BMRB Entry 51735

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51735

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Title:
NT8-13 bound enNTS1DM4
Deposition date:
2022-12-13
Original release date:
2022-12-30
Authors:
Bumbak, Fabian; Ziarek, Joshua; Robson, Scott; Wu, Hongwei
Citation:

Citation: Bumbak, Fabian; Pons, Miquel; Inoue, Asuka; Paniagua, Juan Carlos; Yan, Fei; Wu, Hongwei; Robson, Scott; Bathgate, Ross; Scott, Daniel; Gooley, Paul; Ziarek, Joshua. "Ligands selectively tune the local and global motions of neurotensin receptor 1 (NTS1)"  Cell Rep. 42, 112015-112015 (2023).
PubMed: 36680775

Assembly members:

Assembly members:
entity_1, polymer, 404 residues, 44889.10 Da.
entity_2, polymer, 6 residues, 817 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDS170

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSTSESDTAGPNSDLDVN TDIYSKVLVTAIYLALFVVG TVGNGVTLFTLARKKSLQSL QSRVDYYLGSLALSSLLILL FALPVDVYNFIWVHHPWAFG DAGCKGYYFLREACTYATAL NVVSLSVERYLAICHPFKAK TLLSRSRTKKFISAIWLASA LLSLPMLFTMGLQNLSGDGT HPGGLVCTPIVDTATLRVVI QLNTFMSFLFPMLVASILNT VIARRLTVLVHQAAEQARVS TVGTHNGLEHSTFNVTIEPG RVQALRRGVLVLRAVVIAFV VCWLPYHVRRLMFVYISDEQ WTTALFDFYHYFYMLSNALV YVSAAINPILYNLVSANFRQ VFLSTLASLSPGWRHRRKKR PTFSRKPNSVSSNHAFSTAS GLNDIFEAQKIEWHEGSGLE VLFQ
entity_2: RRPYIL

Data sets:
Data typeCount
13C chemical shifts17
1H chemical shifts51

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1enNTS1DM4, conformer A1
2enNTS1DM4, conformer B1
3enNTS1DM4, conformer C1
4NT8-132

Entities:

Entity 1, enNTS1DM4, conformer A 404 residues - 44889.10 Da.

Thermostabilized rat neurotensin receptor 1 variant starts with the first T (T43) and ends with T416 (truncated). The protein contains a C-terminal Avi-tag and remnants of a 3C-protease cleavage tag (ASGLNDIFEAQKIEWHEGSGLEVLFQ). The N-terminal four residues (GPGS) are remnants of a 3C-protease cleavage site and a short, flexible GS sequence.

1   GLYPROGLYSERTHRSERGLUSERASPTHR
2   ALAGLYPROASNSERASPLEUASPVALASN
3   THRASPILETYRSERLYSVALLEUVALTHR
4   ALAILETYRLEUALALEUPHEVALVALGLY
5   THRVALGLYASNGLYVALTHRLEUPHETHR
6   LEUALAARGLYSLYSSERLEUGLNSERLEU
7   GLNSERARGVALASPTYRTYRLEUGLYSER
8   LEUALALEUSERSERLEULEUILELEULEU
9   PHEALALEUPROVALASPVALTYRASNPHE
10   ILETRPVALHISHISPROTRPALAPHEGLY
11   ASPALAGLYCYSLYSGLYTYRTYRPHELEU
12   ARGGLUALACYSTHRTYRALATHRALALEU
13   ASNVALVALSERLEUSERVALGLUARGTYR
14   LEUALAILECYSHISPROPHELYSALALYS
15   THRLEULEUSERARGSERARGTHRLYSLYS
16   PHEILESERALAILETRPLEUALASERALA
17   LEULEUSERLEUPROMETLEUPHETHRMET
18   GLYLEUGLNASNLEUSERGLYASPGLYTHR
19   HISPROGLYGLYLEUVALCYSTHRPROILE
20   VALASPTHRALATHRLEUARGVALVALILE
21   GLNLEUASNTHRPHEMETSERPHELEUPHE
22   PROMETLEUVALALASERILELEUASNTHR
23   VALILEALAARGARGLEUTHRVALLEUVAL
24   HISGLNALAALAGLUGLNALAARGVALSER
25   THRVALGLYTHRHISASNGLYLEUGLUHIS
26   SERTHRPHEASNVALTHRILEGLUPROGLY
27   ARGVALGLNALALEUARGARGGLYVALLEU
28   VALLEUARGALAVALVALILEALAPHEVAL
29   VALCYSTRPLEUPROTYRHISVALARGARG
30   LEUMETPHEVALTYRILESERASPGLUGLN
31   TRPTHRTHRALALEUPHEASPPHETYRHIS
32   TYRPHETYRMETLEUSERASNALALEUVAL
33   TYRVALSERALAALAILEASNPROILELEU
34   TYRASNLEUVALSERALAASNPHEARGGLN
35   VALPHELEUSERTHRLEUALASERLEUSER
36   PROGLYTRPARGHISARGARGLYSLYSARG
37   PROTHRPHESERARGLYSPROASNSERVAL
38   SERSERASNHISALAPHESERTHRALASER
39   GLYLEUASNASPILEPHEGLUALAGLNLYS
40   ILEGLUTRPHISGLUGLYSERGLYLEUGLU
41   VALLEUPHEGLN

Entity 2, NT8-13 6 residues - 817 Da.

1   ARGARGPROTYRILELEU

Samples:

sample_1: enNTS1DM4, [13CH3-methionine], 66 uM; Potassium phosphate 50 mM; NaCl 100 mM; DSS 20 uM; DDM 0.05%; NT8-13 500 uM

sample_2: enNTS1DM4, [13CH3-methionine], 65 uM; Potassium phosphate 50 mM; NaCl 100 mM; DSS 20 uM; DDM 0.05%; NT8-13 500 uM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_2isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment, data analysis

TOPSPIN - data collection

qMDD - processing

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz