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- PDB-1k45: The Solution Structure of the CBM4-2 Carbohydrate Binding Module ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1k45 | ||||||
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Title | The Solution Structure of the CBM4-2 Carbohydrate Binding Module from a Thermostable Rhodothermus marinus Xylanase. | ||||||
![]() | Xylanase | ||||||
![]() | HYDROLASE / beta-sandwich formed by 11 strands. Binding-site cleft. Solvent exposed aromatics (Trp69 / Phe110) in binding cleft. Two helical twists. Two calcium binding sites. | ||||||
Function / homology | ![]() xylan catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / hybrid distance geometry, simulated annealing using XPLOR | ||||||
Model type details | minimized average | ||||||
![]() | Simpson, P.J. / Jamieson, S.J. / Abou-Hachem, M. / Nordberg-Karlsson, E. / Gilbert, H.J. / Holst, O. / Williamson, M.P. | ||||||
![]() | ![]() Title: The solution structure of the CBM4-2 carbohydrate binding module from a thermostable Rhodothermus marinus xylanase. Authors: Simpson, P.J. / Jamieson, S.J. / Abou-Hachem, M. / Karlsson, E.N. / Gilbert, H.J. / Holst, O. / Williamson, M.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 65.1 KB | Display | ![]() |
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PDB format | ![]() | 49.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 18103.803 Da / Num. of mol.: 1 Fragment: Second family 4 carbohydrate binding module (CBM4-2)(Residues 211-373) 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
Details | Contents: 1.5 mM CBM4-2 15N-labelled, and 13C,15N double labelled protein; 50 mM CaCl2, 50 mM sodium acetate-d3, pH 6.0, 10% D2O, 10 mM sodium azide, 0.1 mM sodium trimethylsilylpropionate (TSP) Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0.2 M / pH: 6 / Pressure: ambient / Temperature: 310 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: hybrid distance geometry, simulated annealing using XPLOR Software ordinal: 1 Details: The final set of restraints contained 1654 non-redundant unambiguous NOEs and 17 ambiguous NOEs, 93 dihedral angle restraints, 72 chi1 and 1 chi2 restraint, and 65 pairs of hydrogen bond ...Details: The final set of restraints contained 1654 non-redundant unambiguous NOEs and 17 ambiguous NOEs, 93 dihedral angle restraints, 72 chi1 and 1 chi2 restraint, and 65 pairs of hydrogen bond restraints, plus 177 backbone dihedral restraints based on 13C shifts from TALOS. | ||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |