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 19315

Title: Solution Structure of the Catalytic Domain of HHARI   PubMed: 24058416

Deposition date: 2013-07-09 Original release date: 2013-11-11

Authors: Mercier, Pascal; Spratt, Donald; Shaw, Gary

Citation: Spratt, Donald; Mercier, Pascal; Gary, Shaw. "Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase"  PLoS ONE 8, e74047-e74047 (2013).

Assembly members:
entity_1, polymer, 74 residues, 8439.303 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity_1: GSKKCDDDSETSNWIAANTK ECPKCHVTIEKDGGSNHMVC RNQNCKAEFCWVCLGPWEPH GSAWYNCNRYNEDD

Data sets:
Data typeCount
13C chemical shifts222
15N chemical shifts87
1H chemical shifts420

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HHARI Catalytic Domain1
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, HHARI Catalytic Domain 74 residues - 8439.303 Da.

Residues 323-324 (N-terminal "GS") results from cloning and remains in the intact protein after TEV cleavage.

1   GLYSERLYSLYSCYSASPASPASPSERGLU
2   THRSERASNTRPILEALAALAASNTHRLYS
3   GLUCYSPROLYSCYSHISVALTHRILEGLU
4   LYSASPGLYGLYSERASNHISMETVALCYS
5   ARGASNGLNASNCYSLYSALAGLUPHECYS
6   TRPVALCYSLEUGLYPROTRPGLUPROHIS
7   GLYSERALATRPTYRASNCYSASNARGTYR
8   ASNGLUASPASP

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: MES 20 mM; sodium chloride 120 mM; DTT 5 mM; entity_1, [U-98% 15N], 2.3 mM

sample_2: MES 20 mM; sodium chloride 120 mM; DTT 5 mM; entity_1, [U-98% 13C; U-98% 15N], 2.3 mM

sample_conditions_1: ionic strength: 0.120 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1
2D HCNsample_2isotropicsample_conditions_1

Software:

VNMRJ vVarian VnmrJ 2.2D, Varian - collection

NMRPipe v2013.021.23.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw vVer 7.9 Rev 2013.021.23.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v9.0.0beta76, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.33, Schwieters, Kuszewski, Tjandra and Clore - refinement

Procheck v3.5.4, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAD92669 BAG35590
EMBL CAA08817 CAA10274 CAB45870 CAF98343 CAH65069
GB AAD28088 AAH38034 AAH51877 AAH57523 AAH57680
REF NP_001013126 NP_001025558 NP_001075183 NP_001089823 NP_001116952
SP A2VEA3 B1H1E4 Q32NS4 Q6NW85 Q6PFJ9
TPG DAA25726

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