BMRB Entry 30047

Title:
Solution structure of Ras Binding Domain (RBD) of B-Raf
Deposition date:
2016-03-29
Original release date:
2016-09-30
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.

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: pET29a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts365
15N chemical shifts76
1H chemical shifts588

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

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

Samples:

sample_1: B-RAF RBD, [U-99% 15N], 200 uM

sample_2: B-RAF RBD, [U-99% 13C; U-99% 15N], 200 uM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_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 HCCH-TOCSYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_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 600 MHz
  • Bruker Avance 700 MHz
  • 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