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 26847

Title: Backbone 1H, 13C, and 15N chemical shift assignments for Protein Tyrosine Phosphatase 1B N193A variant in complex with TCS401   PubMed: 28212750

Deposition date: 2016-07-12 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, Xinyu; 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_N193A_variant, polymer, 308 residues, Formula weight is not available
entity_OTA, non-polymer, 270.262 Da.

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_N193A_variant: GHMASMEMEKEFEQIDKSGS WAAIYQDIRHEASDFPCRVA KLPKNKNRNRYRDVSPFDHS RIKLHQEDNDYINASLIKME EAQRSYILTQGPLPNTCGHF WEMVWEQKSRGVVMLNRVME KGSLKCAQYWPQKEEKEMIF EDTNLKLTLISEDIKSYYTV RQLELENLTTQETREILHFH YTTWPDFGVPESPASFLAFL FKVRESGSLSPEHGPVVVHC SAGIGRSGTFCLADTCLLLM DKRKDPSSVDIKKVLLEMRK FRMGLIQTADQLRFSYLAVI EGAKFIMGDSSVQDQWKELS HEDLEPHN

Data sets:
Data typeCount
13C chemical shifts407
15N chemical shifts206
1H chemical shifts206

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PTP 1B N193A variant1
2TCS4012

Entities:

Entity 1, PTP 1B N193A variant 308 residues - Formula weight is not available

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   GLUSERPROALASERPHELEUALAPHELEU
21   PHELYSVALARGGLUSERGLYSERLEUSER
22   PROGLUHISGLYPROVALVALVALHISCYS
23   SERALAGLYILEGLYARGSERGLYTHRPHE
24   CYSLEUALAASPTHRCYSLEULEULEUMET
25   ASPLYSARGLYSASPPROSERSERVALASP
26   ILELYSLYSVALLEULEUGLUMETARGLYS
27   PHEARGMETGLYLEUILEGLNTHRALAASP
28   GLNLEUARGPHESERTYRLEUALAVALILE
29   GLUGLYALALYSPHEILEMETGLYASPSER
30   SERVALGLNASPGLNTRPLYSGLULEUSER
31   HISGLUASPLEUGLUPROHISASN

Entity 2, TCS401 - C10 H10 N2 O5 S - 270.262 Da.

1   OTA

Samples:

sample_1: PTP 1B N193A variant, [U-99% 2H; U-99% 15N], 0.2 mM; TCS401 0.6 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; H2O 90 % v/v; D2O 10 % v/v

sample_2: PTP 1B N193A variant, [U-99% 2H; U-99% 13C; U-99% 15N], 0.2 mM; TCS401 0.6 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 HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III HD 850 MHz

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