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Biological Magnetic Resonance Data Bank


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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
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Title: NMR structure of the oxidized yeast TOR1 FATC domain bound to DPC micelles at 318K   PubMed: 20042596

Deposition date: 2009-05-07 Original release date: 2010-12-02

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   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

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
13Cnot availablenot availablesotropic
not availablenot availablenot availablesotropic
not availablenot availablenot availablesotropic
not availablenot availablenot availablenot available
not availablenot availablenot availablenot available
not availablenot availablenot availablenot available
not availablenot availablenot availablenot available
not availablenot availablenot availablenot available

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

Download simulated HSQC data in one of the following formats:
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