BMRB Entry 25448

Name: Solution structure of N-terminal domain of human TIG3
Published: 2015-04-07

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PDB ID: 2my9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25448
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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:

Solution structure of N-terminal domain of human TIG3

Deposition date:

2015-01-21

Original release date:

2015-04-07

Authors:

Wei, Hejia; Wang, Lei; Xia, Bin

Citation:

Citation: Wei, Hejia; Wang, Lei; Ren, Xiaobai; Yu, Wenyu; Lin, Jian; Jin, Changwen; Xia, Bin. "Structural and Functional Characterization of Tumor Suppressors TIG3 and H-REV107" FEBS ., .-. (2015).

Assembly members:

Assembly members:
TIG3N, polymer, 125 residues, 14050.996 Da.

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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TIG3N: MASPHQEPKPGDLIEIFRLG YEHWALYIGDGYVIHLAPPS EYPGAGSSSVFSVLSNSAEV KRERLEDVVGGCCYRVNNSL DHEYQPRPVEVIISSAKEMV GQKMKYSIVSRNCEHFVTQL RYGKS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	355
15N chemical shifts	112
1H chemical shifts	744

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TIG3N	1

Entities:

Entity 1, TIG3N 125 residues - 14050.996 Da.

1

MET

ALA

SER

PRO

HIS

GLN

GLU

PRO

LYS

PRO

2

GLY

ASP

LEU

ILE

GLU

ILE

PHE

ARG

LEU

GLY

3

TYR

GLU

HIS

TRP

ALA

LEU

TYR

ILE

GLY

ASP

4

GLY

TYR

VAL

ILE

HIS

LEU

ALA

PRO

SER

5

GLU

TYR

PRO

GLY

ALA

GLY

SER

VAL

6

PHE

SER

VAL

LEU

SER

ASN

SER

ALA

GLU

VAL

7

LYS

ARG

GLU

ARG

LEU

GLU

ASP

VAL

GLY

8

GLY

CYS

TYR

ARG

VAL

ASN

SER

LEU

9

ASP

HIS

GLU

TYR

GLN

PRO

ARG

PRO

VAL

GLU

10

VAL

ILE

SER

ALA

LYS

GLU

MET

VAL

11

GLY

GLN

LYS

MET

LYS

TYR

SER

ILE

VAL

SER

12

ARG

ASN

CYS

GLU

HIS

PHE

VAL

THR

GLN

LEU

13

ARG

TYR

GLY

LYS

SER

Samples:

TIG3N_sample: TIG3N, [U-13C; U-15N], 0.5 mM; DSS 0.03 % w/v; DTT 20 mM; sodium chloride 50 mM; potassium chloride 50 mM; D2O 10%; H2O 90%

TIG3N_condition: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	TIG3N_sample	isotropic	TIG3N_condition
2D 1H-13C HSQC	TIG3N_sample	isotropic	TIG3N_condition
3D CBCA(CO)NH	TIG3N_sample	isotropic	TIG3N_condition
3D HNCA	TIG3N_sample	isotropic	TIG3N_condition
3D HNCACB	TIG3N_sample	isotropic	TIG3N_condition
3D HBHA(CO)NH	TIG3N_sample	isotropic	TIG3N_condition
3D 1H-15N NOESY	TIG3N_sample	isotropic	TIG3N_condition
3D 1H-13C NOESY	TIG3N_sample	isotropic	TIG3N_condition
3D HCCH-COSY	TIG3N_sample	isotropic	TIG3N_condition

Software:

AMBER v9.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

DYANA v3.0, Guntert, Braun and Wuthrich - structure solution

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

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

NMRView v5, Johnson, One Moon Scientific - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SANE, Duggan, Legge, Dyson & Wright - chemical shift assignment

TOPSPIN v3.0, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 500 MHz
Bruker Avance 600 MHz

UNP	Q9UL19
BMRB	18012 2545
PDB	2LKT 2MY9
DBJ	BAB08109 BAG35046 BAG56873 BAH22446
GB	AAC84000 AAF02294 AAH09678 ABM82370 ABM85548
REF	NP_004576 XP_003828577 XP_004051454 XP_508513
SP	Q9UL19
AlphaFold	O95200 Q9UL19