BMRB Entry 5223
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5223
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Citation: Schweimer, K.; Hoffmann, S.; Bauer, F.; Friedrich, U.; Kardinal, C.; Feller, S.; Biesinger, B.; Sticht, H.. "Structural Investigation of the Binding of a Herpesviral Protein to the SH3
Domain of Tyrosine Kinase Lck " Biochemistry 41, 5120-5130 (2002).
PubMed: 11955060
Assembly members:
SH3 domain of the tyrosine-protein kinase Lck, polymer, 63 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 Host organism: Escherichia coli
Entity Sequences (FASTA):
SH3 domain of the tyrosine-protein kinase Lck: GSPLQDNLVIALHSYEPSHD
GDLGFEKGEQLRILEQSGEW
WKAQSLTTGQEGFIPFNFVA
KAN
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 430 |
| 13C chemical shifts | 178 |
| 15N chemical shifts | 68 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LckSH3 | 1 |
Entities:
Entity 1, LckSH3 63 residues - Formula weight is not available
| 1 | GLY | SER | PRO | LEU | GLN | ASP | ASN | LEU | VAL | ILE | ||||
| 2 | ALA | LEU | HIS | SER | TYR | GLU | PRO | SER | HIS | ASP | ||||
| 3 | GLY | ASP | LEU | GLY | PHE | GLU | LYS | GLY | GLU | GLN | ||||
| 4 | LEU | ARG | ILE | LEU | GLU | GLN | SER | GLY | GLU | TRP | ||||
| 5 | TRP | LYS | ALA | GLN | SER | LEU | THR | THR | GLY | GLN | ||||
| 6 | GLU | GLY | PHE | ILE | PRO | PHE | ASN | PHE | VAL | ALA | ||||
| 7 | LYS | ALA | ASN |
Samples:
sample_1: SH3 domain of the tyrosine-protein kinase Lck 1.2 mM
sample_cond_1: pH: 6.4; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-edited NOESY | not available | not available | not available |
| 3D 13C-edited NOESY | not available | not available | not available |
| 2D 15N-filtered NOESY | not available | not available | not available |
| 3D CT-HNCO | not available | not available | not available |
| 3D CT-HNCA | not available | not available | not available |
| 3D HNCACB | not available | not available | not available |
| 3D CBCA(CO)NH | not available | not available | not available |
| 3D HNHA | not available | not available | not available |
| 3D HBHA(CO)NH | not available | not available | not available |
| 3D C(CO)NH | not available | not available | not available |
| 3D H(CCO)NH | not available | not available | not available |
| 1H-13C CT-HSQC | not available | not available | not available |
| 3D H(C)CH-COSY | not available | not available | not available |
Software:
NMRView -
NDEE -
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| BMRB | 4860 5794 |
| PDB | |
| DBJ | BAC40086 BAG64189 BAI45973 |
| EMBL | CAA27234 CAA28691 CAA32211 CAC44027 CAI23831 |
| GB | AAA18225 AAB59674 AAC50287 AAF34794 AAH11474 |
| PRF | 1203381A 2201317A |
| REF | NP_001036236 NP_001094179 NP_001155904 NP_001155905 NP_005347 |
| SP | P06239 P06240 Q01621 |
| TPE | CAD55807 |
| AlphaFold | P06239 P06240 Q01621 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks