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 17027

Title: NMR-derived spatial structure of water-soluble Lynx1   PubMed: 21252236

Deposition date: 2010-06-30 Original release date: 2011-04-01

Authors: Mineev, Konstantin; Shenkarev, Zakhar; Arseniev, Alexander

Citation: Lyukmanova, Ekaterina; Shenkarev, Zakhar; Shulepko, Mikhail; Mineev, Konstantin; Kasheverov, Dieter; Filkin, Igor; Krivolapova, Sergey Yu; Janickova, Alexandra; Dolezal, Helena; Dolgikh, Vladimir; Arseniev, Dmitry; Bertrand, Alexander; Tsetlin, Daniel; Kirpichnikov, Victor. "NMR Structure and Action on Nicotinic Acetylcholine Receptors of Water-soluble Domain of Human LYNX1."  J. Biol. Chem. 286, 10618-10627 (2011).

Assembly members:
Lynx1, polymer, 74 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: PET-22b

Entity Sequences (FASTA):
Lynx1: MLDCHVCAYNGDNCFNPMRC PAMVAYCMTTRTYYTPTRMK VSKSCVPRCFETVYDGYSKH ASTTSCCQYDLCNG

Data sets:
Data typeCount
13C chemical shifts40
15N chemical shifts79
1H chemical shifts458

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lynx11

Entities:

Entity 1, Lynx1 74 residues - Formula weight is not available

1   METLEUASPCYSHISVALCYSALATYRASN
2   GLYASPASNCYSPHEASNPROMETARGCYS
3   PROALAMETVALALATYRCYSMETTHRTHR
4   ARGTHRTYRTYRTHRPROTHRARGMETLYS
5   VALSERLYSSERCYSVALPROARGCYSPHE
6   GLUTHRVALTYRASPGLYTYRSERLYSHIS
7   ALASERTHRTHRSERCYSCYSGLNTYRASP
8   LEUCYSASNGLY

Samples:

sample_1: Lynx1, [U-99% 15N], 0.5 mM; acetic acid 20 mM; sodium azide 1 mM; H2O 90%; D2O 10%

sample_2: Lynx1 1.0 mM; acetic acid 20 mM; sodium azide 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 21 mM; pH: 5.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1

Software:

CARA v1.8.3, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAK01642 AAR00319 AAV74279 AAV74324 EAW82301
REF NP_001012437 NP_001028116 NP_001266926 NP_803252 NP_803429
SP Q5IS42 Q5IS87
AlphaFold Q5IS42 Q5IS87

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