BMRB Entry 52859

Name: Backbone 1H, 13C and 15N chemical shift assignments for human JIP1 116-266
Published: 2025-02-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52859

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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 116-266

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, 151 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: ERAARRPGAGPPKAESGQEP ASRGQGQSQGQSQGPGSGDT YRPKRPTTLNLFPQVPRSQD TLNNNSLGKKHSWQDRVSRS SSPLKTGEQTPPHEHICLSD ELPPQSGPAPTTDRGTSTDS PCRRSTATQMAPPGGPPAAP PGGRGHSHRDR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	411
15N chemical shifts	124
1H chemical shifts	124

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	JIP1 1160266	1

Entities:

Entity 1, JIP1 1160266 151 residues - Formula weight is not available

1

GLU

ARG

ALA

ARG

PRO

GLY

ALA

GLY

2

PRO

LYS

ALA

GLU

SER

GLY

GLN

GLU

PRO

3

ALA

SER

ARG

GLY

GLN

GLY

GLN

SER

GLN

GLY

4

GLN

SER

GLN

GLY

PRO

GLY

SER

GLY

ASP

THR

5

TYR

ARG

PRO

LYS

ARG

PRO

THR

LEU

ASN

6

LEU

PHE

PRO

GLN

VAL

PRO

ARG

SER

GLN

ASP

7

THR

LEU

ASN

SER

LEU

GLY

LYS

8

HIS

SER

TRP

GLN

ASP

ARG

VAL

SER

ARG

SER

9

SER

PRO

LEU

LYS

THR

GLY

GLU

GLN

THR

10

PRO

HIS

GLU

HIS

ILE

CYS

LEU

SER

ASP

11

GLU

LEU

PRO

GLN

SER

GLY

PRO

ALA

PRO

12

THR

ASP

ARG

GLY

THR

SER

THR

ASP

SER

13

PRO

CYS

ARG

SER

THR

ALA

THR

GLN

MET

14

ALA

PRO

GLY

PRO

ALA

PRO

15

PRO

GLY

ARG

GLY

HIS

SER

HIS

ARG

ASP

16

ARG

Samples:

sample_1: JIP1 116-266, [U-100% 13C; U-100% 15N], 1 mM; 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:

NMRPipe - processing

SPARKY - data analysis

MARS - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz