BMRB Entry 7069

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7069
MolProbity Validation Chart

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Title:
Solution structure and intermolecular interactions of the apo form of third metal-binding domain of ATP7A, the menkes disease protein
Deposition date:
2006-04-10
Original release date:
2008-07-07
Authors:
Banci, L.; Bertini, I.; Cantini, F.; DellaMalva, N.; Rosato, A.; Herrmann, T.; Wuthrich, K.
Citation:

Citation: Banci, L.; Bertini, I.; Cantini, F.; DellaMalva, N.; Herrmann, T.; Rosato, A.; Wuthrich, K.. "Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein"  J. Biol. Chem. 281, 29141-29147 (2006).
PubMed: 16873374

Assembly members:

Assembly members:
Copper-transporting ATPase 1 (E.C.3.6.3.4), polymer, 90 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Copper-transporting ATPase 1 (E.C.3.6.3.4): NDSTATFIIDGMHCKSCVSN IESTLSALQYVSSIVVSLEN RSAIVVYNASSVTPESLRKA IEAVSPGLYRVSITSEVEIE GRLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts248
15N chemical shifts79
1H chemical shifts546

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 90 residues - Formula weight is not available

1   ASNASPSERTHRALATHRPHEILEILEASP
2   GLYMETHISCYSLYSSERCYSVALSERASN
3   ILEGLUSERTHRLEUSERALALEUGLNTYR
4   VALSERSERILEVALVALSERLEUGLUASN
5   ARGSERALAILEVALVALTYRASNALASER
6   SERVALTHRPROGLUSERLEUARGLYSALA
7   ILEGLUALAVALSERPROGLYLEUTYRARG
8   VALSERILETHRSERGLUVALGLUILEGLU
9   GLYARGLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: Copper-transporting ATPase 1 (E.C.3.6.3.4) 1 mM; phosphate_buffer 100 mM; H2O 90%; D2O 10%

sample_2: Copper-transporting ATPase 1 (E.C.3.6.3.4), [U-15N], 1 mM; phosphate_buffer 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_3: Copper-transporting ATPase 1 (E.C.3.6.3.4), [U-15N; U-13C], 1 mM; phosphate_buffer 100 mM; DTT 1 mM; H2O 90%; D2O 10%

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

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available
(H)CCH-TOCSYnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
CBCANHnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available

Software:

xwinnmr - collection

XEASY v1.3 - data analysis

CARA - data analysis

ATHNOS-CANDID v1.0 - structure solution

AMBER v8.0 - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 7068
PDB

Download HSQC peak lists in one of the following formats:
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