BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19200

Title: RXFP1 utilises hydrophobic moieties on a signalling surface of the LDLa module to mediate receptor activation   PubMed: 23926099

Deposition date: 2013-04-29 Original release date: 2013-08-12

Authors: Kong, Roy; Petrie, Emma; Mohanty, Biswaranjan; Ling, Jason; Lee, Jeremy; Gooley, Paul; Bathgate, Ross

Citation: Kong, Roy; Petrie, Emma; Mohanty, Biswaranjan; Ling, Jason; Lee, Jeremy; Gooley, Paul; Bathgate, Ross. "The Relaxin Receptor (RXFP1) Utilizes Hydrophobic Moieties on a Signaling Surface of Its N-terminal Low Density Lipoprotein Class A Module to Mediate Receptor Activation."  J. Biol. Chem. 288, 28138-28151 (2013).

Assembly members:
entity, polymer, 42 residues, 4531.963 Da.
ARISTOLOCHENE, non-polymer, 204.351 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: GSQDVTCSLGYFPCGNITKC IPQFWRCDGQVDCDNGSDEQ GC

Data sets:
Data typeCount
13C chemical shifts111
15N chemical shifts42
1H chemical shifts235

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1LDLa1
2ARISTOLOCHENE2

Entities:

Entity 1, LDLa 42 residues - 4531.963 Da.

1   GLYSERGLNASPVALTHRCYSSERLEUGLY
2   TYRPHEPROCYSGLYASNILETHRLYSCYS
3   ILEPROGLNPHETRPARGCYSASPGLYGLN
4   VALASPCYSASPASNGLYSERASPGLUGLN
5   GLYCYS

Entity 2, ARISTOLOCHENE - C15 H24 - 204.351 Da.

1   ION

Samples:

sample_1: LDLA, [U-98% 13C; U-98% 15N], 1 mM; Immidazole 50 mM; CaCl2 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.01 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
3D [1H,1H]-NOESY-15N-HSQCsample_1isotropicsample_conditions_1
3D [1H,1H]-NOESY-13C(ali)-HSQCsample_1isotropicsample_conditions_1
3D [1H,1H]-NOESY-13C(aro)-HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, G ntert P. - refinement

CARA, Keller and Wuthrich - chemical shift assignment

UNIO v2.0.2, Dr. Torsten Herrmann - chemical shift assignment, peak picking, structure solution

TOPSPIN v3.0, BRUKER - collection, processing

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance II 800 MHz

Related Database Links:

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