BMRB Entry 52858

Name: Backbone 1H, 13C and 15N chemical shift assignments for human JIP1 1-145
Published: 2025-02-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52858

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H, 13C and 15N chemical shift assignments for human JIP1 1-145

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, 145 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: MAERESGGLGGGAASPPAAS PFLGLHIASPPNFRLTHDIS LEEFEDEDLSEITDECGISL QCKDTLSLRPPRAGLLSAGG GGAGSRLQAEMLQMDLIDAT GDTPGAEDDEEDDDEERAAR RPGAGPPKAESGQEPASRGQ GQSQG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	402
15N chemical shifts	130
1H chemical shifts	130

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	JIP1 1-145	1

Entities:

Entity 1, JIP1 1-145 145 residues - Formula weight is not available

1

MET

ALA

GLU

ARG

GLU

SER

GLY

LEU

GLY

2

GLY

ALA

SER

PRO

ALA

SER

3

PRO

PHE

LEU

GLY

LEU

HIS

ILE

ALA

SER

PRO

4

PRO

ASN

PHE

ARG

LEU

THR

HIS

ASP

ILE

SER

5

LEU

GLU

PHE

GLU

ASP

GLU

ASP

LEU

SER

6

GLU

ILE

THR

ASP

GLU

CYS

GLY

ILE

SER

LEU

7

GLN

CYS

LYS

ASP

THR

LEU

SER

LEU

ARG

PRO

8

PRO

ARG

ALA

GLY

LEU

SER

ALA

GLY

9

GLY

ALA

GLY

SER

ARG

LEU

GLN

ALA

GLU

10

MET

LEU

GLN

MET

ASP

LEU

ILE

ASP

ALA

THR

11

GLY

ASP

THR

PRO

GLY

ALA

GLU

ASP

GLU

12

GLU

ASP

GLU

ARG

ALA

ARG

13

ARG

PRO

GLY

ALA

GLY

PRO

LYS

ALA

GLU

14

SER

GLY

GLN

GLU

PRO

ALA

SER

ARG

GLY

GLN

15

GLY

GLN

SER

GLN

GLY

Samples:

sample_1: JIP1 1-145, [U-100% 13C; U-100% 15N], 500 uM; HEPES 50 mM; sodium chloride 150 mM; DTT 2 mM

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

SPARKY - peak picking

MARS - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz