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- PDB-1lbj: NMR solution structure of motilin in phospholipid bicellar solution -

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Basic information

Entry
Database: PDB / ID: 1lbj
TitleNMR solution structure of motilin in phospholipid bicellar solution
Componentsmotilin
KeywordsHORMONE/GROWTH FACTOR / a-helix / b-turn of type I / HORMONE-GROWTH FACTOR COMPLEX
Function / homology
Function and homology information


motilin receptor binding / Peptide ligand-binding receptors / hormone activity / G alpha (q) signalling events / extracellular region
Similarity search - Function
Promotilin / Motilin/ghrelin-associated peptide / Motilin/ghrelin / Motilin/ghrelin-associated peptide / Motilin/ghrelin
Similarity search - Domain/homology
MethodSOLUTION NMR / simulated annealing, molecular dynamics
AuthorsAndersson, A. / Maler, L.
Citation
Journal: J.BIOMOL.NMR / Year: 2002
Title: NMR solution structure and dynamics of motilin in isotropic phospholipid bicellar solution
Authors: Andersson, A. / Maler, L.
#1: Journal: Biochemistry / Year: 1997
Title: Three-dimensional structure and position of porcine motilin in sodium dodecyl sulfate micelles determined by 1H NMR
Authors: Jarvet, J. / Zdunek, J. / Damberg, P. / Graslund, A.
History
DepositionApr 3, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 20, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 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_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: motilin


Theoretical massNumber of molelcules
Total (without water)2,7031
Polymers2,7031
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)24 / 100structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1closest to the average

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Components

#1: Protein/peptide motilin


Mass: 2703.079 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: The peptide was chemically synthesized. The sequence of the motilin peptide is naturally found in Homo sapiens (human)
References: UniProt: P12872

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D NOESY
NMR detailsText: this structure was determined using standard 2D homonuclear techniques

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Sample preparation

DetailsContents: 3 mM motilin, 50mM KCl, 15% q=0.5 DMPC,DMPG/DHPC / Solvent system: 90% H2O, 10% D20
Sample conditionsIonic strength: 50 mM KCl / pH: 5.5 / Pressure: ambient / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Felix97msi inc.data analysis
DIANA2.8Guntert, Braun & Wuthrichstructure solution
Amber5Peralmann, Case, Caldwell, Ross, Cheatham, Ferguson, Seibel, Singh, Weiner & Kollmanrefinement
RefinementMethod: simulated annealing, molecular dynamics / Software ordinal: 1
Details: structure based on total of 200 distance and 8 torsion angle constraints
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 24

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