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 26961

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26961

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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for SUSP4(201-300)   PubMed: 28000315

Deposition date: 2016-11-29 Original release date: 2017-02-15

Authors: Kim, Do-Hyoung; Lee, Chewook; Lee, Si-Hyung; Kim, Kyung-Tae; Han, Joan J; Cha, Eun-Ji; Lim, Ji-Eun; Hong, Seung-Hee; Cho, Ye-Jin; Han, Kyou-Hoon

Citation: Kim, Do-Hyoung; Lee, Chewook; Lee, Si-Hyung; Kim, Kyung-Tae; Han, Joan; Cha, Eun-Ji; Lim, Ji-Eun; Cho, Ye-Jin; Hong, Seung-Hee; Han, Kyou-Hoon. "The Mechanism of p53 Rescue by SUSP4"  Angew. Chem. Int. Ed. Engl. 56, 1278-1282 (2017).

Assembly members:
SUMO-specific_protease_4_(SUSP4_201-300), polymer, 100 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

Entity Sequences (FASTA):
SUMO-specific_protease_4_(SUSP4_201-300): EEREKWCSEEKCVTEKKGCV KGEGRRGNSLEPGTRAQIIL DRGRGNSLLPNKMAVLAAEK KPLTDQEKGREMYQILVITE DIEKEIENALGPGPQEEILS

Data sets:
Data typeCount
13C chemical shifts410
15N chemical shifts95
1H chemical shifts611

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SUMO-specific protease 4 (SUSP4 201-300)1

Entities:

Entity 1, SUMO-specific protease 4 (SUSP4 201-300) 100 residues - Formula weight is not available

1   GLUGLUARGGLULYSTRPCYSSERGLUGLU
2   LYSCYSVALTHRGLULYSLYSGLYCYSVAL
3   LYSGLYGLUGLYARGARGGLYASNSERLEU
4   GLUPROGLYTHRARGALAGLNILEILELEU
5   ASPARGGLYARGGLYASNSERLEULEUPRO
6   ASNLYSMETALAVALLEUALAALAGLULYS
7   LYSPROLEUTHRASPGLNGLULYSGLYARG
8   GLUMETTYRGLNILELEUVALILETHRGLU
9   ASPILEGLULYSGLUILEGLUASNALALEU
10   GLYPROGLYPROGLNGLUGLUILELEUSER

Samples:

P4-201: SUMO-specific protease 4 (SUSP4 201-300), [U-98% 13C; U-98% 15N], 0.4 mM; SUMO-specific protease 4 (SUSP4 201-300), [U-98% 15N], 0.5 mM; sodium acetate 20 mM; PMSF 0.1 mM; EDTA 0.01 mM; DTT 1 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCP4-201isotropicsample_conditions_1
3D CBCA(CO)NHP4-201isotropicsample_conditions_1
3D C(CO)NHP4-201isotropicsample_conditions_1
3D HNCOP4-201isotropicsample_conditions_1
3D HNCACBP4-201isotropicsample_conditions_1
3D HN(CO)CAP4-201isotropicsample_conditions_1
3D H(CCO)NHP4-201isotropicsample_conditions_1
3D HNHAP4-201isotropicsample_conditions_1
3D 1H-15N NOESYP4-201isotropicsample_conditions_1
3D 1H-15N TOCSYP4-201isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 900 MHz

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