BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17594

Title: Solution NMR structure of a helical bundle domain from human E3 ligase HECTD1. Northeast structural genomics consortium (NESG) target HT6305A

Deposition date: 2011-04-15 Original release date: 2012-08-07

Authors: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Arrowsmith, Cheryl; Dhe-Paganon, Sirano

Citation: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Arrowsmith, Cheryl; Dhe-Paganon, Sirano. "NMR solution structure of a helical bundle from the E3 ligase HECTD1"  Not known ., .-..

Assembly members:
entity, polymer, 88 residues, 10079.442 Da.

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):
entity: MKDSDKEKENGKMGCWSIEH VEQYLGTDELPKNDLITYLQ KNADAAFLRHWKLTGTNKSI RKNRNCSQLIAAYKDFCEHG TKSGLNQG

Data typeCount
13C chemical shifts356
15N chemical shifts96
1H chemical shifts564

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hs004111

Entities:

Entity 1, hs00411 88 residues - 10079.442 Da.

1   METLYSASPSERASPLYSGLULYSGLUASN
2   GLYLYSMETGLYCYSTRPSERILEGLUHIS
3   VALGLUGLNTYRLEUGLYTHRASPGLULEU
4   PROLYSASNASPLEUILETHRTYRLEUGLN
5   LYSASNALAASPALAALAPHELEUARGHIS
6   TRPLYSLEUTHRGLYTHRASNLYSSERILE
7   ARGLYSASNARGASNCYSSERGLNLEUILE
8   ALAALATYRLYSASPPHECYSGLUHISGLY
9   THRLYSSERGLYLEUASNGLNGLY

Samples:

sample_1: hs00411, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 500 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 500 mM; pH: 7.7; 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 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA86445 BAD32384 BAG54248
EMBL CAB53681
GB AAI72391 AAP13073 AAW65983 EAW65950 EAW65952
REF NP_001248188 NP_056197 NP_659037 XP_001489913 XP_002696742
SP Q69ZR2 Q9ULT8
TPG DAA17475

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts