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 16295

Title: The solution struture of the reduced yeast TOR1 FATC domain bound to DPC micelles at 298K   PubMed: 20042596

Deposition date: 2009-05-11 Original release date: 2011-10-07

Authors: Dames, Sonja

Citation: Dames, Sonja. "Structural basis for the association of the redox-sensitive target of rapamycin FATC domain with membrane-mimetic micelles"  J. Biol. Chem. 285, 7766-7775 (2010).

Assembly members:
y1fatc, polymer, 33 residues, 3960.4 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEV2

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts119
15N chemical shifts36
1H chemical shifts233

Additional metadata:

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


Entity Assembly IDEntity NameEntity ID


Entity 1, y1fatc 33 residues - 3960.4 Da.



sample_1: y1fatc, [U-13C; U-15N], 0.5 mM; Tris 50 mM; NaCl 100 mM; TCEP 20 mM; dodecylphophocholine (DPC) 170 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HACAHB-COSYsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
{15N} SED 1H-13C HSQCsample_1isotropicsample_conditions_1
{13C'} SED 1H-13C HSQCsample_1isotropicsample_conditions_1
15N T1sample_1isotropicsample_conditions_1
15N T2sample_1isotropicsample_conditions_1


X-PLOR NIH v2.16.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMRView v5.2.2_01, Johnson, One Moon Scientific - chemical shift assignment

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

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

ProcheckNMR, Laskowski and MacArthur - structure analysis

Molmol, Koradi, Billeter and Wuthrich - structure visualization

xwinnmr v3.5, Bruker Biospin - processing

Tensor2 v2, P. Dosset, D. Marion, M. Blackledge - analysis of 15N relaxation data

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 16284
DBJ GAA24414
EMBL CAA52849 CAA89594 CAY80780
GB AAB39292 AAB66881 AHY79052 AJP39753 AJR54018
PRF 2010264A
REF NP_012600
SP P35169
TPG DAA08853
AlphaFold P35169

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