BMRB Entry 19037

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19037

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Title:
1H, 13C, and 15N Chemical Shift Assignments of h-prune C-terminal domain
Deposition date:
2013-02-14
Original release date:
2013-03-04
Authors:
Diana, Donatella; Fattorusso, Roberto
Citation:

Citation: Carotenuto, Marianeve; Pedone, Emilia; Diana, Donatella; de Antonellis, Pasqualino; Deroski, Sao; Marino, Natascia; Navas, Luigi; Di Dato, Valeria; Scoppettuolo, Maria Nunzia; Cimmino, Flora; Correale, Stefania; Pirone, Luciano; Monti, Simona Maria; Bruder, Elisabeth; Zenko, Bernard; Slavkov, Ivica; Pastorino, Fabio; Ponzoni, Mirco; Schulte, Johannes; Schramm, Alexander; Eggert, Angelika; Westermann, Frank; Arrigoni, Gianluigi; Accordi, Benedetta; Basso, Giuseppe; Saviano, Michele; Fattorusso, Roberto; Zollo, Massimo. "Neuroblastoma tumorigenesis is regulated through the Nm23-H1/h-Prune C-terminal interaction."  Sci. Rep. 3, 1351-1351 (2013).
PubMed: 23448979

Assembly members:

Assembly members:
h-prune_C-terminal_domain, polymer, 100 residues, Formula weight is not available

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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
h-prune_C-terminal_domain: LLQEALSAYFDSMKIPSGQP ETADVSREQVDKELDRASNS LISGLSQDEEDPPLPPTPMN SLVDECPLDQGLPKLSAEAV FEKCSQISLSQSTTASLSKK

Data sets:
Data typeCount
13C chemical shifts247
15N chemical shifts86
1H chemical shifts201

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1h-prune C-terminal domain1

Entities:

Entity 1, h-prune C-terminal domain 100 residues - Formula weight is not available

1   LEULEUGLNGLUALALEUSERALATYRPHE
2   ASPSERMETLYSILEPROSERGLYGLNPRO
3   GLUTHRALAASPVALSERARGGLUGLNVAL
4   ASPLYSGLULEUASPARGALASERASNSER
5   LEUILESERGLYLEUSERGLNASPGLUGLU
6   ASPPROPROLEUPROPROTHRPROMETASN
7   SERLEUVALASPGLUCYSPROLEUASPGLN
8   GLYLEUPROLYSLEUSERALAGLUALAVAL
9   PHEGLULYSCYSSERGLNILESERLEUSER
10   GLNSERTHRTHRALASERLEUSERLYSLYS

Samples:

sample_1: h-prune C-terminal domain, [U-100% 13C; U-100% 15N], 0.6 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CARA v1.5, 1.8, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

DBJ BAB55423 BAG37575 BAG57478 BAG60534 BAH14908
EMBL CAH56396
GB AAC95290 AAF04914 AAH14886 AAH25304 AAH63481
REF NP_001267140 NP_001290158 NP_001290171 NP_001290172 NP_067045
SP Q86TP1
AlphaFold Q86TP1

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