BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 15164

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15164

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Title: Backbone chemical shifts assignment of the soluble N-terminal region of the ATP7A   PubMed: 17545667

Deposition date: 2007-03-07 Original release date: 2007-10-24

Authors: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Della Malva, Nunzia; Migliardi, Manuele; Rosato, Antonio

Citation: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Della Malva, Nunzia; Migliardi, Manuele; Rosato, Antonio. "The different intermolecular interactions of the soluble copper-binding domains of the menkes protein, ATP7A.THE DIFFERENT INTERMOLECULAR INTERACTIONS OF THE SOLUBLE COPPER-BINDING DOMAINS OF THE MENKES PROTEIN, ATP7A"  J. Biol. Chem. 282, 23140-23146 (2007).

Assembly members:
ATP7A, polymer, 629 residues, 68620.7 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   Vector: pDEST17

Entity Sequences (FASTA):
ATP7A: MGVNSVTISVEGMTCNSCVW TIEQQIGKVNGVHHIKVSLE EKNATIIYDPKLQTPKTLQE AIDDMGFDAVIHNPDPLPVL TDTLFLTVTASLTLPWDHIQ STLLKTKGVTDIKIYPQKRT VAVTIIPSIVNANQIKELVP ELSLDTGTLEKKSGACEDHS MAQAGEVVLKMKVEGMTCHS CTSTIEGKIGKLQGVQRIKV SLDNQEATIVYQPHLISVEE MKKQIEAMGFPAFVKKQPKY LKLGAIDVERLKNTPVKSSE GSQQRSPSYTNDSTATFIID GMHCKSCVSNIESTLSALQY VSSIVVSLENRSAIVKYNAS SVTPESLRKAIEAVSPGLYR VSITSEVESTSNSPSSSSLQ KIPLNVVSQPLTQETVINID GMTCNSCVQSIEGVISKKPG VKSIRVSLANSNGTVEYDPL LTSPETLRGAIEDMGFDATL SDTNEPLVVIAQPSSEMPLL TSTNEFYTKGMTPVQDKEEG KNSSKCYIQVTGMTCASCVA NIERNLRREEGIYSILVALM AGKAEVRYNPAVIQPPMIAE FIRELGFGATVIENADEGDG VLELVVRGMTCASCVHKIES SLTKHRGILYCSVALATNKA HIKYDPEIIGPRDIIHTIES LGFEASLVK

Data sets:
Data typeCount
13C chemical shifts833
15N chemical shifts376
1H chemical shifts368

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ATP7A1

Entities:

Entity 1, ATP7A 629 residues - 68620.7 Da.

1   METGLYVALASNSERVALTHRILESERVAL
2   GLUGLYMETTHRCYSASNSERCYSVALTRP
3   THRILEGLUGLNGLNILEGLYLYSVALASN
4   GLYVALHISHISILELYSVALSERLEUGLU
5   GLULYSASNALATHRILEILETYRASPPRO
6   LYSLEUGLNTHRPROLYSTHRLEUGLNGLU
7   ALAILEASPASPMETGLYPHEASPALAVAL
8   ILEHISASNPROASPPROLEUPROVALLEU
9   THRASPTHRLEUPHELEUTHRVALTHRALA
10   SERLEUTHRLEUPROTRPASPHISILEGLN
11   SERTHRLEULEULYSTHRLYSGLYVALTHR
12   ASPILELYSILETYRPROGLNLYSARGTHR
13   VALALAVALTHRILEILEPROSERILEVAL
14   ASNALAASNGLNILELYSGLULEUVALPRO
15   GLULEUSERLEUASPTHRGLYTHRLEUGLU
16   LYSLYSSERGLYALACYSGLUASPHISSER
17   METALAGLNALAGLYGLUVALVALLEULYS
18   METLYSVALGLUGLYMETTHRCYSHISSER
19   CYSTHRSERTHRILEGLUGLYLYSILEGLY
20   LYSLEUGLNGLYVALGLNARGILELYSVAL
21   SERLEUASPASNGLNGLUALATHRILEVAL
22   TYRGLNPROHISLEUILESERVALGLUGLU
23   METLYSLYSGLNILEGLUALAMETGLYPHE
24   PROALAPHEVALLYSLYSGLNPROLYSTYR
25   LEULYSLEUGLYALAILEASPVALGLUARG
26   LEULYSASNTHRPROVALLYSSERSERGLU
27   GLYSERGLNGLNARGSERPROSERTYRTHR
28   ASNASPSERTHRALATHRPHEILEILEASP
29   GLYMETHISCYSLYSSERCYSVALSERASN
30   ILEGLUSERTHRLEUSERALALEUGLNTYR
31   VALSERSERILEVALVALSERLEUGLUASN
32   ARGSERALAILEVALLYSTYRASNALASER
33   SERVALTHRPROGLUSERLEUARGLYSALA
34   ILEGLUALAVALSERPROGLYLEUTYRARG
35   VALSERILETHRSERGLUVALGLUSERTHR
36   SERASNSERPROSERSERSERSERLEUGLN
37   LYSILEPROLEUASNVALVALSERGLNPRO
38   LEUTHRGLNGLUTHRVALILEASNILEASP
39   GLYMETTHRCYSASNSERCYSVALGLNSER
40   ILEGLUGLYVALILESERLYSLYSPROGLY
41   VALLYSSERILEARGVALSERLEUALAASN
42   SERASNGLYTHRVALGLUTYRASPPROLEU
43   LEUTHRSERPROGLUTHRLEUARGGLYALA
44   ILEGLUASPMETGLYPHEASPALATHRLEU
45   SERASPTHRASNGLUPROLEUVALVALILE
46   ALAGLNPROSERSERGLUMETPROLEULEU
47   THRSERTHRASNGLUPHETYRTHRLYSGLY
48   METTHRPROVALGLNASPLYSGLUGLUGLY
49   LYSASNSERSERLYSCYSTYRILEGLNVAL
50   THRGLYMETTHRCYSALASERCYSVALALA
51   ASNILEGLUARGASNLEUARGARGGLUGLU
52   GLYILETYRSERILELEUVALALALEUMET
53   ALAGLYLYSALAGLUVALARGTYRASNPRO
54   ALAVALILEGLNPROPROMETILEALAGLU
55   PHEILEARGGLULEUGLYPHEGLYALATHR
56   VALILEGLUASNALAASPGLUGLYASPGLY
57   VALLEUGLULEUVALVALARGGLYMETTHR
58   CYSALASERCYSVALHISLYSILEGLUSER
59   SERLEUTHRLYSHISARGGLYILELEUTYR
60   CYSSERVALALALEUALATHRASNLYSALA
61   HISILELYSTYRASPPROGLUILEILEGLY
62   PROARGASPILEILEHISTHRILEGLUSER
63   LEUGLYPHEGLUALASERLEUVALLYS

Samples:

sample_1: ATP7A, [U-100% 15N], 0.7 mM; DTT 1 mM; potassium phosphate 50 mM

sample_2: ATP7A, [U-99% 13C; U-99% 15N], 0.3 mM; DTT 1 mM; potassium phosphate 50 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1

Software:

CARA v1.5.3, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

BMRB 7375

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