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 25921

Title: NMR assignment of the 65-residue-long inactivating factor of glutanmine synthetase I from cyanobacterirum Synechocystis sp. PCC 6803   PubMed: 27232663

Deposition date: 2015-12-15 Original release date: 2016-06-13

Authors: Pantoja-Uceda, David; Neira, Jose; Santoro, Jorge

Citation: Pantoja-Uceda, David; Neira, Jose; Saelices, Lorena; Robles-Rengel, Rocio; Florencio, Francsico; Muro-Pastor, M. Isabel; Santoro, Jorge. "Dissecting the Binding between Glutamine Synthetase and Its Two Natively Unfolded Protein Inhibitors"  Biochemistry 55, 3370-3382 (2016).

Assembly members:
IF7, polymer, 85 residues, Formula weight is not available

Natural source:   Common Name: cyanobacteria   Taxonomy ID: 1148   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis sp. PPC 6803

Experimental source:   Production method: recombinant technology   Host organism: E.coli (BL21)   Vector: pet24

Entity Sequences (FASTA):
IF7: MGSSHHHHHHSSGLVPRGSH MSTQQQARALMMRHHQFIKN RQQSMLSRAAAEIGVEAEKD FWTTVQGKPQSSFRTTYDRS NASLS

Data sets:
Data typeCount
13C chemical shifts226
15N chemical shifts74
1H chemical shifts272

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IF71

Entities:

Entity 1, IF7 85 residues - Formula weight is not available

Residues 1-20 are not presente in native IF7 renumbering -20 numbers

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERTHRGLNGLNGLNALAARGALALEU
4   METMETARGHISHISGLNPHEILELYSASN
5   ARGGLNGLNSERMETLEUSERARGALAALA
6   ALAGLUILEGLYVALGLUALAGLULYSASP
7   PHETRPTHRTHRVALGLNGLYLYSPROGLN
8   SERSERPHEARGTHRTHRTYRASPARGSER
9   ASNALASERLEUSER

Samples:

sample_1: IF7, [U-99% 13C; U-99% 15N], 1.7 mM; ammonium acetate 10 mM; H2O 90%; D2O, [U-2H], 10%; DSS 50 uM

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCA-intrasample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACB-intrasample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 15N-13COsample_1isotropicsample_conditions_1
3D (H)N(COCA)NCOsample_1isotropicsample_conditions_1
3D (HN)CO(CA)NCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v216, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

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