BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16620

Title: Solution NMR structure of zinc binding N-terminal domain of ubiquitin-protein ligase E3A from Homo Sapience. Northeast Structural Genomics Consortium (NESG) target HR3662A.

Deposition date: 2009-11-27 Original release date: 2010-01-06

Authors: Lemak, Alexander; Yee, Adelinda; Fares, Christophe; Semesi, Antony; Xiao, Rong; Montelione, Gaetano; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Yee, Adelinda; Fares, Christophe; Semesi, Antony; Xiao, Rong; Montelione, Gaetano; Dhe-Paganon, Sirano; Arrowsmith, Cheryl. "Solution structure of zinc binding domain of human ubiquitin-protein ligase E3A isoform 2"  .

Assembly members:
hs00184, polymer, 82 residues, 13259.014 Da.
ZN, non-polymer, 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   Vector: pET28-MHL

Entity Sequences (FASTA):
hs00184: MHHHHHHSSGRENLYFQGMK RAAAKHLIERYYHQLTEGCG NEACTNEFCASCPTFLRMDN NAAAIKALELYKINAKLCDP HP

Data typeCount
13C chemical shifts244
15N chemical shifts60
1H chemical shifts405

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hs001841
2Zinc2

Entities:

Entity 1, hs00184 82 residues - 13259.014 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   ARGGLUASNLEUTYRPHEGLNGLYMETLYS
3   ARGALAALAALALYSHISLEUILEGLUARG
4   TYRTYRHISGLNLEUTHRGLUGLYCYSGLY
5   ASNGLUALACYSTHRASNGLUPHECYSALA
6   SERCYSPROTHRPHELEUARGMETASPASN
7   ASNALAALAALAILELYSALALEUGLULEU
8   TYRLYSILEASNALALYSLEUCYSASPPRO
9   HISPRO

Entity 2, Zinc - Formula weight is not available

1   ZN

Samples:

sample_1: hs00184, [U-13C; U-15N], 0.5 mM; mops 10 mM; sodium chloride 450 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; D2O 10%; H2O 90%

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 NOESYsample_1isotropicsample_conditions_1
3D 1H-13C_arom NOESYsample_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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC26314 BAD69554 BAF84094 BAF85203
EMBL CAA04534 CAA66653 CAA66654 CAA66655 CAA66656
GB AAA35542 AAB47756 AAB49301 AAB69154 AAC83345
PIR A38920
REF NP_000453 NP_001029134 NP_001091932 NP_001126699 NP_001230110
SP Q05086
TPG DAA17742
AlphaFold Q05086

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