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 26814

Title: Backbone 1H, 13C, and 15N chemical shift assignments for Protein Tyrosine Phosphatase 1B residues 1-284   PubMed: 28212750

Deposition date: 2016-06-13 Original release date: 2017-02-20

Authors: Peti, Wolfgang; Page, Rebecca; Li, Yang; Choy, Meng; Machado, Luciana

Citation: Choy, Meng; Li, Yang; Machado, Luciana; Connors, Christopher; Wei, Xingyu; Page, Rebecca; Peti, Wolfgang. "Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery"  Mol. Cell. 65, 644-658 (2017).

Assembly members:
PTP1B_residues_1-284, polymer, 289 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):
PTP1B_residues_1-284: GHMASMEMEKEFEQIDKSGS WAAIYQDIRHEASDFPCRVA KLPKNKNRNRYRDVSPFDHS RIKLHQEDNDYINASLIKME EAQRSYILTQGPLPNTCGHF WEMVWEQKSRGVVMLNRVME KGSLKCAQYWPQKEEKEMIF EDTNLKLTLISEDIKSYYTV RQLELENLTTQETREILHFH YTTWPDFGVPESPASFLNFL FKVRESGSLSPEHGPVVVHC SAGIGRSGTFCLADTCLLLM DKRKDPSSVDIKKVLLEMRK FRMGLIQTADQLRFSYLAVI EGAKFIMGD

Data sets:
Data typeCount
13C chemical shifts443
15N chemical shifts223
1H chemical shifts223

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protein Tyrosine Phosphatase 1B residues 1-2841

Entities:

Entity 1, Protein Tyrosine Phosphatase 1B residues 1-284 289 residues - Formula weight is not available

GHMAS are a cloning artefact; PTP1B sequence starts with MEMEK

1   GLYHISMETALASERMETGLUMETGLULYS
2   GLUPHEGLUGLNILEASPLYSSERGLYSER
3   TRPALAALAILETYRGLNASPILEARGHIS
4   GLUALASERASPPHEPROCYSARGVALALA
5   LYSLEUPROLYSASNLYSASNARGASNARG
6   TYRARGASPVALSERPROPHEASPHISSER
7   ARGILELYSLEUHISGLNGLUASPASNASP
8   TYRILEASNALASERLEUILELYSMETGLU
9   GLUALAGLNARGSERTYRILELEUTHRGLN
10   GLYPROLEUPROASNTHRCYSGLYHISPHE
11   TRPGLUMETVALTRPGLUGLNLYSSERARG
12   GLYVALVALMETLEUASNARGVALMETGLU
13   LYSGLYSERLEULYSCYSALAGLNTYRTRP
14   PROGLNLYSGLUGLULYSGLUMETILEPHE
15   GLUASPTHRASNLEULYSLEUTHRLEUILE
16   SERGLUASPILELYSSERTYRTYRTHRVAL
17   ARGGLNLEUGLULEUGLUASNLEUTHRTHR
18   GLNGLUTHRARGGLUILELEUHISPHEHIS
19   TYRTHRTHRTRPPROASPPHEGLYVALPRO
20   GLUSERPROALASERPHELEUASNPHELEU
21   PHELYSVALARGGLUSERGLYSERLEUSER
22   PROGLUHISGLYPROVALVALVALHISCYS
23   SERALAGLYILEGLYARGSERGLYTHRPHE
24   CYSLEUALAASPTHRCYSLEULEULEUMET
25   ASPLYSARGLYSASPPROSERSERVALASP
26   ILELYSLYSVALLEULEUGLUMETARGLYS
27   PHEARGMETGLYLEUILEGLNTHRALAASP
28   GLNLEUARGPHESERTYRLEUALAVALILE
29   GLUGLYALALYSPHEILEMETGLYASP

Samples:

sample_1: PTP1B residues 1-284, [U-99% 2H; U-99% 15N], 0.2 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_2: PTP1B residues 1-284, [U-99% 2H; U-99% 13C; U-99% 15N], 0.2 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CcpNMR, CCPN - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance IIIHD 850 MHz

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