BMRB Entry 15949

Title:
1H, 15N, 13C Resonance Assignments of the Reduced and Active Form of Human Protein Tyrosine Phosphatase, PRL-1
Deposition date:
2008-09-10
Original release date:
2009-01-15
Authors:
Skinner, Andria; Laurence, Jennifer
Citation:

Citation: Skinner, Andria; Laurence, Jennifer. "1H, 15N, 13C resonance assignments of the reduced and active form of human Protein Tyrosine Phosphatase, PRL-1."  Biomol. NMR Assignments 3, 61-65 (2009).
PubMed: 19636948

Assembly members:

Assembly members:
PRL-1-C170-171S, polymer, 173 residues, 19815 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32XaLIC

Data sets:
Data typeCount
13C chemical shifts632
15N chemical shifts148
1H chemical shifts148

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PRL-1-C170-171S1

Entities:

Entity 1, PRL-1-C170-171S 173 residues - 19815 Da.

1   METALAARGMETASNARGPROALAPROVAL
2   GLUVALTHRTYRLYSASNMETARGPHELEU
3   ILETHRHISASNPROTHRASNALATHRLEU
4   ASNLYSPHEILEGLUGLULEULYSLYSTYR
5   GLYVALTHRTHRILEVALARGVALCYSGLU
6   ALATHRTYRASPTHRTHRLEUVALGLULYS
7   GLUGLYILEHISVALLEUASPTRPPROPHE
8   ASPASPGLYALAPROPROSERASNGLNILE
9   VALASPASPTRPLEUSERLEUVALLYSILE
10   LYSPHEARGGLUGLUPROGLYCYSCYSILE
11   ALAVALHISCYSVALALAGLYLEUGLYARG
12   ALAPROVALLEUVALALALEUALALEUILE
13   GLUGLYGLYMETLYSTYRGLUASPALAVAL
14   GLNPHEILEARGGLNLYSARGARGGLYALA
15   PHEASNSERLYSGLNLEULEUTYRLEUGLU
16   LYSTYRARGPROLYSMETARGLEUARGPHE
17   LYSASPSERASNGLYHISARGASNASNSER
18   SERILEGLN

Samples:

sample_1: PRL-1-C170-171S mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.169 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment, peak picking

PISTACHIO vPINE, Eghbalnia, Bahrami, Wang, Assadi and Markley - chemical shift assignment, refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC38233 BAE28460 BAE29619 BAE30480 BAE90330
EMBL CAH18292 CAH92262
GB AAA41935 AAB40597 AAB58913 AAC39836 AAF05715
PIR A56059
REF NP_001126324 NP_001193053 NP_001233568 NP_003454 NP_035330
SP Q5R7J8 Q63739 Q78EG7 Q93096 Q9TSM6
TPG DAA26421 DAA26422
AlphaFold Q9TSM6 Q5R7J8 Q63739 Q78EG7 Q93096

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