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Open data
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Basic information
Entry | Database: PDB / ID: 1nbc | ||||||
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Title | BACTERIAL TYPE 3A CELLULOSE-BINDING DOMAIN | ||||||
![]() | CELLULOSOMAL SCAFFOLDING PROTEIN A | ||||||
![]() | CELLULOSE DEGRADATION / CELLULOSE-BINDING DOMAIN / ![]() | ||||||
Function / homology | ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Tormo, J. / Lamed, R. / Steitz, T.A. | ||||||
![]() | ![]() Title: Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. Authors: Tormo, J. / Lamed, R. / Chirino, A.J. / Morag, E. / Bayer, E.A. / Shoham, Y. / Steitz, T.A. #1: ![]() Title: Expression, Purification, and Characterization of the Cellulose-Binding Domain of the Scaffoldin Subunit from the Cellulosome of Clostridium Thermocellum Authors: Morag, E. / Lapidot, A. / Govorko, D. / Lamed, R. / Wilchek, M. / Bayer, E.A. / Shoham, Y. #2: ![]() Title: Crystallization and Preliminary X-Ray Analysis of the Major Cellulose-Binding Domain of the Cellulosome from Clostridium Thermocellum Authors: Lamed, R. / Tormo, J. / Chirino, A.J. / Morag, E. / Bayer, E.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.7 KB | Display | ![]() |
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PDB format | ![]() | 58.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.999769, -0.006031, -0.020615), Vector ![]() Details | THE ASYMMETRIC UNIT OF THE CRYSTAL CONTAINS TWO COPIES OF THE PROTEIN MOLECULE. CHAIN IDENTIFIER A: PROTOMER 1, CHAIN IDENTIFIER B: PROTOMER 2. | |
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Components
#1: Protein | Mass: 17228.727 Da / Num. of mol.: 2 / Fragment: CELLULOSE-BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 12 ℃ / pH: 6.5 / Method: unknown | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Details: YALE MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.75→10 Å / Num. obs: 26267 / % possible obs: 87.4 % / Redundancy: 4.3 % / Biso Wilson estimate: 31.4 Å2 / Rmerge(I) obs: 0.082 |
Reflection | *PLUS Num. measured all: 113902 |
Reflection shell | *PLUS Highest resolution: 1.75 Å / Lowest resolution: 7.83 Å / % possible obs: 51 % |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Displacement parameters | Biso mean: 29.6 Å2
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Refine analyze | Luzzati coordinate error obs: 0.23 Å / Luzzati d res low obs: 5 Å / Luzzati sigma a obs: 0.22 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→10 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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