BMRB Entry 15300

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15300

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Title:
1H, 15N, 13C chemical shift assignment of the THAP domain 1-90 from human THAP1 protein
Deposition date:
2007-06-12
Original release date:
2008-02-21
Authors:
BESSIERE, Damien; CAMPAGNE, Sebastien; MILON, Alain; GERVAIS, Virginie
Citation:

Citation: Bessiere, Damien; Lacroix, Chrystelle; Campagne, Sebastien; Ecochard, Vincent; Guillet, Valerie; Mourey, Lionel; Lopez, Frederic; Czaplicki, J.; Demange, Pascal; Milon, Alain; Cirard, Jean-Philippe; Gervais, Virginie. "Structure-Function Analysis of the THAP Zinc Finger of THAP1, a Large C2CH DNA-binding Module Linked to Rb/E2F Pathways."  J. Biol. Chem. 283, 4352-4363 (2008).
PubMed: 18073205

Assembly members:

Assembly members:
THAP_domain, polymer, 96 residues, Formula weight is not available
ZN, 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: pet26bII

Entity Sequences (FASTA):

Entity Sequences (FASTA):
THAP_domain: MVQSCSAYGCKNRYDKDKPV SFHKFPLTRPSLCKEWEAAV RRKNFKPTKYSSICSEHFTP DCFKRECNNKLLKENAVPTI FLCTEPHDKKLELVPR

Data sets:
Data typeCount
13C chemical shifts177
15N chemical shifts61
1H chemical shifts510

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1THAP domain polypeptide1
2ZINC ION2

Entities:

Entity 1, THAP domain polypeptide 96 residues - Formula weight is not available

1   METVALGLNSERCYSSERALATYRGLYCYS
2   LYSASNARGTYRASPLYSASPLYSPROVAL
3   SERPHEHISLYSPHEPROLEUTHRARGPRO
4   SERLEUCYSLYSGLUTRPGLUALAALAVAL
5   ARGARGLYSASNPHELYSPROTHRLYSTYR
6   SERSERILECYSSERGLUHISPHETHRPRO
7   ASPCYSPHELYSARGGLUCYSASNASNLYS
8   LEULEULYSGLUASNALAVALPROTHRILE
9   PHELEUCYSTHRGLUPROHISASPLYSLYS
10   LEUGLULEUVALPROARG

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_U: THAP domain 1 mM; NaCl 10 mM; Tris 50 mM; DTT 1 mM

sample_U-15N-13C: THAP domain, [U-13C; U-15N], 1 mM; NaCl 10 mM; Tris 50 mM; DTT 1 mM

sample_conditions: ionic strength: 10 mM; pH: 6.8; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_Uisotropicsample_conditions
2D 1H-1H TOCSYsample_Uisotropicsample_conditions
2D 1H-1H COSYsample_Uisotropicsample_conditions
2D 1H-15N HSQCsample_U-15N-13Cisotropicsample_conditions
3D 1H-15N NOESYsample_U-15N-13Cisotropicsample_conditions
3D 1H-15N TOCSYsample_U-15N-13Cisotropicsample_conditions
3D CBCA(CO)NHsample_U-15N-13Cisotropicsample_conditions
3D HNCOsample_U-15N-13Cisotropicsample_conditions
3D HNCAsample_U-15N-13Cisotropicsample_conditions
3D HNCACBsample_U-15N-13Cisotropicsample_conditions
3D HBHA(CO)NHsample_U-15N-13Cisotropicsample_conditions
3D HN(CO)CAsample_U-15N-13Cisotropicsample_conditions
3D HNHAsample_U-15N-13Cisotropicsample_conditions

Software:

XEASY, Bartels et al. - chemical shift assignment

NMRView, Johnson, One Moon Scientific - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

DBJ BAA91635 BAD96951 BAE02260 BAI45652
EMBL CAG33537 CAH90563
GB AAH21721 AAI02410 ADZ15806 AIC51723 AKI69887
REF NP_001029820 NP_001125299 NP_001244808 NP_001271632 NP_060575
SP Q3T0G1 Q4R3Q6 Q5RCE4 Q9NVV9
TPG DAA14452
AlphaFold Q3T0G1 Q4R3Q6 Q5RCE4 Q9NVV9

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