+Open data
-Basic information
Entry | Database: PDB / ID: 1.0E+15 | ||||||
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Title | Chitinase B from Serratia Marcescens | ||||||
Components | CHITINASE B | ||||||
Keywords | HYDROLASE / CHITIN DEGRADATION | ||||||
Function / homology | Function and homology information chitin binding / polysaccharide catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate binding / extracellular region Similarity search - Function | ||||||
Biological species | SERRATIA MARCESCENS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 1.9 Å | ||||||
Authors | Van Aalten, D.M.F. / Synstad, B. / Brurberg, M.B. / Hough, E. / Riise, B.W. / Eijsink, V.G.H. / Wierenga, R.K. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2000 Title: Structure of a Two-Domain Chitotriosidase from Serratia Marcescens at 1.9 Angstrom Resoltuion Authors: Van Aalten, D.M.F. / Synstad, B. / Brurberg, M.B. / Hough, E. / Riise, B.W. / Eijsink, V.G.H. / Wierenga, R.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e15.cif.gz | 199.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e15.ent.gz | 166.9 KB | Display | PDB format |
PDBx/mmJSON format | 1e15.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e1/1e15 ftp://data.pdbj.org/pub/pdb/validation_reports/e1/1e15 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | BIOMOLECULETHERE IS A DIMER IN THE ASYMMETRIC UNIT, BUT THEBIOLOGICALLY ACTIVE FORM IS A MONOMER. |
-Components
#1: Protein | Mass: 55518.012 Da / Num. of mol.: 2 / Fragment: COMPLETE MOLECULE Source method: isolated from a genetically manipulated source Source: (gene. exp.) SERRATIA MARCESCENS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q54276 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 50.62 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.6 Details: 0.25 M LI2SO4, 1.0 M(NH4)2SO4, CITRATE BUFFER PH 5.6 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS 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: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 0.909 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.909 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. obs: 88458 / % possible obs: 100 % / Observed criterion σ(I): 1 / Redundancy: 5.3 % / Biso Wilson estimate: 15.3 Å2 / Rmerge(I) obs: 0.087 / Net I/σ(I): 11.5 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.344 / Mean I/σ(I) obs: 3.3 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 1.9→38.87 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 2020983.56 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 40.59 Å2 / ksol: 0.321208 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→38.87 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→2.02 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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