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Open data
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Basic information
Entry | Database: PDB / ID: 3fth | ||||||
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Title | NFLVHSS segment from Islet Amyloid Polypeptide (IAPP or Amylin) | ||||||
![]() | NFLVHSS heptapeptide from Islet Amyloid Polypeptide | ||||||
![]() | PROTEIN FIBRIL / amyloid-like protofibril | ||||||
Function / homology | ![]() : / amylin receptor signaling pathway / Calcitonin-like ligand receptors / negative regulation of amyloid fibril formation / negative regulation of bone resorption / eating behavior / negative regulation of osteoclast differentiation / positive regulation of protein kinase A signaling / Regulation of gene expression in beta cells / negative regulation of protein-containing complex assembly ...: / amylin receptor signaling pathway / Calcitonin-like ligand receptors / negative regulation of amyloid fibril formation / negative regulation of bone resorption / eating behavior / negative regulation of osteoclast differentiation / positive regulation of protein kinase A signaling / Regulation of gene expression in beta cells / negative regulation of protein-containing complex assembly / positive regulation of calcium-mediated signaling / bone resorption / sensory perception of pain / osteoclast differentiation / hormone activity / cell-cell signaling / amyloid-beta binding / G alpha (s) signalling events / positive regulation of MAPK cascade / receptor ligand activity / positive regulation of apoptotic process / Amyloid fiber formation / signaling receptor binding / lipid binding / apoptotic process / signal transduction / extracellular space / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Wiltzius, J.J.W. / Sawaya, M.R. / Eisenberg, D. | ||||||
![]() | ![]() Title: Molecular mechanisms for protein-encoded inheritance Authors: Wiltzius, J.J. / Landau, M. / Nelson, R. / Sawaya, M.R. / Apostol, M.I. / Goldschmidt, L. / Soriaga, A.B. / Cascio, D. / Rajashankar, K. / Eisenberg, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 11.8 KB | Display | ![]() |
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PDB format | ![]() | 7.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 419.4 KB | Display | ![]() |
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Full document | ![]() | 419.5 KB | Display | |
Data in XML | ![]() | 2.9 KB | Display | |
Data in CIF | ![]() | 3.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3fodC ![]() 3fpoC ![]() 3fr1C ![]() 3ftkC ![]() 3ftlC ![]() 3ftrC ![]() 3fvaC ![]() 4np8C 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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1 | ![]()
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2 |
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Unit cell |
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Details | THE AUTHORS STATE THAT THE BIOLOGICAL UNIT IS A INDEFINITELY LONG PAIR OF SHEETS (A PROTOFIBRIL). ONE SHEET FORMED BY CHAINS A AND B AND THEIR CRYSTALLOGRAPHIC TRANSLATIONS ALONG THE "A" CELL DIMENSION (E.G. X,Y,Z AND X+1,Y,Z). THE SECOND SHEET IS CONSTRUCTED FROM -X, Y+1/2,-Z AND THEIR CRYSTALLOGRAPHIC TRANSLATIONS ALONG THE "A" CELL DIMENSION (E.G. -X+1, Y+1/2,-Z). |
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Components
#1: Protein/peptide | Mass: 803.883 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) ![]() #2: Chemical | ChemComp-SO4 / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.7 Å3/Da / Density % sol: 27.5 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 1.5M Ammonium Sulfate, 0.1 M Sodium acetate trihydrate pH 4.6, vapor diffusion, hanging drop, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 8, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→90 Å / Num. all: 932 / Num. obs: 932 / % possible obs: 95.2 % / Observed criterion σ(I): -3 / Redundancy: 2.8 % / Rmerge(I) obs: 0.189 / Χ2: 1.054 |
Reflection shell | Resolution: 1.8→1.94 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 2.3 / Num. unique all: 180 / Χ2: 1.122 / % possible all: 89.1 |
-Phasing
Phasing | Method: ![]() |
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Phasing MR | Model details: Phaser MODE: MR_AUTO |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 38.59 Å2 / Biso mean: 8.193 Å2 / Biso min: 0 Å2
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Refinement step | Cycle: LAST / Resolution: 1.84→16.6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.84→1.892 Å / Total num. of bins used: 20
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