BMRB Entry 30332

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30332
MolProbity Validation Chart

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Title:
Abl1b Regulatory Module 'Activating' conformation
Deposition date:
2017-08-11
Original release date:
2017-09-25
Authors:
Kalodimos, C.; Rossi, P.; Saleh, T.
Citation:

Citation: Kalodimos, C.; Rossi, P.; Saleh, T.. "Atomic view of the energy landscape in the allosteric regulation of Abl kinase"  Nat. Struct. Mol. Biol. 24, 893-901 (2017).
PubMed: 28945248

Assembly members:

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

Entity Sequences (FASTA):

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 shifts834
15N chemical shifts180
1H chemical shifts1257

Additional metadata:

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

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: 120 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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