BMRB Entry 34101

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PDB ID:
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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NMR-STAR v3 text file.
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Title:
Solution structure of the Dbl-homology domain of Bcr-Abl
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:

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).
PubMed: 29235475

Assembly members:

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

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

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts1008
15N chemical shifts210
1H chemical shifts1656

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 218 residues - 24844.432 Da.

1   ALAMETALASERGLULEUASPLEUGLULYS
2   GLYLEUGLUMETARGLYSTRPVALLEUSER
3   GLYILELEUALASERGLUGLUTHRTYRLEU
4   SERHISLEUGLUALALEULEULEUPROMET
5   LYSPROLEULYSALAALAALATHRTHRSER
6   GLNPROVALLEUTHRSERGLNGLNILEGLU
7   THRILEPHEPHELYSVALPROGLULEUTYR
8   GLUILEHISLYSGLUPHETYRASPGLYLEU
9   PHEPROARGVALGLNGLNTRPSERHISGLN
10   GLNARGVALGLYASPLEUPHEGLNLYSLEU
11   ALASERGLNLEUGLYVALTYRARGALAPHE
12   VALASPASNTYRGLYVALALAMETGLUMET
13   ALAGLULYSCYSCYSGLNALAASNALAGLN
14   PHEALAGLUILESERGLUASNLEUARGALA
15   ARGSERASNLYSASPALALYSASPPROTHR
16   THRLYSASNSERLEUGLUTHRLEULEUTYR
17   LYSPROVALASPARGVALTHRARGSERTHR
18   LEUVALLEUHISASPLEULEULYSHISTHR
19   PROALASERHISPROASPHISPROLEULEU
20   GLNASPALALEUARGILESERGLNASNPHE
21   LEUSERSERILEASNGLUGLUILETHRPRO
22   ARGARGGLNSERMETTHRVALLYS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)HAsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D (H)CC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCCO)NH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks