BMRB Entry 19732

Title:
The solution NMR structure of the NLRC5 caspase recruitment domain (CARD)
Deposition date:
2014-01-12
Original release date:
2014-05-13
Authors:
Gutte, Petrus; Zerbe, Oliver
Citation:

Citation: Gutte, Petrus; Jurt, Simon; Gruetter, Markus; Zerbe, Oliver. "The solution NMR structure of the NLRC5 caspase recruitment domain (CARD) reveals unusual structural features"  Biochemistry 53, 3106-3117.

Assembly members:

Assembly members:
entity, polymer, 101 residues, 11669.501 Da.

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6p-1

Data sets:
Data typeCount
13C chemical shifts429
15N chemical shifts99
1H chemical shifts674

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NLRC5_CARD1

Entities:

Entity 1, NLRC5_CARD 101 residues - 11669.501 Da.

1   GLYPROLEUGLYSERMETASPALAGLUSER
2   ILEARGLEUASNASNGLUASNLEUTRPALA
3   TRPLEUVALARGLEULEUSERLYSASNPRO
4   GLUTRPLEUSERALALYSLEUARGSERPHE
5   LEUPROTHRMETASPLEUASPCYSSERTYR
6   GLUPROSERASNPROGLUVALILEHISARG
7   GLNLEUASNARGLEUPHEALAGLNGLYMET
8   ALATHRTRPLYSSERPHEILEASNASPLEU
9   CYSPHEGLULEUASPVALPROLEUASPMET
10   GLUILEPROLEUVALSERILETRPGLYPRO
11   ARG

Samples:

sample_1: NLRC5_CARD, [U-100% 13C; U-100% 15N], 600 uM; MES 20 mM; sodium chloride 100 mM; potassium chloride 50 mM; TCEP 2 mM; H2O 95%; D2O, [U-100% 2H], 5%

sample_conditions_1: ionic strength: 0 M; pH: 6.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
HB(CBCGCD)HDsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - processing

CARA v1.8.6, Keller and Wuthrich - data analysis

UNIO v10, Torsten Herrmann - peak picking, structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CHARMM, B. R. Brooks, C. L. Brooks III, D. M. York, and M. Karplus - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

UNP C3VPR6
PDB
GB ACP40992
REF NP_001028379 XP_006531225 XP_006531226 XP_006531227 XP_006531228
SP C3VPR6
AlphaFold Q571H9 C3VPR6

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