BMRB Entry 27601

Name: RXDP2ext(1-73)
Published: 2018-10-09

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27601

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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:

RXDP2ext(1-73)

Deposition date:

2018-09-09

Original release date:

2018-10-09

Authors:

Sethi, Ashish; Gooley, Paul

Citation:

Citation: Hoare, Bradley; Bruell, Shoni; Sethi, Ashish; Gooley, Paul; Lew, Michael; Hossain, Mohammed; Inoue, Asuka; Scott, Daniel; Bathgate, Ross. "Multi-Component Mechanism of H2 Relaxin Binding to RXFP1 through NanoBRET Kinetic Analysis." iScience 11, 93-9113 (2019).
PubMed: 30594862

Assembly members:

Assembly members:
RXFP2ext, polymer, 128 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RXFP2ext: MITFSCQKGYFPCGNLTKCL PRAFHCDGKDDCGNGADEEN CGDTSGWATIFGKYFASYYT VHGNANSVALTQEQYKLALN GKTLKGETTTEAVDAATAEK VFKQYANDNGVDGEWTYDDA TKTFTVTE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	249
15N chemical shifts	125
1H chemical shifts	125

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RXFP2ext	1

Entities:

Entity 1, RXFP2ext 128 residues - Formula weight is not available

1

MET

ILE

THR

PHE

SER

CYS

GLN

LYS

GLY

TYR

2

PHE

PRO

CYS

GLY

ASN

LEU

THR

LYS

CYS

LEU

3

PRO

ARG

ALA

PHE

HIS

CYS

ASP

GLY

LYS

ASP

4

ASP

CYS

GLY

ASN

GLY

ALA

ASP

GLU

ASN

5

CYS

GLY

ASP

THR

SER

GLY

TRP

ALA

THR

ILE

6

PHE

GLY

LYS

TYR

PHE

ALA

SER

TYR

THR

7

VAL

HIS

GLY

ASN

ALA

ASN

SER

VAL

ALA

LEU

8

THR

GLN

GLU

GLN

TYR

LYS

LEU

ALA

LEU

ASN

9

GLY

LYS

THR

LEU

LYS

GLY

GLU

THR

10

GLU

ALA

VAL

ASP

ALA

THR

ALA

GLU

LYS

11

VAL

PHE

LYS

GLN

TYR

ALA

ASN

ASP

ASN

GLY

12

VAL

ASP

GLY

GLU

TRP

THR

TYR

ASP

ALA

13

THR

LYS

THR

PHE

THR

VAL

THR

GLU

Samples:

sample_1: RXFP2ext, [U-100% 13C; U-100% 15N], 65 uM; imidazole 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks