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 6130

Title: Solution structure and backbone dynamics of the Cu(I) and apo-forms of the second metal-binding domain of the Menkes protein ATP7A   PubMed: 15035611

Deposition date: 2004-03-03 Original release date: 2004-05-15

Authors: Banci, L.; Bertini, I.; Del Conte, R.; D'Onofrio, M.; Rosato, A.

Citation: Banci, L.; Bertini, I.; Del Conte, R.; D'Onofrio, M.; Rosato, A.. "Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7A"  Biochemistry 43, 3396-3403 (2004).

Assembly members:
ATPase, polymer, 76 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):
ATPase: GEVVLKMKVEGMTCHSCTST IEGKIGKLQGVQRIKVSLDN QEATIVYQPHLISVEEMKKQ IEAMGFPAFVKKIEGR

Data sets:
Data typeCount
13C chemical shifts320
15N chemical shifts77
1H chemical shifts524

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Copper-transporting ATPase 11

Entities:

Entity 1, Copper-transporting ATPase 1 76 residues - Formula weight is not available

1   GLYGLUVALVALLEULYSMETLYSVALGLU
2   GLYMETTHRCYSHISSERCYSTHRSERTHR
3   ILEGLUGLYLYSILEGLYLYSLEUGLNGLY
4   VALGLNARGILELYSVALSERLEUASPASN
5   GLNGLUALATHRILEVALTYRGLNPROHIS
6   LEUILESERVALGLUGLUMETLYSLYSGLN
7   ILEGLUALAMETGLYPHEPROALAPHEVAL
8   LYSLYSILEGLUGLYARG

Samples:

sample_1: ATPase 1 mM; phosphate 100 mM; H2O 90%; D2O 10%

sample_2: ATPase, [U-15N], 1 mM; phosphate 100 mM; H2O 90%; D2O 10%

sample_3: ATPase, [U-13C; U-15N], 1 mM; phosphate 100 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
[1H-1H]-NOESYnot availablenot availablesample_cond_1
13C-NOESY-HSQCnot availablenot availablesample_cond_1
15N-NOESY-HSQCnot availablenot availablesample_cond_1
HNHAnot availablenot availablesample_cond_1

Software:

DYANA v1.5 - refinement, structure solution

NMR spectrometers:

  • unknown unknown 0 MHz

Related Database Links:

BMRB 6022 6129
PDB

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