BMRB Entry 25548

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25548
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
structure of a peptide
Deposition date:
2015-03-23
Original release date:
2015-07-27
Authors:
Heddi, Brahim; Cheong, Vee Vee; Martadinata, Herry; Phan, Anh Tuan
Citation:

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).
PubMed: 26195789

Assembly members:

Assembly members:
entity, polymer, 20 residues, 2360.817 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: pET32 Ek/LIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SMHPGHLKGREIGMWYAKKQ

Data sets:
Data typeCount
13C chemical shifts77
15N chemical shifts17
1H chemical shifts113

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 20 residues - 2360.817 Da.

1   SERMETHISPROGLYHISLEULYSGLYARG
2   GLUILEGLYMETTRPTYRALALYSLYSGLN

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.1 – 1 mM; potassium chloride10 – 70 mM; potassium phosphate10 – 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 90 mM; pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

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

Software:

CYANA, Guntert, Braun and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

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