BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27121

Title: Sequence Specific Backbone Assignment of the catalytic domain of HePTP (residues 44-339) at pH 7.8   PubMed: 28856606

Authors: de Souza Fraga Machado, Luciana Elena; Page, Rebecca; Peti, Wolfgang

Citation: de Souza Fraga Machado, Luciana Elena; Page, Rebecca; Peti, Wolfgang. "1H, 15N and 13C sequence specific backbone assignment of the vanadate inhibited hematopoietic tyrosine phosphatase"  Biomol. NMR Assign. ., .-. (2017).

Assembly members:
Hematopoietic_Protein_Tyrosine_Phosphatase_(PTPN7,_HePTP), polymer, 299 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
Hematopoietic_Protein_Tyrosine_Phosphatase_(PTPN7,_HePTP): GHMNTPREVTLHFLRTAGHP LTRWALQRQPPSPKQLEEEF LKIPSNFVSPEDLDIPGHAS KDRYKTILPNPQSRVCLGRA QSQEDGDYINANYIRGYDGK EKVYIATQGPMPNTVSDFWE MVWQEEVSLIVMLTQLREGK EKCVHYWPTEEETYGPFQIR IQDMKECPEYTVRQLTIQYQ EERRSVKHILFSAWPDHQTP ESAGPLLRLVAEVEESPETA AHPGPIVVHCSAGIGRTGCF IATRIGCQQLKARGEVDILG IVCQLRLDRGGMIQTAEQYQ FLHHTLALYAGQLPEEPSP

Data sets:
Data typeCount
13C chemical shifts404
15N chemical shifts237
1H chemical shifts237

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PTP domain1

Entities:

Entity 1, PTP domain 299 residues - Formula weight is not available

GHM are TEV cleavage and cloning artifacts

1   GLYHISMETASNTHRPROARGGLUVALTHR
2   LEUHISPHELEUARGTHRALAGLYHISPRO
3   LEUTHRARGTRPALALEUGLNARGGLNPRO
4   PROSERPROLYSGLNLEUGLUGLUGLUPHE
5   LEULYSILEPROSERASNPHEVALSERPRO
6   GLUASPLEUASPILEPROGLYHISALASER
7   LYSASPARGTYRLYSTHRILELEUPROASN
8   PROGLNSERARGVALCYSLEUGLYARGALA
9   GLNSERGLNGLUASPGLYASPTYRILEASN
10   ALAASNTYRILEARGGLYTYRASPGLYLYS
11   GLULYSVALTYRILEALATHRGLNGLYPRO
12   METPROASNTHRVALSERASPPHETRPGLU
13   METVALTRPGLNGLUGLUVALSERLEUILE
14   VALMETLEUTHRGLNLEUARGGLUGLYLYS
15   GLULYSCYSVALHISTYRTRPPROTHRGLU
16   GLUGLUTHRTYRGLYPROPHEGLNILEARG
17   ILEGLNASPMETLYSGLUCYSPROGLUTYR
18   THRVALARGGLNLEUTHRILEGLNTYRGLN
19   GLUGLUARGARGSERVALLYSHISILELEU
20   PHESERALATRPPROASPHISGLNTHRPRO
21   GLUSERALAGLYPROLEULEUARGLEUVAL
22   ALAGLUVALGLUGLUSERPROGLUTHRALA
23   ALAHISPROGLYPROILEVALVALHISCYS
24   SERALAGLYILEGLYARGTHRGLYCYSPHE
25   ILEALATHRARGILEGLYCYSGLNGLNLEU
26   LYSALAARGGLYGLUVALASPILELEUGLY
27   ILEVALCYSGLNLEUARGLEUASPARGGLY
28   GLYMETILEGLNTHRALAGLUGLNTYRGLN
29   PHELEUHISHISTHRLEUALALEUTYRALA
30   GLYGLNLEUPROGLUGLUPROSERPRO

Samples:

sample_1: TRIS 20 mM; sodium chloride 100 mM; TCEP 0.5 mM; PTP domain 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 TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 500 MHz

Related Database Links: