BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18228

Title: Backbone and side chain assignment of TpbA   PubMed: 22392344

Deposition date: 2012-01-27 Original release date: 2012-03-08

Authors: Koveal, Dorothy; Peti, Wolfgang; Page, Rebecca

Citation: Koveal, Dorothy; Jayasundera, Thusitha; Wood, Thomas; Peti, Wolfgang; Page, Rebecca. "Backbone and sidechain (1)H, (15)N and (13)C assignments of Tyrosine Phosphatase related to Biofilm formation A (TpbA) of Pseudomonas aeruginosa."  Biomol. NMR Assignments 7, 57-59 (2013).

Assembly members:
TpbA, polymer, 193 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRP1B

Entity Sequences (FASTA):
TpbA: GHMAETAAPRSPAWAQAVDP SINLYRMSPTLYRSALPNAQ SVALLQRLQVKTVVSFIKDD DRAWLGQAPVRVVSLPTHAD RVDDAEVLSVLRQLQAAERE GPVLMHCKHGNNRTGLFAAM YRIVVQGWDKQAALEEMQRG GFGDEDDMRDASAYVRGADV DGLRLAMANGECSPSRFALC HVREWMAQALDRP

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts172
1H chemical shifts1205

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TpbA monomer1

Entities:

Entity 1, TpbA monomer 193 residues - Formula weight is not available

G26, H27 and M28 are cloning artifacts.

1   GLYHISMETALAGLUTHRALAALAPROARG
2   SERPROALATRPALAGLNALAVALASPPRO
3   SERILEASNLEUTYRARGMETSERPROTHR
4   LEUTYRARGSERALALEUPROASNALAGLN
5   SERVALALALEULEUGLNARGLEUGLNVAL
6   LYSTHRVALVALSERPHEILELYSASPASP
7   ASPARGALATRPLEUGLYGLNALAPROVAL
8   ARGVALVALSERLEUPROTHRHISALAASP
9   ARGVALASPASPALAGLUVALLEUSERVAL
10   LEUARGGLNLEUGLNALAALAGLUARGGLU
11   GLYPROVALLEUMETHISCYSLYSHISGLY
12   ASNASNARGTHRGLYLEUPHEALAALAMET
13   TYRARGILEVALVALGLNGLYTRPASPLYS
14   GLNALAALALEUGLUGLUMETGLNARGGLY
15   GLYPHEGLYASPGLUASPASPMETARGASP
16   ALASERALATYRVALARGGLYALAASPVAL
17   ASPGLYLEUARGLEUALAMETALAASNGLY
18   GLUCYSSERPROSERARGPHEALALEUCYS
19   HISVALARGGLUTRPMETALAGLNALALEU
20   ASPARGPRO

Samples:

sample_1: TpbA, [U-15N], 1.1 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_2: TpbA, [U-13C, U-15N], 1.0 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_3: TpbA 1.0 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18977
PDB
DBJ BAK91895 BAP20213 BAP49072 BAQ37900 BAR66014
EMBL CDH75498 CDM50177 CDO83381 CEI03735 CEI78250
GB AAG07272 AAT49761 ABJ13157 AFM63275 AGI79981
REF NP_252574 WP_003092976 WP_003105672 WP_003111594 WP_003118289

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