BMRB Entry 51496

Name: 1H, 13C and 15N Backbone Chemical Shift Assignments of the R502E SH3 variant of the JNK-interacting protein 1
Published: 2024-08-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51496

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C and 15N Backbone Chemical Shift Assignments of the R502E SH3 variant of the JNK-interacting protein 1

Deposition date:

2022-06-20

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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMEQTHRAIFRFVPEHEDE LELEVDDPLLVELQAEDYWY EAYNMRTGARGVFPAYYAIE VTK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	181
15N chemical shifts	56
1H chemical shifts	56

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	R502E JIP1-SH3	1

Entities:

Entity 1, R502E JIP1-SH3 63 residues - Formula weight is not available

1

GLY

HIS

MET

GLU

GLN

THR

HIS

ARG

ALA

ILE

2

PHE

ARG

PHE

VAL

PRO

GLU

HIS

GLU

ASP

GLU

3

LEU

GLU

LEU

GLU

VAL

ASP

PRO

LEU

4

VAL

GLU

LEU

GLN

ALA

GLU

ASP

TYR

TRP

TYR

5

GLU

ALA

TYR

ASN

MET

ARG

THR

GLY

ALA

ARG

6

GLY

VAL

PHE

PRO

ALA

TYR

ALA

ILE

GLU

7

VAL

THR

LYS

Samples:

sample_1: JIP1-SH3 R502E, [U-95% 13C; U-95% 15N], 750 uM; NaCl 150 mM; HEPES 50 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D BT_HNCO	sample_1	isotropic	sample_conditions_1
3D BT_HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D BT_HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D BT_iHNCACB	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

MARS - chemical shift assignment

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

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III 850 MHz

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