BMRB Entry 34754

Title:
Structural insights reveal a heterotetramer between oncogenic K-Ras4BG12V and Rgl2, a RalA/B activator
Deposition date:
2022-08-25
Original release date:
2023-10-31
Authors:
Tariq, M.; Ikeya, T.; Togashi, N.; Fairall, L.; Alejo, C.; Kamei, S.; Alonso, B.; Campillo, M.; Hudson, A.; Ito, Y.; Schwabe, J.; Dominguez, C.; Tanaka, K.
Citation:

Citation: Tariq, M.; Ikeya, T.; Togashi, N.; Fairall, L.; Kamei, S.; Mayooramurugan, S.; Abbott, L.; Hasan, A.; Bueno-Alejo, C.; Sukegawa, S.; Romartinez-Alonso, B.; Muro Campillo, M.; Hudson, A.; Ito, Y.; Schwabe, J.; Dominguez, C.; Tanaka, K.. "Structural insights into the complex of oncogenic KRas4B G12V and Rgl2, a RalA/B activator."  Life Sci. Alliance 7, e202302080-e202302080 (2023).
PubMed: 37833074

Assembly members:

Assembly members:
entity_1, polymer, 100 residues, 10972.406 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 BL21(DE3)

Data sets:
Data typeCount
13C chemical shifts415
15N chemical shifts100
1H chemical shifts672

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 100 residues - 10972.406 Da.

1   SERMETGLYPROGLYALASERASPCYSARG
2   ILEILEARGVALGLNMETGLULEUGLYGLU
3   ASPGLYSERVALTYRLYSSERILELEUVAL
4   THRSERGLNASPLYSALAPROSERVALILE
5   SERARGVALLEULYSLYSASNASNARGASP
6   SERALAVALALASERGLUTYRGLULEUVAL
7   GLNLEULEUPROGLYGLUARGGLULEUTHR
8   ILEPROALASERALAASNVALPHETYRALA
9   METASPGLYALASERHISASPPHELEULEU
10   ARGGLNARGARGARGSERSERTHRALATHR

Samples:

sample_1: Rgl2, [U-100% 15N], 1 mM; NaCl 150 mM; KH2PO4 1 mM; Na2HPO4 2.9 mM

sample_2: Rgl2, [U-100% 13C; U-100% 15N], 1 mM; NaCl 150 mM; KH2PO4 1 mM; Na2HPO4 2.9 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v3.99.0, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, structure calculation

TopSpin v3.6.2, Bruker Biospin - collection

Azara v2.8.1, Boucher - processing

CcpNmr Analysis v2.5.0, CCPN - chemical shift assignment, peak picking

OPALp v1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker AVANCE III HD 600 MHz

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