BMRB Entry 25386

Title:
Chemical shift assignments of Zinc finger Domain of Methionine amino peptidase 1 from Homo sapiens
Deposition date:
2014-12-10
Original release date:
2015-02-25
Authors:
Rachineni, Kavitha; Arya, Tarun; singarapu, kiran kumar; Bharatam, Jagadeesh; Addlagatta, Anthony
Citation:

Citation: Rachineni, Kavitha; Arya, Tarun; Singarapu, Kiran kumar; Addlagatta, Anthony; Bharatam, Jagadeesh. "Chemical shift assignments of zinc finger domain of methionine aminopeptidase 1 (MetAP1) from Homo sapiens"  Biomol NMR Assign. 9, 351-353 (2015).
PubMed: 25921012

Assembly members:

Assembly members:
zinc_finger_domain_of_METAP1, polymer, 104 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

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   Host organism: Escherichia coli   Vector: pET-28a(+)

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts267
15N chemical shifts78
1H chemical shifts426

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zinc finger domain of METap 11
2ZINC ION, 12
3ZINC ION, 22

Entities:

Entity 1, zinc finger domain of METap 1 104 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METMETALAALAVALGLUTHRARGVALCYS
4   GLUTHRASPGLYCYSSERSERGLUALALYS
5   LEUGLNCYSPROTHRCYSILELYSLEUGLY
6   ILEGLNGLYSERTYRPHECYSSERGLNGLU
7   CYSPHELYSGLYSERTRPALATHRHISLYS
8   LEULEUHISLYSLYSALALYSASPGLULYS
9   ALALYSARGGLUVALSERSERTRPTHRVAL
10   GLUGLYASPILEASNTHRASPPROTRPALA
11   GLYTYRARGTYR

Entity 2, ZINC ION, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zinc finger domain of METAP1, [U-98% 13C; U-98% 15N], 300 uM; Tris 25 mM; H2O 90%; D2O, U-2H, 10%

sample_2: zinc finger domain of METAP1, [U-98% 15N], 300 uM; Tris 25 mM; H2O 90%; D2O, U-2H, 10%

sample_conditions_1: ionic strength: 25 mM; pH: 8.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PINE, Bahrami, Markley, Assadi, and Eghbalnia - data analysis

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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