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 6483

Title: The loss of stability of a naturally occurring ATP7A mutant is the cause of Menkes disease   PubMed: 16083905

Deposition date: 2005-02-02 Original release date: 2005-11-14

Authors: Banci, L.; Bertini, I.; Cantini, F.; Migliardi, M.; Rosato, A.; Wang, S.

Citation: Banci, L.; Bertini, I.; Cantini, F.; Migliardi, M.; Rosato, A.; Wang, S.. "An Atomic-level Investigation of the Disease-causing A629P Mutant of the Menkes Protein, ATP7A."  J. Mol. Biol. 352, 409-417 (2005).

Assembly members:
Copper-transporting ATPase 1, polymer, 75 residues, 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

Entity Sequences (FASTA):
Copper-transporting ATPase 1: MGDGVLELVVRGMTCASCVH KIESSLTKHRGILYCSVALA TNKAHIKYDPEIIGPRDIIH TIESLGFEPSLVKIE

Data sets:
Data typeCount
15N chemical shifts68
1H chemical shifts454

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Copper-transporting ATPase 11

Entities:

Entity 1, Copper-transporting ATPase 1 75 residues - Formula weight is not available

1   METGLYASPGLYVALLEUGLULEUVALVAL
2   ARGGLYMETTHRCYSALASERCYSVALHIS
3   LYSILEGLUSERSERLEUTHRLYSHISARG
4   GLYILELEUTYRCYSSERVALALALEUALA
5   THRASNLYSALAHISILELYSTYRASPPRO
6   GLUILEILEGLYPROARGASPILEILEHIS
7   THRILEGLUSERLEUGLYPHEGLUPROSER
8   LEUVALLYSILEGLU

Samples:

sample_1: Copper-transporting ATPase 1, [U-15N], 0.8 mM; DTT 5 mM; phosphate buffer 100 mM; H2O 90%; D2O 10%

sample_2: Copper-transporting ATPase 1, [U-15N; U-13C], 0.8 mM; DTT 5 mM; phosphate buffer 100 mM; H2O 90%; D2O 10%

sample_3: Copper-transporting ATPase 1 1.0 mM; DTT 5 mM; phosphate buffer 100 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablenot available
CBCANHnot availablenot availablenot available
CBCACONHnot availablenot availablenot available
HNCOnot availablenot availablenot available
HNCACOnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
HNHAnot availablenot availablenot available

Software:

xwinnmr - collection

CARA v1.2 - data analysis

DYANA v1.5 - structure solution

AMBER v5.0 - refinement

NMR spectrometers:

  • Bruker AVANCE 500 MHz

Related Database Links:

BMRB 6480 6481 6482
PDB

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