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 17880

Title: 1H, 13C, and 15N Chemical Shift Assignments for a yeast protein   PubMed: 22488857

Deposition date: 2011-08-23 Original release date: 2012-04-23

Authors: Wang, Tao

Citation: Wang, Tao; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming. "Solution structure of SWI1 AT-rich interaction domain from Saccharomyces cerevisiae and its nonspecific binding to DNA."  Proteins 80, 1911-1917 (2012).

Assembly members:
yeast_protein, polymer, 125 residues, Formula weight is not available

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
yeast_protein: MQSLNPALQEKISTELNNKQ YELFMKSLIENCKKRNMPLQ SIPEIGNRKINLFYLYMLVQ KFGGADQVTRTQQWSMVAQR LQISDYQQLESIYFRILLPY ERHMISQEGIKETQAKRLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts303
15N chemical shifts110
1H chemical shifts485

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1yeast_protein1

Entities:

Entity 1, yeast_protein 125 residues - Formula weight is not available

1   METGLNSERLEUASNPROALALEUGLNGLU
2   LYSILESERTHRGLULEUASNASNLYSGLN
3   TYRGLULEUPHEMETLYSSERLEUILEGLU
4   ASNCYSLYSLYSARGASNMETPROLEUGLN
5   SERILEPROGLUILEGLYASNARGLYSILE
6   ASNLEUPHETYRLEUTYRMETLEUVALGLN
7   LYSPHEGLYGLYALAASPGLNVALTHRARG
8   THRGLNGLNTRPSERMETVALALAGLNARG
9   LEUGLNILESERASPTYRGLNGLNLEUGLU
10   SERILETYRPHEARGILELEULEUPROTYR
11   GLUARGHISMETILESERGLNGLUGLYILE
12   LYSGLUTHRGLNALALYSARGLEUGLUHIS
13   HISHISHISHISHIS

Samples:

sample_1: yeast protein, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 100 mM; sodium phosphate 2 mM; EDTA 1.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; 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 HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_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
DBJ GAA26956
EMBL CAA31013 CAY86943
GB AAB68089 AHY78155 AJP42124 AJV91214 AJV91652
REF NP_015309
SP P09547
TPG DAA11412

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