BMRB Entry 51361

Title:
1H, 13C and 15N Backbone Chemical Shift Assignments of the SH3 domain of the JNK-interacting protein 2, conformations corresponding to proline 664 cis-trans isomerization
Deposition date:
2022-03-14
Original release date:
2024-08-09
Authors:
Marino Perez, Laura; Ringkjobing Jensen, Malene
Citation:

Citation: Marino Perez, Laura; Ielasi, Francesco; Lee, Alexandra; Delaforge, Elise; Juyoux, Pauline; Tengo, Maud; Davis, Roger; Palencia, Andres; Jensen, Malene Ringkjobing. "Structural basis of homodimerization of the JNK scaffold protein JIP2 and its heterodimerization with JIP1"  Structure ., .-. (2024).
PubMed: 39013462

Assembly members:

Assembly members:
entity_1, polymer, 63 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: pESPRIT

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts346
15N chemical shifts112
1H chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WT JIP2-SH3, cis conformer1
2WT JIP2-SH3, trans conformer1

Entities:

Entity 1, WT JIP2-SH3, cis conformer 63 residues - Formula weight is not available

1   GLYARGARGGLUGLNTHRHISARGALAVAL
2   PHEARGPHEILEPROARGHISPROASPGLU
3   LEUGLULEUASPVALASPASPPROVALLEU
4   VALGLUALAGLUGLUASPASPPHETRPPHE
5   ARGGLYPHEASNMETARGTHRGLYGLUARG
6   GLYVALPHEPROALAPHETYRALAHISALA
7   VALPROGLY

Samples:

sample_1: JIP2-SH3 WT, [U-95% 13C; U-95% 15N], 2 mM; NaCl 150 mM; HEPES 50 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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