BMRB Entry 19182

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19182

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the catalytic domain of human Aprataxin
Deposition date:
2013-04-19
Original release date:
2013-05-17
Authors:
Bellstedt, Peter; Seiboth, Thomas; Goerlach, Matthias
Citation:

Citation: Bellstedt, Peter; Seiboth, Thomas; Haefner, Sabine; Kutscha, Henriette; Ramachandran, Ramadurai; Goerlach, Matthias. "Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets"  J. Biomol. NMR 57, 65-72 (2013).
PubMed: 23943084

Assembly members:

Assembly members:
Aprataxin, polymer, 202 residues, 23387 Da.
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-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Aprataxin: GSHMLECSVPLKKGKDAPIK KESLGHWSQGLKISMQDPKM QVYKDEQVVVIKDKYPKARY HWLVLPWTSISSLKAVAREH LELLKHMHTVGEKVIVDFAG SSKLRFRLGYHAIPSMSHVH LHVISQDFDSPCLKNKKHWN SFNTEYFLESQAVIEMVQEA GRVTVRDGMPELLKLPLRCH ECQQLLPSIPQLKEHLRKHW TQ

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts150
1H chemical shifts150

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Aprataxin, chain 11
2Aprataxin, chain 21
3zinc ion2

Entities:

Entity 1, Aprataxin, chain 1 202 residues - 23387 Da.

Residues 1-6 are vector coded residues

1   GLYSERHISMETLEUGLUCYSSERVALPRO
2   LEULYSLYSGLYLYSASPALAPROILELYS
3   LYSGLUSERLEUGLYHISTRPSERGLNGLY
4   LEULYSILESERMETGLNASPPROLYSMET
5   GLNVALTYRLYSASPGLUGLNVALVALVAL
6   ILELYSASPLYSTYRPROLYSALAARGTYR
7   HISTRPLEUVALLEUPROTRPTHRSERILE
8   SERSERLEULYSALAVALALAARGGLUHIS
9   LEUGLULEULEULYSHISMETHISTHRVAL
10   GLYGLULYSVALILEVALASPPHEALAGLY
11   SERSERLYSLEUARGPHEARGLEUGLYTYR
12   HISALAILEPROSERMETSERHISVALHIS
13   LEUHISVALILESERGLNASPPHEASPSER
14   PROCYSLEULYSASNLYSLYSHISTRPASN
15   SERPHEASNTHRGLUTYRPHELEUGLUSER
16   GLNALAVALILEGLUMETVALGLNGLUALA
17   GLYARGVALTHRVALARGASPGLYMETPRO
18   GLULEULEULYSLEUPROLEUARGCYSHIS
19   GLUCYSGLNGLNLEULEUPROSERILEPRO
20   GLNLEULYSGLUHISLEUARGLYSHISTRP
21   THRGLN

Entity 2, zinc ion - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Aprataxin, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-2H], 10 mM; sodium chloride 150 mM; sodium azide 0.05 w/v; H2O 90%; D2O 10%

sample_2: Aprataxin, [U-13C; U-15N]; [U-14N; U12C]-specific amino acid, 0.38 mM; TRIS, [U-2H], 10 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

standard_condition: ionic strength: 160 mM; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicstandard_condition
3D HNCOsample_1isotropicstandard_condition
3D HN(CA)COsample_1isotropicstandard_condition
3D HNCAsample_1isotropicstandard_condition
3D HN(CO)CAsample_1isotropicstandard_condition
2D 1H-15N HSQCsample_2isotropicstandard_condition
2D HN(CO)sample_1isotropicstandard_condition

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CcpNMR v2.2.2, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 750 MHz

Related Database Links:

UniProtKB Q7Z2E3-1

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