BMRB Entry 27867

Name: chemical shifts assignments of TGIF1-RD2a
Published: 2019-05-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27867

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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:

chemical shifts assignments of TGIF1-RD2a

Deposition date:

2019-04-04

Original release date:

2019-05-06

Authors:

Nie, Yao; Cai, Cong; Zhu, Jiang; Yang, Yunhuang

Citation:

Citation: Cai, Cong; Nie, Yao; Yue, Xiali; Zhu, Jiang; Hu, Rui; Liu, Maili; Yang, Yunhuang. "Backbone and side chain resonance assignments of the C-terminal domain of human TGIF1" Biomol. NMR Assignments 13, 357-360 (2019).
PubMed: 31388821

Assembly members:

Assembly members:
TGIF1-TD2a, polymer, 122 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32m

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TGIF1-TD2a: GSMGIKNFMPALEETPFHSC TAGPNPTLGRPLSPKPSSPG SVLARPSVICHTTVTALKDV PFSLCQSVGVGQNTDIQQIA AKNFTDTSLMYPEDTCKSGP STNTQSGLFNTPPPTPPDLN QD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	463
15N chemical shifts	104
1H chemical shifts	706

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TGIF2-RD2a monomer	1

Entities:

Entity 1, TGIF2-RD2a monomer 122 residues - Formula weight is not available

1

GLY

SER

MET

GLY

ILE

LYS

ASN

PHE

MET

PRO

2

ALA

LEU

GLU

THR

PRO

PHE

HIS

SER

CYS

3

THR

ALA

GLY

PRO

ASN

PRO

THR

LEU

GLY

ARG

4

PRO

LEU

SER

PRO

LYS

PRO

SER

PRO

GLY

5

SER

VAL

LEU

ALA

ARG

PRO

SER

VAL

ILE

CYS

6

HIS

THR

VAL

THR

ALA

LEU

LYS

ASP

VAL

7

PRO

PHE

SER

LEU

CYS

GLN

SER

VAL

GLY

VAL

8

GLY

GLN

ASN

THR

ASP

ILE

GLN

ILE

ALA

9

ALA

LYS

ASN

PHE

THR

ASP

THR

SER

LEU

MET

10

TYR

PRO

GLU

ASP

THR

CYS

LYS

SER

GLY

PRO

11

SER

THR

ASN

THR

GLN

SER

GLY

LEU

PHE

ASN

12

THR

PRO

THR

PRO

ASP

LEU

ASN

13

GLN

ASP

Samples:

sample_1: TGIF1-TD2a, [U-100% 13C; U-100% 15N], 0.5 mM; HEPES 20 mM; NaCl 80 mM; DTT 2 mM; PMSF 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.4; pressure: 1 atm; temperature: 293 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-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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