2KJ7

Three-Dimensional NMR Structure of Rat Islet Amyloid Polypeptide in DPC micelles

> Summary

Summary for 2KJ7

DescriptorIslet amyloid polypeptide (1 entity in total)
Functional Keywordsiapp, amylin, islet amyloid polypeptide, rat iapp, amidation, amyloid, cleavage on pair of basic residues, disulfide bond, hormone, secreted
Biological sourceRattus norvegicus (brown rat,rat,rats)
Cellular locationSecreted P12969
Total number of polymer chains1
Total molecular weight3924.43
Authors
Nanga, R.,Brender, J.R.,Xu, J.,Hartman, K.,Subramanian, V.,Ramamoorthy, A. (deposition date: 2009-05-22, release date: 2009-06-23, Last modification date: 2011-07-13)
Primary citation
Nanga, R.P.,Brender, J.R.,Xu, J.,Hartman, K.,Subramanian, V.,Ramamoorthy, A.
Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy.
J.Am.Chem.Soc., 131:8252-8261, 2009
PubMed: 19456151 (PDB entries with the same primary citation)
DOI: 10.1021/ja9010095
MImport into Mendeley
Experimental method
SOLUTION NMR
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers181041.8%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures

More Asymmetric unit images

Molmil generated image of 2kj7
no rotation
Molmil generated image of 2kj7
rotated about x axis by 90°
Molmil generated image of 2kj7
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
AIslet amyloid polypeptidepolymer383924.41
UniProt (P12969)
Rattus norvegicus (brown rat rat rats)@PDBjAmylin, Diabetes-associated peptide, DAP

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight3924.4
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight3924.4
*Water molecules are not included.

> Experimental details

Spectrometer

Experimental method:SOLUTION NMR

Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength
1BrukerAvanceBruker Avance900

Experiment

experiment idconditions idsolution idExperiment type
1112D 1H-1H TOCSY
2112D 1H-1H NOESY

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature
17.3ambient303

Conformers

Conformers Calculated Total Number100
Conformers Submitted Total Number10

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005615cellular_componentextracellular space
A0043025cellular_componentneuronal cell body
A0030141cellular_componentsecretory granule
A0005179molecular_functionhormone activity
A0042802molecular_functionidentical protein binding
A0097647biological_processamylin receptor signaling pathway
A0042755biological_processeating behavior
A0006006biological_processglucose metabolic process
A0045779biological_processnegative regulation of bone resorption
A0045596biological_processnegative regulation of cell differentiation
A0030816biological_processpositive regulation of cAMP metabolic process
A0019233biological_processsensory perception of pain
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
PS0025815Calcitonin / CGRP / IAPP family signature. C-[SAGDN]-[STN]-x(0,1)-[SA]-T-C-[VMA]-x(3)-[LYF]-x(3)-[LYF]
ChainResidueDetails
ACYS2-LEU16

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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
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Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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