BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51766

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

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: 15N, 1H, 13CA, 13CB and 13CO assignment of human SENP1 419-644   PubMed: 36921622

Deposition date: 2023-01-09 Original release date: 2023-05-01

Authors: Fischer, Patrick

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).

Assembly members:
entity_1, polymer, 226 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: pET28a

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
  • Hide all

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 shifts
SPARKY: Backbone or all simulated shifts