BMRB Entry 15313

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15313
MolProbity Validation Chart

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Title:
1H, 15N and 13C backbone and side chain chemical shifts of human ASC (apoptosis-associated speck-like protein containing a CARD domain)
Deposition date:
2007-06-18
Original release date:
2007-08-22
Authors:
de Alba, Eva
Citation:

Citation: de Alba, Eva. "1H, 15N and 13C backbone and side chain chemical shifts of human ASC (apoptosis-associated speck-like protein containing a CARD domain)"  Biomol. NMR Assignments 1, 135-137 (2007).
PubMed: 19636848

Assembly members:

Assembly members:
ASC, polymer, 215 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: PET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ASC: MGSSHHHHHHSSGLVPRGSH MGRARDAILDALENLTAEEL KKFKLKLLSVPLREGYGRIP RGALLSMDALDLTDKLVSFY LETYGAELTANVLRDMGLQE MAGQLQAATHQGSGAAPAGI QAPPQSAAKPGLHFIDQHRA ALIARVTNVEWLLDALYGKV LTDEQYQAVRAEPTNPSKMR KLFSFTPAWNWTCKDLLLQA LRESQSYLVEDLERS

Data sets:
Data typeCount
13C chemical shifts801
15N chemical shifts199
1H chemical shifts1331

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ASC1

Entities:

Entity 1, ASC 215 residues - Formula weight is not available

residues 1-20 contain a His-tag and a thrombin cleavage site. ASC protein starts at M21 which is numbered as M1 in the NMR assignment file

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLYARGALAARGASPALAILELEUASP
4   ALALEUGLUASNLEUTHRALAGLUGLULEU
5   LYSLYSPHELYSLEULYSLEULEUSERVAL
6   PROLEUARGGLUGLYTYRGLYARGILEPRO
7   ARGGLYALALEULEUSERMETASPALALEU
8   ASPLEUTHRASPLYSLEUVALSERPHETYR
9   LEUGLUTHRTYRGLYALAGLULEUTHRALA
10   ASNVALLEUARGASPMETGLYLEUGLNGLU
11   METALAGLYGLNLEUGLNALAALATHRHIS
12   GLNGLYSERGLYALAALAPROALAGLYILE
13   GLNALAPROPROGLNSERALAALALYSPRO
14   GLYLEUHISPHEILEASPGLNHISARGALA
15   ALALEUILEALAARGVALTHRASNVALGLU
16   TRPLEULEUASPALALEUTYRGLYLYSVAL
17   LEUTHRASPGLUGLNTYRGLNALAVALARG
18   ALAGLUPROTHRASNPROSERLYSMETARG
19   LYSLEUPHESERPHETHRPROALATRPASN
20   TRPTHRCYSLYSASPLEULEULEUGLNALA
21   LEUARGGLUSERGLNSERTYRLEUVALGLU
22   ASPLEUGLUARGSER

Samples:

sample_1: ASC, [U-99% 13C; U-99% 15N], 0.2 mM; TCEP, [U-99% 2H], 5 mM

sample_2: ASC, [U-99% 13C; U-99% 15N], 0.2 mM; TCEP, [U-99% 2H], 5 mM

sample_3: ASC, [U-99% 15N], 0.2 mM; TCEP, [U-99% 2H], 5 mM

sample_conditions_1: ionic strength: 0 M; pH: 3.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
4D [1H,13C-1H,13C]-NOESYsample_2isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA87339 BAA91012 BAG37041 BAG73625
GB AAG01187 AAG01188 AAG30286 AAH13569 AAK63850
REF NP_037390 XP_001158687 XP_002826422 XP_003280507 XP_003807544
SP Q9ULZ3
AlphaFold Q9ULZ3

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