BMRB Entry 25082
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25082
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: Fyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide
Deposition date: 2014-07-09 Original release date: 2015-07-13
Authors: Huculeci, Radu; Buts, Lieven; Lenaerts, Tom; van Nuland, Nico
Citation: Huculeci, Radu; Cilia, Elisa; Buts, Lieven; Houben, Klaartje; van Nuland, Nico; Lenaerts, Tom. "Dynamically coupled residues within the SH2 domain of FYN are key to unlock its activity" Not known ., .-..
Assembly members:
entity_1, polymer, 122 residues, 11690.439 Da.
entity_2, polymer, 10 residues, 1254.209 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):
entity_1: MGSSHHHHHHSSGLVPRGSH
MEWYFGKLGRKDAERQLLSF
GNPRGTFLIRESETTKGAYS
LSIRDWDDMKGDHVKHYKIR
KLDNGGYYITTRAQFETLQQ
LVQHYSERAAGLCCRLVVPC
HK
entity_2: EPQYQPGENL
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 57 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Fyn SH2 domain | 1 |
| 2 | natural inhibitory phosphotyrosine peptide | 2 |
Entities:
Entity 1, Fyn SH2 domain 122 residues - 11690.439 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | GLU | TRP | TYR | PHE | GLY | LYS | LEU | GLY | ARG | ||||
| 4 | LYS | ASP | ALA | GLU | ARG | GLN | LEU | LEU | SER | PHE | ||||
| 5 | GLY | ASN | PRO | ARG | GLY | THR | PHE | LEU | ILE | ARG | ||||
| 6 | GLU | SER | GLU | THR | THR | LYS | GLY | ALA | TYR | SER | ||||
| 7 | LEU | SER | ILE | ARG | ASP | TRP | ASP | ASP | MET | LYS | ||||
| 8 | GLY | ASP | HIS | VAL | LYS | HIS | TYR | LYS | ILE | ARG | ||||
| 9 | LYS | LEU | ASP | ASN | GLY | GLY | TYR | TYR | ILE | THR | ||||
| 10 | THR | ARG | ALA | GLN | PHE | GLU | THR | LEU | GLN | GLN | ||||
| 11 | LEU | VAL | GLN | HIS | TYR | SER | GLU | ARG | ALA | ALA | ||||
| 12 | GLY | LEU | CYS | CYS | ARG | LEU | VAL | VAL | PRO | CYS | ||||
| 13 | HIS | LYS |
Entity 2, natural inhibitory phosphotyrosine peptide 10 residues - 1254.209 Da.
| 1 | GLU | PRO | GLN | PTR | GLN | PRO | GLY | GLU | ASN | LEU |
Samples:
sample_1: entity_1, [U-99% 13C; U-99% 15N], 0.93 mM; entity_2 1.2 mM
sample_conditions_1: ionic strength: 0 M; pH: 6.50; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CCPNMR, CCPN - chemical shift assignment, peak picking
HADDOCK, Alexandre Bonvin - refinement, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Varian Varian NMR Systems 600 MHz
- Varian Varian NMR Systems 800 MHz
Related Database Links:
| BMRB | 25081 |
| PDB | |
| DBJ | BAE33766 BAG70107 BAG70240 BAI46902 |
| EMBL | CAA36435 |
| GB | AAA36615 AAA49719 AAA82942 AAC08285 AAH32496 |
| REF | NP_001071440 NP_001073675 NP_001079077 NP_001080120 NP_001116365 |
| SP | A0JNB0 A1Y2K1 P06241 P13406 P39688 |
| TPG | DAA26259 |