BMRB Entry 52861

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52861

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Title:
Backbone 1H, 13C and 15N chemical shift assignments for human JIP1 353-553
Deposition date:
2025-01-15
Original release date:
2025-02-10
Authors:
Orand, Thibault; Delaforge, Elise; Jensen, Malene
Citation:

Citation: Orand, Thibault; Delaforge, Elise; Lee, Alexandra; Kragelj, Jaka; Tengo, Maud; Tengo, Laura; Blackledge, Martin; Boeri Erba, Elisabetta; Davis, Roger; Palencia, Andres; Jensen, Malene Ringkjobing. "Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1"  Proc. Natl. Acad. Sci. U.S.A. 122, e2419915122-e2419915122 (2025).
PubMed: 39999166

Assembly members:

Assembly members:
entity_1, polymer, 201 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: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: RGSLGEPPPPPRASLSSDTS ALSYDSVKYTLVVDEHAQLE LVSLRPCFGDYSDESDSATV YDNCASVSSPYESAIGEEYE EAPRPQPPACLSEDSTPDEP DVHFSKKFLNVFMSGRSRSS SAESFGLFSCIINGEEQEQT HRAIFRFVPRHEDELELEVD DPLLVELQAEDYWYEAYNMR TGARGVFPAYYAIEVTKEPE H

Data sets:
Data typeCount
13C chemical shifts283
15N chemical shifts88
1H chemical shifts88

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1JIP1 353-5531

Entities:

Entity 1, JIP1 353-553 201 residues - Formula weight is not available

1   ARGGLYSERLEUGLYGLUPROPROPROPRO
2   PROARGALASERLEUSERSERASPTHRSER
3   ALALEUSERTYRASPSERVALLYSTYRTHR
4   LEUVALVALASPGLUHISALAGLNLEUGLU
5   LEUVALSERLEUARGPROCYSPHEGLYASP
6   TYRSERASPGLUSERASPSERALATHRVAL
7   TYRASPASNCYSALASERVALSERSERPRO
8   TYRGLUSERALAILEGLYGLUGLUTYRGLU
9   GLUALAPROARGPROGLNPROPROALACYS
10   LEUSERGLUASPSERTHRPROASPGLUPRO
11   ASPVALHISPHESERLYSLYSPHELEUASN
12   VALPHEMETSERGLYARGSERARGSERSER
13   SERALAGLUSERPHEGLYLEUPHESERCYS
14   ILEILEASNGLYGLUGLUGLNGLUGLNTHR
15   HISARGALAILEPHEARGPHEVALPROARG
16   HISGLUASPGLULEUGLULEUGLUVALASP
17   ASPPROLEULEUVALGLULEUGLNALAGLU
18   ASPTYRTRPTYRGLUALATYRASNMETARG
19   THRGLYALAARGGLYVALPHEPROALATYR
20   TYRALAILEGLUVALTHRLYSGLUPROGLU
21   HIS

Samples:

sample_1: JIP1 353-553, [U-100% 13C; U-100% 15N], 385 uM; HEPES 50 mM; sodium chloride 150 mM; glycerol 5 % v/v; DTT 2 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.1; pressure: 1 atm; temperature: 278.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

SPARKY - peak picking

MARS - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

UNP Q9UQF2

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