BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34294

Title: Solution structure of rat RIP2 caspase recruitment domain   PubMed: 30352081

Deposition date: 2018-06-25 Original release date: 2018-10-29

Authors: Mineev, K.; Goncharuk, S.; Artemieva, L.; Arseniev, A.

Citation: Goncharuk, S.; Artemieva, L.; Tabakmakher, V.; Arseniev, A.; Mineev, K.. "CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactions."  PLoS ONE 13, e0206244-e0206244 (2018).

Assembly members:
entity_1, polymer, 125 residues, 14075.079 Da.

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: MHHHHHHGSGSGLVPRGSGI AQQWIQSKREAIVSQMTEAC LNQSLDALLSRDLIMKEDYE LISTKPTRTAKVRQLLDTSD IQGEEFARVIVQKLKDNKQM GLQPYPEVLLVSRTPSSNVL QNKTL

Data sets:
Data typeCount
13C chemical shifts530
15N chemical shifts131
1H chemical shifts881

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 125 residues - 14075.079 Da.

1   METHISHISHISHISHISHISGLYSERGLY
2   SERGLYLEUVALPROARGGLYSERGLYILE
3   ALAGLNGLNTRPILEGLNSERLYSARGGLU
4   ALAILEVALSERGLNMETTHRGLUALACYS
5   LEUASNGLNSERLEUASPALALEULEUSER
6   ARGASPLEUILEMETLYSGLUASPTYRGLU
7   LEUILESERTHRLYSPROTHRARGTHRALA
8   LYSVALARGGLNLEULEUASPTHRSERASP
9   ILEGLNGLYGLUGLUPHEALAARGVALILE
10   VALGLNLYSLEULYSASPASNLYSGLNMET
11   GLYLEUGLNPROTYRPROGLUVALLEULEU
12   VALSERARGTHRPROSERSERASNVALLEU
13   GLNASNLYSTHRLEU

Samples:

sample_1: CARD domain of rat RIP2, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; TCEP 1 mM; sodium azide 0.001%

sample_conditions_1: ionic strength: 0 mM; pH: 4.2; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

CYANA v3.97, Guntert P. - structure calculation

CARA v1.9.4, Keller and Wuthrich - chemical shift assignment

TOPSPIN v3.2, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AvanceIII 800 MHz

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