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 18471

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for PWWP domain from Trypanosoma brucei   PubMed: 22836947

Deposition date: 2012-05-17 Original release date: 2012-08-29

Authors: Dai, Kun; Liao, Shanhui; Zhang, Jiahai; Tu, Xiaoming

Citation: Zhang, Jiahai; Dai, Kun; Liao, Shanhui; Tu, Xiaoming. "H, C and N resonance assignments of TbTFIIS2-2 PWWP domain from Trypanosoma brucei."  Biomol. NMR Assignments 7, 207-209 (2013).

Assembly members:
PWWP_domain, polymer, 118 residues, Formula weight is not available

Natural source:   Common Name: Kinetoplastids   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: Pet22(b)

Entity Sequences (FASTA):
PWWP_domain: MIPSFAPGTLVWLKQDRFPW WPGFVMDPDEVRDITLPEGS DVWVCCLPRDSLTLSAANSE DEGQIRYFLPDRDEGMMEEG KLDASCAVAIEEAIQLYEEQ LKAQAGGTNELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts298
15N chemical shifts101
1H chemical shifts645

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PWWP_domain1

Entities:

Entity 1, PWWP_domain 118 residues - Formula weight is not available

1   METILEPROSERPHEALAPROGLYTHRLEU
2   VALTRPLEULYSGLNASPARGPHEPROTRP
3   TRPPROGLYPHEVALMETASPPROASPGLU
4   VALARGASPILETHRLEUPROGLUGLYSER
5   ASPVALTRPVALCYSCYSLEUPROARGASP
6   SERLEUTHRLEUSERALAALAASNSERGLU
7   ASPGLUGLYGLNILEARGTYRPHELEUPRO
8   ASPARGASPGLUGLYMETMETGLUGLUGLY
9   LYSLEUASPALASERCYSALAVALALAILE
10   GLUGLUALAILEGLNLEUTYRGLUGLUGLN
11   LEULYSALAGLNALAGLYGLYTHRASNGLU
12   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: PWWP_domain, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 25 mM; sodium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 125 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

EMBL CBH09455
GB AAQ15805 AAX79611
REF XP_011771760 XP_951596

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