BMRB Entry 27275

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27275

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Title:
Backbone assignment of SGTA TPR_C-terminal(deltaQ) domains
Deposition date:
2017-10-05
Original release date:
2018-06-19
Authors:
Martinez Lumbreras, Santiago; Thapaliya, Arjun; Isaacson, Rivka
Citation:

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).
PubMed: 29996828

Assembly members:

Assembly members:
SGTA_TPR-NNP, polymer, 192 residues, Formula weight is not available

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: pET28_Txr_6xH_TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SGTA_TPR-NNP: GSEEDSAEAERLKTEGNEQM KVENFEAAVHFYGKAIELNP ANAVYFCNRAAAYSKLGNYA GAVQDCERAICIDPAYSKAY GRMGLALSSLNKHVEAVAYY KKALELDPDNETYKSNLKIA ELKLREAPSPTGGVGSFDIA GLLNNPGFMSMASNLMNNPQ IQQLMSGMISGGNNPLGTPG TSPSQNDLASLI

Data sets:
Data typeCount
13C chemical shifts462
15N chemical shifts152
1H chemical shifts152

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SGTA_TPR-NNP1

Entities:

Entity 1, SGTA_TPR-NNP 192 residues - Formula weight is not available

1   GLYSERGLUGLUASPSERALAGLUALAGLU
2   ARGLEULYSTHRGLUGLYASNGLUGLNMET
3   LYSVALGLUASNPHEGLUALAALAVALHIS
4   PHETYRGLYLYSALAILEGLULEUASNPRO
5   ALAASNALAVALTYRPHECYSASNARGALA
6   ALAALATYRSERLYSLEUGLYASNTYRALA
7   GLYALAVALGLNASPCYSGLUARGALAILE
8   CYSILEASPPROALATYRSERLYSALATYR
9   GLYARGMETGLYLEUALALEUSERSERLEU
10   ASNLYSHISVALGLUALAVALALATYRTYR
11   LYSLYSALALEUGLULEUASPPROASPASN
12   GLUTHRTYRLYSSERASNLEULYSILEALA
13   GLULEULYSLEUARGGLUALAPROSERPRO
14   THRGLYGLYVALGLYSERPHEASPILEALA
15   GLYLEULEUASNASNPROGLYPHEMETSER
16   METALASERASNLEUMETASNASNPROGLN
17   ILEGLNGLNLEUMETSERGLYMETILESER
18   GLYGLYASNASNPROLEUGLYTHRPROGLY
19   THRSERPROSERGLNASNASPLEUALASER
20   LEUILE

Samples:

sample_1: SGTA_TPR-NNP, [U-100% 13C; U-100% 15N], 900 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 HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_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 700 MHz

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