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- PDB-7jrl: The structure of CBM51-2 in complex with GlcNAc and INT domains f... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7jrl | |||||||||
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Title | The structure of CBM51-2 in complex with GlcNAc and INT domains from Clostridium perfringens ZmpB | |||||||||
![]() | F5/8 type C domain protein | |||||||||
![]() | SUGAR BINDING PROTEIN / Carbohydrate binding module | |||||||||
Function / homology | ![]() hydrolase activity, acting on glycosyl bonds / metabolic process / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() ![]() | |||||||||
![]() | Pluvinage, B. / Boraston, A.B. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Architecturally complex O -glycopeptidases are customized for mucin recognition and hydrolysis. Authors: Pluvinage, B. / Ficko-Blean, E. / Noach, I. / Stuart, C. / Thompson, N. / McClure, H. / Buenbrazo, N. / Wakarchuk, W. / Boraston, A.B. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 120.7 KB | Display | ![]() |
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PDB format | ![]() | 88.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 772 KB | Display | ![]() |
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Full document | ![]() | 772.7 KB | Display | |
Data in XML | ![]() | 22.9 KB | Display | |
Data in CIF | ![]() | 36.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7jfsC ![]() 7jnbC ![]() 7jndC ![]() 7jnfC ![]() 7jrmC ![]() 7js4C ![]() 2vmgS S: Starting model for refinement 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
-Protein / Sugars , 2 types, 2 molecules A![](data/chem/img/NAG.gif)
![](data/chem/img/NAG.gif)
#1: Protein | Mass: 53592.801 Da / Num. of mol.: 1 Fragment: Carbohydrate binding module (UNP residues 1227-1687) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A Gene: CPF_1489 / Plasmid: pET28a / Production host: ![]() ![]() |
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#3: Sugar | ChemComp-NAG / |
-Non-polymers , 5 types, 554 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/TRS.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/TRS.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-CA / | ||||||
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#4: Chemical | ChemComp-EDO / #5: Chemical | ChemComp-PO4 / | #6: Chemical | ChemComp-TRS / | #7: Water | ChemComp-HOH / | |
-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 51.55 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.15 M sodium phosphate monobasic, 18% PEG3350, 0.1 M Tris-HCl |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Apr 11, 2011 |
Radiation | Monochromator: Liquid nitrogen-cooled double crystal Si(111) Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91966 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→42.86 Å / Num. obs: 86269 / % possible obs: 100 % / Redundancy: 5 % / CC1/2: 0.998 / Rmerge(I) obs: 0.082 / Rpim(I) all: 0.04 / Net I/σ(I): 13.2 |
Reflection shell | Resolution: 1.5→1.58 Å / Redundancy: 5 % / Rmerge(I) obs: 0.581 / Mean I/σ(I) obs: 3.6 / Num. unique obs: 12539 / CC1/2: 0.735 / Rpim(I) all: 0.283 / % possible all: 100 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2VMG Resolution: 1.5→38.93 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.951 / SU B: 1.147 / SU ML: 0.043 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.071 / ESU R Free: 0.067 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 62.74 Å2 / Biso mean: 16.24 Å2 / Biso min: 6.44 Å2
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Refinement step | Cycle: final / Resolution: 1.5→38.93 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.5→1.539 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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