+Open data
-Basic information
Entry | Database: PDB / ID: 2k1v | |||||||||
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Title | R3/I5 relaxin chimera | |||||||||
Components |
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Keywords | HORMONE / peptide hormone / relaxin-3 / insl5 / chimera / Cleavage on pair of basic residues / Secreted / SIGNALING PROTEIN | |||||||||
Function / homology | Function and homology information Relaxin receptors / positive regulation of feeding behavior / G protein-coupled receptor binding / hormone activity / G alpha (i) signalling events / G alpha (s) signalling events / extracellular region Similarity search - Function | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Model details | Solution structure of the relaxin-3 B-chain / INSL5 A-chain chimeric peptide. | |||||||||
Authors | Rosengren, K. / Haugaard-Jonsson, L.M. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2008 Title: Structure of the R3/I5 Chimeric Relaxin Peptide, a Selective GPCR135 and GPCR142 Agonist. Authors: Haugaard-Jonsson, L.M. / Hossain, M.A. / Daly, N.L. / Bathgate, R.A. / Wade, J.D. / Craik, D.J. / Rosengren, K.J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k1v.cif.gz | 277 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2k1v.ent.gz | 240.6 KB | Display | PDB format |
PDBx/mmJSON format | 2k1v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2k1v_validation.pdf.gz | 355.2 KB | Display | wwPDB validaton report |
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Full document | 2k1v_full_validation.pdf.gz | 549.2 KB | Display | |
Data in XML | 2k1v_validation.xml.gz | 17.7 KB | Display | |
Data in CIF | 2k1v_validation.cif.gz | 29.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k1/2k1v ftp://data.pdbj.org/pub/pdb/validation_reports/k1/2k1v | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3047.586 Da / Num. of mol.: 1 / Fragment: Relaxin-3 B chain / Source method: obtained synthetically Details: Peptide chain was assembled by solid phase peptide synthesis. References: UniProt: Q8WXF3 |
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#2: Protein/peptide | Mass: 2202.509 Da / Num. of mol.: 1 / Fragment: Insulin-like peptide INSL5 A chain / Source method: obtained synthetically Details: Peptide chain was assembled by solid phase peptide synthesis. References: UniProt: Q9Y5Q6 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Solution structure of the relaxin-3 B-chain / INSL5 A-chain chimeric peptide. | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures were generated using torsion angle dynamics in CNS and subsequently refined and energy minimized in a water shell using cartesian dynamics in CNS. | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 522 / NOE intraresidue total count: 0 / NOE long range total count: 243 / NOE medium range total count: 32 / NOE sequential total count: 247 / Hydrogen bond constraints total count: 20 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 / Maximum upper distance constraint violation: 0.29 Å |