BMRB Entry 26832

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26832

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Title:
Backbone 1H, 13C, and 15N Chemical shift assignments for Protein Tyrosine Phosphatase 1B YAYA (Y152A, Y153A) variant.
Deposition date:
2016-06-22
Original release date:
2017-02-20
Authors:
Peti, Wolfgang; Page, Rebecca; Li, Yang; Choy, Meng; Machado, Luciana
Citation:

Citation: Choy, Meng; Li, Yang; Machado, Luciana; Connors, Christopher; Wei, Xinyu; Page, Rebecca; Peti, Wolfgang. "Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery"  Mol. Cell. 65, 644-658 (2017).
PubMed: 28212750

Assembly members:

Assembly members:
PTP1B_Y152A_Y153A_mutant, polymer, 308 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PTP1B_Y152A_Y153A_mutant: GHMASMEMEKEFEQIDKSGS WAAIYQDIRHEASDFPCRVA KLPKNKNRNRYRDVSPFDHS RIKLHQEDNDYINASLIKME EAQRSYILTQGPLPNTCGHF WEMVWEQKSRGVVMLNRVME KGSLKCAQYWPQKEEKEMIF EDTNLKLTLISEDIKSAATV RQLELENLTTQETREILHFH YTTWPDFGVPESPASFLNFL FKVRESGSLSPEHGPVVVHC SAGIGRSGTFCLADTCLLLM DKRKDPSSVDIKKVLLEMRK FRMGLIQTADQLRFSYLAVI EGAKFIMGDSSVQDQWKELS HEDLEPHN

Data sets:
Data typeCount
13C chemical shifts494
15N chemical shifts246
1H chemical shifts246

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protein Tyrosine Phosphatase 1B YAYA (Y152A, Y153A) variant1

Entities:

Entity 1, Protein Tyrosine Phosphatase 1B YAYA (Y152A, Y153A) variant 308 residues - Formula weight is not available

GHMAS are 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   SERGLUASPILELYSSERALAALATHRVAL
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   GLUGLYALALYSPHEILEMETGLYASPSER
30   SERVALGLNASPGLNTRPLYSGLULEUSER
31   HISGLUASPLEUGLUPROHISASN

Samples:

sample_1: PTP1B Y152A, Y153A mutant, [U-99% 2H; U-99% 15N], 0.2 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; H2O 90 % v/v; D2O 10 % v/v

sample_2: PTP1B Y152A, Y153A mutant, [U-99% 2H; U-99% 15N; U-99% 13C], 0.2 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; H2O 90 % v/v; D2O 10 % v/v

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

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

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance IIIHD 850 MHz

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