BMRB Entry 16295

Name: The solution struture of the reduced yeast TOR1 FATC domain bound to DPC micelles at 298K
Published: 2011-10-07

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PDB ID: 2kit
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16295
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2009-05-11

Original release date:

2011-10-07

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:

assigned_chemical_shifts
- assignments_y1fatc_dpcred298

Data type	Count
13C chemical shifts	119
15N chemical shifts	36
1H chemical shifts	233

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	y1fatc	1

Entities:

Entity 1, y1fatc 33 residues - 3960.4 Da.

1

ASN

GLU

LEU

ASP

VAL

PRO

GLU

GLN

VAL

ASP

2

LYS

LEU

ILE

GLN

ALA

THR

SER

ILE

GLU

3

ARG

LEU

CYS

GLN

HIS

TYR

ILE

GLY

TRP

CYS

4

PRO

PHE

TRP

Samples:

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HACAHB-COSY	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
{15N} SED 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
{13C'} SED 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
15N T1	sample_1	isotropic	sample_conditions_1
15N T2	sample_1	isotropic	sample_conditions_1
{1H}-15N-NOE	sample_1	isotropic	sample_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

BMRB	16284
PDB	1W1N 2KIO 2KIT
DBJ	GAA24414
EMBL	CAA52849 CAA89594 CAY80780
GB	AAB39292 AAB66881 AHY79052 AJP39753 AJR54018
PRF	2010264A
REF	NP_012600
SP	P35169
TPG	DAA08853
AlphaFold	P35169