BMRB Entry 25448

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

Data sets:
Data typeCount
13C chemical shifts355
15N chemical shifts112
1H chemical shifts744

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TIG3N1

Entities:

Entity 1, TIG3N 125 residues - 14050.996 Da.

1   METALASERPROHISGLNGLUPROLYSPRO
2   GLYASPLEUILEGLUILEPHEARGLEUGLY
3   TYRGLUHISTRPALALEUTYRILEGLYASP
4   GLYTYRVALILEHISLEUALAPROPROSER
5   GLUTYRPROGLYALAGLYSERSERSERVAL
6   PHESERVALLEUSERASNSERALAGLUVAL
7   LYSARGGLUARGLEUGLUASPVALVALGLY
8   GLYCYSCYSTYRARGVALASNASNSERLEU
9   ASPHISGLUTYRGLNPROARGPROVALGLU
10   VALILEILESERSERALALYSGLUMETVAL
11   GLYGLNLYSMETLYSTYRSERILEVALSER
12   ARGASNCYSGLUHISPHEVALTHRGLNLEU
13   ARGTYRGLYLYSSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCTIG3N_sampleisotropicTIG3N_condition
2D 1H-13C HSQCTIG3N_sampleisotropicTIG3N_condition
3D CBCA(CO)NHTIG3N_sampleisotropicTIG3N_condition
3D HNCATIG3N_sampleisotropicTIG3N_condition
3D HNCACBTIG3N_sampleisotropicTIG3N_condition
3D HBHA(CO)NHTIG3N_sampleisotropicTIG3N_condition
3D 1H-15N NOESYTIG3N_sampleisotropicTIG3N_condition
3D 1H-13C NOESYTIG3N_sampleisotropicTIG3N_condition
3D HCCH-COSYTIG3N_sampleisotropicTIG3N_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

Related Database Links:

UNP Q9UL19
BMRB 18012 2545
PDB
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

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