BMRB Entry 51766

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51766

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Title:
15N, 1H, 13CA, 13CB and 13CO assignment of human SENP1 419-644
Deposition date:
2023-01-09
Original release date:
2023-05-01
Authors:
Fischer, Patrick
Citation:

Citation: Liu, Weihai; Wang, Yun; Bozi, Luiz; Fischer, Patrick; Jedrychowski, Mark; Xiao, Haopeng; Wu, Tao; Darabedian, Narek; He, Xiadi; Mills, Evanna; Burger, Nils; Shin, Sanghee; Reddy, Anita; Sprenger, Hans-Georg; Tran, Nhien; Winther, Sally; Hinshaw, Stephen; Shen, Jingnan; Seo, Hyuk-Soo; Song, Kijun; Xu, Andrew; Sebastian, Luke; Zhao, Jean; Dhe-Paganon, Sirano; Che, Jianwei; Gygi, Steven; Arthanari, Haribabu; Chouchani, Edward. "Lactate regulates cell cycle by remodelling the anaphase promoting complex"  Nature 616, 790-797 (2023).
PubMed: 36921622

Assembly members:

Assembly members:
entity_1, polymer, 226 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: EFPEITEEMEKEIKNVFRNG NQDEVLSEAFRLTITRKDIQ TLNHLNWLNDEIINFYMNML MERSKEKGLPSVHAFNTFFF TKLKTAGYQAVKRWTKKVDV FSVDILLVPIHLGVHWCLAV VDFRKKNITYYDSMGGINNE ACRILLQYLKQESIDKKRKE FDTNGWQLFSKKSQEIPQQM NGSDCGMFACKYADCITKDR PINFTQQHMPYFRKRMVWEI LHRKLL

Data sets:
Data typeCount
13C chemical shifts571
15N chemical shifts190
1H chemical shifts190

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1SENP1 single polypeptide chain1

Entities:

Entity 1, SENP1 single polypeptide chain 226 residues - Formula weight is not available

1   GLUPHEPROGLUILETHRGLUGLUMETGLU
2   LYSGLUILELYSASNVALPHEARGASNGLY
3   ASNGLNASPGLUVALLEUSERGLUALAPHE
4   ARGLEUTHRILETHRARGLYSASPILEGLN
5   THRLEUASNHISLEUASNTRPLEUASNASP
6   GLUILEILEASNPHETYRMETASNMETLEU
7   METGLUARGSERLYSGLULYSGLYLEUPRO
8   SERVALHISALAPHEASNTHRPHEPHEPHE
9   THRLYSLEULYSTHRALAGLYTYRGLNALA
10   VALLYSARGTRPTHRLYSLYSVALASPVAL
11   PHESERVALASPILELEULEUVALPROILE
12   HISLEUGLYVALHISTRPCYSLEUALAVAL
13   VALASPPHEARGLYSLYSASNILETHRTYR
14   TYRASPSERMETGLYGLYILEASNASNGLU
15   ALACYSARGILELEULEUGLNTYRLEULYS
16   GLNGLUSERILEASPLYSLYSARGLYSGLU
17   PHEASPTHRASNGLYTRPGLNLEUPHESER
18   LYSLYSSERGLNGLUILEPROGLNGLNMET
19   ASNGLYSERASPCYSGLYMETPHEALACYS
20   LYSTYRALAASPCYSILETHRLYSASPARG
21   PROILEASNPHETHRGLNGLNHISMETPRO
22   TYRPHEARGLYSARGMETVALTRPGLUILE
23   LEUHISARGLYSLEULEU

Samples:

sample_1: SENP1 419-644, [U-13C; U-15N; U-2H], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CcpNMR - 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