BMRB Entry 30027

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30027
MolProbity Validation Chart

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Title:
GCN4p pH 6.6
Deposition date:
2016-02-25
Original release date:
2017-03-09
Authors:
Brady, M.; Kaplan, A.; Alexandrescu, A.
Citation:

Citation: Kaplan, Anne; Brady, Megan; Maciejewski, Mark; Kammerer, Richard; Alexandrescu, Andrei. "Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix"  Biochemistry 56, 1604-1619 (2017).
PubMed: 28230348

Assembly members:

Assembly members:
General control protein GCN4, polymer, 33 residues, 3835.406 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
General control protein GCN4: GSMKQLEDKVEELLSKNYHL ENEVARLKKLVGE

Data sets:
Data typeCount
13C chemical shifts114
15N chemical shifts36
1H chemical shifts253

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, chain 11
2entity_1, chain 21

Entities:

Entity 1, entity_1, chain 1 33 residues - 3835.406 Da.

1   GLYSERMETLYSGLNLEUGLUASPLYSVAL
2   GLUGLULEULEUSERLYSASNTYRHISLEU
3   GLUASNGLUVALALAARGLEULYSLYSLEU
4   VALGLYGLU

Samples:

sample_1: GCN4p, [U-99% 13C; U-99% 15N], 1.5 mM; H2O 90%; D2O 10%; NaCl 10 mM; phosphate buffer 10 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

CcpNMR, CCPN - chemical shift assignment

Felix, Accelrys Software Inc. - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Varian INOVA 600 MHz

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