BMRB Entry 53319

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53319

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Title:
Dynamic and Selective Competition Govern Binding of Large Tumor Suppressor 1 to KIBRA and YAP
Deposition date:
2025-08-14
Original release date:
2025-11-14
Authors:
Ramprasad, Sanjay; Baker, Kasie; Rodriguez, Diego; Kwok, Ethiene; Pung, Lydia; Nyarko, Afua
Citation:

Citation: Ramprasad, Sanjay; Baker, Kasie; Rodriguez, Diego; Kwok, Ethiene; Pung, Lydia; Nyarko, Afua. "1H, 13C, 15N assigned chemical shifts for LATS1 residues 357-604"  Protein Sci. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 248 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: pET24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MIHQNVVPAGTVNRQPPPPY PLTAANGQSPSALQTGGSAA PSSYTNGSIPQSMMVPNRNS HNMELYNISVPGLQTNWPQS SSAPAQSSPSSGHEIPTWQP NIPVRSNSFNNPLGNRASHS ANSQPSATTVTAITPAPIQQ PVKSMRVLKPELQTALAPTH PSWIPQPIQTVQPSPFPEGT ASNVTVMPPVAEAPNYQGPP PPYPKHLLHQNPSVPPYESI SKPSKEDQPSLPKEDESEKS YENVDSGD

Data sets:
Data typeCount
13C chemical shifts550
15N chemical shifts164
1H chemical shifts262

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LATS11

Entities:

Entity 1, LATS1 248 residues - Formula weight is not available

1   METILEHISGLNASNVALVALPROALAGLY
2   THRVALASNARGGLNPROPROPROPROTYR
3   PROLEUTHRALAALAASNGLYGLNSERPRO
4   SERALALEUGLNTHRGLYGLYSERALAALA
5   PROSERSERTYRTHRASNGLYSERILEPRO
6   GLNSERMETMETVALPROASNARGASNSER
7   HISASNMETGLULEUTYRASNILESERVAL
8   PROGLYLEUGLNTHRASNTRPPROGLNSER
9   SERSERALAPROALAGLNSERSERPROSER
10   SERGLYHISGLUILEPROTHRTRPGLNPRO
11   ASNILEPROVALARGSERASNSERPHEASN
12   ASNPROLEUGLYASNARGALASERHISSER
13   ALAASNSERGLNPROSERALATHRTHRVAL
14   THRALAILETHRPROALAPROILEGLNGLN
15   PROVALLYSSERMETARGVALLEULYSPRO
16   GLULEUGLNTHRALALEUALAPROTHRHIS
17   PROSERTRPILEPROGLNPROILEGLNTHR
18   VALGLNPROSERPROPHEPROGLUGLYTHR
19   ALASERASNVALTHRVALMETPROPROVAL
20   ALAGLUALAPROASNTYRGLNGLYPROPRO
21   PROPROTYRPROLYSHISLEULEUHISGLN
22   ASNPROSERVALPROPROTYRGLUSERILE
23   SERLYSPROSERLYSGLUASPGLNPROSER
24   LEUPROLYSGLUASPGLUSERGLULYSSER
25   TYRGLUASNVALASPSERGLYASP

Samples:

sample_1: LATS1, [U-13C; U-15N], mM; sodium phosphate 10 mM; sodium chloride 100 mM; TCEP 2 mM; DSS 5%

sample_conditions_1: ionic strength: 0.121 M; pH: 7.3; pressure: 1 atm; temperature: 283.15 K

Experiments:

NameSampleSample stateSample conditions
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

Sparky - chemical shift assignment

NMRViewJ - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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