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Biological Magnetic Resonance Data Bank


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BMRB Entry 16672

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16672
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Title: NMR structures of TM domain of the n-Acetylcholine receptor b2 subunit   PubMed: 20441771

Deposition date: 2010-01-12 Original release date: 2010-05-18

Authors: Bondarenko, Vasyl; Tillman, Tommy; Xu, Yan; Tang, Pei

Citation: Bondarenko, Vasyl; Tillman, Tommy; Xu, Yan; Tang, Pei. "NMR structure of the transmembrane domain of the n-acetylcholine receptor beta2 subunit."  Biochim. Biophys. Acta 1798, 1608-1614 (2010).

Assembly members:
transmembrane domain of the n-acetylcholine receptor beta2 subunit, polymer, 164 residues, 18456.0 Da.

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

Entity Sequences (FASTA):
transmembrane domain of the n-acetylcholine receptor beta2 subunit: MHHHHHHSTSVDLGTENLYF QSNARRKPLFYTINLIIPCV LITSLAILVFYLPSDCGEKM TLCISVLLALTVFLLLISKI VPPTSLDVPLVGKYLMFTMV LVTFSIVTSVCVLNVHHRSP TTHTPRGGGGYVAMVIDRLF LWIFVFVCVFGTIGMFLQPL FQNY

Data sets:
Data typeCount
13C chemical shifts458
15N chemical shifts134
1H chemical shifts966

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 164 residues - 18456.0 Da.

1   METHISHISHISHISHISHISSERTHRSER
2   VALASPLEUGLYTHRGLUASNLEUTYRPHE
3   GLNSERASNALAARGARGLYSPROLEUPHE
4   TYRTHRILEASNLEUILEILEPROCYSVAL
5   LEUILETHRSERLEUALAILELEUVALPHE
6   TYRLEUPROSERASPCYSGLYGLULYSMET
7   THRLEUCYSILESERVALLEULEUALALEU
8   THRVALPHELEULEULEUILESERLYSILE
9   VALPROPROTHRSERLEUASPVALPROLEU
10   VALGLYLYSTYRLEUMETPHETHRMETVAL
11   LEUVALTHRPHESERILEVALTHRSERVAL
12   CYSVALLEUASNVALHISHISARGSERPRO
13   THRTHRHISTHRPROARGGLYGLYGLYGLY
14   TYRVALALAMETVALILEASPARGLEUPHE
15   LEUTRPILEPHEVALPHEVALCYSVALPHE
16   GLYTHRILEGLYMETPHELEUGLNPROLEU
17   PHEGLNASNTYR

Samples:

sample_1: TM123, [U-100% 13C; U-100% 15N], 0.2 mM; HFIP 50%; H2O 50%

sample_2: TM1234, [U-100% 13C; U-100% 15N], 0.2 mM; HFIP 50%; H2O 50%

sample_conditions_1: pH: 3.8; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAB53256
GB AAM34453 ELK02820 ELK27604 KFQ65111
REF XP_005628186 XP_005628187 XP_006767267 XP_007662125 XP_007885008

Download simulated HSQC data in one of the following formats:
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