BMRB Entry 50151

Title:
Partial backbone resonance assignments for Human DND1-RRM2
Deposition date:
2020-01-07
Original release date:
2021-08-12
Authors:
Kumari, Pooja
Citation:

Citation: Kumari, Pooja; Bhavesh, Neel Sarovar. "Human DND1-RRM2 forms a non-canonical domain swapped dimer"  Protein Sci. 30, 1184-1195 (2021).
PubMed: 33860980

Assembly members:

Assembly members:
DND1-RRM2, polymer, 100 residues, 10553.19 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: pet28a

Data sets:
Data typeCount
13C chemical shifts190
15N chemical shifts67
1H chemical shifts67

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DND1-RRM21

Entities:

Entity 1, DND1-RRM2 100 residues - 10553.19 Da.

Residue 1-21 belongs to hexa-histidine tag

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLULEUSERVALASPGLYLEUPROPRO
4   ASNLEUTHRARGSERALALEULEULEUALA
5   LEUGLNPROLEUGLYPROGLYLEUGLNGLU
6   ALAARGLEULEUPROSERPROGLYPROALA
7   PROGLYGLNILEALALEULEULYSPHESER
8   SERHISARGALAALAALAMETALALYSLYS
9   ALALEUVALGLUGLYGLNSERHISLEUCYS
10   GLYGLUGLNVALALAVALGLUTRPLEULYS

Samples:

sample_1_RRM2: DND1-RRM2, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 25 mM; sodium chloride 100 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1_RRM2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1_RRM2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1_RRM2isotropicsample_conditions_1
3D HNCOsample_1_RRM2isotropicsample_conditions_1
3D HNCACBsample_1_RRM2isotropicsample_conditions_1
3D HNCAsample_1_RRM2isotropicsample_conditions_1

Software:

TOPSPIN v3.6.0, Bruker Biospin - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PIR Q8IYX4

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