BMRB Entry 52860

Name: Backbone 1H, 13C and 15N chemical shift assignments for human JIP1 245-372
Published: 2025-02-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52860

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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:

Backbone 1H, 13C and 15N chemical shift assignments for human JIP1 245-372

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, 128 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: MAPPGGPPAAPPGGRGHSHR DRIHYQADVRLEATEEIYLT PVQRPPDAAEPTSAFLPPTE SRMSVSSDPDPAAYPSTAGR PHPSISEEEEGFDCLSSPER AEPPGGGWRGSLGEPPPPPR ASLSSDTS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	334
15N chemical shifts	102
1H chemical shifts	102

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	JIP1 245-372	1

Entities:

Entity 1, JIP1 245-372 128 residues - Formula weight is not available

1

MET

ALA

PRO

GLY

PRO

ALA

2

PRO

GLY

ARG

GLY

HIS

SER

HIS

ARG

3

ASP

ARG

ILE

HIS

TYR

GLN

ALA

ASP

VAL

ARG

4

LEU

GLU

ALA

THR

GLU

ILE

TYR

LEU

THR

5

PRO

VAL

GLN

ARG

PRO

ASP

ALA

GLU

6

PRO

THR

SER

ALA

PHE

LEU

PRO

THR

GLU

7

SER

ARG

MET

SER

VAL

SER

ASP

PRO

ASP

8

PRO

ALA

TYR

PRO

SER

THR

ALA

GLY

ARG

9

PRO

HIS

PRO

SER

ILE

SER

GLU

10

GLY

PHE

ASP

CYS

LEU

SER

PRO

GLU

ARG

11

ALA

GLU

PRO

GLY

TRP

ARG

GLY

12

SER

LEU

GLY

GLU

PRO

ARG

13

ALA

SER

LEU

SER

ASP

THR

SER

Samples:

sample_1: JIP1 245-372, [U-100% 13C; U-100% 15N], 800 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

SPARKY - peak picking

MARS - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 850 MHz