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 18474

Title: the pwwp domain of TFIIS2-1 from Trypanosoma brucei   PubMed: 22836947

Deposition date: 2012-05-18 Original release date: 2012-08-29

Authors: Wang, Rui; Fan, Kai; 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:
entity, polymer, 118 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
entity: MLQERVFHINDRVWLKTGAN TWWPAKVTSVTGVEGVDGRS SETGTSTVTVLTYPGTQNKA TYKNVDSHSSAITFFEPSSE KAVTANEDLLQAIRNAEEDK ESNALRFEPTLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts294
15N chemical shifts107
1H chemical shifts614

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pwwp domain of TFIIS2-11

Entities:

Entity 1, pwwp domain of TFIIS2-1 118 residues - Formula weight is not available

1   METLEUGLNGLUARGVALPHEHISILEASN
2   ASPARGVALTRPLEULYSTHRGLYALAASN
3   THRTRPTRPPROALALYSVALTHRSERVAL
4   THRGLYVALGLUGLYVALASPGLYARGSER
5   SERGLUTHRGLYTHRSERTHRVALTHRVAL
6   LEUTHRTYRPROGLYTHRGLNASNLYSALA
7   THRTYRLYSASNVALASPSERHISSERSER
8   ALAILETHRPHEPHEGLUPROSERSERGLU
9   LYSALAVALTHRALAASNGLUASPLEULEU
10   GLNALAILEARGASNALAGLUGLUASPLYS
11   GLUSERASNALALEUARGPHEGLUPROTHR
12   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: Tbpwwp, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%; Na2HPO4 25 mM; NaCl 150 mM; EDTA 2 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.7; 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 HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

PDB
EMBL CBH09458
GB AAQ15815 AAX79612
REF XP_011771763 XP_951597

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