BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27272

Title: Backbone assignment of SGTA C-terminal domain   PubMed: 29996828

Deposition date: 2017-10-04 Original release date: 2018-06-19

Authors: Martinez Lumbreras, Santiago; Isaacson, Rivka

Citation: Martinez-Lumbreras, Santiago; Krysztofinska, Ewelina; Thapaliya, Arjun; Spilotros, Alessandro; Matak-Vinkovic, Dijana; Salvadori, Enrico; Roboti, Peristera; Nyathi, Yvonne; Muench, Janina; Roessler, Maxie; Svergun, Dmitri; High, Stephen; Isaacson, Rivka. "Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control"  BMC Biol. 16, 76-76 (2018).

Assembly members:
SGTA_Cter, polymer, 103 residues, Formula weight is not available

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: pET28_Txr_6xH_TEV

Entity Sequences (FASTA):
SGTA_Cter: GSTGGVGSFDIAGLLNNPGF MSMASNLMNNPQIQQLMSGM ISGGNNPLGTPGTSPSQNDL ASLIQAGQQFAQQMQQQNPE LIEQLRSQIRSRTPSASNDD QQE

Data sets:
Data typeCount
13C chemical shifts173
15N chemical shifts53
1H chemical shifts68

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SGTA_Cter1

Entities:

Entity 1, SGTA_Cter 103 residues - Formula weight is not available

1   GLYSERTHRGLYGLYVALGLYSERPHEASP
2   ILEALAGLYLEULEUASNASNPROGLYPHE
3   METSERMETALASERASNLEUMETASNASN
4   PROGLNILEGLNGLNLEUMETSERGLYMET
5   ILESERGLYGLYASNASNPROLEUGLYTHR
6   PROGLYTHRSERPROSERGLNASNASPLEU
7   ALASERLEUILEGLNALAGLYGLNGLNPHE
8   ALAGLNGLNMETGLNGLNGLNASNPROGLU
9   LEUILEGLUGLNLEUARGSERGLNILEARG
10   SERARGTHRPROSERALASERASNASPASP
11   GLNGLNGLU

Samples:

Cter_CND: SGTA_Cter, [U-13C; U-15N; U-2H], 300 uM; potassium phosphate 10 mM; sodium chloride 100 mM; TCEP 250 uM; DDM 0.025%

sample_conditions_1: ionic strength: 130 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCCter_CNDisotropicsample_conditions_1
3D CBCA(CO)NHCter_CNDisotropicsample_conditions_1
3D HNCACBCter_CNDisotropicsample_conditions_1
3D HNCOCter_CNDisotropicsample_conditions_1
3D HN(CA)COCter_CNDisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CCPN_Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 950 MHz

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