BMRB Entry 17411

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17411

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for CHIP (carboxyl terminal of Hsc70-interacting protein)
Deposition date:
2011-01-14
Original release date:
2011-05-03
Authors:
Soss, Sarah; Chazin, Walter; Yue, Yuanyuan
Citation:

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).
PubMed: 21518764

Assembly members:

Assembly members:
CHIP_U-box_domain, polymer, 90 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pBG102

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CHIP_U-box_domain: GPGSVDEKRKKRDIPDYLCG KISFELMREPCITPSGITYD RKDIEEHLQRVGHFDPVTRS PLTQEQLIPNLAMKEVIDAF ISENGWVEDY

Data sets:
Data typeCount
13C chemical shifts167
15N chemical shifts78
1H chemical shifts78

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1CHIP U-box domain1

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   GLYPROGLYSERVALASPGLULYSARGLYS
2   LYSARGASPILEPROASPTYRLEUCYSGLY
3   LYSILESERPHEGLULEUMETARGGLUPRO
4   CYSILETHRPROSERGLYILETHRTYRASP
5   ARGLYSASPILEGLUGLUHISLEUGLNARG
6   VALGLYHISPHEASPPROVALTHRARGSER
7   PROLEUTHRGLNGLUGLNLEUILEPROASN
8   LEUALAMETLYSGLUVALILEASPALAPHE
9   ILESERGLUASNGLYTRPVALGLUASPTYR

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_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
AlphaFold Q5ZHY5 Q9UNE7 Q9WUD1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks