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 25582

Title: structure of a protein   PubMed: 26195789

Authors: heddi, brahim; Cheong, Vee Vee; Martadinata, Herry; Phan, Anh Tuan

Citation: Heddi, Brahim; Cheong, Vee Vee; Martadinata, Herry; Phan, Anh Tuan. "Insights into G-quadruplex specific recognition by the DEAH-box helicase RHAU: Solution structure of a peptide-quadruplex complex"  Proc. Natl. Acad. Sci. U.S.A. 112, 9608-9613 (2015).

Assembly members:
entity_1, polymer, 20 residues, 2360.817 Da.
DNA, polymer, 18 residues, 5730.718 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
entity_1: SMHPGHLKGREIGMWYAKKQ
DNA: TTGGGTGGGTGGGTGGGT

Data sets:
Data typeCount
13C chemical shifts76
15N chemical shifts14
1H chemical shifts119

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2DNA (5'-D(*TP*TP*GP*GP*GP*TP*GP*GP*GP*TP*GP*GP*GP*TP*GP*GP*GP*T)-3')2

Entities:

Entity 1, entity_1 20 residues - 2360.817 Da.

1   SERMETHISPROGLYHISLEULYSGLYARG
2   GLUILEGLYMETTRPTYRALALYSLYSGLN

Entity 2, DNA (5'-D(*TP*TP*GP*GP*GP*TP*GP*GP*GP*TP*GP*GP*GP*TP*GP*GP*GP*T)-3') 18 residues - 5730.718 Da.

1   DTDTDGDGDGDTDGDGDGDT
2   DGDGDGDTDGDGDGDT

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.1 – 1 mM; DNA (5'-D(*TP*TP*GP*GP*GP*TP*GP*GP*GP*TP*GP*GP*GP*TP*GP*GP*GP*T)-3')0.1 – 1 mM; potassium chloride10 – 70 mM; potassium phosphate10 – 20 mM; entity_10.1 – 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.9 M; pH: 6.65; pressure: 1 atm; temperature: 299 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH, Goddard, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, geometry optimization, refinement

NMR spectrometers:

  • Bruker AMX 600 MHz
  • Bruker AMX 700 MHz

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