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 16440

Title: Solution structure of the nucleotide binding domain of the human Menkes protein in the ATP-free form   PubMed: 19917612

Deposition date: 2009-08-05 Original release date: 2009-11-19

Authors: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Inagaki, Sayaka; Migliardi, Manuele; Rosato, Antonio

Citation: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Inagaki, Sayaka; Migliardi, Manuele; Rosato, Antonio. "The Binding Mode of ATP Revealed by the Solution Structure of the N-domain of Human ATP7A."  J. Biol. Chem. 285, 2537-2544 (2010).

Assembly members:
human Menkes protein, polymer, 185 residues, 19803.387 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):
human Menkes protein: SFTMHGTPVVNQVKVLTESN RISHHKILAIVGTAESNSEH PLGTAITKYCKQELDTETLG TCIDFQVVPGCGISCKVTNI EGLLHKNNWNIEDNNIKNAS LVQIDASNEQSSTSSSMIID AQISNALNAQQYKVLIGNRE WMIRNGLVINNDVNDFMTEH ERKGRTAVLVAVDDELCGLI AIADT

Data sets:
Data typeCount
13C chemical shifts671
15N chemical shifts188
1H chemical shifts1162

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human Menkes protein1

Entities:

Entity 1, human Menkes protein 185 residues - 19803.387 Da.

After cleavage of the tag, four amino acids (SFTM) from the restriction site are left at the N-terminus of the protein.

1   SERPHETHRMETHISGLYTHRPROVALVAL
2   ASNGLNVALLYSVALLEUTHRGLUSERASN
3   ARGILESERHISHISLYSILELEUALAILE
4   VALGLYTHRALAGLUSERASNSERGLUHIS
5   PROLEUGLYTHRALAILETHRLYSTYRCYS
6   LYSGLNGLULEUASPTHRGLUTHRLEUGLY
7   THRCYSILEASPPHEGLNVALVALPROGLY
8   CYSGLYILESERCYSLYSVALTHRASNILE
9   GLUGLYLEULEUHISLYSASNASNTRPASN
10   ILEGLUASPASNASNILELYSASNALASER
11   LEUVALGLNILEASPALASERASNGLUGLN
12   SERSERTHRSERSERSERMETILEILEASP
13   ALAGLNILESERASNALALEUASNALAGLN
14   GLNTYRLYSVALLEUILEGLYASNARGGLU
15   TRPMETILEARGASNGLYLEUVALILEASN
16   ASNASPVALASNASPPHEMETTHRGLUHIS
17   GLUARGLYSGLYARGTHRALAVALLEUVAL
18   ALAVALASPASPGLULEUCYSGLYLEUILE
19   ALAILEALAASPTHR

Samples:

sample_1: ATPfree N-MNK, [U-99% 15N], 1.2 – 1.5 mM; phosphate 50 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_2: ATPfree N-MNK, [U-95% 13C; U-95% 15N], 0.8 – 1.0 mM; phosphate 50 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; 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
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

XEASY, Bartels et al. - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v10, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

PSVS, Bhattacharya and Montelione - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 16441
PDB
DBJ BAG61422
EMBL CAB08162 CAB94714
GB AAA35580 AAA96010 AAI56438 EAW98605 EAW98606
REF NP_000043 NP_001269153 XP_002831882 XP_003824455 XP_004064479
SP Q04656

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