E. COLI METHIONINE AMINOPEPTIDASE:NORLEUCINE PHOSPHONATE COMPLEX | ||||||
Components | METHIONINE AMINOPEPTIDASE | ||||||
Keywords | HYDROLASE / PRODUCT COMPLEX | ||||||
Function / homology | Function and homology information : / initiator methionyl aminopeptidase activity / methionyl aminopeptidase / metalloaminopeptidase activity / ferrous iron binding / proteolysis / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.95 Å | ||||||
Authors | Lowther, W.T. / Zhang, Y. / Sampson, P.B. / Honek, J.F. / Matthews, B.W. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues. Authors: Lowther, W.T. / Zhang, Y. / Sampson, P.B. / Honek, J.F. / Matthews, B.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1c27.cif.gz | 66.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c27.ent.gz | 47.5 KB | Display | PDB format |
PDBx/mmJSON format | 1c27.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1c27_validation.pdf.gz | 432.8 KB | Display | wwPDB validaton report |
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Full document | 1c27_full_validation.pdf.gz | 441 KB | Display | |
Data in XML | 1c27_validation.xml.gz | 13.3 KB | Display | |
Data in CIF | 1c27_validation.cif.gz | 18.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c2/1c27 ftp://data.pdbj.org/pub/pdb/validation_reports/c2/1c27 | 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: 29210.580 Da / Num. of mol.: 1 / Fragment: NORLEUCINE PHOSPHONATE / Mutation: R175Q Source method: isolated from a genetically manipulated source Details: NORLEUCINE PHOSPHONATE COMPLEX / Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET28B / Production host: Escherichia coli (E. coli) References: UniProt: P07906, UniProt: P0AE18*PLUS, methionyl aminopeptidase | ||||||||
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#2: Chemical | #3: Chemical | ChemComp-NA / | #4: Chemical | ChemComp-NLP / ( | #5: Water | ChemComp-HOH / | Sequence details | THERE ARE FOUR ADDITIONAL RESIDUES ON THE C-TERMINUS LEFT OVER FROM A THROMBIN DIGEST OF THE HIS- ...THERE ARE FOUR ADDITIONAL | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.42 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: Hepes, NaCl, CoCl2, K2SO4, methionine, N-octanoyl sucrose, PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Apr 1, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→36.6 Å / Num. all: 16281 / Num. obs: 68595 / % possible obs: 93.6 % / Redundancy: 4.2 % / Biso Wilson estimate: 19.5 Å2 / Rmerge(I) obs: 0.056 / Net I/σ(I): 28.8 |
Reflection shell | Resolution: 1.95→2.02 Å / Rmerge(I) obs: 0.267 / Mean I/σ(I) obs: 4.6 / % possible all: 88.6 |
Reflection | *PLUS Num. obs: 16281 / Num. measured all: 68595 |
Reflection shell | *PLUS % possible obs: 88.6 % |
-Processing
Software |
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Refinement | Resolution: 1.95→36.6 Å / Stereochemistry target values: TNT /
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Solvent computation | Solvent model: TNT / Bsol: 294.4 Å2 / ksol: 0.908 e/Å3 | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.95→36.6 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | |||||||||||||||
Refinement | *PLUS Num. reflection obs: 16281 / Rfactor obs: 0.17 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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