BMRB Entry 15230

Title:
1H, 13C and 15N resonance assignments for the small GTPase RalB in its active conformation
Deposition date:
2007-04-30
Original release date:
2007-08-22
Authors:
Prasannan, Sunil; Fenwick, R.; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen
Citation:

Citation: Prasannan, Sunil; Fenwick, R. Bryn; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen. "1H, 13C and 15N resonance assignments for the small G protein RalB in its active conformation"  Biomol. NMR Assignments 1, 147-149 (2007).
PubMed: 19636851

Assembly members:

Assembly members:
RalB, polymer, 186 residues, Formula weight is not available
GNP, non-polymer, Formula weight is not available
MG, non-polymer, Formula weight is not available
WATER, water, 18.015 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: pET16b

Data sets:
Data typeCount
13C chemical shifts776
15N chemical shifts178
1H chemical shifts1243
T1 relaxation values127
T2 relaxation values127
heteronuclear NOE values127
order parameters127

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RalB1
2GMPPNP2
3MAGNESIUM ION3
4BOUND WATER, 14
5BOUND WATER, 24

Entities:

Entity 1, RalB 186 residues - Formula weight is not available

Residues 0 (H) from His-Tag. Residues Met1 to Ser11 not assigned, due to proteolysis

1   HISMETALAALAASNLYSSERLYSGLYGLN
2   SERSERLEUALALEUHISLYSVALILEMET
3   VALGLYSERGLYGLYVALGLYLYSSERALA
4   LEUTHRLEUGLNPHEMETTYRASPGLUPHE
5   VALGLUASPTYRGLUPROTHRLYSALAASP
6   SERTYRARGLYSLYSVALVALLEUASPGLY
7   GLUGLUVALGLNILEASPILELEUASPTHR
8   ALAGLYLEUGLUASPTYRALAALAILEARG
9   ASPASNTYRPHEARGSERGLYGLUGLYPHE
10   LEULEUVALPHESERILETHRGLUHISGLU
11   SERPHETHRALATHRALAGLUPHEARGGLU
12   GLNILELEUARGVALLYSALAGLUGLUASP
13   LYSILEPROLEULEUVALVALGLYASNLYS
14   SERASPLEUGLUGLUARGARGGLNVALPRO
15   VALGLUGLUALAARGSERLYSALAGLUGLU
16   TRPGLYVALGLNTYRVALGLUTHRSERALA
17   LYSTHRARGALAASNVALASPLYSVALPHE
18   PHEASPLEUMETARGGLUILEARGTHRLYS
19   LYSMETSERGLUASNLYS

Entity 2, GMPPNP - Formula weight is not available

1   GNP

Entity 3, MAGNESIUM ION - Formula weight is not available

1   MG

Entity 4, BOUND WATER, 1 - 18.015 Da.

1   HOH

Samples:

sample_1: RalB, [U-99% 13C; U-99% 15N], 0.6 mM; GMPPNP, none, 0.6 mM; Magnesium chloride, none, 1 mM; sodium chloride, none, 100 mM; D2O, none, 10%; sodium azide, none, 0.05%; sodium phosphate, none, 50 mM

sample_2: RalB, [U-99% 15N], 0.6 mM; GMPPNP, none, 0.6 mM; Magnesium chloride, none, 1 mM; sodium chloride, none, 100 mM; D2O, none, 10%; sodium azide, none, 0.05%; sodium phosphate, none, 50 mM

sample_3: RalB, none, 0.6 mM; GMPPNP, none, 0.6 mM; Magnesium chloride, none, 1 mM; sodium chloride, none, 100 mM; D2O, none, 10%; sodium azide, none, 0.05%; sodium phosphate, none, 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

AZARA, W Boucher - processing

ANALYSIS, W. Vranken, W. Boucher, T. Stevens, R. Fogh, A. Pajon, M. Llinas, E. Ulrich, J. Markley, J. Ionides, E. Laue - chemical shift assignment, data analysis, peak picking

CNS, A Brunger, P Adams, M Clore, P Gros, M Nilges and R Read - refinement, structure solution

TALOS, G Cornilescu, F Delaglio and A Bax - torsion angle prediction

ARIA, J Linge, S O'Donoghue and M Nilges - refinement, structure solution

Tensor2, P. Dosset, J-C. Hus, M. Blackledge, D. Marion - Model-free analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 800 MHz

Related Database Links:

GB AAM12625

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