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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.
XML gzip file.
RDF gzip file.
All files associated with the entry
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).
PubMed: 21915608
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 Vector: pET16b
Entity Sequences (FASTA):
RLIP76-GAP-GBD: HMPNLKPIFGIPLADAVERT
MMYDGIRLPAVFRECIDYVE
KYGMKCEGIYRVSGIKSKVD
ELKAAYDREESTNLEDYEPN
TVASLLKQYLRDLPENLLTK
ELMPRFEEACGRTTETEKVQ
EFQRLLKELPECNYLLISWL
IVHMDHVIAKELETKMNIQN
ISIVLSPTVQISNRVLYVFF
THVQELFGNVVLKQVMKPLR
WSNMATMPTLPETQAGIKEE
IRRQEFLLNCLHRDLQGGIK
DLSKEERLWEVQRILTALKR
KLREA
Data type | Count |
13C chemical shifts | 1122 |
15N chemical shifts | 269 |
1H chemical shifts | 1871 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RLIP76-GAP-GBD | 1 |
Entity 1, RLIP76-GAP-GBD 265 residues - 30973 Da.
Residues 182- 446
1 | HIS | MET | PRO | ASN | LEU | LYS | PRO | ILE | PHE | GLY | ||||
2 | ILE | PRO | LEU | ALA | ASP | ALA | VAL | GLU | ARG | THR | ||||
3 | MET | MET | TYR | ASP | GLY | ILE | ARG | LEU | PRO | ALA | ||||
4 | VAL | PHE | ARG | GLU | CYS | ILE | ASP | TYR | VAL | GLU | ||||
5 | LYS | TYR | GLY | MET | LYS | CYS | GLU | GLY | ILE | TYR | ||||
6 | ARG | VAL | SER | GLY | ILE | LYS | SER | LYS | VAL | ASP | ||||
7 | GLU | LEU | LYS | ALA | ALA | TYR | ASP | ARG | GLU | GLU | ||||
8 | SER | THR | ASN | LEU | GLU | ASP | TYR | GLU | PRO | ASN | ||||
9 | THR | VAL | ALA | SER | LEU | LEU | LYS | GLN | TYR | LEU | ||||
10 | ARG | ASP | LEU | PRO | GLU | ASN | LEU | LEU | THR | LYS | ||||
11 | GLU | LEU | MET | PRO | ARG | PHE | GLU | GLU | ALA | CYS | ||||
12 | GLY | ARG | THR | THR | GLU | THR | GLU | LYS | VAL | GLN | ||||
13 | GLU | PHE | GLN | ARG | LEU | LEU | LYS | GLU | LEU | PRO | ||||
14 | GLU | CYS | ASN | TYR | LEU | LEU | ILE | SER | TRP | LEU | ||||
15 | ILE | VAL | HIS | MET | ASP | HIS | VAL | ILE | ALA | LYS | ||||
16 | GLU | LEU | GLU | THR | LYS | MET | ASN | ILE | GLN | ASN | ||||
17 | ILE | SER | ILE | VAL | LEU | SER | PRO | THR | VAL | GLN | ||||
18 | ILE | SER | ASN | ARG | VAL | LEU | TYR | VAL | PHE | PHE | ||||
19 | THR | HIS | VAL | GLN | GLU | LEU | PHE | GLY | ASN | VAL | ||||
20 | VAL | LEU | LYS | GLN | VAL | MET | LYS | PRO | LEU | ARG | ||||
21 | TRP | SER | ASN | MET | ALA | THR | MET | PRO | THR | LEU | ||||
22 | PRO | GLU | THR | GLN | ALA | GLY | ILE | LYS | GLU | GLU | ||||
23 | ILE | ARG | ARG | GLN | GLU | PHE | LEU | LEU | ASN | CYS | ||||
24 | LEU | HIS | ARG | ASP | LEU | GLN | GLY | GLY | ILE | LYS | ||||
25 | ASP | LEU | SER | LYS | GLU | GLU | ARG | LEU | TRP | GLU | ||||
26 | VAL | GLN | ARG | ILE | LEU | THR | ALA | LEU | LYS | ARG | ||||
27 | LYS | LEU | ARG | GLU | ALA |
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
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N-TROSY | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_4 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_4 | isotropic | sample_conditions_1 |
3D HN(CA)CB | sample_4 | isotropic | sample_conditions_1 |
3D HN(COCA)CB | sample_4 | isotropic | sample_conditions_1 |
3D HNCO | sample_4 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CBCACO)NH | sample_3 | isotropic | sample_conditions_1 |
3D H(C)CH TOCSY | sample_3 | isotropic | sample_conditions_1 |
3D (H)CCH TOCSY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
3D H(C)CH COSY | sample_3 | isotropic | sample_conditions_1 |
AZARA, Boucher - processing
CCPN-Analysis, (CCPN)- Vranken et al. - chemical shift assignment
PDB | |
DBJ | BAD93161 BAJ20384 |
GB | AAB00103 AAH13126 AAT44527 ABM82530 ABW03389 |
REF | NP_006779 XP_001138420 XP_001138511 XP_002757099 XP_002828087 |
SP | Q15311 |
AlphaFold | Q15311 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks