BMRB Entry 25710

Title:
Structure of high-density lipoprotein particles
Deposition date:
2015-07-15
Original release date:
2016-12-15
Authors:
Bibow, Stefan; Polyhach, Yevhen; Eichmann, Cedric; Chi, Celestine; Kowal, Julia; Stahlberg, Henning; Jeschke, Gunnar; Guentert, Peter; Riek, Roland
Citation:

Citation: Bibow, Stefan; Polyhach, Yevhen; Eichmann, Cedric; Chi, Celestine; Kowal, Julia; Albiez, Stefan; McLeod, Robert; Stahlberg, Henning; Jeschke, Gunnar; Guntert, Peter; Riek, Roland. "Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I"  Nat. Struct. Mol. Biol. 24, 187-193 (2017).
PubMed: 28024148

Assembly members:

Assembly members:
entity, polymer, 167 residues, 19462.148 Da.

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: pet28a

Data sets:
Data typeCount
13C chemical shifts391
15N chemical shifts149
1H chemical shifts149

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 167 residues - 19462.148 Da.

1   SERTHRPHESERLYSLEUARGGLUGLNLEU
2   GLYPROVALTHRGLNGLUPHETRPASPASN
3   LEUGLULYSGLUTHRGLUGLYLEUARGGLN
4   GLUMETSERLYSASPLEUGLUGLUVALLYS
5   ALALYSVALGLNPROTYRLEUASPASPPHE
6   GLNLYSLYSTRPGLNGLUGLUMETGLULEU
7   TYRARGGLNLYSVALGLUPROLEUGLYGLU
8   GLUMETARGASPARGALAARGALAHISVAL
9   ASPALALEUARGTHRHISLEUALAPROTYR
10   SERASPGLULEUARGGLNARGLEUALAALA
11   ARGLEUGLUALALEULYSGLUASNGLYGLY
12   ALAARGLEUALAGLUTYRHISALALYSALA
13   THRGLUHISLEUSERTHRLEUSERGLULYS
14   ALALYSPROALALEUGLUASPLEUARGGLN
15   GLYLEULEUPROVALLEUGLUSERPHELYS
16   VALSERPHELEUSERALALEUGLUGLUTYR
17   THRLYSLYSLEUASNTHRGLN

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.75 mM; entity, stereospecific Methyl-labeling, 1 mM; entity, selective unlabeling, 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 316 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

Cyana, Guntert, Braun and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 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