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Yorodumi- PDB-1lbj: NMR solution structure of motilin in phospholipid bicellar solution -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lbj | ||||||
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Title | NMR solution structure of motilin in phospholipid bicellar solution | ||||||
Components | motilin | ||||||
Keywords | HORMONE/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 | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Authors | Andersson, 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lbj.cif.gz | 159.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lbj.ent.gz | 112.1 KB | Display | PDB format |
PDBx/mmJSON format | 1lbj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lbj_validation.pdf.gz | 343.2 KB | Display | wwPDB validaton report |
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Full document | 1lbj_full_validation.pdf.gz | 455.1 KB | Display | |
Data in XML | 1lbj_validation.xml.gz | 8.5 KB | Display | |
Data in CIF | 1lbj_validation.cif.gz | 14.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lb/1lbj ftp://data.pdbj.org/pub/pdb/validation_reports/lb/1lbj | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homologyF&H Search |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | 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
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
NMR details | Text: this structure was determined using standard 2D homonuclear techniques |
-Sample preparation
Details | Contents: 3 mM motilin, 50mM KCl, 15% q=0.5 DMPC,DMPG/DHPC / Solvent system: 90% H2O, 10% D20 |
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Sample conditions | Ionic strength: 50 mM KCl / pH: 5.5 / Pressure: ambient / Temperature: 310 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 Details: structure based on total of 200 distance and 8 torsion angle constraints | ||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 24 |