BMRB Entry 17367
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17367
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Title: Assignments of Drosophila cytotoxic T-lymphocyte antigen 2 (CTLA-2) like protein, crammer at pH3 PubMed: 22150223
Deposition date: 2010-12-19 Original release date: 2012-07-25
Authors: Tzeng, Tien-Sheng; Hsu, Shang-Te Danny; Lyu, Ping-Chiang
Citation: Tseng, Tien-Sheng; Cheng, Chao-Sheng; Chen, Dian-Jiun; Shih, Min-Fang; Liu, Yu-Nan; Hsu, Shang-Te; Lyu, Ping-Chiang. "A Molten Globule-to-Ordered Structure Transition of Drosophila melanogaster Crammer Is Required for its Ability to Inhibit Cathepsin" Biochem. J. 442, 563-572 (2012).
Assembly members:
C72S_monomer, polymer, 80 residues, Formula weight is not available
Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
C72S_monomer: MMSLVSDEEWVEYKSKFDKN
YEAEEDLMRRRIYAESKARI
EEHNRKFEKGEVTWKMGINH
LADLTPEEFAQRSGKKVPPN
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 224 |
15N chemical shifts | 74 |
1H chemical shifts | 73 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | C72S monomer | 1 |
Entities:
Entity 1, C72S monomer 80 residues - Formula weight is not available
1 | MET | MET | SER | LEU | VAL | SER | ASP | GLU | GLU | TRP | |
2 | VAL | GLU | TYR | LYS | SER | LYS | PHE | ASP | LYS | ASN | |
3 | TYR | GLU | ALA | GLU | GLU | ASP | LEU | MET | ARG | ARG | |
4 | ARG | ILE | TYR | ALA | GLU | SER | LYS | ALA | ARG | ILE | |
5 | GLU | GLU | HIS | ASN | ARG | LYS | PHE | GLU | LYS | GLY | |
6 | GLU | VAL | THR | TRP | LYS | MET | GLY | ILE | ASN | HIS | |
7 | LEU | ALA | ASP | LEU | THR | PRO | GLU | GLU | PHE | ALA | |
8 | GLN | ARG | SER | GLY | LYS | LYS | VAL | PRO | PRO | ASN |
Samples:
sample_1: C72S_monomer, [U-98% 13C; U-98% 15N], 0.5 mM
sample_conditions_1: pH: 3; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HCACO | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY_and_NMRpipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, processing
NMR spectrometers:
- Varian INOVA 700 MHz
Related Database Links:
BMRB | 16719 |
PDB | |
GB | AAF57567 ACJ13252 EDV55205 EDW48595 EDX07811 |
REF | NP_611420 XP_001974805 XP_002034582 XP_002082226 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts