BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15921

Title: 1H, 13C and 15N assignment of a double transmembrane domain from human Y4 receptor, a G-protein coupled receptor   PubMed: 18937032

Deposition date: 2008-08-14 Original release date: 2008-08-19

Authors: Zou, Chao; Naider, Fred; Zerbe, Oliver

Citation: Zou, Chao; Naider, Fred; Zerbe, Oliver. "Biosynthesis and NMR-studies of a double transmembrane domain from the Y4 receptor, a human GPCR"  J. Biomol. NMR 42, 257-269 (2008).

Assembly members:
N-TM1-TM2, polymer, 121 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
N-TM1-TM2: MNTSHLLALLLPKSPQGENR SKPLGTPYNFSEHCQDSVDV MVFIVTSYSIETVVGVLGNL CLMCVTVRQKEKANVTNLLI ANLAFSDFLMCLLCQPLTAV YTIMDYWIFGETLCKHHHHH H

Data sets:
Data typeCount
13C chemical shifts315
15N chemical shifts108
1H chemical shifts108

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-TM1-YM21

Entities:

Entity 1, N-TM1-YM2 121 residues - Formula weight is not available

1   METASNTHRSERHISLEULEUALALEULEU
2   LEUPROLYSSERPROGLNGLYGLUASNARG
3   SERLYSPROLEUGLYTHRPROTYRASNPHE
4   SERGLUHISCYSGLNASPSERVALASPVAL
5   METVALPHEILEVALTHRSERTYRSERILE
6   GLUTHRVALVALGLYVALLEUGLYASNLEU
7   CYSLEUMETCYSVALTHRVALARGGLNLYS
8   GLULYSALAASNVALTHRASNLEULEUILE
9   ALAASNLEUALAPHESERASPPHELEUMET
10   CYSLEULEUCYSGLNPROLEUTHRALAVAL
11   TYRTHRILEMETASPTYRTRPILEPHEGLY
12   GLUTHRLEUCYSLYSHISHISHISHISHIS
13   HIS

Samples:

sample_1: N-TM1-TM2, [U-100% 13C; U-100% 15N; 80% 2H], 0.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.0; pressure: 1 atm; temperature: 320 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.0, Bruker - collection

CARA v1.8.4, Rochus Keller - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 18319
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

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