BMRB Entry 26835

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26835

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Title:
Backbone 1H, 13C, 15N Chemical shift assignments for Protein Phosphatase 1B T178A variant
Deposition date:
2016-06-23
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_T178A_mutant, polymer, 308 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: humans   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_T178A_mutant: GHMASMEMEKEFEQIDKSGS WAAIYQDIRHEASDFPCRVA KLPKNKNRNRYRDVSPFDHS RIKLHQEDNDYINASLIKME EAQRSYILTQGPLPNTCGHF WEMVWEQKSRGVVMLNRVME KGSLKCAQYWPQKEEKEMIF EDTNLKLTLISEDIKSYYTV RQLELENLTTQETREILHFH YTAWPDFGVPESPASFLNFL FKVRESGSLSPEHGPVVVHC SAGIGRSGTFCLADTCLLLM DKRKDPSSVDIKKVLLEMRK FRMGLIQTADQLRFSYLAVI EGAKFIMGDSSVQDQWKELS HEDLEPHN

Data sets:
Data typeCount
13C chemical shifts484
15N chemical shifts238
1H chemical shifts238

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protein Phosphatase 1B T178A variant1

Entities:

Entity 1, Protein Phosphatase 1B T178A variant 308 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   TYRTHRALATRPPROASPPHEGLYVALPRO
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 T178A mutant, [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 T178A mutant, [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

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

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III HD 850 MHz

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