BMRB Entry 17080
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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/BMR17080
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Title: Shc-PTB:biphosphorylated integrin beta3 cytoplasmic tail complex (1:1) PubMed: 20739287
Deposition date: 2010-07-27 Original release date: 2010-09-02
Authors: Deshmukh, Lalit; Gorbatyuk, Vitaliy; Vinogradova, Olga
Citation: Deshmukh, Lalit; Gorbatyuk, Vitaliy; Vinogradova, Olga. "Integrin {beta}3 phosphorylation dictates its complex with the Shc phosphotyrosine-binding (PTB) domain." J. Biol. Chem. 285, 34875-34884 (2010).
Assembly members:
Shc-PTB, polymer, 211 residues, 20996.234 Da.
Integrin_beta3, polymer, 27 residues, 3284.411 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):
Shc-PTB: GSSHHHHHHSSGLVPRGSHM
GQLGGEEWTRHGSFVNKPTR
GWLHPNDKVMGPGVSYLVRY
MGCVEVLQSMRALDFNTRTQ
VTREAISLVCEAVPGAKGAT
RRRKPCSRPLSSILGRSNLK
FAGMPITLTVSTSSLNLMAA
DCKQIIANHHMQSISFASGG
DPDTAEYVAYVAKDPVNQRA
CHILECPEGLAQDVISTIGQ
AFELRFKQYLR
Integrin_beta3: RAKWDTANNPLXKEATSTFT
NITXRGT
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 720 |
| 15N chemical shifts | 181 |
| 1H chemical shifts | 1322 |
| heteronuclear NOE values | 154 |
| T1 relaxation values | 154 |
| T2 relaxation values | 154 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Shc PTB domain | 1 |
| 2 | Integrin beta3 | 2 |
Entities:
Entity 1, Shc PTB domain 211 residues - 20996.234 Da.
| 1 | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | SER | ||||
| 2 | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | MET | ||||
| 3 | GLY | GLN | LEU | GLY | GLY | GLU | GLU | TRP | THR | ARG | ||||
| 4 | HIS | GLY | SER | PHE | VAL | ASN | LYS | PRO | THR | ARG | ||||
| 5 | GLY | TRP | LEU | HIS | PRO | ASN | ASP | LYS | VAL | MET | ||||
| 6 | GLY | PRO | GLY | VAL | SER | TYR | LEU | VAL | ARG | TYR | ||||
| 7 | MET | GLY | CYS | VAL | GLU | VAL | LEU | GLN | SER | MET | ||||
| 8 | ARG | ALA | LEU | ASP | PHE | ASN | THR | ARG | THR | GLN | ||||
| 9 | VAL | THR | ARG | GLU | ALA | ILE | SER | LEU | VAL | CYS | ||||
| 10 | GLU | ALA | VAL | PRO | GLY | ALA | LYS | GLY | ALA | THR | ||||
| 11 | ARG | ARG | ARG | LYS | PRO | CYS | SER | ARG | PRO | LEU | ||||
| 12 | SER | SER | ILE | LEU | GLY | ARG | SER | ASN | LEU | LYS | ||||
| 13 | PHE | ALA | GLY | MET | PRO | ILE | THR | LEU | THR | VAL | ||||
| 14 | SER | THR | SER | SER | LEU | ASN | LEU | MET | ALA | ALA | ||||
| 15 | ASP | CYS | LYS | GLN | ILE | ILE | ALA | ASN | HIS | HIS | ||||
| 16 | MET | GLN | SER | ILE | SER | PHE | ALA | SER | GLY | GLY | ||||
| 17 | ASP | PRO | ASP | THR | ALA | GLU | TYR | VAL | ALA | TYR | ||||
| 18 | VAL | ALA | LYS | ASP | PRO | VAL | ASN | GLN | ARG | ALA | ||||
| 19 | CYS | HIS | ILE | LEU | GLU | CYS | PRO | GLU | GLY | LEU | ||||
| 20 | ALA | GLN | ASP | VAL | ILE | SER | THR | ILE | GLY | GLN | ||||
| 21 | ALA | PHE | GLU | LEU | ARG | PHE | LYS | GLN | TYR | LEU | ||||
| 22 | ARG |
Entity 2, Integrin beta3 27 residues - 3284.411 Da.
| 1 | ARG | ALA | LYS | TRP | ASP | THR | ALA | ASN | ASN | PRO | ||||
| 2 | LEU | PTR | LYS | GLU | ALA | THR | SER | THR | PHE | THR | ||||
| 3 | ASN | ILE | THR | PTR | ARG | GLY | THR |
Samples:
sample_1: Shc-PTB, [U-99% 13C; U-99% 15N], 0.4 mM; Integrin_beta3 0.8 mM; DTT 5 mM; sodium chloride 50 mM; sodium phosphate 50 mM; DSS 1 mM; H2O 93%; D2O 7%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N edited NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C edited NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C aromatic NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C,15N FilteredTOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C,15N Filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D F1 13C,15N Filtered, F2 13C edited NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N Het NOE | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N T1-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N T2-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMRJ, Varian - collection
CCPN-Analysis v2.1.3, (CCPN-Analysis)-Vranken,Boucher, Stevens, Fogh, Pajon,Llinas,Ulrich,Markley,Ionides,Laue - data analysis, peak picking
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA74950 BAC33706 BAE33083 BAF84832 BAF98733 |
| EMBL | CAA48251 CAA70977 CAH92143 |
| GB | AAA91777 AAB49972 AAC52146 AAH14158 AAH36172 |
| REF | NP_001068773 NP_001106802 NP_001123512 NP_001123513 NP_001126253 |
| SP | P29353 P98083 Q0IIE2 Q5M824 Q5R7W7 |
| TPG | DAA31779 DAA31780 |
| BMRB | 17931 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts