+Open data
-Basic information
Entry | Database: PDB / ID: 2man | |||||||||
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Title | MANNOTRIOSE COMPLEX OF THERMOMONOSPORA FUSCA BETA-MANNANASE | |||||||||
Components | PROTEIN (BETA-MANNANASE) | |||||||||
Keywords | HYDROLASE / MANNANASE / GLYCOSYL HYDROLASE / FAMILY 5 / THERMOMONOSPORA FUSCA | |||||||||
Function / homology | Function and homology information mannan endo-1,4-beta-mannosidase / mannan endo-1,4-beta-mannosidase activity / organic substance metabolic process Similarity search - Function | |||||||||
Biological species | Thermobifida fusca (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | |||||||||
Authors | Hilge, M. / Gloor, S.M. / Piontek, K. | |||||||||
Citation | Journal: Structure / Year: 1998 Title: High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5. Authors: Hilge, M. / Gloor, S.M. / Rypniewski, W. / Sauer, O. / Heightman, T.D. / Zimmermann, W. / Winterhalter, K. / Piontek, K. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2man.cif.gz | 75.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2man.ent.gz | 54.6 KB | Display | PDB format |
PDBx/mmJSON format | 2man.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ma/2man ftp://data.pdbj.org/pub/pdb/validation_reports/ma/2man | HTTPS FTP |
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-Related structure data
Related structure data | 1bqcC 3manC 1manS S: Starting model for refinement C: citing same article (ref.) |
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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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-Components
#1: Protein | Mass: 33123.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: GERMAN COLLECTION OF MICROORGANISMS (DSM) / Source: (natural) Thermobifida fusca (bacteria) / Strain: KW3 References: GenBank: 3970820, UniProt: Q9ZF13*PLUS, mannan endo-1,4-beta-mannosidase |
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#2: Polysaccharide | beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose Source method: isolated from a genetically manipulated source |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 50.42 % | ||||||||||||||||||
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Crystal grow | pH: 7 / Details: 1.85M AMMONIUM SULFATE, 0.1M HEPES, PH 7.0 | ||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 1 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→30 Å / Num. obs: 26662 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 3.34 % / Rmerge(I) obs: 0.109 / Rsym value: 0.109 / Net I/σ(I): 10.6 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.399 / Mean I/σ(I) obs: 2.9 / % possible all: 97 |
Reflection shell | *PLUS % possible obs: 97 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1MAN Resolution: 1.9→30 Å / SU B: 2.96 / SU ML: 0.09 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.15 / ESU R Free: 0.13
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Displacement parameters | Biso mean: 20.3 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→30 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.9 Å / % reflection Rfree: 5 % / Rfactor obs: 0.178 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 20.3 Å2 |