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- PDB-1aiw: NMR STRUCTURES OF THE CELLULOSE-BINDING DOMAIN OF THE ENDOGLUCANA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1aiw | ||||||
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Title | NMR STRUCTURES OF THE CELLULOSE-BINDING DOMAIN OF THE ENDOGLUCANASE Z FROM ERWINIA CHRYSANTHEMI, 23 STRUCTURES | ||||||
![]() | ENDOGLUCANASE Z | ||||||
![]() | CELLULOSE DEGRADATION / ENDOGLUCANASE / CELLULOSE-BINDING DOMAIN / ERWINIA CHRYSANTHEMI | ||||||
Function / homology | ![]() cellulase / cellulase activity / cellulose catabolic process / carbohydrate binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
![]() | Brun, E. / Moriaud, F. / Gans, P. / Blackledge, M.J. / Barras, F. / Marion, D. | ||||||
![]() | ![]() Title: Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi. Authors: Brun, E. / Moriaud, F. / Gans, P. / Blackledge, M.J. / Barras, F. / Marion, D. #1: ![]() Title: Overproduction, Purification and Characterization of the Cellulose-Binding Domain of the Erwinia Chrysanthemi Secreted Endoglucanase Egz Authors: Brun, E. / Gans, P. / Marion, D. / Barras, F. #2: ![]() Title: Periplasmic Disulphide Bond Formation is Essential for Cellulase Secretion by the Plant Pathogen Erwinia Chrysanthemi Authors: Bortoli-German, I. / Brun, E. / Py, B. / Chippaux, M. / Barras, F. #3: ![]() Title: Cellulase Egz of Erwinia Chrysanthemi: Structural Organization and Importance of His98 and Glu133 Residues for Catalysis Authors: Py, B. / Bortoli-German, I. / Haiech, J. / Chippaux, M. / Barras, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 219.8 KB | Display | ![]() |
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PDB format | ![]() | 179.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 356.1 KB | Display | ![]() |
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Full document | ![]() | 463.9 KB | Display | |
Data in XML | ![]() | 20.5 KB | Display | |
Data in CIF | ![]() | 36.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 6660.123 Da / Num. of mol.: 1 / Fragment: C-TERMINAL CELLULOSE-BINDING DOMAIN / Mutation: T1M, A2G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 4.6 / Temperature: 310 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX 600 / Manufacturer: Bruker / Model: AMX 600 / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 30 / Conformers submitted total number: 23 |