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- PDB-2fhw: Solution structure of human relaxin-3 -

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Basic information

Entry
Database: PDB / ID: 2fhw
TitleSolution structure of human relaxin-3
Components(Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7)) x 2
KeywordsSIGNALING PROTEIN / insulin/relaxin super-family fold
Function / homology
Function and homology information


Relaxin receptors / G protein-coupled receptor binding / hormone activity / G alpha (i) signalling events / G alpha (s) signalling events / extracellular region
Similarity search - Function
Insulin family / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin family signature. / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin-like superfamily
Similarity search - Domain/homology
MethodSOLUTION NMR / Structures were calculated using torsion angle dynamics, further refined using Cartesian dynamics in explicit solvent.
AuthorsRosengren, K.J. / Craik, D.J.
CitationJournal: J.Biol.Chem. / Year: 2006
Title: Solution structure and novel insights into the determinants of the receptor specificity of human relaxin-3.
Authors: Rosengren, K.J. / Lin, F. / Bathgate, R.A. / Tregear, G.W. / Daly, N.L. / Wade, J.D. / Craik, D.J.
History
DepositionDec 27, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 24, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 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
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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
B: Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7)
A: Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7)


Theoretical massNumber of molelcules
Total (without water)5,5132
Polymers5,5132
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)20 / 50structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7)


Mass: 3047.586 Da / Num. of mol.: 1 / Fragment: Relaxin 3 B chain / Source method: obtained synthetically
Details: This sequence occurs naturally in humans. For this study the peptide has been generated by solid phase peptide synthesis.
References: UniProt: Q8WXF3
#2: Protein/peptide Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7)


Mass: 2465.845 Da / Num. of mol.: 1 / Fragment: Relaxin 3 A chain / Source method: obtained synthetically
Details: This sequence occurs naturally in humans. For this study the peptide has been generated by solid phase peptide synthesis.
References: UniProt: Q8WXF3

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DQF-COSY
1212D TOCSY
1312D NOESY
1422D TOCSY
1522D NOESY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques.

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Sample preparation

Details
Solution-IDContentsSolvent system
11mM human relaxin-3; 90% H2O, 10% D2O90% H2O/10% D2O
21mM human relaxin-3; 100% D2O100% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
10 3 ambient 298 K
20 3 ambient 303 K
30 3 ambient 293 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE6001
Bruker DMXBrukerDMX7502

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR1.3.5Brukercollection
XwinNMR1.3.5Brukerprocessing
XEASY1.3.7Bartels, C. et al.data analysis
CYANA1Guntert, P. et al.structure solution
CNS1.1Brunger A.T. et al.structure solution
CNS1.1Brunger A.T. et al.refinement
RefinementMethod: Structures were calculated using torsion angle dynamics, further refined using Cartesian dynamics in explicit solvent.
Software ordinal: 1
Details: Structure calculations and refinements were done in CNS using protocols from ARIA.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 20

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