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 25893

Title: 1H, 13C and 15N chemical shift assignments for PARP-1 F3 domain   PubMed: 26626479

Deposition date: 2015-10-08 Original release date: 2015-11-25

Authors: Neuhaus, David; Eustermann, Sebastian; Yang, Ji-Chun; Wu, Wing-Fung

Citation: Eustermann, Sebastian; Wu, Wing-Fung; Langelier, Marie-France; Yang, Ji-Chun; Easton, Laura; Riccio, Amanda; Pascal, John; Neuhaus, David. "Structural basis of detection and signaling of DNA single-strand breaks by human PARP 1"  Mol. Cell 60, 742-754 (2015).

Assembly members:
PARP-1_215-362, polymer, 162 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 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):
PARP-1_215-362: GPLGSGVDEVAKKKSKKEKD KDSKLEKALKAQNDLIWNIK DELKKVCSTNDLKELLIFNK QQVPSGESAILDRVADGMVF GALLPCEECSGQLVFKSDAY YCTGDVTAWTKCMVKTQTPN RKEWVTPKEFREISYLKKLK VKKQDRIFPPETSNSSGRIV TD

Data sets:
Data typeCount
13C chemical shifts545
15N chemical shifts162
1H chemical shifts1094

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PARP-1_215-3621
2ZN32

Entities:

Entity 1, PARP-1_215-362 162 residues - Formula weight is not available

1   GLYPROLEUGLYSERGLYVALASPGLUVAL
2   ALALYSLYSLYSSERLYSLYSGLULYSASP
3   LYSASPSERLYSLEUGLULYSALALEULYS
4   ALAGLNASNASPLEUILETRPASNILELYS
5   ASPGLULEULYSLYSVALCYSSERTHRASN
6   ASPLEULYSGLULEULEUILEPHEASNLYS
7   GLNGLNVALPROSERGLYGLUSERALAILE
8   LEUASPARGVALALAASPGLYMETVALPHE
9   GLYALALEULEUPROCYSGLUGLUCYSSER
10   GLYGLNLEUVALPHELYSSERASPALATYR
11   TYRCYSTHRGLYASPVALTHRALATRPTHR
12   LYSCYSMETVALLYSTHRGLNTHRPROASN
13   ARGLYSGLUTRPVALTHRPROLYSGLUPHE
14   ARGGLUILESERTYRLEULYSLYSLEULYS
15   VALLYSLYSGLNASPARGILEPHEPROPRO
16   GLUTHRSERASNSERSERGLYARGILEVAL
17   THRASP

Entity 2, ZN3 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: PARP-1_215-362, [U-13C; U-15N], 0.2 mM; TRIS, [U-2H], 50 mM; DTT, [U-2H], 1 mM; ZnSO4 0.1 mM; H2O 95%; D2O, [U-2H], 5%; sodium chloride 200 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 7.2; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic (constant time)sample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-HSQC aliphaticsample_1isotropicsample_conditions_1
3D HC[C]H-TOCSYsample_1isotropicsample_conditions_1
3D [H]CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - processing

Analysis v2.4.1, CCPN - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker Avance I 800 MHz
  • Bruker Avance II+ 700 MHz
  • Bruker DMX 600 MHz
  • Bruker DRX 500 MHz

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