BMRB Entry 6261
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6261
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Title: NMR STRUCTURE OF THE SH3 DOMAIN OF HUMAN LYN TYROSINE KINASE PubMed: 16155203
Deposition date: 2004-07-13 Original release date: 2005-10-17
Authors: Bauer, Finn; Schweimer, Kristian; Hoffmann, Silke; Roesch, Paul; Sticht, Heinrich
Citation: Bauer, Finn; Schweimer, Kristian; Meiselbach, Heike; Hoffmann, Silke; Roesch, Paul; Sticht, Heinrich. "Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity" Protein Sci. 14, 2487-2498 (2005).
Assembly members:
SH3 domain of the Lyn kinase, polymer, 68 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: recombinant technology
Entity Sequences (FASTA):
SH3 domain of the Lyn kinase: GPLGSPEEQGDIVVALYPYD
GIHPDDLSFKKGEKMKVLEE
HGEWWKAKSLLTKKEGFIPS
NYVAKLNT
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 495 |
| 13C chemical shifts | 275 |
| 15N chemical shifts | 67 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LynSH3 monomer | 1 |
Entities:
Entity 1, LynSH3 monomer 68 residues - Formula weight is not available
| 1 | GLY | PRO | LEU | GLY | SER | PRO | GLU | GLU | GLN | GLY | ||||
| 2 | ASP | ILE | VAL | VAL | ALA | LEU | TYR | PRO | TYR | ASP | ||||
| 3 | GLY | ILE | HIS | PRO | ASP | ASP | LEU | SER | PHE | LYS | ||||
| 4 | LYS | GLY | GLU | LYS | MET | LYS | VAL | LEU | GLU | GLU | ||||
| 5 | HIS | GLY | GLU | TRP | TRP | LYS | ALA | LYS | SER | LEU | ||||
| 6 | LEU | THR | LYS | LYS | GLU | GLY | PHE | ILE | PRO | SER | ||||
| 7 | ASN | TYR | VAL | ALA | LYS | LEU | ASN | THR |
Samples:
sample_1: SH3 domain of the Lyn kinase, [U-99% 13C; U-98% 15N], 1.5 mM
Ex-cond_1: pH: 6.4; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-13C NOESY | sample_1 | not available | Ex-cond_1 |
| 1H-15N NOESY | sample_1 | not available | Ex-cond_1 |
| CBCACONH | sample_1 | not available | Ex-cond_1 |
| HNCA | sample_1 | not available | Ex-cond_1 |
| HNCACB | sample_1 | not available | Ex-cond_1 |
| HNCO | sample_1 | not available | Ex-cond_1 |
| CCONH | sample_1 | not available | Ex-cond_1 |
| HNHA | sample_1 | not available | Ex-cond_1 |
| HCCHTOCSY | sample_1 | not available | Ex-cond_1 |
Software:
NMRview v5.0.4 -
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAF83183 BAG60841 BAI45692 |
| GB | AAA59540 AAB50019 AAH59394 AAH68551 AAH75001 |
| PRF | 2006286C |
| REF | NP_001104567 NP_002341 XP_001087049 XP_002805388 XP_002805389 |
| SP | P07948 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts