BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17608

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17608
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: RLIP76 (GAP-GBD)   PubMed: 21915608

Deposition date: 2011-04-28 Original release date: 2011-10-12

Authors: Rajasekar, Karthik; Campbell, Louise; Nietlispach, Daniel; Owen, Darerca; Mott, Helen

Citation: Rajasekar, Karthik; Campbell, Louise; Nietlispach, Daniel; Owen, Darerca; Mott, Helen. "1H, 13C and 15N resonance assignments of the GTPase-activating (GAP) and Ral binding domains (GBD) of RLIP76 (RalBP1)."  Biomol. NMR Assignments 6, 119-122 (2012).

Assembly members:
RLIP76-GAP-GBD, polymer, 265 residues, 30973 Da.

Natural source:   Common Name: Humans   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-GAP-GBD: HMPNLKPIFGIPLADAVERT MMYDGIRLPAVFRECIDYVE KYGMKCEGIYRVSGIKSKVD ELKAAYDREESTNLEDYEPN TVASLLKQYLRDLPENLLTK ELMPRFEEACGRTTETEKVQ EFQRLLKELPECNYLLISWL IVHMDHVIAKELETKMNIQN ISIVLSPTVQISNRVLYVFF THVQELFGNVVLKQVMKPLR WSNMATMPTLPETQAGIKEE IRRQEFLLNCLHRDLQGGIK DLSKEERLWEVQRILTALKR KLREA

Data sets:
Data typeCount
13C chemical shifts1122
15N chemical shifts269
1H chemical shifts1871

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RLIP76-GAP-GBD1

Entities:

Entity 1, RLIP76-GAP-GBD 265 residues - 30973 Da.

Residues 182- 446

1   HISMETPROASNLEULYSPROILEPHEGLY
2   ILEPROLEUALAASPALAVALGLUARGTHR
3   METMETTYRASPGLYILEARGLEUPROALA
4   VALPHEARGGLUCYSILEASPTYRVALGLU
5   LYSTYRGLYMETLYSCYSGLUGLYILETYR
6   ARGVALSERGLYILELYSSERLYSVALASP
7   GLULEULYSALAALATYRASPARGGLUGLU
8   SERTHRASNLEUGLUASPTYRGLUPROASN
9   THRVALALASERLEULEULYSGLNTYRLEU
10   ARGASPLEUPROGLUASNLEULEUTHRLYS
11   GLULEUMETPROARGPHEGLUGLUALACYS
12   GLYARGTHRTHRGLUTHRGLULYSVALGLN
13   GLUPHEGLNARGLEULEULYSGLULEUPRO
14   GLUCYSASNTYRLEULEUILESERTRPLEU
15   ILEVALHISMETASPHISVALILEALALYS
16   GLULEUGLUTHRLYSMETASNILEGLNASN
17   ILESERILEVALLEUSERPROTHRVALGLN
18   ILESERASNARGVALLEUTYRVALPHEPHE
19   THRHISVALGLNGLULEUPHEGLYASNVAL
20   VALLEULYSGLNVALMETLYSPROLEUARG
21   TRPSERASNMETALATHRMETPROTHRLEU
22   PROGLUTHRGLNALAGLYILELYSGLUGLU
23   ILEARGARGGLNGLUPHELEULEUASNCYS
24   LEUHISARGASPLEUGLNGLYGLYILELYS
25   ASPLEUSERLYSGLUGLUARGLEUTRPGLU
26   VALGLNARGILELEUTHRALALEULYSARG
27   LYSLEUARGGLUALA

Samples:

sample_1: RLIP76-GAP-GBD 0.7 mM; TRIS 20 mM; sodium chloride 100 mM; sodium azide 0.05%; DTT 5 mM; H20 90%; D20 10%

sample_2: RLIP76-GAP-GBD, [U-100% 15N], 0.7 mM; TRIS 20 mM; sodium chloride 100 mM; sodium azide 0.05%; DTT 5 mM; H20 90%; D20 10%

sample_3: RLIP76-GAP-GBD, [U-100% 13C; U-100% 15N], 0.6 mM; TRIS 20 mM; sodium chloride 100 mM; sodium azide 0.05%; DTT 5 mM; H20 90%; D20 10%

sample_4: RLIP76-GAP-GBD, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; TRIS 20 mM; sodium chloride 100 mM; sodium azide 0.05%; DTT 5 mM; H20 90%; D20 10%

sample_conditions_1: pH: 7.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N-TROSYsample_2isotropicsample_conditions_1
3D HNCAsample_4isotropicsample_conditions_1
3D HN(CO)CAsample_4isotropicsample_conditions_1
3D HN(CA)CBsample_4isotropicsample_conditions_1
3D HN(COCA)CBsample_4isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HBHA(CBCACO)NHsample_3isotropicsample_conditions_1
3D H(C)CH TOCSYsample_3isotropicsample_conditions_1
3D (H)CCH TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D H(C)CH COSYsample_3isotropicsample_conditions_1

Software:

AZARA, Boucher - processing

CCPN-Analysis, (CCPN)- Vranken et al. - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAD93161 BAJ20384
GB AAB00103 AAH13126 AAT44527 ABM82530 ABW03389
REF NP_006779 XP_001138420 XP_001138511 XP_002757099 XP_002828087
SP Q15311

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts