BMRB Entry 18791

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18791

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Title:
Sequence-specific backbone 1H, 13C and 15N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc
Deposition date:
2012-10-15
Original release date:
2013-01-29
Authors:
Temel, Deniz; Dutta, Kaushik; Ghose, Ranajeet
Citation:

Citation: Temel, Deniz; Dutta, Kaushik; Ghose, Ranajeet. "Sequence-specific backbone (1)H, (13)C and (15)N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc."  Biomol. NMR Assignments ., .-. (2012).
PubMed: 23225198

Assembly members:

Assembly members:
WzcCD, polymer, 295 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WzcCD: MGSSHHHHHHSSGLVPRGSH MSLFNRGIESPQVLEEHGIS VYASIPLSEWQKARDSVKTI KGIKRYKQSQLLAVGNPTDL AIEAIRSLRTSLHFAMMQAQ NNVLMMTGVSPSIGKTFVCA NLAAVISQTNKRVLLIDCDM RKGYTHELLGTNNVNGLSEI LIGQGDITTAAKPTSIAKFD LIPRGQVPPNPSELLMSERF AELVNWASKNYDLVLIDTPP ILAVTDAAIVGRHVGTTLMV ARYAVNTLKEVETSLSRFEQ NGIPVKGVILNSIFRRASAY QDYGYYEYEYKSDAK

Data sets:
Data typeCount
13C chemical shifts702
15N chemical shifts229
1H chemical shifts229

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WzcCD1

Entities:

Entity 1, WzcCD 295 residues - Formula weight is not available

Residue 426-445 is from the his tag. Protein sequence starts from 446-720

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERLEUPHEASNARGGLYILEGLUSER
4   PROGLNVALLEUGLUGLUHISGLYILESER
5   VALTYRALASERILEPROLEUSERGLUTRP
6   GLNLYSALAARGASPSERVALLYSTHRILE
7   LYSGLYILELYSARGTYRLYSGLNSERGLN
8   LEULEUALAVALGLYASNPROTHRASPLEU
9   ALAILEGLUALAILEARGSERLEUARGTHR
10   SERLEUHISPHEALAMETMETGLNALAGLN
11   ASNASNVALLEUMETMETTHRGLYVALSER
12   PROSERILEGLYLYSTHRPHEVALCYSALA
13   ASNLEUALAALAVALILESERGLNTHRASN
14   LYSARGVALLEULEUILEASPCYSASPMET
15   ARGLYSGLYTYRTHRHISGLULEULEUGLY
16   THRASNASNVALASNGLYLEUSERGLUILE
17   LEUILEGLYGLNGLYASPILETHRTHRALA
18   ALALYSPROTHRSERILEALALYSPHEASP
19   LEUILEPROARGGLYGLNVALPROPROASN
20   PROSERGLULEULEUMETSERGLUARGPHE
21   ALAGLULEUVALASNTRPALASERLYSASN
22   TYRASPLEUVALLEUILEASPTHRPROPRO
23   ILELEUALAVALTHRASPALAALAILEVAL
24   GLYARGHISVALGLYTHRTHRLEUMETVAL
25   ALAARGTYRALAVALASNTHRLEULYSGLU
26   VALGLUTHRSERLEUSERARGPHEGLUGLN
27   ASNGLYILEPROVALLYSGLYVALILELEU
28   ASNSERILEPHEARGARGALASERALATYR
29   GLNASPTYRGLYTYRTYRGLUTYRGLUTYR
30   LYSSERASPALALYS

Samples:

NMR_Sample_1: WzcCD, [U-15N; U-2H], 300 uM; D20 10%; H20 90%; Sodium phosphate 50 mM; NaCl 50 mM; DTT 25 mM; EDTA 5 mM

NMR_Sample_2: WzcCD, [U-13C; U-15N; U-2H], 300 uM; D20 10%; H20 90%; Sodium phosphate 50 mM; NaCl 50 mM; DTT 25 mM; EDTA 5 mM

NMR: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBNMR_Sample_2isotropicNMR
3D HNCONMR_Sample_2isotropicNMR
3D HNCANMR_Sample_2isotropicNMR
3D TROSYNMR_Sample_1isotropicNMR
3D HNCOCACBNMR_Sample_2isotropicNMR
3D HNCOCANMR_Sample_2isotropicNMR
3D HNCACONMR_Sample_2isotropicNMR

Software:

NMRView v8.2.23, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz

Related Database Links:

DBJ BAA15913 BAB36288 BAG11866 BAG11924 BAG11980
EMBL CAP76567 CAQ32472 CAQ89647 CAQ98983 CAR03444
GB AAC75121 AAC77835 AAG57120 AAN43661 AAN81042
REF NP_310892 NP_416564 NP_707954 WP_000105997 WP_000137082
SP P76387 Q8X7L9
AlphaFold P76387 Q8X7L9

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