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- PDB-7bg0: Fusion of MBP and the backbone of the long-acting amylin analog AM833. -
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Open data
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Basic information
Entry | Database: PDB / ID: 7bg0 | ||||||
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Title | Fusion of MBP and the backbone of the long-acting amylin analog AM833. | ||||||
![]() | Maltose/maltodextrin-binding periplasmic protein,Islet amyloid polypeptide | ||||||
![]() | HORMONE / Amylin / AM833 / cagrilintide | ||||||
Function / homology | ![]() : / amylin receptor signaling pathway / Calcitonin-like ligand receptors / negative regulation of amyloid fibril formation / negative regulation of bone resorption / eating behavior / detection of maltose stimulus / maltose transport complex / negative regulation of osteoclast differentiation / positive regulation of protein kinase A signaling ...: / amylin receptor signaling pathway / Calcitonin-like ligand receptors / negative regulation of amyloid fibril formation / negative regulation of bone resorption / eating behavior / detection of maltose stimulus / maltose transport complex / negative regulation of osteoclast differentiation / positive regulation of protein kinase A signaling / carbohydrate transport / Regulation of gene expression in beta cells / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / negative regulation of protein-containing complex assembly / positive regulation of calcium-mediated signaling / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / bone resorption / sensory perception of pain / ATP-binding cassette (ABC) transporter complex / osteoclast differentiation / cell chemotaxis / hormone activity / cell-cell signaling / amyloid-beta binding / outer membrane-bounded periplasmic space / G alpha (s) signalling events / positive regulation of MAPK cascade / periplasmic space / receptor ligand activity / positive regulation of apoptotic process / Amyloid fiber formation / signaling receptor binding / lipid binding / apoptotic process / DNA damage response / signal transduction / extracellular space / extracellular region / identical protein binding / membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Johansson, E. | ||||||
![]() | ![]() Title: Development of Cagrilintide, a Long-Acting Amylin Analogue. Authors: Kruse, T. / Hansen, J.L. / Dahl, K. / Schaffer, L. / Sensfuss, U. / Poulsen, C. / Schlein, M. / Hansen, A.M.K. / Jeppesen, C.B. / Dornonville de la Cour, C. / Clausen, T.R. / Johansson, E. / ...Authors: Kruse, T. / Hansen, J.L. / Dahl, K. / Schaffer, L. / Sensfuss, U. / Poulsen, C. / Schlein, M. / Hansen, A.M.K. / Jeppesen, C.B. / Dornonville de la Cour, C. / Clausen, T.R. / Johansson, E. / Fulle, S. / Skyggebjerg, R.B. / Raun, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 369.9 KB | Display | ![]() |
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PDB format | ![]() | 243.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 929.7 KB | Display | ![]() |
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Full document | ![]() | 954.3 KB | Display | |
Data in XML | ![]() | 52.5 KB | Display | |
Data in CIF | ![]() | 71.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3g7vS S: Starting model for refinement |
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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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
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Components
#1: Protein | Mass: 44495.297 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Strain: K12 / Gene: malE, b4034, JW3994, IAPP / Production host: ![]() ![]() #2: Polysaccharide | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.8 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 20mM Tris pH 7.4, 50mM NaCl, 0.02 M magnesium chloride, 0.1 M HEPES pH 7.5, 22 %(w/v) polyacrylic acid 5100 sodium salt |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Apr 11, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.89→37.55 Å / Num. obs: 40035 / % possible obs: 99.77 % / Redundancy: 5.7 % / Biso Wilson estimate: 63.76 Å2 / CC1/2: 0.995 / CC star: 0.999 / Rmerge(I) obs: 0.09446 / Rpim(I) all: 0.04386 / Rrim(I) all: 0.1042 / Net I/σ(I): 16.7 |
Reflection shell | Resolution: 2.895→2.998 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.5807 / Mean I/σ(I) obs: 2.43 / Num. unique obs: 3961 / CC1/2: 0.887 / CC star: 0.969 / Rpim(I) all: 0.2675 / Rrim(I) all: 0.6397 / % possible all: 98.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3G7V Resolution: 2.89→37.55 Å / SU ML: 0.4209 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 31.0437 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 68.32 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.89→37.55 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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