BMRB Entry 6843

Name: Solution structure of the NOD1 Caspase Activating and Recruitment Domain
Published: 2007-11-14

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PDB ID: 2b1w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6843
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
Caspase recruitment domain protein 4: GAMESHPHIQLLKSNRELLV THIRNTQCLVDNLLKNDYFS AEDAEIVCACPTQPDKVRKI LDLVQSKGEEVSEFFLYLLQ QLADAYVDLRPWLLEIGFSP SLLTQSKVVVNTDPVSRYTQ QLRHHLG

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	419
15N chemical shifts	97
1H chemical shifts	654

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Caspase recruitment domain protein 4	1

Entities:

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

1

GLY

ALA

MET

GLU

SER

HIS

PRO

HIS

ILE

GLN

2

LEU

LYS

SER

ASN

ARG

GLU

LEU

VAL

3

THR

HIS

ILE

ARG

ASN

THR

GLN

CYS

LEU

VAL

4

ASP

ASN

LEU

LYS

ASN

ASP

TYR

PHE

SER

5

ALA

GLU

ASP

ALA

GLU

ILE

VAL

CYS

ALA

CYS

6

PRO

THR

GLN

PRO

ASP

LYS

VAL

ARG

LYS

ILE

7

LEU

ASP

LEU

VAL

GLN

SER

LYS

GLY

GLU

8

VAL

SER

GLU

PHE

LEU

TYR

LEU

GLN

9

GLN

LEU

ALA

ASP

ALA

TYR

VAL

ASP

LEU

ARG

10

PRO

TRP

LEU

GLU

ILE

GLY

PHE

SER

PRO

11

SER

LEU

THR

GLN

SER

LYS

VAL

12

ASN

THR

ASP

PRO

VAL

SER

ARG

TYR

THR

GLN

13

GLN

LEU

ARG

HIS

LEU

GLY

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:

Name	Sample	Sample state	Sample conditions
HNCO	not available	not available	not available
HNCA	not available	not available	not available
HNCACB	not available	not available	not available
CBCA(CO)NH	not available	not available	not available
HN(CA)CO	not available	not available	not available
H(C)CH-TOCSY3D 13C-separated NOESY	not available	not available	not available
3D_15N-separated NOESY	not available	not available	not available
3D methyl selected NOESY-HSQC	not available	not available	not 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

PDB	2B1W 2DBD 2NSN 2NZ7 4E9M 4JQW
DBJ	BAG51242 BAG62105
GB	AAD28350 AAD29125 AAD43922 AAH40339 AAS46897
REF	NP_006083 XP_001165528 XP_002818131 XP_003270528 XP_003833425
SP	Q9Y239
AlphaFold	Q9Y239