BMRB Entry 4451

Title:
Structure of the CAD Domain of Caspase-activated DNase and Interaction with the CAD Domain of its Inhibitor
Deposition date:
1999-11-04
Original release date:
2000-12-15
Authors:
Uegaki, Koichi; Otomo, Takanori; Sakahira, Hideki; Shimizu, Masato; Yumoto, Noboru; Kyogoku, Yoshimasa; Nagata, Shigekazu; Yamazaki, Toshio
Citation:

Citation: Uegaki, Koichi; Otomo, Takanori; Sakahira, Hideki; Shimizu, Masato; Yumoto, Noboru; Kyogoku, Yoshimasa; Nagata, Shigekazu; Yamazaki, Toshio. "Structure of the CAD Domain of Caspase-activated DNase and Interaction with the CAD Domain of its Inhibitor"  J. Mol. Biol. 297, 1121-1128 (2000).

Assembly members:

Assembly members:
N-terminal domain of caspase activated DNase, polymer, 87 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal domain of caspase activated DNase: MCAVLRQPKCVKLRALHSAC KFGVAARSCQELLRKGCVRF QLPMPGSRLCLYEDGTEVTD DCFPGLPNDAELLLLTAGET WHGYVSD

Data sets:
Data typeCount
1H chemical shifts611
13C chemical shifts379
15N chemical shifts93

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CAD domain1

Entities:

Entity 1, CAD domain 87 residues - Formula weight is not available

1   METCYSALAVALLEUARGGLNPROLYSCYS
2   VALLYSLEUARGALALEUHISSERALACYS
3   LYSPHEGLYVALALAALAARGSERCYSGLN
4   GLULEULEUARGLYSGLYCYSVALARGPHE
5   GLNLEUPROMETPROGLYSERARGLEUCYS
6   LEUTYRGLUASPGLYTHRGLUVALTHRASP
7   ASPCYSPHEPROGLYLEUPROASNASPALA
8   GLULEULEULEULEUTHRALAGLYGLUTHR
9   TRPHISGLYTYRVALSERASP

Samples:

sample_1: N-terminal domain of caspase activated DNase, [U-15N; U-13C], 1.0 mM

Sample_conditions_set_1: pH: 5.6; temperature: 298 K; ionic strength: 0.05 M

Experiments:

NameSampleSample stateSample conditions
1H-15N NOESYnot availablenot availablenot available
1H-15N TOCSYnot availablenot availablenot available
1H-15N HSQCnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available
1H-13C NOESYnot availablenot availablenot available
C(CO)NHnot availablenot availablenot available
HNCOnot availablenot availablenot available

Software:

NMRPipe -

PIPP -

PROCHEK-NMR -

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

PDB
DBJ BAA24977 BAC36905
GB AAH53052 EDL14950
REF NP_031885 XP_006538580 XP_011248488
SP O54788
AlphaFold O54788

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