BMRB Entry 17750

Title:
Solution NMR structure of N-terminal domain of human E3 ubiquitin-protein ligase HECW2. Northeast structural genomics consortium (NESG) target ht6306a
Deposition date:
2011-06-29
Original release date:
2011-08-03
Authors:
Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Chitayat, Seth; Dhe-Paganon, Sirano; Arrowsmith, Cheryl
Citation:

Citation: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Arrowsmith, Cheryl; Dhe-Paganon, Sirano. "NMR solution structure of N-terminal domain of E3 ligase HECW2"  .

Assembly members:

Assembly members:
entity, polymer, 138 residues, 12144.793 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: not applicable

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts119
1H chemical shifts806

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of E3 ligase HECW21

Entities:

Entity 1, N-terminal domain of E3 ligase HECW2 138 residues - 12144.793 Da.

1   METHISHISHISHISHISHISSERSERGLN
2   ARGGLUASNLEUTYRPHEGLNGLYLEUGLN
3   ARGALAASNSERASPTHRASPLEUVALTHR
4   SERGLUSERARGSERSERLEUTHRALASER
5   METTYRGLUTYRTHRLEUGLYGLNALAGLN
6   ASNLEUILEILEPHETRPASPILELYSGLU
7   GLUVALASPPROSERASPTRPILEGLYLEU
8   TYRHISILEASPGLUASNSERPROALAASN
9   PHETRPASPSERLYSASNARGGLYVALTHR
10   GLYTHRGLNLYSGLYGLNILEVALTRPARG
11   ILEGLUPROGLYPROTYRPHEMETGLUPRO
12   GLUILELYSILECYSPHELYSTYRTYRHIS
13   GLYILESERGLYALALEUARGALATHRTHR
14   PROCYSILETHRVALLYSASNPRO

Samples:

sample_1: N-terminal domain of E3 ligase HECW2, [U-13C; U-15N], 0.5 mM; MOPS 10 mM; sodium chloride 450 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 1 mM; H2O 90%; D2) 10%

sample_conditions_1: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

FMC, Lemak,Steren,Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - validation

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC33094 BAD23960
GB AAI56406 EDL00004 EDL99066 EHB01577 EPY77263
REF NP_001001883 NP_001101688 XP_001369853 XP_003463417 XP_003764123
SP Q6I6G8
AlphaFold Q6I6G8

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