BMRB Entry 18319

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

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts123
1H chemical shifts837

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Y4_TM1-TM21

Entities:

Entity 1, Y4_TM1-TM2 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: 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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

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

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