BMRB Entry 6843

Title:
Solution structure of the NOD1 Caspase Activating and Recruitment Domain
Deposition date:
2005-10-03
Original release date:
2007-11-14
Authors:
Manon, F.; Favier, A.; Simorre, J.; Cusack, S.
Citation:

Citation: Manon, F.; Favier, A.; Nunez, G.; Simorre, J.; Cusack, S.. "Solution Structure of NOD1 CARD and Mutational Analysis of its Interaction with the CARD of Downstream Kinase RICK"  J. Mol. Biol. 365, 160-174 (2007).
PubMed: 17054981

Assembly members:

Assembly members:
Caspase recruitment domain protein 4, polymer, 127 residues, 14502 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   Vector: pET-M11

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts97
1H chemical shifts654

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Caspase recruitment domain protein 41

Entities:

Entity 1, Caspase recruitment domain protein 4 127 residues - 14502 Da.

1   GLYALAMETGLUSERHISPROHISILEGLN
2   LEULEULYSSERASNARGGLULEULEUVAL
3   THRHISILEARGASNTHRGLNCYSLEUVAL
4   ASPASNLEULEULYSASNASPTYRPHESER
5   ALAGLUASPALAGLUILEVALCYSALACYS
6   PROTHRGLNPROASPLYSVALARGLYSILE
7   LEUASPLEUVALGLNSERLYSGLYGLUGLU
8   VALSERGLUPHEPHELEUTYRLEULEUGLN
9   GLNLEUALAASPALATYRVALASPLEUARG
10   PROTRPLEULEUGLUILEGLYPHESERPRO
11   SERLEULEUTHRGLNSERLYSVALVALVAL
12   ASNTHRASPPROVALSERARGTYRTHRGLN
13   GLNLEUARGHISHISLEUGLY

Samples:

sample_1: Caspase recruitment domain protein 4, [U-95% 13C; U-90% 15N], 1.4 mM; phosphate buffer 25 mM; NaCl 100 mM; DTT 5 mM; H2O 95%; D2O 5%

sample_2: Caspase recruitment domain protein 4, [U-90% 15N], 1.4 mM; phosphate buffer 25 mM; NaCl 100 mM; DTT 5 mM; H2O 95%; D2O 5%

sample_cond_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
HNCOnot availablenot availablenot available
HNCAnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
HN(CA)COnot availablenot availablenot available
H(C)CH-TOCSY3D 13C-separated NOESYnot availablenot availablenot available
3D_15N-separated NOESYnot availablenot availablenot available
3D methyl selected NOESY-HSQCnot availablenot availablenot available

Software:

NMRPipe v2.3 - processing

VNMR v6.1C - collection

CNS v1.1 - structure solution

ARIA v2.0 - refinement, structure solution

NMRDraw v2.3 - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAG51242 BAG62105
GB AAD28350 AAD29125 AAD43922 AAH40339 AAS46897
REF NP_006083 XP_001165528 XP_002818131 XP_003270528 XP_003833425
SP Q9Y239
AlphaFold Q9Y239

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