BMRB Entry 16284

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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/BMR16284
MolProbity Validation Chart

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Title:
NMR structure of the oxidized yeast TOR1 FATC domain bound to DPC micelles at 318K
Deposition date:
2009-05-07
Original release date:
2010-12-02
Authors:
Dames, Sonja
Citation:

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).
PubMed: 20042596

Assembly members:

Assembly members:
y1fatc, polymer, 33 residues, 3960.4 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   Vector: pGEV2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
y1fatc: NELDVPEQVDKLIQQATSIE RLCQHYIGWCPFW

Data sets:
Data typeCount
13C chemical shifts123
15N chemical shifts36
1H chemical shifts234

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1y1fatc1

Entities:

Entity 1, y1fatc 33 residues - 3960.4 Da.

1   ASNGLULEUASPVALPROGLUGLNVALASP
2   LYSLEUILEGLNGLNALATHRSERILEGLU
3   ARGLEUCYSGLNHISTYRILEGLYTRPCYS
4   PROPHETRP

Samples:

sample_1: y1fatc, [U-13C; U-15N], 0.40-0.46 mM; H2O 95%; D2O 5%; Tris 50 mM; NaCl 100 mM; dodecylphophocholine (DPC) 190-220 mM

sample_2: y1fatc, [U-13C; U-15N], 0.40 mM; D2O 100%; Tris 50 mM; NaCl 100 mM; dodecylphophocholine (DPC) 190-220 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 318 K

Experiments:

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 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
13C'-{13Cg} SED 1H-15N HSQCsample_1isotropicsample_conditions_1
15N-{13Cg} SED 1H-15N HSQCsample_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
{1H}-15N-NOEsample_1isotropicsample_conditions_1

Software:

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 16295
PDB
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 peaks
SPARKY: Backbone or all simulated peaks