BMRB Entry 15524

Title:
1H and 15N Resonance assignments for the human RLIP76 Ral binding domain
Deposition date:
2007-10-15
Original release date:
2008-10-14
Authors:
Fenwick, Robert; Prasannan, Sunil; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen
Citation:

Citation: Fenwick, R Bryn; Prasannan, Sunil; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen. "Resonance assignments for the RLIP76 Ral binding domain in its free form and in complex with the small G protein RalB"  Biomol. NMR Assignments 2, 191-194 (2008).
PubMed: 19636902

Assembly members:

Assembly members:
RLIP76, polymer, 56 residues, Formula weight is not available

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: pGEX-2T

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts60
1H chemical shifts419

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RLIP761

Entities:

Entity 1, RLIP76 56 residues - Formula weight is not available

The first two residues are a tag remnant. The protein starts at E393 and ends at A446

1   GLYSERGLUTHRGLNALAGLYILELYSGLU
2   GLUILEARGARGGLNGLUPHELEULEUASN
3   SERLEUHISARGASPLEUGLNGLYGLYILE
4   LYSASPLEUSERLYSGLUGLUARGLEUTRP
5   GLUVALGLNARGILELEUTHRALALEULYS
6   ARGLYSLEUARGGLUALA

Samples:

sample_1: RLIP76, [U-98% 15N], 0.8 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 10 mM; magnesium chloride 1 mM

sample_conditions_1: pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

AZARA, Boucher - processing

Analysis, Vranken, Boucher, Stevens, Fogh, Pajon, Llinas, Ulrich, Markley, Ionides and Laue - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 15525
PDB
GB AAI45321
REF XP_004656898

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