BMRB Entry 11277
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11277
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: Solution Structure of the RA Domain in the Human Link Guanine Nucleotide Exchange Factor II (Link-GEFII)
Deposition date: 2010-08-09 Original release date: 2011-08-18
Authors: Zhao, C.; Kigawa, T.; Yoneyama, M.; Koshiba, S.; Harada, T.; Watanabe, S.; Yokoyama, S.
Citation: Zhao, C.; Kigawa, T.; Yoneyama, M.; Koshiba, S.; Harada, T.; Watanabe, S.; Yokoyama, S.. "Solution Structure of the RA Domain in the Human Link Guanine Nucleotide Exchange Factor II (Link-GEFII)" . ., .-..
Assembly members:
RA domain, polymer, 120 residues, Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
RA domain: GSSGSSGDEIFCRVYMPDHS
YVTIRSRLSASVQDILGSVT
EKLQYSEEPAGREDSLILVA
VSSSGEKVLLQPTEDCVFTA
LGINSHLFACTRDSYEALVP
LPEEIQVSPGDTEISGPSSG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 487 |
15N chemical shifts | 108 |
1H chemical shifts | 752 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RA domain | 1 |
Entities:
Entity 1, RA domain 120 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | ASP | GLU | ILE | |
2 | PHE | CYS | ARG | VAL | TYR | MET | PRO | ASP | HIS | SER | |
3 | TYR | VAL | THR | ILE | ARG | SER | ARG | LEU | SER | ALA | |
4 | SER | VAL | GLN | ASP | ILE | LEU | GLY | SER | VAL | THR | |
5 | GLU | LYS | LEU | GLN | TYR | SER | GLU | GLU | PRO | ALA | |
6 | GLY | ARG | GLU | ASP | SER | LEU | ILE | LEU | VAL | ALA | |
7 | VAL | SER | SER | SER | GLY | GLU | LYS | VAL | LEU | LEU | |
8 | GLN | PRO | THR | GLU | ASP | CYS | VAL | PHE | THR | ALA | |
9 | LEU | GLY | ILE | ASN | SER | HIS | LEU | PHE | ALA | CYS | |
10 | THR | ARG | ASP | SER | TYR | GLU | ALA | LEU | VAL | PRO | |
11 | LEU | PRO | GLU | GLU | ILE | GLN | VAL | SER | PRO | GLY | |
12 | ASP | THR | GLU | ILE | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: RA domain, [U-13C; U-15N], 1.21 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296.0 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20030801, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B. A. - data analysis
Kujira v0.9732, Kobayashi, N. - data analysis
CYANA v1.0.8, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
PDB | |
DBJ | BAG36274 BAG57820 BAH14121 |
EMBL | CAH91648 |
GB | AAF22003 AAI15375 AAI15376 ABG81429 EAW60645 |
REF | NP_001125968 NP_001192336 NP_001290462 NP_001290463 NP_057423 |
SP | Q5R9B2 Q9UHV5 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts