BMRB Entry 30492

Name: NMR solution structure of the CARD9 CARD
Published: 2018-09-10

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PDB ID: 6e26
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30492
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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:

NMR solution structure of the CARD9 CARD

Deposition date:

2018-07-10

Original release date:

2018-09-10

Authors:

Holliday, M.; Dueber, E.; Fairbrother, W.

Citation:

Citation: Holliday, Michael; Ferrao, Ryan; de Leon Boenig, Gladys; Estevez, Alberto; Helgason, Elizabeth; Rohou, Alexis; Dueber, Erin; Fairbrother, Wayne. "Picomolar zinc binding modulates formation of Bcl10-nucleating assemblies of the caspase recruitment domain (CARD) of CARD9." J. Biol. Chem. 293, 16803-16817 (2018).
PubMed: 30206119

Assembly members:

Assembly members:
entity_1, polymer, 97 residues, 11264.877 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSDYENDDECWSVLEGFRVT LTSVIDPSRITPYLRQCKVL NPDDEEQVLSDPNLVIRKRK VGVLLDILQRTGHKGYVAFL ESLELYYPQLYKKVTGK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	449
15N chemical shifts	96
1H chemical shifts	714

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 97 residues - 11264.877 Da.

1

MET

SER

ASP

TYR

GLU

ASN

ASP

GLU

CYS

2

TRP

SER

VAL

LEU

GLU

GLY

PHE

ARG

VAL

THR

3

LEU

THR

SER

VAL

ILE

ASP

PRO

SER

ARG

ILE

4

THR

PRO

TYR

LEU

ARG

GLN

CYS

LYS

VAL

LEU

5

ASN

PRO

ASP

GLU

GLN

VAL

LEU

SER

6

ASP

PRO

ASN

LEU

VAL

ILE

ARG

LYS

ARG

LYS

7

VAL

GLY

VAL

LEU

ASP

ILE

LEU

GLN

ARG

8

THR

GLY

HIS

LYS

GLY

TYR

VAL

ALA

PHE

LEU

9

GLU

SER

LEU

GLU

LEU

TYR

PRO

GLN

LEU

10

TYR

LYS

VAL

THR

GLY

LYS

Samples:

sample_1: CARD9 CARD, [U-13C; U-15N], 0.40 mM

sample_2: CARD9 CARD, [U-13C; U-15N], 0.4 mM

sample_conditions_1: ionic strength: 350 mM; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger A. T. et.al. - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AvanceIII 800 MHz

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