BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51399

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51399

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Title: PARP14 macro domain 2 ADPr bound   PubMed: 36107366

Deposition date: 2022-04-14 Original release date: 2022-09-19

Authors: Charalampous, Periklis; Fourkiotis, Nikolaos; Tsika, Aikaterini; Gallo, Angelo; Spyroulias, Georgios

Citation: Fourkiotis, Nikolaos; Charalampous, Periklis; Tsika, Aikaterini; Kravvariti, Konstantina; Sideras-Bisdekis, Christos; Gallo, Angelo; Spyroulias, Georgios. "NMR study of human macroPARPs domains: 1 H, 15 N and 13 C resonance assignment of hPARP14 macro domain 2 in the free and the ADPr bound state"  Biomol. NMR Assign. 16, 399-406 (2022).

Assembly members:
entity_1, polymer, 197 residues, Formula weight is not available
entity_APR, non-polymer, 559.316 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: pETm41

Entity Sequences (FASTA):
entity_1: GAMGGKTSWEKGSLVSPGGL QMLLVKEGVQNAKTDVVVNS VPLDLVLSRGPLSKSLLEKA GPELQEELDTVGQGVAVSMG TVLKTSSWNLDCRYVLHVVA PEWRNGSTSSLKIMEDIIRE CMEITESLSLKSIAFPAIGT GNLGFPKNIFAELIISEVFK FSSKNQLKTLQEVHFLLHPS DHENIQAFSDEFARRAN

Data sets:
Data typeCount
13C chemical shifts704
15N chemical shifts160
1H chemical shifts1153

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PARP14 macro domain 21
2ADPr2

Entities:

Entity 1, PARP14 macro domain 2 197 residues - Formula weight is not available

G first residue in the chemical shifts assignment file (GAMG) tag included, native sequence starts at G999.

1   GLYALAMETGLYGLYLYSTHRSERTRPGLU
2   LYSGLYSERLEUVALSERPROGLYGLYLEU
3   GLNMETLEULEUVALLYSGLUGLYVALGLN
4   ASNALALYSTHRASPVALVALVALASNSER
5   VALPROLEUASPLEUVALLEUSERARGGLY
6   PROLEUSERLYSSERLEULEUGLULYSALA
7   GLYPROGLULEUGLNGLUGLULEUASPTHR
8   VALGLYGLNGLYVALALAVALSERMETGLY
9   THRVALLEULYSTHRSERSERTRPASNLEU
10   ASPCYSARGTYRVALLEUHISVALVALALA
11   PROGLUTRPARGASNGLYSERTHRSERSER
12   LEULYSILEMETGLUASPILEILEARGGLU
13   CYSMETGLUILETHRGLUSERLEUSERLEU
14   LYSSERILEALAPHEPROALAILEGLYTHR
15   GLYASNLEUGLYPHEPROLYSASNILEPHE
16   ALAGLULEUILEILESERGLUVALPHELYS
17   PHESERSERLYSASNGLNLEULYSTHRLEU
18   GLNGLUVALHISPHELEULEUHISPROSER
19   ASPHISGLUASNILEGLNALAPHESERASP
20   GLUPHEALAARGARGALAASN

Entity 2, ADPr - C15 H23 N5 O14 P2 - 559.316 Da.

1   APR

Samples:

sample_1: PARP14 macro domain 2, [U-100% 13C; U-100% 15N], 0.7 mM; APR 5 ratio; D2O, [U-100% 2H], 90%; H2O 10%; DTT 2 mM; HEPES 50 mM; sodium chloride 100 mM; EDTA 0.4 mM; proteases inhibitors 0.1%; DSS 1%

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.1.1 - collection, processing

CARA v1.9.1.7 - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

UNP Q460N5
AlphaFold Q9ULF2

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