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Biological Magnetic Resonance Data Bank


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BMRB Entry 30331

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30331
MolProbity Validation Chart

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Title: Abl 1b Regulatory Module 'inhibiting state'   PubMed: 28945248

Deposition date: 2017-08-11 Original release date: 2017-09-25

Authors: Kalodimos, C.; Saleh, T.; Rossi, P.

Citation: Saleh, T.; Rossi, P.; Kalodimos, C.. "Atomic view of the energy landscape in the allosteric regulation of Abl kinase"  Nat. Struct. Mol. Biol. 24, 893-901 (2017).

Assembly members:
Tyrosine-protein kinase ABL1, polymer, 255 residues, 28350.389 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 BL21

Entity Sequences (FASTA):
Tyrosine-protein kinase ABL1: MGQQPGKVLGDQRRPSLPAL HFIKGAGKRESSRHGGPHCN VFVEHEALQRPVASDFEPQG LSEAARWNSKENLLAGPSEN DPNLFVALYDFVASGDNTLS ITKGEKLRVLGYNHNGEWAE AQTKNGQGWVPSNYITPVNS LEKHSWYHGPVSRNAAEYLL SSGINGSFLVRESESSPGQR SISLRYEGRVYHYRINTASD GKLYVSSESRFNTLAELVHH HSTVADGLITTLHYPAPKRN KPTVYGVSPNYDKWE

Data sets:
Data typeCount
13C chemical shifts869
15N chemical shifts224
1H chemical shifts792

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 255 residues - 28350.389 Da.

1   METGLYGLNGLNPROGLYLYSVALLEUGLY
2   ASPGLNARGARGPROSERLEUPROALALEU
3   HISPHEILELYSGLYALAGLYLYSARGGLU
4   SERSERARGHISGLYGLYPROHISCYSASN
5   VALPHEVALGLUHISGLUALALEUGLNARG
6   PROVALALASERASPPHEGLUPROGLNGLY
7   LEUSERGLUALAALAARGTRPASNSERLYS
8   GLUASNLEULEUALAGLYPROSERGLUASN
9   ASPPROASNLEUPHEVALALALEUTYRASP
10   PHEVALALASERGLYASPASNTHRLEUSER
11   ILETHRLYSGLYGLULYSLEUARGVALLEU
12   GLYTYRASNHISASNGLYGLUTRPALAGLU
13   ALAGLNTHRLYSASNGLYGLNGLYTRPVAL
14   PROSERASNTYRILETHRPROVALASNSER
15   LEUGLULYSHISSERTRPTYRHISGLYPRO
16   VALSERARGASNALAALAGLUTYRLEULEU
17   SERSERGLYILEASNGLYSERPHELEUVAL
18   ARGGLUSERGLUSERSERPROGLYGLNARG
19   SERILESERLEUARGTYRGLUGLYARGVAL
20   TYRHISTYRARGILEASNTHRALASERASP
21   GLYLYSLEUTYRVALSERSERGLUSERARG
22   PHEASNTHRLEUALAGLULEUVALHISHIS
23   HISSERTHRVALALAASPGLYLEUILETHR
24   THRLEUHISTYRPROALAPROLYSARGASN
25   LYSPROTHRVALTYRGLYVALSERPROASN
26   TYRASPLYSTRPGLU

Samples:

sample_1: Abl1b, [U-99% 13C; U-99% 15N], 0.3 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.05%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker AvanceIII 850 MHz
  • Bruker AvanceIII 700 MHz

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