BMRB Entry 26935

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for KISS-1
Deposition date:
2016-11-07
Original release date:
2017-04-26
Authors:
Blanco, Francisco J; Ibanez de Opakua, Alain; Merino, Nekane; Villate, Maider
Citation:

Citation: Ibanez de Opakua, Alain; Merino, Nekane; Villate, Maider; Cordeiro, Tiago; Ormaza, Georgina; Sanchez-Carbayo, Marta; Diercks, Tammo; Bernado, Pau; Blanco, Francisco. "The metastasis suppressor Kiss1 is an intrinsically disordered protein slightly more extended than a random coil"  PLoS ONE 12, e0172507-e0172507 (2017).
PubMed: 28207895

Assembly members:

Assembly members:
KISS-1, polymer, 120 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: pet11d

Data sets:
Data typeCount
13C chemical shifts324
15N chemical shifts103
1H chemical shifts225

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KISS-11

Entities:

Entity 1, KISS-1 120 residues - Formula weight is not available

1   GLYGLUPROLEUGLULYSVALALASERVAL
2   GLYASNSERARGPROTHRGLYGLNGLNLEU
3   GLUSERLEUGLYLEULEUALAPROGLYGLU
4   GLNSERLEUPROCYSTHRGLUARGLYSPRO
5   ALAALATHRALAARGLEUSERARGARGGLY
6   THRSERLEUSERPROPROPROGLUSERSER
7   GLYSERPROGLNGLNPROGLYLEUSERALA
8   PROHISSERARGGLNILEPROALAPROGLN
9   GLYALAVALLEUVALGLNARGGLULYSASP
10   LEUPROASNTYRASNTRPASNSERPHEGLY
11   LEUARGPHEGLYLYSARGGLUALAALAPRO
12   GLYASNHISGLYARGSERALAGLYARGGLY

Samples:

sample_1: KISS-1, [U-99% 13C; U-99% 15N], 112 uM; D2O, [U-2H], 5%; H2O 95%; DTT 2 mM; DSS 25 uM

sample_conditions_1: pH: 5.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(COCA)HAsample_1isotropicsample_conditions_1
3D HN(CA)HAsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker - collection

MDD_NMR, V. Orekhov - processing

SPARKY, T. D. Goddard and D. G. Kneller - chemical shift assignment, data analysis, peak picking

MARS, Markus Zweckstetter - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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