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 15802

Title: 1H, 13C, and 15N resonance assignments of a RNA binding protein GSP13 from Bacillus subtilis   PubMed: 19636895

Deposition date: 2008-06-11 Original release date: 2008-07-29

Authors: Yu, Wenyu; Yu, Bingke; Hu, Jicheng; Jin, Changwen; Xia, Bin

Citation: Yu, Wenyu; Yu, Bingke; Hu, Jicheng; Xia, Wei; Jin, Changwen; Xia, Bin. "1H, 13C, and 15N resonance assignments of a general stress protein GSP13 from Bacillus subtilis"  Biomol. NMR Assignments 2, 163-165 (2008).

Assembly members:
GSP13, polymer, 130 residues, Formula weight is not available

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-21a

Entity Sequences (FASTA):
GSP13: MAAKFEVGSVYTGKVTGLQA YGAFVALDEETQGLVHISEV THGFVKDINEHLSVGDEVQV KVLAVDEEKGKISLSIRATQ AAPEKKESKPRKPKAAQVSE EASTPQGFNTLKDKLEEWIE MSNRKDLIKK

Data sets:
Data typeCount
13C chemical shifts525
15N chemical shifts131
1H chemical shifts886

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GSP131

Entities:

Entity 1, GSP13 130 residues - Formula weight is not available

1   METALAALALYSPHEGLUVALGLYSERVAL
2   TYRTHRGLYLYSVALTHRGLYLEUGLNALA
3   TYRGLYALAPHEVALALALEUASPGLUGLU
4   THRGLNGLYLEUVALHISILESERGLUVAL
5   THRHISGLYPHEVALLYSASPILEASNGLU
6   HISLEUSERVALGLYASPGLUVALGLNVAL
7   LYSVALLEUALAVALASPGLUGLULYSGLY
8   LYSILESERLEUSERILEARGALATHRGLN
9   ALAALAPROGLULYSLYSGLUSERLYSPRO
10   ARGLYSPROLYSALAALAGLNVALSERGLU
11   GLUALASERTHRPROGLNGLYPHEASNTHR
12   LEULYSASPLYSLEUGLUGLUTRPILEGLU
13   METSERASNARGLYSASPLEUILELYSLYS

Samples:

sample_1: GSP13, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 20 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_2: GSP13, [U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.07 M; pH: 7.0; pressure: 1 atm; temperature: 298 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
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAI86662 BAM55208 BAM59221 GAK80090
EMBL CAB07921 CAB15128 CBI44065 CCU60178 CEI58372
GB ADM39092 ADV93943 AEB25277 AEB64738 AEK90308
REF NP_391017 WP_003220769 WP_003228864 WP_010331658 WP_013353366
SP P80870
AlphaFold P80870

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