BMRB Entry 34101

Name: Solution structure of the Dbl-homology domain of Bcr-Abl
Published: 2017-12-21

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PDB ID: 5n6r
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34101
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the Dbl-homology domain of Bcr-Abl PubMed: 29235475

Deposition date: 2017-02-16 Original release date: 2017-12-21

Authors: Reckel, S.; Lohr, F.; Buchner, L.; Guntert, P.; Dotsch, V.; Hantschel, O.

Citation: Reckel, Sina; Gehin, Charlotte; Tardivon, Delphine; Georgeon, Sandrine; Kukenshoner, Tim; Lohr, Frank; Koide, Akiko; Buchner, Lena; Panjkovich, Alejandro; Reynaud, Aline; Pinho, Sara; Gerig, Barbara; Svergun, Dmitri; Pojer, Florence; Guntert, Peter; Dotsch, Volker; Koide, Shohei; Gavin, Anne-Claude; Hantschel, Oliver. "Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase" Nat. Commun. 8, 2101-2101 (2017).

Assembly members:
entity_1, polymer, 218 residues, 24844.432 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: AMASELDLEKGLEMRKWVLS GILASEETYLSHLEALLLPM KPLKAAATTSQPVLTSQQIE TIFFKVPELYEIHKEFYDGL FPRVQQWSHQQRVGDLFQKL ASQLGVYRAFVDNYGVAMEM AEKCCQANAQFAEISENLRA RSNKDAKDPTTKNSLETLLY KPVDRVTRSTLVLHDLLKHT PASHPDHPLLQDALRISQNF LSSINEEITPRRQSMTVK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	1008
15N chemical shifts	210
1H chemical shifts	1656

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 218 residues - 24844.432 Da.

1

ALA

MET

ALA

SER

GLU

LEU

ASP

LEU

GLU

LYS

2

GLY

LEU

GLU

MET

ARG

LYS

TRP

VAL

LEU

SER

3

GLY

ILE

LEU

ALA

SER

GLU

THR

TYR

LEU

4

SER

HIS

LEU

GLU

ALA

LEU

PRO

MET

5

LYS

PRO

LEU

LYS

ALA

THR

SER

6

GLN

PRO

VAL

LEU

THR

SER

GLN

ILE

GLU

7

THR

ILE

PHE

LYS

VAL

PRO

GLU

LEU

TYR

8

GLU

ILE

HIS

LYS

GLU

PHE

TYR

ASP

GLY

LEU

9

PHE

PRO

ARG

VAL

GLN

TRP

SER

HIS

GLN

10

GLN

ARG

VAL

GLY

ASP

LEU

PHE

GLN

LYS

LEU

11

ALA

SER

GLN

LEU

GLY

VAL

TYR

ARG

ALA

PHE

12

VAL

ASP

ASN

TYR

GLY

VAL

ALA

MET

GLU

MET

13

ALA

GLU

LYS

CYS

GLN

ALA

ASN

ALA

GLN

14

PHE

ALA

GLU

ILE

SER

GLU

ASN

LEU

ARG

ALA

15

ARG

SER

ASN

LYS

ASP

ALA

LYS

ASP

PRO

THR

16

THR

LYS

ASN

SER

LEU

GLU

THR

LEU

TYR

17

LYS

PRO

VAL

ASP

ARG

VAL

THR

ARG

SER

THR

18

LEU

VAL

LEU

HIS

ASP

LEU

LYS

HIS

THR

19

PRO

ALA

SER

HIS

PRO

ASP

HIS

PRO

LEU

20

GLN

ASP

ALA

LEU

ARG

ILE

SER

GLN

ASN

PHE

21

LEU

SER

ILE

ASN

GLU

ILE

THR

PRO

22

ARG

GLN

SER

MET

THR

VAL

LYS

Samples:

sample_1: DH, [U-13C; U-15N], 0.85 mM; Hepes 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)HA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	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 (H)CC(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCCO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert P. - structure calculation

FLYA, Guntert P. - chemical shift assignment

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker 600 Bruker Avance 600 MHz
Bruker Avance 700 MHz
Bruker 800 Bruker Avance 800 MHz
Bruker 900 Bruker Avance 900 MHz
Bruker 950 Bruker Avance 950 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts