BMRB Entry 51695

Name: Chemical shift assignment of the intracellular domain of the prolactin receptor, residues 236-396
Published: 2023-06-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51695

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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:

Chemical shift assignment of the intracellular domain of the prolactin receptor, residues 236-396

Deposition date:

2022-11-14

Original release date:

2023-06-06

Authors:

Haxholm, Gitte; Seiffert, Pernille; Kragelund, Birthe

Citation:

Citation: Araya-Secchi, Raul; Bugge, Katrine; Seiffert, Pernille; Petry, Amalie; Haxholm, Gitte; Lindorff-Larsen, Kresten; Pedersen, Stine; Arleth, Lise; Kragelund, Birthe. "The prolactin receptor scaffolds Janus kinase 2 via co-structure formation with phosphoinositide-4,5-bisphosphate" eLife 12, e84645-e84645 (2023).
PubMed: 37232489

Assembly members:

Assembly members:
entity_1, polymer, 161 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: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GYSMVTCIFPPVPGPKIKGF DAHLLEKGKSEELLSALGCQ DFPPTSDYEDLLVEYLEVDD SEDQHLMSVHSKEHPSQGMK PTYLDPDTDSGRGSCDSPSL LSEKCEEPQANPSTFYDPEV IEKPENPETTHTWDPQCISM EGKIPYFHAGGSKCSTWPLP Q

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	453
15N chemical shifts	136
1H chemical shifts	136

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PRLR-ICD(236-396)	1

Entities:

Entity 1, PRLR-ICD(236-396) 161 residues - Formula weight is not available

1

GLY

TYR

SER

MET

VAL

THR

CYS

ILE

PHE

PRO

2

PRO

VAL

PRO

GLY

PRO

LYS

ILE

LYS

GLY

PHE

3

ASP

ALA

HIS

LEU

GLU

LYS

GLY

LYS

SER

4

GLU

LEU

SER

ALA

LEU

GLY

CYS

GLN

5

ASP

PHE

PRO

THR

SER

ASP

TYR

GLU

ASP

6

LEU

VAL

GLU

TYR

LEU

GLU

VAL

ASP

7

SER

GLU

ASP

GLN

HIS

LEU

MET

SER

VAL

HIS

8

SER

LYS

GLU

HIS

PRO

SER

GLN

GLY

MET

LYS

9

PRO

THR

TYR

LEU

ASP

PRO

ASP

THR

ASP

SER

10

GLY

ARG

GLY

SER

CYS

ASP

SER

PRO

SER

LEU

11

LEU

SER

GLU

LYS

CYS

GLU

PRO

GLN

ALA

12

ASN

PRO

SER

THR

PHE

TYR

ASP

PRO

GLU

VAL

13

ILE

GLU

LYS

PRO

GLU

ASN

PRO

GLU

THR

14

HIS

THR

TRP

ASP

PRO

GLN

CYS

ILE

SER

MET

15

GLU

GLY

LYS

ILE

PRO

TYR

PHE

HIS

ALA

GLY

16

GLY

SER

LYS

CYS

SER

THR

TRP

PRO

LEU

PRO

17

GLN

Samples:

sample_1: sodium phosphate 20 mM; PRLR-ICD(236-396), [U-100% 13C; U-100% 15N], 650 uM; D2O 10%; TCEP 6.5 mM; DSS 0.5 mM

sample_conditions_1: pH: 7.3; pressure: 1 atm; temperature: 277.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - data analysis

NMR spectrometers:

Varian INOVA 750 MHz

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