BMRB Entry 25817

Title:
Structure of the transmembrane domain of human nicastrin in SDS micelles
Deposition date:
2015-09-17
Original release date:
2016-04-25
Authors:
Li, Yan; Liew, Lynette; Li, Qingxin; Kang, CongBao
Citation:

Citation: Li, Yan; Liew, Lynette; Li, Qingxin; Kang, CongBao. "Structure of the transmembrane domain of human nicastrin-a component of -secretase"  Sci. Rep. 6, 19522-19522 (2016).
PubMed: 26776682

Assembly members:

Assembly members:
transmembrane_domain_of_human_nicastrin, polymer, 54 residues, 4960.896 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
transmembrane_domain_of_human_nicastrin: MAHHHHHHASKELELITLTV GFGILIFSLIVTYCINAKAD VLFIAPREPGAVSY

Data sets:
Data typeCount
13C chemical shifts128
15N chemical shifts44
1H chemical shifts262

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1transmembrane_domain_of_human_nicastrin1

Entities:

Entity 1, transmembrane_domain_of_human_nicastrin 54 residues - 4960.896 Da.

1   METALAHISHISHISHISHISHISALASER
2   LYSGLULEUGLULEUILETHRLEUTHRVAL
3   GLYPHEGLYILELEUILEPHESERLEUILE
4   VALTHRTYRCYSILEASNALALYSALAASP
5   VALLEUPHEILEALAPROARGGLUPROGLY
6   ALAVALSERTYR

Samples:

sample_1: transmembrane domain of human nicastrin, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 20 mM; SDS 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, processing, structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

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