BMRB Entry 26331

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for tyrosine kinase A domain 5
Published: 2022-08-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26331

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for tyrosine kinase A domain 5

Deposition date:

2022-06-15

Original release date:

2022-08-11

Authors:

Suzuki, Rika; Ekimoto, Toru; Tosaka, Ayami; Takahashi, Maho; Sakakura, Masayoshi; Yamane, Tsutomu; Mizukoshi, Yumiko; Takeuchi, Koh; Simada, Ichio; Ikeguchi, Mitsunori; Takahash, Hideo

Citation:

Citation: Suzuki, Rika; Ekimoto, Toru; Tosaka, Ayami; Takahashi, Maho; Sakakura, Masayoshi; Yamane, Tsutomu; Mizukoshi, Yumiko; Takeuchi, Koh; Simada, Ichio; Ikeguchi, Mitsunori; Takahash, Hideo. "Dynamic Interaction Modes of Peptide Ligands Revealed by Integrated Use of NMR and REST Simulations" J. Chem. Inf. Model. ., .-..

Assembly members:

Assembly members:
TrkAd5, polymer, 108 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: pet21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TrkAd5: GSHMVNVSFPASVQLHTAVE MHHWCIPFSVDGQPAPSLRW LFNGSVLNETSFIFTEFLEP AANETVRHGCLRLNQPTHVN NGNYTLLAANPFGQASASIM AAFMDNPF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	175
15N chemical shifts	91
1H chemical shifts	91

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TrkAd5	1

Entities:

Entity 1, TrkAd5 108 residues - Formula weight is not available

1

GLY

SER

HIS

MET

VAL

ASN

VAL

SER

PHE

PRO

2

ALA

SER

VAL

GLN

LEU

HIS

THR

ALA

VAL

GLU

3

MET

HIS

TRP

CYS

ILE

PRO

PHE

SER

VAL

4

ASP

GLY

GLN

PRO

ALA

PRO

SER

LEU

ARG

TRP

5

LEU

PHE

ASN

GLY

SER

VAL

LEU

ASN

GLU

THR

6

SER

PHE

ILE

PHE

THR

GLU

PHE

LEU

GLU

PRO

7

ALA

ASN

GLU

THR

VAL

ARG

HIS

GLY

CYS

8

LEU

ARG

LEU

ASN

GLN

PRO

THR

HIS

VAL

ASN

9

ASN

GLY

ASN

TYR

THR

LEU

ALA

ASN

10

PRO

PHE

GLY

GLN

ALA

SER

ALA

SER

ILE

MET

11

ALA

PHE

MET

ASP

ASN

PRO

PHE

Samples:

sample_1: TrkAd5, [U-13C; U-15N], protein mM; DSS 2 mM; sodium phosphate 50 mM; sodium chloride 150 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: pH: 7.0; temperature: 298 K

Experiments:

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

Software:

CARA - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

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