BMRB Entry 17411
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17411
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for CHIP (carboxyl terminal of Hsc70-interacting protein) PubMed: 21518764
Deposition date: 2011-01-14 Original release date: 2011-05-03
Authors: Soss, Sarah; Chazin, Walter; Yue, Yuanyuan
Citation: Soss, Sarah; Yue, Yuanyuan; Dhe-Paganon, Sirano; Chazin, Walter. "E2 Conjugating Enzyme Selectivity and Requirements for Function of the E3 Ubiquitin Ligase CHIP." J. Biol. Chem. 286, 21277-21286 (2011).
Assembly members:
CHIP_U-box_domain, polymer, 90 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):
CHIP_U-box_domain: GPGSVDEKRKKRDIPDYLCG
KISFELMREPCITPSGITYD
RKDIEEHLQRVGHFDPVTRS
PLTQEQLIPNLAMKEVIDAF
ISENGWVEDY
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 167 |
15N chemical shifts | 78 |
1H chemical shifts | 78 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | CHIP U-box domain | 1 |
Entities:
Entity 1, CHIP U-box domain 90 residues - Formula weight is not available
Residues 1-4 are artifacts from the insertion of a cleavage site.
1 | GLY | PRO | GLY | SER | VAL | ASP | GLU | LYS | ARG | LYS | |
2 | LYS | ARG | ASP | ILE | PRO | ASP | TYR | LEU | CYS | GLY | |
3 | LYS | ILE | SER | PHE | GLU | LEU | MET | ARG | GLU | PRO | |
4 | CYS | ILE | THR | PRO | SER | GLY | ILE | THR | TYR | ASP | |
5 | ARG | LYS | ASP | ILE | GLU | GLU | HIS | LEU | GLN | ARG | |
6 | VAL | GLY | HIS | PHE | ASP | PRO | VAL | THR | ARG | SER | |
7 | PRO | LEU | THR | GLN | GLU | GLN | LEU | ILE | PRO | ASN | |
8 | LEU | ALA | MET | LYS | GLU | VAL | ILE | ASP | ALA | PHE | |
9 | ILE | SER | GLU | ASN | GLY | TRP | VAL | GLU | ASP | TYR |
Samples:
sample_1: CHIP U-box domain, [U-99% 13C; U-99% 15N], 300 uM; HEPES 20 mM; sodium chloride 50 mM; DTT 1 mM
sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
PDB | |
DBJ | BAB22329 BAB23315 BAC32489 BAE34573 BAE38905 |
EMBL | CAG04345 CAG32658 |
GB | AAC18038 AAD33400 AAD33401 AAG17211 AAH07545 |
REF | NP_001020796 NP_001026577 NP_001068634 NP_001072347 NP_001244487 |
SP | Q5ZHY5 Q9UNE7 Q9WUD1 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts