BMRB Entry 19200

Name: RXFP1 utilises hydrophobic moieties on a signalling surface of the LDLa module to mediate receptor activation
Published: 2013-08-12

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PDB ID: 2m7p
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19200
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

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:

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).
PubMed: 23926099

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEV-LB2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSQDVTCSLGYFPCGNITKC IPQFWRCDGQVDCDNGSDEQ GC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	111
15N chemical shifts	42
1H chemical shifts	235

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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