BMRB Entry 19951

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19951

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Resonance assignments and secondary structure of apolipoprotein E C-terminal domain in complex with DHPC
Deposition date:
2014-05-02
Original release date:
2015-05-05
Authors:
Lo, Chi-Jen; Chen, Yi-Chen; Chang, Chi-Fon; Shiao, Ming-Shi; Huang, Hsien-bin; Lin, Ta-Hsien
Citation:

Citation: Lo, Chi-Jen; Chyan, Chia-Lin; Chen, Yi-Chen; Chang, Chi-Fon; Huang, Hsien-bin; Lin, Ta-Hsien. "Resonance assignments and secondary structure of apolipoprotein E C-terminal domain in DHPC micelles"  Biomol. NMR Assign. 9, 187-190 (2015).

Assembly members:

Assembly members:
apoE(195-299), polymer, 108 residues, Formula weight is not available

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: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
apoE(195-299): GSMVGSLAGQPLQERAQAWG ERLRARMEEMGSRTRDRLDE VKEQVAEVRAKLEEQAQQIR LQAEAFQARLKSWFEPLVED MQRQWAGLVEKVQAAVGTSA APVPSDNH

Data sets:
Data typeCount
13C chemical shifts306
15N chemical shifts94
1H chemical shifts212

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1apoE(195-299)1

Entities:

Entity 1, apoE(195-299) 108 residues - Formula weight is not available

1   GLYSERMETVALGLYSERLEUALAGLYGLN
2   PROLEUGLNGLUARGALAGLNALATRPGLY
3   GLUARGLEUARGALAARGMETGLUGLUMET
4   GLYSERARGTHRARGASPARGLEUASPGLU
5   VALLYSGLUGLNVALALAGLUVALARGALA
6   LYSLEUGLUGLUGLNALAGLNGLNILEARG
7   LEUGLNALAGLUALAPHEGLNALAARGLEU
8   LYSSERTRPPHEGLUPROLEUVALGLUASP
9   METGLNARGGLNTRPALAGLYLEUVALGLU
10   LYSVALGLNALAALAVALGLYTHRSERALA
11   ALAPROVALPROSERASPASNHIS

Samples:

sample_1: apoE(195-299), [U-13C; U-15N; U-2H], 1 mM; potassium phosphate 50 mM; sodium azide 0.02 mM; TSP, [U-2H], 0.02 mM; EDTA 0.5 mM; dihexanoyl phosphatidylcholine (DHPC) micelles mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HBHA(CBCA)NHsample_1isotropicsample_conditions_1
3D H(CCCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

AURELIA v3.6, Neidig, Geyer, Gorler, Antz, Saffrich, Beneicke, Kalbitzer - chemical shift assignment

TOPSPIN v3.1, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

DBJ BAG37412 BAG72927
GB AAB59397 AAB59518 AAB59546 AAD02505 AAG27089
PRF 1506383A
REF NP_000032 NP_001289617 NP_001289618 NP_001289619 NP_001289620
SP P02649
AlphaFold P02649

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