BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18622

Title: Solution structure of second CARD of human RIG-I.   PubMed: 23063562

Deposition date: 2012-07-27 Original release date: 2012-10-19

Authors: Dutta, Kaushik; Patel, Jenish

Citation: Ferrage, Fabien; Dutta, Kaushik; Nistal-Villan, Estanislao; Patel, Jenish; Sanchez-Aparicio, Maria; De Ioannes, Pablo; Buku, Angeliki; Aseguinolaza, Gloria Gonzalez; Garcia-Sastre, Adolfo; Aggarwal, Aneel. "Structure and dynamics of the second CARD of human RIG-I provide mechanistic insights into regulation of RIG-I activation."  Structure 20, 2048-2061 (2012).

Assembly members:
second CARD of human RIG-I, polymer, 100 residues, 11369.512 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
second CARD of human RIG-I: GSHMKKIEKLEEYRLLLKRL QPEFKTRIIPTDIISDLSEC LINQECEEILQICSTKGMMA GAEKLVECLLRSDKENWPKT LKLALEKERNKFSELWIVEK

Data sets:
Data typeCount
13C chemical shifts448
15N chemical shifts96
1H chemical shifts671

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1second CARD of human RIG-I1

Entities:

Entity 1, second CARD of human RIG-I 100 residues - 11369.512 Da.

1   GLYSERHISMETLYSLYSILEGLULYSLEU
2   GLUGLUTYRARGLEULEULEULYSARGLEU
3   GLNPROGLUPHELYSTHRARGILEILEPRO
4   THRASPILEILESERASPLEUSERGLUCYS
5   LEUILEASNGLNGLUCYSGLUGLUILELEU
6   GLNILECYSSERTHRLYSGLYMETMETALA
7   GLYALAGLULYSLEUVALGLUCYSLEULEU
8   ARGSERASPLYSGLUASNTRPPROLYSTHR
9   LEULYSLEUALALEUGLULYSGLUARGASN
10   LYSPHESERGLULEUTRPILEVALGLULYS

Samples:

sample_1: card2, [U-100% 15N], 300 uM; H2O 95%; D2O 5%; Bis-Tris 50 mM; sodium chloride 250 mM

sample_2: card2, [U-100% 13C; U-100% 15N], 300 uM; H2O 95%; D2O 5%; Bis-Tris 50 mM; sodium chloride 250 mM

sample_3: card2, [U-100% 13C; U-100% 15N], 300 uM; D2O 100%; Bis-Tris 50 mM; sodium chloride 250 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O, . - chemical shift assignment

NMRView v8.3, Johnson, One Moon Scientific - chemical shift assignment, chemical shift calculation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 18623
PDB
DBJ BAG11006 BAG54273
EMBL CAI46068
GB AAD19826 AAI07732 AAI32787 AAI36611 EAW58547
REF NP_055129 XP_001156662 XP_002819761 XP_003830148 XP_004047964
SP O95786

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts