BMRB Entry 25806

Name: NMR structure of the prolactin receptor transmembrane domain
Published: 2016-05-23

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PDB ID: 2n7i
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25806
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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:

NMR structure of the prolactin receptor transmembrane domain

Deposition date:

2015-09-11

Original release date:

2016-05-23

Authors:

Bugge, Katrine; Kragelund, Birthe

Citation:

Citation: Bugge, Katrine; Papaleo, Elena; Haxholm, Gitte; Hopper, Jonathan; Dagil, Robert; Robinson, Carol; Olsen, Johan; Lindorff-Larsen, Kresten; Kragelund, Birthe. "A combined computational and structural model of the full-length human prolactin receptor" Nat. Commun. 7, 11578-11578 (2016).
PubMed: 27174498

Assembly members:

Assembly members:
PRLRTMD, polymer, 37 residues, 3960.773 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: pGEX 4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PRLRTMD: GSFTMNDTTVWISVAVLSAV ICLIIVWAVALKGYSMV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	161
15N chemical shifts	37
1H chemical shifts	242

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	prolactin receptor transmembrane domain	1

Entities:

Entity 1, prolactin receptor transmembrane domain 37 residues - 3960.773 Da.

Residues 204-205 represent non-native residues left over from thrombin digestion. This is the transmembrane domain of a receptor

1

GLY

SER

PHE

THR

MET

ASN

ASP

THR

VAL

2

TRP

ILE

SER

VAL

ALA

VAL

LEU

SER

ALA

VAL

3

ILE

CYS

LEU

ILE

VAL

TRP

ALA

VAL

ALA

4

LEU

LYS

GLY

TYR

SER

MET

VAL

Samples:

sample_1: PRLRTMD, [U-13C; U-15N], 0.8 mM; DSS 2 mM; sodium azide 0.05%; DHPC 560 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: PRLRTMD, [U-13C; U-15N], 1 mM; DSS 2 mM; sodium azide 0.05%; DHPC, [U-2H], 700 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample15N: PRLRTMD, [U-15N], 0.7 mM; DSS 2 mM; sodium azide 0.05%; DHPC 490 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNHA	sample15N	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample15N	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1

Software:

ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 750 MHz
Bruker Avance 900 MHz

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