BMRB Entry 18319

Name: 1H, 13C and 15N full assignment of transmembrane domain TM12 from human Y4 receptor
Published: 2012-09-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18319

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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:

1H, 13C and 15N full assignment of transmembrane domain TM12 from human Y4 receptor

Deposition date:

2012-03-09

Original release date:

2012-09-14

Authors:

Shao, Xuan; Zou, Chao; Naider, Fred; Zerbe, Oliver

Citation:

Citation: Shao, Xuan; Zou, Chao; Naider, Fred; Zerbe, Oliver. "Comparison of fragments comprising the first two helices of the human y4 and the yeast ste2p g-protein-coupled receptors." Biophys. J. 103, 817-826 (2012).
PubMed: 22947943

Assembly members:

Assembly members:
Y4_TM1-TM2, polymer, 121 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pLC01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Y4_TM1-TM2: MNTSHLLALLLPKSPQGENR SKPLGTPYNFSEHCQDSVDV MVFIVTSYSIETVVGVLGNL CLMCVTVRQKEKANVTNLLI ANLAFSDFLMCLLCQPLTAV YTIMDYWIFGETLCKHHHHH H

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	479
15N chemical shifts	123
1H chemical shifts	837

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Y4_TM1-TM2	1

Entities:

Entity 1, Y4_TM1-TM2 121 residues - Formula weight is not available

1

MET

ASN

THR

SER

HIS

LEU

ALA

LEU

2

LEU

PRO

LYS

SER

PRO

GLN

GLY

GLU

ASN

ARG

3

SER

LYS

PRO

LEU

GLY

THR

PRO

TYR

ASN

PHE

4

SER

GLU

HIS

CYS

GLN

ASP

SER

VAL

ASP

VAL

5

MET

VAL

PHE

ILE

VAL

THR

SER

TYR

SER

ILE

6

GLU

THR

VAL

GLY

VAL

LEU

GLY

ASN

LEU

7

CYS

LEU

MET

CYS

VAL

THR

VAL

ARG

GLN

LYS

8

GLU

LYS

ALA

ASN

VAL

THR

ASN

LEU

ILE

9

ALA

ASN

LEU

ALA

PHE

SER

ASP

PHE

LEU

MET

10

CYS

LEU

CYS

GLN

PRO

LEU

THR

ALA

VAL

11

TYR

THR

ILE

MET

ASP

TYR

TRP

ILE

PHE

GLY

12

GLU

THR

LEU

CYS

LYS

HIS

13

HIS

Samples:

sample_1: Y4_TM1-TM2, [U-15N], 0.5 mM; H2O 90%; D2O 10%

sample_2: Y4_TM1-TM2, [U-13C; U-15N], 0.5 mM; H2O 90%; D2O 10%

sample_3: Y4_TM1-TM2, [U-13C; U-15N; U-2H], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 40 mM; pH: 6.0; pressure: 1 atm; temperature: 320 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

BMRB	15921
DBJ	BAG74162
EMBL	CAA91433 CAG46748 CAI13318
GB	AAB07759 AAC50280 AAH96238 AAH99637 AAP23199
REF	NP_001265723 NP_001265724 NP_005963 XP_003804406 XP_003804407
SP	P50391
AlphaFold	P50391