BMRB Entry 30137

Title:
Structure of the C-terminal transmembrane domain of scavenger receptor BI (SR-BI)
Deposition date:
2016-07-11
Original release date:
2017-03-02
Authors:
Chadwick, A.; Peterson, F.; Volkman, B.; Sahoo, D.
Citation:

Citation: Chadwick, Alexandra; Jensen, Davin; Hanson, Paul; Lange, Philip; Proudfoot, Sarah; Peterson, Francis; Volkman, Brian; Sahoo, Daisy. "NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif"  Structure 25, 446-457 (2017).
PubMed: 28162952

Assembly members:

Assembly members:
entity_1, polymer, 73 residues, 8185.792 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE30-SMT

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts68
1H chemical shifts496

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 73 residues - 8185.792 Da.

1   GLYSERLYSILEGLUPROVALVALLEUPRO
2   LEULEUTRPPHEGLUGLNSERGLYALAMET
3   GLYGLYLYSPROLEUSERTHRPHETYRTHR
4   GLNLEUVALLEUMETPROGLNVALLEUHIS
5   TYRALAGLNTYRVALLEULEUGLYLEUGLY
6   GLYLEULEULEULEUVALPROILEILECYS
7   GLNLEUARGSERGLNGLULYSCYSPHELEU
8   PHETRPSER

Samples:

sample_1: LPPG, [U-2H], 5.0 w/v; scavenger receptor BI (SR-BI), [U-99% 13C; U-99% 15N], 1 mM; sodium azide 0.02 w/v

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1anisotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization

XEASY, Bartels et al. - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceIII 500 MHz
  • Bruker Avance 600 MHz

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