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 27290

Title: (1)H, (13)C, (15)N resonance assignment of human YAP 50-171 fragment   PubMed: 29372459

Deposition date: 2017-10-24 Original release date: 2018-01-25

Authors: Feichtinger, Michael; Sara, Tomas; Platzer, Gerald; Mateos, Borja; Bokhovchuk, Fedir; Chene, Patrick; Konrat, Robert

Citation: Feichtinger, Michael; Sara, Tomas; Platzer, Gerald; Mateos, Borja; Bokhovchuk, Fedir; Chene, Patrick; Konrat, Robert. "1H, 13C, 15N resonance assignment of human YAP 50-171 fragment"  Biomol. NMR Assign. 12, 179-182 (2018).

Assembly members:
YAP_50-171, polymer, 122 residues, Formula weight is not available

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: PETM14

Entity Sequences (FASTA):
YAP_50-171: AGHQIVHVRGDSETDLEALF NAVMNPKTANVPQTVPMRLR KLPDSFFKPPEPKSHSRQAS TDAGTAGALTPQHVRAHSSP ASLQLGAVSPGTLTPTGVVS GPAATPTAQHLRQSSFEIPD DV

Data sets:
Data typeCount
13C chemical shifts274
15N chemical shifts102
1H chemical shifts101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human YAP 50-171 fragment1

Entities:

Entity 1, human YAP 50-171 fragment 122 residues - Formula weight is not available

1   ALAGLYHISGLNILEVALHISVALARGGLY
2   ASPSERGLUTHRASPLEUGLUALALEUPHE
3   ASNALAVALMETASNPROLYSTHRALAASN
4   VALPROGLNTHRVALPROMETARGLEUARG
5   LYSLEUPROASPSERPHEPHELYSPROPRO
6   GLUPROLYSSERHISSERARGGLNALASER
7   THRASPALAGLYTHRALAGLYALALEUTHR
8   PROGLNHISVALARGALAHISSERSERPRO
9   ALASERLEUGLNLEUGLYALAVALSERPRO
10   GLYTHRLEUTHRPROTHRGLYVALVALSER
11   GLYPROALAALATHRPROTHRALAGLNHIS
12   LEUARGGLNSERSERPHEGLUILEPROASP
13   ASPVAL

Samples:

sample_1: YAP 50-171, [U-95% 13C; U-90% 15N], 0.5 mM; sodium chloride 150 mM; EDTA 1 mM; TRIS 20 mM

sample_conditions_1: ionic strength: 171 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCANNHsample_1isotropicsample_conditions_1
3D HN(COCA)NNHsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment

SPARKY, Goddard - data analysis

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

NMR spectrometers:

  • Bruker Avance 800 MHz

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