BMRB Entry 52073

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52073
MolProbity Validation Chart

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

Title:
Solution NMR Assignments of oncogenic G12D mutant of T35S-C118S KRAS4b-GppNHp
Deposition date:
2023-08-07
Original release date:
2026-08-14
Authors:
Sharma, Alok; Dyba, Marcin; Smith, Brian; Rigby, Megan; Tonelli, Marco; Maciag, Anna
Citation:

Citation: Sharma, Alok; Dyba, Marcin; Smith, Brian; Rigby, Megan; Tonelli, Marco; Maciag, Anna. "Solution Structures of the G12C and G12D oncogenic mutants of state 1 conformation of KRAS-GppNHp show distinct modulation of protein function in the Helix3-Switch2 pocket. "  .

Assembly members:

Assembly members:
entity_1, polymer, 169 residues, Formula weight is not available
entity_GNP, non-polymer, 522.196 Da.
entity_MG, non-polymer, 24.305 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: pDest-566

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTEYKLVVVGADGVGKSALT IQLIQNHFVDEYDPSIEDSY RKQVVIDGETCLLDILDTAG QEEYSAMRDQYMRTGEGFLC VFAINNTKSFEDIHHYREQI KRVKDSEDVPMVLVGNKSDL PSRTVDTKQAQDLARSYGIP FIETSAKTRQGVDDAFYTLV REIRKHKEK

Data sets:
Data typeCount
13C chemical shifts753
15N chemical shifts187
1H chemical shifts1198

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GTPase K-Ras1
2GppNHp2
3Mg ion3

Entities:

Entity 1, GTPase K-Ras 169 residues - Formula weight is not available

1   METTHRGLUTYRLYSLEUVALVALVALGLY
2   ALAASPGLYVALGLYLYSSERALALEUTHR
3   ILEGLNLEUILEGLNASNHISPHEVALASP
4   GLUTYRASPPROSERILEGLUASPSERTYR
5   ARGLYSGLNVALVALILEASPGLYGLUTHR
6   CYSLEULEUASPILELEUASPTHRALAGLY
7   GLNGLUGLUTYRSERALAMETARGASPGLN
8   TYRMETARGTHRGLYGLUGLYPHELEUCYS
9   VALPHEALAILEASNASNTHRLYSSERPHE
10   GLUASPILEHISHISTYRARGGLUGLNILE
11   LYSARGVALLYSASPSERGLUASPVALPRO
12   METVALLEUVALGLYASNLYSSERASPLEU
13   PROSERARGTHRVALASPTHRLYSGLNALA
14   GLNASPLEUALAARGSERTYRGLYILEPRO
15   PHEILEGLUTHRSERALALYSTHRARGGLN
16   GLYVALASPASPALAPHETYRTHRLEUVAL
17   ARGGLUILEARGLYSHISLYSGLULYS

Entity 2, GppNHp - C10 H17 N6 O13 P3 - 522.196 Da.

1   GNP

Entity 3, Mg ion - Mg - 24.305 Da.

1   MG

Samples:

sample_1: KRAS4b protein, [U-100% 13C; U-100% 15N], 0.8 ± 0.02 mM; GppNHp 0.8 ± 0.02 mM; MES, [U-2H], 20 mM; KCl 100 mM; NaCl 50 mM; MgCl2 2 mM; TCEP, [U-2H], 1 mM; NaN3 0.02%; DSS 250 uM; D2O 7%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
T1rho/R1rho relaxationsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRPipe vv10.9 - processing

NMRDraw vv10.9 - data analysis

CcpNMR vv2.4 - peak picking and chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 750 MHz
  • Varian INOVA 750 MHz

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