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- PDB-4v1k: SeMet structure of a novel carbohydrate binding module from glyco... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4v1k | ||||||
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Title | SeMet structure of a novel carbohydrate binding module from glycoside hydrolase family 9 (Cel9A) from Ruminococcus flavefaciens FD-1 | ||||||
![]() | CARBOHYDRATE BINDING MODULE | ||||||
![]() | SUGAR BINDING PROTEIN / CARBOHYDRATE BINDING MODULE / GLYCOSIDE HYDROLASE FAMILY 9 / CEL9A / CELLULOSOME / RUMINOCOCCUS FLAVEFACIENS FD-1 | ||||||
Function / homology | Domain of unknown function DUF5620 / Domain of unknown function (DUF5620) / 2-HYDROXY BUTANE-1,4-DIOL / Carbohydrate binding module![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Venditto, I. / Goyal, A. / Thompson, A. / Ferreira, L.M.A. / Fontes, C.M.G.A. / Najmudin, S. | ||||||
![]() | ![]() Title: Complexity of the Ruminococcus Flavefaciens Cellulosome Reflects an Expansion in Glycan Recognition. Authors: Venditto, I. / Luis, A.S. / Rydahl, M. / Schuckel, J. / Fernandes, V.O. / Vidal-Melgosa, S. / Bule, P. / Goyal, A. / Pires, V.M.R. / Dourado, C.G. / Ferreira, L.M.A. / Coutinho, P.M. / ...Authors: Venditto, I. / Luis, A.S. / Rydahl, M. / Schuckel, J. / Fernandes, V.O. / Vidal-Melgosa, S. / Bule, P. / Goyal, A. / Pires, V.M.R. / Dourado, C.G. / Ferreira, L.M.A. / Coutinho, P.M. / Henrissat, B. / Knox, J.P. / Basle, A. / Najmudin, S. / Gilbert, H.J. / Willats, W.G.T. / Fontes, C.M.G.A. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2014 Title: Expression, Purification and Crystallization of a Novel Carbohydrate-Binding Module from the Ruminococcus Flavefaciens Cellulosome. Authors: Venditto, I. / Centeno, M.S.J. / Ferreira, L.M.A. / Fontes, C.M.G.A. / Najmudin, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75 KB | Display | ![]() |
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PDB format | ![]() | 61 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 9.9 KB | Display | |
Data in CIF | ![]() | 13.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4d3lC ![]() 4v17C ![]() 4v18C ![]() 4v1bC ![]() 4v1iC ![]() 4v1lC ![]() 5aosC ![]() 5aotC ![]() 5fu2C ![]() 5fu3C ![]() 5fu4C ![]() 5fu5C C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 15470.633 Da / Num. of mol.: 1 / Fragment: RESIDUES 492-629 Source method: isolated from a genetically manipulated source Details: SELENOMETHIONINE DERIVATIVE / Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 5 types, 150 molecules ![](data/chem/img/2PE.gif)
![](data/chem/img/P6G.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/BGQ.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/P6G.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/BGQ.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-2PE / | ||||
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#3: Chemical | ChemComp-P6G / | ||||
#4: Chemical | #5: Chemical | ChemComp-BGQ / | #6: Water | ChemComp-HOH / | |
-Details
Sequence details | SELENOMETH |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.89 Å3/Da / Density % sol: 58 % Description: DATA WAS ALSO COLLECTED AT THE SE-PEAK EDGE WITH AN INVERSE BEAM. |
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Crystal grow | pH: 7 Details: 0.2 M AMMONIUM ACETATE, 1.5 M K2HPO4, 1.5 M NAH2PO4 CRYO USED WAS PARATONE-N., pH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 18, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95372 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→42.48 Å / Num. obs: 24839 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 11.2 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 14.5 |
Reflection shell | Resolution: 1.6→1.69 Å / Redundancy: 11.1 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 1.3 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 1.6→42.48 Å / Cor.coef. Fo:Fc: 0.979 / Cor.coef. Fo:Fc free: 0.974 / SU B: 2.383 / SU ML: 0.037 / Cross valid method: THROUGHOUT / ESU R: 0.064 / ESU R Free: 0.059 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.3 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.386 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→42.48 Å
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Refine LS restraints |
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