BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15525

Title: 1H, 13C and 15N Resonance assignments for the human RLIP76 Ral binding domain and RalB in complex   PubMed: 19636902

Authors: Fenwick, Robert; Prasannan, Sunil; Campbell, Louise; Evetts, Katrina; Nietlispach, Daniel; Owen, Darerca; Mott, Helen

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).

Assembly members:
RLIP76, polymer, 56 residues, Formula weight is not available
RalB, polymer, 188 residues, Formula weight is not available
GNP, non-polymer, 522.196 Da.
MG, non-polymer, 24.305 Da.
HOH, non-polymer, 18.015 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
RLIP76: GSETQAGIKEEIRRQEFLLN SLHRDLQGGIKDLSKEERLW EVQRILTALKRKLREA
RalB: GSHMAANKSKGQSSLALHKV IMVGSGGVGKSALTLQFMYD EFVEDYEPTKADSYRKKVVL DGEEVQIDILDTAGLEDYAA IRDNYFRSGEGFLLVFSITE HESFTATAEFREQILRVKAE EDKIPLLVVGNKSDLEERRQ VPVEEARSKAEEWGVQYVET SAKTRANVDKVFFDLMREIR TKKMSENK

Data sets:
Data typeCount
13C chemical shifts1007
15N chemical shifts250
1H chemical shifts1707

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RLIP761
2RalB2
3GMPPNP3
4Magnesium ion4
5BOUND WATER, 15
6BOUND WATER, 25

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

Entity 2, RalB 188 residues - Formula weight is not available

The first three residues are a tag remnant. The protein starts at M1 and ends at K185

1   GLYSERHISMETALAALAASNLYSSERLYS
2   GLYGLNSERSERLEUALALEUHISLYSVAL
3   ILEMETVALGLYSERGLYGLYVALGLYLYS
4   SERALALEUTHRLEUGLNPHEMETTYRASP
5   GLUPHEVALGLUASPTYRGLUPROTHRLYS
6   ALAASPSERTYRARGLYSLYSVALVALLEU
7   ASPGLYGLUGLUVALGLNILEASPILELEU
8   ASPTHRALAGLYLEUGLUASPTYRALAALA
9   ILEARGASPASNTYRPHEARGSERGLYGLU
10   GLYPHELEULEUVALPHESERILETHRGLU
11   HISGLUSERPHETHRALATHRALAGLUPHE
12   ARGGLUGLNILELEUARGVALLYSALAGLU
13   GLUASPLYSILEPROLEULEUVALVALGLY
14   ASNLYSSERASPLEUGLUGLUARGARGGLN
15   VALPROVALGLUGLUALAARGSERLYSALA
16   GLUGLUTRPGLYVALGLNTYRVALGLUTHR
17   SERALALYSTHRARGALAASNVALASPLYS
18   VALPHEPHEASPLEUMETARGGLUILEARG
19   THRLYSLYSMETSERGLUASNLYS

Entity 3, GMPPNP - C10 H17 N6 O13 P3 - 522.196 Da.

1   GNP

Entity 4, Magnesium ion - Mg - 24.305 Da.

1   MG

Entity 5, BOUND WATER, 1 - H2 O - 18.015 Da.

1   HOH

Samples:

15N_RLIP76: RLIP76, [U-98% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; RalB 0.66 mM; magnesium chloride 1 mM

13C_15N_RLIP76: RLIP76, [U-98% 13C; U-98% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; RalB 0.66 mM; magnesium chloride 1 mM

15N_RalB: RalB, [U-98% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; RLIP76 0.66 mM; magnesium chloride 1 mM

13C_15N_RalB: RalB, [U-98% 13C; U-98% 15N], 0.6 mM; D2O, [U-100% 2H], 10%; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; RLIP76 0.66 mM; magnesium chloride 1 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C_15N_RLIP76isotropicsample_conditions_1
3D HNCA13C_15N_RLIP76isotropicsample_conditions_1
3D HNCO13C_15N_RLIP76isotropicsample_conditions_1
3D HN(CO)CA13C_15N_RLIP76isotropicsample_conditions_1
3D HNCACB13C_15N_RLIP76isotropicsample_conditions_1
3D (H)C(CCO)NH13C_15N_RLIP76isotropicsample_conditions_1
3D HBHA(CO)NH13C_15N_RLIP76isotropicsample_conditions_1
3D HCCH-TOCSY13C_15N_RLIP76isotropicsample_conditions_1
3D 1H-15N NOESY15N_RLIP76isotropicsample_conditions_1
3D 1H-13C NOESY13C_15N_RLIP76isotropicsample_conditions_1
2D 1H-13C HSQC13C_15N_RLIP76isotropicsample_conditions_1
2D 1H-15N HSQC13C_15N_RalBisotropicsample_conditions_2
3D HNCA13C_15N_RalBisotropicsample_conditions_2
3D HNCO13C_15N_RalBisotropicsample_conditions_2
3D HN(CO)CA13C_15N_RalBisotropicsample_conditions_2
3D HNCACB13C_15N_RalBisotropicsample_conditions_2
3D (H)C(CCO)NH13C_15N_RalBisotropicsample_conditions_2
3D CBCA(CO)NH13C_15N_RalBisotropicsample_conditions_2
3D HCCH-TOCSY13C_15N_RalBisotropicsample_conditions_2
3D 1H-15N NOESY15N_RalBisotropicsample_conditions_2
3D 1H-13C NOESY13C_15N_RalBisotropicsample_conditions_2
2D 1H-13C HSQC13C_15N_RalBisotropicsample_conditions_2

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
  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 15524 15230 15803
PDB
GB AAI45321 AAA60250 AAH18163 AAI46174 AAM12625 AAP35599
REF XP_004656898 NP_001091454 NP_001126995 NP_001244728 NP_002872 XP_001492315
DBJ BAE02438 BAG35360 BAG64302 BAJ20798
EMBL CAA33119 CAH93398
SP P11234 Q4R379 Q5R4B8
TPG DAA32595