BMRB Entry 18012

Title:
Solution structure of N-terminal domain of human TIG3
Deposition date:
2011-10-21
Original release date:
2012-02-10
Authors:
Wang, Lei; Yu, Wenyu; Xia, Bin
Citation:

Citation: Wang, Lei; Yu, Wenyu; Ren, Xiaobai; Lin, Jian; Jin, Changwen; Xia, Bin. "1H, 13C, and 15N resonance assignments of the N-terminal domain of human TIG3."  Biomol. NMR Assignments 6, 201-203 (2012).
PubMed: 22290676

Assembly members:

Assembly members:
entity, 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: pET-21a

Data sets:
Data typeCount
13C chemical shifts452
15N chemical shifts103
1H chemical shifts729

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of human TIG31

Entities:

Entity 1, N-terminal domain of human TIG3 125 residues - 14050.996 Da.

This is the N-terminal domain of human tumor suppressor protein

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:

sample_1: TIG3N protein, [U-13C; U-15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 20 mM; urea 2 M; H2O 95%; D2O, [U-2H], 5%; DSS 0.01%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

AMBER v9.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - 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 v5.0, Johnson, One Moon Scientific - peak picking

ProcheckNMR, Laskowski and MacArthur - geometry optimization

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

TOPSPIN v3.0, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 25448 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 Q9UL19

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