BMRB Entry 5534

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5534

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Title:
Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipase
Deposition date:
2002-09-18
Original release date:
2003-03-14
Authors:
Zdunek, Janusz; Martinez, Gary; Schleucher, Jurgen; Lycksell, Per-Olof; Yin, Yinliang; Nilsson, Solveig; Shen, Yan; Olivecrona, Gunilla; Wijmenga, Sybren
Citation:

Citation: Zdunek, Janusz; Martinez, Gary; Schleucher, Jurgen; Lycksell, Per-Olof; Yin, Yinliang; Nilsson, Solveig; Shen, Yan; Olivecrona, Gunilla; Wijmenga, Sybren. "Global Structure and Dynamics of Human Apolipoprotein CII in Complex with Micelles: Evidence for Increased Mobility of the Helix involved in the Activation of Lipoprotein Lipase"  Biochemistry 42, 1872-1889 (2003).
PubMed: 12590574

Assembly members:

Assembly members:
Apolipoprotein CII, polymer, 79 residues, 8204 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Apolipoprotein CII: TQQPQQDEMPSPTFLTQVKE SLSSYWESAKTAAQNLYEKT YLPAVDEKLRDLYSKSTAAM STYTGIFTDQVLSVLKGEE

Data sets:
Data typeCount
1H chemical shifts138
13C chemical shifts134
15N chemical shifts68

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ApoCII1

Entities:

Entity 1, ApoCII 79 residues - 8204 Da.

1   THRGLNGLNPROGLNGLNASPGLUMETPRO
2   SERPROTHRPHELEUTHRGLNVALLYSGLU
3   SERLEUSERSERTYRTRPGLUSERALALYS
4   THRALAALAGLNASNLEUTYRGLULYSTHR
5   TYRLEUPROALAVALASPGLULYSLEUARG
6   ASPLEUTYRSERLYSSERTHRALAALAMET
7   SERTHRTYRTHRGLYILEPHETHRASPGLN
8   VALLEUSERVALLEULYSGLYGLUGLU

Samples:

sample_1: Apolipoprotein CII, [U-13C; U-15N], 0.5 mM; SDS, [U-2H], 380 mM

condition_1: pH: 4.5; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
CBCANHsample_1not availablecondition_1
CBCA(CO)NHsample_1not availablecondition_1
CBCACO(N)Hsample_1not availablecondition_1
HNCOsample_1not availablecondition_1
spin-lock HCANHsample_1not availablecondition_1
HCC(CO)NHsample_1not availablecondition_1
1H-15N NOESY-HSQCsample_1not availablecondition_1
2D NOESYsample_1not availablecondition_1
1H-15N HNHAsample_1not availablecondition_1
15N T1sample_1not availablecondition_1
15N T2sample_1not availablecondition_1
15N-{1H} NOEsample_1not availablecondition_1

Software:

XWIN-NMR - acquisition, processing

XEASY - assignment

SYBYL - integration of relaxation data

PINATA - analysis of relaxation data

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 400 MHz
  • Bruker AMXII 500 MHz

Related Database Links:

BMRB 6143
PDB
EMBL CAA25234 CAA28798
GB AAA51743 AAA98743 AAB21042 AAB59380 AAH05348
PRF 1303321A
REF NP_000474 NP_001230828 XP_008969010
SP P02655
AlphaFold P02655

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