BMRB Entry 19200
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19200
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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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 111 |
| 15N chemical shifts | 42 |
| 1H chemical shifts | 235 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LDLa | 1 |
| 2 | ARISTOLOCHENE | 2 |
Entities:
Entity 1, LDLa 42 residues - 4531.963 Da.
| 1 | GLY | SER | GLN | ASP | VAL | THR | CYS | SER | LEU | GLY | ||||
| 2 | TYR | PHE | PRO | CYS | GLY | ASN | ILE | THR | LYS | CYS | ||||
| 3 | ILE | PRO | GLN | PHE | TRP | ARG | CYS | ASP | GLY | GLN | ||||
| 4 | VAL | ASP | CYS | ASP | ASN | GLY | SER | ASP | GLU | GLN | ||||
| 5 | GLY | CYS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 3D [1H,1H]-NOESY-15N-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D [1H,1H]-NOESY-13C(ali)-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D [1H,1H]-NOESY-13C(aro)-HSQC | sample_1 | isotropic | sample_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:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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