BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27235

Title: Solution NMR assignment of the C-terminal domain of chTOG   PubMed: 29582386

Deposition date: 2017-08-25 Original release date: 2018-03-29

Authors: Pfuhl, Mark

Citation: Rostkova, Elena; Burgess, Selena; Bayliss, Richard; Pfuhl, Mark. "Solution NMR assignment of the C-terminal domain of human chTOG"  Biomol. NMR Assign. 12, 221-224 (2018).

Assembly members:
chTOG, polymer, 141 residues, 15.9 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET6a

Entity Sequences (FASTA):
chTOG: ASRIDEKSSKAKVNDFLAEI FKKIGSKENTKEGLAELYEY KKKYSDADIEPFLKNSSQFF QSYVERGLRVIEMEREGKGR ISTSTGISPQMEVTCVPTPT STVSSIGNTNGEEVGPSVYL ERLKILRQRCGLDNTKQDDR P

Data sets:
Data typeCount
13C chemical shifts617
15N chemical shifts142
1H chemical shifts979

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal domain of chTOG1

Entities:

Entity 1, C-terminal domain of chTOG 141 residues - 15.9 Da.

the first residue A1817 is a cloning atifact

1   ALASERARGILEASPGLULYSSERSERLYS
2   ALALYSVALASNASPPHELEUALAGLUILE
3   PHELYSLYSILEGLYSERLYSGLUASNTHR
4   LYSGLUGLYLEUALAGLULEUTYRGLUTYR
5   LYSLYSLYSTYRSERASPALAASPILEGLU
6   PROPHELEULYSASNSERSERGLNPHEPHE
7   GLNSERTYRVALGLUARGGLYLEUARGVAL
8   ILEGLUMETGLUARGGLUGLYLYSGLYARG
9   ILESERTHRSERTHRGLYILESERPROGLN
10   METGLUVALTHRCYSVALPROTHRPROTHR
11   SERTHRVALSERSERILEGLYASNTHRASN
12   GLYGLUGLUVALGLYPROSERVALTYRLEU
13   GLUARGLEULYSILELEUARGGLNARGCYS
14   GLYLEUASPASNTHRLYSGLNASPASPARG
15   PRO

Samples:

CTD_15N: chTOG, [U-98% 15N], 200 ± 10 uM; HEPES 20 ± 0.5 mM; sodium chloride 50 ± 1 mM; DTT 2 ± 0.1 mM

CTD_15N_13C: chTOG, [U-95% 13C; U-95% 15N], 200 ± 10 uM; HEPES 20 ± 0.5 mM; sodium chloride 50 ± 1 mM; DTT 2 ± 0.1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.10; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCCTD_15Nisotropicsample_conditions_1
3D 1H-15N NOESYCTD_15Nisotropicsample_conditions_1
3D HNCACBCTD_15N_13Cisotropicsample_conditions_1
3D HNCOCTD_15N_13Cisotropicsample_conditions_1
3D CBCA(CO)NHCTD_15N_13Cisotropicsample_conditions_1
3D HBHA(CO)NHCTD_15N_13Cisotropicsample_conditions_1
3D H(CCO)NHCTD_15N_13Cisotropicsample_conditions_1
3D (H)C(CO)NHCTD_15N_13Cisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticCTD_15N_13Cisotropicsample_conditions_1
2D 1H-13C TROSY aromaticCTD_15N_13Cisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticCTD_15N_13Cisotropicsample_conditions_1
3D 1H-13C NOESY aromaticCTD_15N_13Cisotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

CCPN_Analysis v2.4, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz

Related Database Links:

SP Q14008
AlphaFold Q6NSH4

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