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 17157

Title: DNA repair protein zinc finger 1   PubMed: 21262234

Deposition date: 2010-08-30 Original release date: 2011-01-27

Authors: Neuhaus, David; Eustermann, Sebastian; Yang, Ji-Chun; Videler, Hortense

Citation: Eustermann, Sebastian; Videler, Hortense; Yang, Ji-Chun; Cole, Paul; Gruszka, Dominika; Veprintsev, Dmitry; Neuhaus, David. "The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger."  J. Mol. Biol. 407, 149-170 (2011).

Assembly members:
PARP-1_Finger_1, polymer, 108 residues, 12132.885 Da.
ZN, 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   Vector: PET28A

Entity Sequences (FASTA):
PARP-1_Finger_1: MAESSDKLYRVEYAKSGRAS CKKCSESIPKDSLRMAIMVQ SPMFDGKVPHWYHFSCFWKV GHSIRHPDVEVDGFSELRWD DQQKVKKTAEAGGVTGKGQD GIGSKAEK

Data sets:
Data typeCount
13C chemical shifts363
15N chemical shifts102
1H chemical shifts703

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PARP-1 Finger 11
2ZINC ION2

Entities:

Entity 1, PARP-1 Finger 1 108 residues - 12132.885 Da.

1   METALAGLUSERSERASPLYSLEUTYRARG
2   VALGLUTYRALALYSSERGLYARGALASER
3   CYSLYSLYSCYSSERGLUSERILEPROLYS
4   ASPSERLEUARGMETALAILEMETVALGLN
5   SERPROMETPHEASPGLYLYSVALPROHIS
6   TRPTYRHISPHESERCYSPHETRPLYSVAL
7   GLYHISSERILEARGHISPROASPVALGLU
8   VALASPGLYPHESERGLULEUARGTRPASP
9   ASPGLNGLNLYSVALLYSLYSTHRALAGLU
10   ALAGLYGLYVALTHRGLYLYSGLYGLNASP
11   GLYILEGLYSERLYSALAGLULYS

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: PARP-1 Finger 1, [U-98% 15N; U-98% 13C], 0.5 – 1 mM; TRIS, [U-99% 2H], 50 mM; sodium chloride 200 mM; zinc sulfate 150 uM; DTT, [U-99% 2H], 4 mM; H2O 95%; D2O 5%; TRIS, [U-99% 2H], 50 mM

sample_conditions_1: ionic strength: 0.201 M; pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESY 15N-filteredsample_1isotropicsample_conditions_1
3D CBCAHNsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHAHNsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D [1H-13C-1H] HCCH-TOCSYsample_1isotropicsample_conditions_1
3D [13C-13C-1H] HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DMX 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB
EMBL CAA39606
REF XP_011359180

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