BMRB Entry 52074

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52074
MolProbity Validation Chart

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

Title:
Solution NMR assignments of T35S mutant of KRAS4b-GppNHp
Deposition date:
2023-08-07
Original release date:
2026-08-14
Authors:
Sharma, Alok; Dyba, Marcin; Tonelli, Marco; Smith, Brian; William, Gillette; Esposito, Dominic; Nissley, Dwight; McCormick, Frank; Maciag, Anna
Citation:

Citation: Sharma, Alok; Dyba, Marcin; Tonelli, Marco; Smith, Brian; Gillette, William; Esposito, Dominic; Nissley, Dwight; McCormick, Frank; Maciag, Anna. "NMR 1H, 13C, 15N backbone resonance assignments of the T35S and oncogenic T35S/Q61L mutants of human KRAS4b in the active, GppNHp-bound conformation "  Biomol. NMR Assign. 16, 1-8 (2022).
PubMed: 34686998

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: pET

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts729
15N chemical shifts188
1H chemical shifts1199

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   ALAGLYGLYVALGLYLYSSERALALEUTHR
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: K-Ras4b(1-169), [U-99% 13C; U-99% 15N], 0.8 mM; K-Ras protein, [U-98% 15N], 0.8 mM; GppNHp 0.8 mM; MgCl2 2 mM; potassium chloride 100 mM; sodium chloride 50 mM; TCEP, [U-2H], 1 mM; MES, [U-2H], 20 mM; DSS 250 uM; D2O 7%

sample_2: K-Ras4b(1-169), [U-99% 13C; U-99% 15N], 0.8 mM; K-Ras protein, [U-98% 15N], 0.8 mM; GppNHp 0.8 mM; MgCl2 2 mM; potassium chloride 100 mM; sodium chloride 50 mM; TCEP, [U-2H], 1 mM; MES, [U-2H], 20 mM

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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_2isotropicsample_conditions_1
T2/R2 relaxationsample_2isotropicsample_conditions_1
1H-15N heteronoesample_2isotropicsample_conditions_1
T1rho/R1rho relaxationsample_2isotropicsample_conditions_1

Software:

NMRDraw v10.9 - Data were visualized and analyzed

NMRPipe v10.9 - Data were processed

CcpNMR v2.4 - NMR data analysis and assignments

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz
  • Varian INOVA 800 MHz

Related Database Links:

UniProtKB - P01116 (RASK_HUMAN) P01116-2

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