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- PDB-1aoh: SINGLE COHESIN DOMAIN FROM THE SCAFFOLDING PROTEIN CIPA OF THE CL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1aoh | ||||||
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Title | SINGLE COHESIN DOMAIN FROM THE SCAFFOLDING PROTEIN CIPA OF THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME | ||||||
![]() | Cellulosomal-scaffolding protein A | ||||||
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Function / homology | ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Alzari, P.M. / Tavares, G. | ||||||
![]() | ![]() Title: The crystal structure of a type I cohesin domain at 1.7 A resolution. Authors: Tavares, G.A. / Beguin, P. / Alzari, P.M. #1: ![]() Title: Subcloning of a DNA Fragment Encoding a Single Cohesin Domain of the Clostridium Thermocellum Cellulosome-Integrating Protein Cipa: Purification, Crystallization, and Preliminary Diffraction ...Title: Subcloning of a DNA Fragment Encoding a Single Cohesin Domain of the Clostridium Thermocellum Cellulosome-Integrating Protein Cipa: Purification, Crystallization, and Preliminary Diffraction Analysis of the Encoded Polypeptide Authors: Beguin, P. / Raynaud, O. / Chaveroche, M.K. / Dridi, A. / Alzari, P.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 72.5 KB | Display | ![]() |
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PDB format | ![]() | 54.6 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.99976, 0.0207, -0.0073), Vector ![]() |
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Components
#1: Protein | Mass: 15760.738 Da / Num. of mol.: 2 / Fragment: COHESIN DOMAIN residues 1216-1361 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372 Cell line: BL21 / Cellular location: CYTOPLASM ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | ![]() Compound details | THE WILD TYPE PROTEIN CIPA CONTAINS NINE HOMOLOGOUS COHESIN DOMAINS (THE STRUCTURE PRESENTED HERE ...THE WILD TYPE PROTEIN CIPA CONTAINS NINE HOMOLOGOUS | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 40 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 6.25 Details: PROTEIN WAS CRYSTALLIZED FROM 18% PEG-8000, 0.2 M CALCIUM ACETATE, 6% GLYCEROL AND 0.05 M SODIUM CACODYLATE, PH 6.25 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Beguin, P., (1996) Protein Sci., 5, 1192 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.7→20 Å / Num. obs: 29669 / % possible obs: 92.2 % / Redundancy: 5.8 % / Biso Wilson estimate: 14 Å2 / Rmerge(I) obs: 0.055 / Net I/σ(I): 22.2 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.253 / Mean I/σ(I) obs: 4.5 / % possible all: 86.6 |
Reflection | *PLUS Num. measured all: 175259 |
Reflection shell | *PLUS % possible obs: 86.6 % |
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Processing
Software |
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Refinement | Method to determine structure![]() ![]()
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Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: UNRESTRAINED | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.7→1.78 Å / Total num. of bins used: 8
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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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LS refinement shell | *PLUS Rfactor Rwork: 0.29 |