BMRB Entry 34300

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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/BMR34300
MolProbity Validation Chart

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Title:
Structural characterization of the Mycobacterium tuberculosis Protein Tyrosine Kinase A (PtkA)
Deposition date:
2017-11-27
Original release date:
2019-08-15
Authors:
Niesteruk, A.; Jonker, H.; Sreeramulu, S.; Richter, C.; Hutchison, M.; Linhard, V.; Schwalbe, H.
Citation:

Citation: Niesteruk, A.; Jonker, H.; Richter, C.; Linhard, V.; Sreeramulu, S.; Schwalbe, H.. "The domain architecture of the PtkA, the first tyrosine kinase from Mycobacterium tuberculosis differs from the conventional kinase architecture."  J. Biol. Chem. 293, 11823-11836 (2018).
PubMed: 29884774

Assembly members:

Assembly members:
entity_1, polymer, 216 residues, 22874.760 Da.

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 83332   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET151/D-TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GESPQLVIFDLDGTLTDSAR GIVSSFRHALNHIGAPVPEG DLATHIVGPPMHETLRAMGL GESAEEAIVAYRADYSARGW AMNSLFDGIGPLLADLRTAG VRLAVATSKAEPTARRILRH FGIEQHFEVIAGASTDGSRG SKVDVLAHALAQLRPLPERL VMVGDRSHDVDGAAAHGIDT VVVGWGYGRADFIDKTSTTV VTHAATIDELREALGV

Data sets:
Data typeCount
13C chemical shifts691
15N chemical shifts167
1H chemical shifts1077

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 216 residues - 22874.760 Da.

1   GLYGLUSERPROGLNLEUVALILEPHEASP
2   LEUASPGLYTHRLEUTHRASPSERALAARG
3   GLYILEVALSERSERPHEARGHISALALEU
4   ASNHISILEGLYALAPROVALPROGLUGLY
5   ASPLEUALATHRHISILEVALGLYPROPRO
6   METHISGLUTHRLEUARGALAMETGLYLEU
7   GLYGLUSERALAGLUGLUALAILEVALALA
8   TYRARGALAASPTYRSERALAARGGLYTRP
9   ALAMETASNSERLEUPHEASPGLYILEGLY
10   PROLEULEUALAASPLEUARGTHRALAGLY
11   VALARGLEUALAVALALATHRSERLYSALA
12   GLUPROTHRALAARGARGILELEUARGHIS
13   PHEGLYILEGLUGLNHISPHEGLUVALILE
14   ALAGLYALASERTHRASPGLYSERARGGLY
15   SERLYSVALASPVALLEUALAHISALALEU
16   ALAGLNLEUARGPROLEUPROGLUARGLEU
17   VALMETVALGLYASPARGSERHISASPVAL
18   ASPGLYALAALAALAHISGLYILEASPTHR
19   VALVALVALGLYTRPGLYTYRGLYARGALA
20   ASPPHEILEASPLYSTHRSERTHRTHRVAL
21   VALTHRHISALAALATHRILEASPGLULEU
22   ARGGLUALALEUGLYVAL

Samples:

sample_1: PtkA, [U-15N], 0.2 mM; HEPES 50 mM; sodium chloride 300 mM; DTT 10 mM; magnesium chloride 10 mM

sample_2: PtkA, [U-13C; U-15N], 0.2 mM; HEPES 50 mM; sodium chloride 300 mM; DTT 10 mM; magnesium chloride 10 mM

sample_conditions_1: ionic strength: 354 mM; pH: 7.5; pressure: 1 mbar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCC(CO)NHsample_2isotropicsample_conditions_1
3D CC(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HETNOEsample_1isotropicsample_conditions_1
2D 1H-15N T1sample_1isotropicsample_conditions_1
2D 1H-15N T2sample_1isotropicsample_conditions_1
2D 1H-15N IPAP-HSQCsample_1isotropicsample_conditions_1
2D 1H-15N IPAP-HSQCsample_1anisotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

SPARKY v3.114, Goddard and Kneller - chemical shift assignment, data analysis, peak picking

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

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

ARIA v1.2 HJ development version, Linge, O'Donoghue and Nilges - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz
  • 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