BMRB Entry 26818

Title:
1H, 13C and 15N backbone and side chain chemical shift assignments of CHIP-TPR
Deposition date:
2016-06-17
Original release date:
2016-10-13
Authors:
Zhang, Huaqun; Page, Richard
Citation:

Citation: Zhang, Huaqun; McGlone, Cameron; Mannion, Matthew; Page, Richard. "1H, 15N and 13C resonance assignments for free and IEEVD peptide-bound forms of the tetratricopeptide repeat domain from the human E3 ubiquitin ligase CHIP"  Biomol. NMR Assign. 11, 5-9 (2016).
PubMed: 27709416

Assembly members:

Assembly members:
CHIP-TPR, polymer, 139 residues, 15860 Da.

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: pHis//2

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts124
1H chemical shifts727

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CHIP-TPR1

Entities:

Entity 1, CHIP-TPR 139 residues - 15860 Da.

Residues 1-5 are from a non-native affinity tag after cleavage by TEV protease.

1   GLYALAMETGLYSERGLULYSSERPROSER
2   ALAGLNGLULEULYSGLUGLNGLYASNARG
3   LEUPHEVALGLYARGLYSTYRPROGLUALA
4   ALAALACYSTYRGLYARGALAILETHRARG
5   ASNPROLEUVALALAVALTYRTYRTHRASN
6   ARGALALEUCYSTYRLEULYSMETGLNGLN
7   HISGLUGLNALALEUALAASPCYSARGARG
8   ALALEUGLULEUASPGLYGLNSERVALLYS
9   ALAHISPHEPHELEUGLYGLNCYSGLNLEU
10   GLUMETGLUSERTYRASPGLUALAILEALA
11   ASNLEUGLNARGALATYRSERLEUALALYS
12   GLUGLNARGLEUASNPHEGLYASPASPILE
13   PROSERALALEUARGILEALALYSLYSLYS
14   ARGTRPASNSERILEGLUGLUARGARG

Samples:

sample_1: CHIP-TPR, [U-100% 15N], 0.45 mM; sodium chloride 150 mM; HEPES 20 mM; beta-mercaptoethanol 5 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TCOSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment

NMRDraw v8.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - refinement

NMRPipe v2012.090.12.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP Q9UNE7
AlphaFold Q9HBT1

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