BMRB Entry 26721

Name: RXFP1-LDLa linker
Published: 2016-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26721

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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-LDLa linker

Deposition date:

2015-12-13

Original release date:

2016-02-12

Authors:

Sethi, Ashish; Gooley, Paul

Citation:

Citation: Tailhades, J.; Sethi, Ashish; Petrie, Emma; Gooley, Paul; Bathgate, Ross; Wade, R.; Hossain, Mohammed. "Native Chemical Ligation to Minimize Aspartimide Formation during Chemical Synthesis of Small LDLa Protein" Chemistry 22, 1146-1151 (2016).
PubMed: 26612092

Assembly members:

Assembly members:
RXFP1(1-72), polymer, 72 residues, 8128.9 Da.
entity_CA, non-polymer, 40.078 Da.

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: pGEV2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RXFP1(1-72): QDVKCSLGYFPCGNITKCLP QLLHCNGVDDCGNQADEDNC GDNNGWSLQFDKYFASYYKM TSQYPFEAETPE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	198
15N chemical shifts	66
1H chemical shifts	132

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RXFP1(1-72)	1
2	Calcium	2

Entities:

Entity 1, RXFP1(1-72) 72 residues - 8128.9 Da.

1

GLN

ASP

VAL

LYS

CYS

SER

LEU

GLY

TYR

PHE

2

PRO

CYS

GLY

ASN

ILE

THR

LYS

CYS

LEU

PRO

3

GLN

LEU

HIS

CYS

ASN

GLY

VAL

ASP

4

CYS

GLY

ASN

GLN

ALA

ASP

GLU

ASP

ASN

CYS

5

GLY

ASP

ASN

GLY

TRP

SER

LEU

GLN

PHE

6

ASP

LYS

TYR

PHE

ALA

SER

TYR

LYS

MET

7

THR

SER

GLN

TYR

PRO

PHE

GLU

ALA

GLU

THR

8

PRO

GLU

Entity 2, Calcium - Ca - 40.078 Da.

1

CA

Samples:

sample_1: RXFP1(1-72), [U-100% 13C; U-100% 15N; U-80% 2H], 100 uM; calcium 10 mM; imidazole 50 mM

sample_2: RXFP1(1-72), [U-100% 13C; U-100% 15N], 100 uM; calcium 10 mM; imidazole 50 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNHA	sample_2	isotropic	sample_conditions_2

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 700 MHz

UNP	Q9HBX9
AlphaFold	Q3KU26