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 16536

Title: Structure of the E1064A mutant of the N-domain of Wilson Disease Associated Protein

Deposition date: 2009-10-03 Original release date: 2012-08-03

Authors: Dmitriev, Oleg

Citation: Dmitriev, Oleg; Lutsenko, Svetlana; Uhelmann, Eva-Maria. "The structure of the E1064A mutant reveals ATP-dependent conformational changes in the ATP7B N-domain."  Biochemistry ., .-..

Assembly members:
E1064A mutant, polymer, 141 residues, 14752.269 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):
E1064A mutant: AGHMVPRVMRVLLLGDVATL PLRKVLAVVGTAAASSEHPL GVAVTKYCKEELGTETLGYC TDFQAVPGCGIGCKVSNVEG ILAAVPQTFSVLIGNREWLR RNGLTISSDVSDAMTDHEMK GQTAILVAIDGVLCGMIAIA D

Data sets:
Data typeCount
13C chemical shifts523
15N chemical shifts141
1H chemical shifts865

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E1064A mutant1

Entities:

Entity 1, E1064A mutant 141 residues - 14752.269 Da.

1   ALAGLYHISMETVALPROARGVALMETARG
2   VALLEULEULEUGLYASPVALALATHRLEU
3   PROLEUARGLYSVALLEUALAVALVALGLY
4   THRALAALAALASERSERGLUHISPROLEU
5   GLYVALALAVALTHRLYSTYRCYSLYSGLU
6   GLULEUGLYTHRGLUTHRLEUGLYTYRCYS
7   THRASPPHEGLNALAVALPROGLYCYSGLY
8   ILEGLYCYSLYSVALSERASNVALGLUGLY
9   ILELEUALAALAVALPROGLNTHRPHESER
10   VALLEUILEGLYASNARGGLUTRPLEUARG
11   ARGASNGLYLEUTHRILESERSERASPVAL
12   SERASPALAMETTHRASPHISGLUMETLYS
13   GLYGLNTHRALAILELEUVALALAILEASP
14   GLYVALLEUCYSGLYMETILEALAILEALA
15   ASP

Samples:

sample_1: sodium phosphate 50 mM; DTT 5 mM; DSS 0.3 mM; H2O 95%; D2O 5%; protein, [13C; 15N], 0.8 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

FELIX v2007, Accelrys Software Inc. - peak picking

TALOS, Cornilescu, Delaglio and Bax - refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB

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