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- PDB-1f8p: PORCINE NEUROPEPTIDE Y BOUND TO DPC MICELLES -

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Basic information

Entry
Database: PDB / ID: 1f8p
TitlePORCINE NEUROPEPTIDE Y BOUND TO DPC MICELLES
ComponentsNEUROPEPTIDE Y (PNPY)
KeywordsNEUROPEPTIDE / HELIX
Function / homology
Function and homology information


neuropeptide Y receptor binding / positive regulation of appetite / adult feeding behavior / neuropeptide hormone activity / feeding behavior / neuronal dense core vesicle / neuropeptide signaling pathway / extracellular space
Similarity search - Function
Pancreatic hormone-like / Pancreatic hormone-like, conserved site / Pancreatic hormone peptide / Pancreatic hormone family signature. / Pancreatic hormone family profile. / Pancreatic hormones / neuropeptide F / peptide YY family
Similarity search - Domain/homology
MethodSOLUTION NMR / simmulated annealing in torsion angle space
AuthorsBader, R. / Beck-Sickinger, A.G. / Zerbe, O.
CitationJournal: J.Mol.Biol. / Year: 2001
Title: Structure and dynamics of micelle-bound neuropeptide Y: comparison with unligated NPY and implications for receptor selection.
Authors: Bader, R. / Bettio, A. / Beck-Sickinger, A.G. / Zerbe, O.
History
DepositionJul 3, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 3, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: NEUROPEPTIDE Y (PNPY)


Theoretical massNumber of molelcules
Total (without water)4,2591
Polymers4,2591
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)17 / 100structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy,target function
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide NEUROPEPTIDE Y (PNPY)


Mass: 4258.690 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: occurs in nervous system of pigs / References: UniProt: P01304

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
122E-COSY
1322D NOESY
NMR detailsText: 75 ms NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
13mM pNPY, 300mM d-38 DPC90% H2O/10% D2O
23mM pNPY, 300mM d-38 DPC100% D2O
Sample conditionsIonic strength: 0 / pH: 6.0 / Pressure: 1 atm / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.1Brukerprocessing
XEASY1.3.13Bartels, Wuthrichdata analysis
DYANA1.5Guntert, Wuthrichstructure solution
Amber4.1Kollmanrefinement
RefinementMethod: simmulated annealing in torsion angle space / Software ordinal: 1
Details: 344 NOE-based distance restraints 145 dihedral angle constraints
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy,target function
Conformers calculated total number: 100 / Conformers submitted total number: 17

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