BMRB Entry 28015

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28015

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Full assignment of 13C,15N-labeled oncogenic mutant human KRas4B-G12C(1-169) bound to GTP at physiological pH
Deposition date:
2019-09-12
Original release date:
2020-09-01
Authors:
Palfy, Gyula; Vida, Istvan; Perczel, Andras
Citation:

Citation: Menyhard, Dora; Palfy, Gyula; Orgovan, Zoltan; Vida, Istvan; Keseru, Gyorgy; Perczel, Andras. "Structural impact of GTP binding on downstream KRAS signaling"  Chem. Sci. 11, 9272-9289 (2020).

Assembly members:

Assembly members:
K-Ras-G12C, polymer, 171 residues, Formula weight is not available
MAGNESIUM ION, non-polymer, 24.305 Da.
GUANOSINE-5'-TRIPHOSPHATE, non-polymer, 523.180 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-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
K-Ras-G12C: GHMTEYKLVVVGACGVGKSA LTIQLIQNHFVDEYDPTIED SYRKQVVIDGETCLLDILDT AGQEEYSAMRDQYMRTGEGF LCVFAINNTKSFEDIHHYRE QIKRVKDSEDVPMVLVGNKC DLPSRTVDTKQAQDLARSYG IPFIETSAKTRQGVDDAFYT LVREIRKHKEK

Data sets:
Data typeCount
13C chemical shifts326
15N chemical shifts134
1H chemical shifts276

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1K-Ras-G12C1
2Mg2+2
3GTP3

Entities:

Entity 1, K-Ras-G12C 171 residues - Formula weight is not available

1   GLYHISMETTHRGLUTYRLYSLEUVALVAL
2   VALGLYALACYSGLYVALGLYLYSSERALA
3   LEUTHRILEGLNLEUILEGLNASNHISPHE
4   VALASPGLUTYRASPPROTHRILEGLUASP
5   SERTYRARGLYSGLNVALVALILEASPGLY
6   GLUTHRCYSLEULEUASPILELEUASPTHR
7   ALAGLYGLNGLUGLUTYRSERALAMETARG
8   ASPGLNTYRMETARGTHRGLYGLUGLYPHE
9   LEUCYSVALPHEALAILEASNASNTHRLYS
10   SERPHEGLUASPILEHISHISTYRARGGLU
11   GLNILELYSARGVALLYSASPSERGLUASP
12   VALPROMETVALLEUVALGLYASNLYSCYS
13   ASPLEUPROSERARGTHRVALASPTHRLYS
14   GLNALAGLNASPLEUALAARGSERTYRGLY
15   ILEPROPHEILEGLUTHRSERALALYSTHR
16   ARGGLNGLYVALASPASPALAPHETYRTHR
17   LEUVALARGGLUILEARGLYSHISLYSGLU
18   LYS

Entity 2, Mg2+ - Mg - 24.305 Da.

1   MG

Entity 3, GTP - C10 H16 N5 O14 P3 - 523.180 Da.

1   GTP

Samples:

sample_1: K-Ras-G12C, [U-100% 13C; U-100% 15N], 0.4 mM; GTP 90 mM; MgCl2 15 mM; EDTA 10 mM; D2O, [U-100% 2H], 10%; DSS 1%; NaN3 6 mM; NaCl 137 mM; KCl 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM

sample_2: K-Ras-G12C, [U-100% 15N], 0.47 mM; GTP 82 mM; MgCl2 15 mM; EDTA 10 mM; D2O, [U-100% 2H], 10%; DSS 1%; NaN3 3 mM; NaCl 137 mM; KCl 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.35; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 150 mM; pH: 7.39; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D BEST-HNCOsample_1isotropicsample_conditions_1
3D BEST-HNCAsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D BEST-HNCACBsample_1isotropicsample_conditions_1
3D BEST-HN(CO)CAsample_1isotropicsample_conditions_1
3D BEST-HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_2

Software:

TOPSPIN v3.6, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III 700 MHz

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