BMRB Entry 6503
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6503
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Title: 1H, 13C, and 15N complete chemical shift assignments for the apo v-Src SH2 domain PubMed: 16211495
Deposition date: 2005-02-16 Original release date: 2005-10-24
Authors: Taylor, Jonathan; Williams, Mark; Ababou, Abdessamad; Ladbury, John
Citation: Taylor, Jonathan; Fawaz, Radwan; Ababou, Abdessamad; Williams, Mark; Ladbury, John. "NMR Assignment of the Apo and Peptide-bound SH2 Domain from the Rous Sarcoma Viral Protein Src" J. Biomol. NMR 32, 339-339 (2005).
Assembly members:
v-Src SH2 domain, polymer, 106 residues, 12168 Da.
Natural source: Common Name: Rous Sarcoma Virus Taxonomy ID: 11886 Superkingdom: viruses Kingdom: not available Genus/species: Alpharetrovirus Rous Sarcoma Virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
v-Src SH2 domain: QAEEWYFGKITRRESERLLL
NPENPRGTFLVRESETTKGA
YCLSVSDFDNAKGLNVKHYK
IRKLDSGGFYITSRTQFSSL
QQLVAYYSKHADGLCHRLTN
VCPTSK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 456 |
15N chemical shifts | 120 |
1H chemical shifts | 702 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | v-Src SH2 | 1 |
Entities:
Entity 1, v-Src SH2 106 residues - 12168 Da.
1 | GLN | ALA | GLU | GLU | TRP | TYR | PHE | GLY | LYS | ILE | ||||
2 | THR | ARG | ARG | GLU | SER | GLU | ARG | LEU | LEU | LEU | ||||
3 | ASN | PRO | GLU | ASN | PRO | ARG | GLY | THR | PHE | LEU | ||||
4 | VAL | ARG | GLU | SER | GLU | THR | THR | LYS | GLY | ALA | ||||
5 | TYR | CYS | LEU | SER | VAL | SER | ASP | PHE | ASP | ASN | ||||
6 | ALA | LYS | GLY | LEU | ASN | VAL | LYS | HIS | TYR | LYS | ||||
7 | ILE | ARG | LYS | LEU | ASP | SER | GLY | GLY | PHE | TYR | ||||
8 | ILE | THR | SER | ARG | THR | GLN | PHE | SER | SER | LEU | ||||
9 | GLN | GLN | LEU | VAL | ALA | TYR | TYR | SER | LYS | HIS | ||||
10 | ALA | ASP | GLY | LEU | CYS | HIS | ARG | LEU | THR | ASN | ||||
11 | VAL | CYS | PRO | THR | SER | LYS |
Samples:
Sample_1: v-Src SH2 domain, [U-95% 13C; U-90% 15N], 0.5 mM; NaCl 50 mM
Sample_2: v-Src SH2 domain, [U-90% 15N], 0.5 mM
Conditions: ionic strength: 0.05 M; pH: 6.0; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
HNCA | not available | not available | not available |
HNCACB | not available | not available | not available |
HNCO | not available | not available | not available |
CBCACONH | not available | not available | not available |
C(CO)NH | not available | not available | not available |
1H-15N HSQC | not available | not available | not available |
1H-13C HSQC | not available | not available | not available |
1H-15N NOESY-HSQC | not available | not available | not available |
1H-15N TOWNY-HSQC | not available | not available | not available |
1H-13C NOESY-HSQC | not available | not available | not available |
1H-13C HCCH-TOCSY | not available | not available | not available |
HNHA | not available | not available | not available |
HNHB | not available | not available | not available |
CBHD | not available | not available | not available |
Software:
ANSIG v3.3 - Manual peak assignment
NMR spectrometers:
- Varian UNITY-INOVA 800 MHz
- Varian UNITY-INOVA 600 MHz
- Varian UNITY-INOVA 500 MHz
Related Database Links:
PDB | |
DBJ | BAA01500 BAE26865 BAI47379 |
EMBL | CAA23696 CAA24495 CAA26485 CAA32012 CAA36156 |
GB | AAA40135 AAA42563 AAA42565 AAA42573 AAA42581 |
PRF | 0903255A |
REF | NP_001020566 NP_001104274 NP_001248263 NP_005408 NP_033297 |
SP | P00523 P00524 P00525 P05480 P12931 |
TPG | DAA23281 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts