BMRB Entry 30048

Title:
Solution structure of Ras Binding Domain (RBD) of B-Raf complexed with Rigosertib (Complex I)
Deposition date:
2016-03-29
Original release date:
2016-06-20
Authors:
Dutta, K.; Vasquez-Del Carpio, R.; Aggarwal, A.; Reddy, E.
Citation:

Citation: Athuluri-Divakar, S.; Vasquez-Del Carpio, R.; Dutta, K.; Baker, S.; Cosenza, S.; Basu, I.; Gupta, Y.; Reddy, M.; Ueno, L.; Hart, J.; Vogt, P.; Mulholland, D.; Guha, C.; Aggarwal, A.; Reddy, E.. "A Small Molecule RAS-Mimetic Disrupts RAS Association with Effector Proteins to Block Signaling"  Cell 165, 643-655 (2016).
PubMed: 27104980

Assembly members:

Assembly members:
entity_1, polymer, 92 residues, 10311.078 Da.
entity_6FS, non-polymer, 451.490 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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts378
15N chemical shifts76
1H chemical shifts603

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 92 residues - 10311.078 Da.

1   GLYSERLEUGLUVALLEUPHEGLNGLYPRO
2   SERPROGLNLYSPROILEVALARGVALPHE
3   LEUPROASNLYSGLNARGTHRVALVALPRO
4   ALAARGCYSGLYVALTHRVALARGASPSER
5   LEULYSLYSALALEUMETMETARGGLYLEU
6   ILEPROGLUCYSCYSALAVALTYRARGILE
7   GLNASPGLYGLULYSLYSPROILEGLYTRP
8   ASPTHRASPILESERTRPLEUTHRGLYGLU
9   GLULEUHISVALGLUVALLEUGLUASNVAL
10   PROLEU

Entity 2, entity_2 - C21 H25 N O8 S - 451.490 Da.

1   6FS

Samples:

sample_1: B-RAF-RBD:Rigosertib Complex I, [U-99% 13C; U-99% 15N], 200 uM; 6FS ligand, [U-99% 13C; U-99% 15N], 200 uM; NaCl 200 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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