BMRB Entry 25375

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25375

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Title:
Assignment of PTP1B bound to the inhibitor CPT-157633
Deposition date:
2014-12-01
Original release date:
2015-08-04
Authors:
Peti, Wolfgang; Connors, Christopher; Page, Rebecca
Citation:

Citation: Krishnan, Navasona; Krishnan, Keerthi; Connors, Christopher; Choy, Meng; Page, Rebecca; Peti, Wolfgang; Van Aelst, Linda; Shea, Stephen; Tonks, Nicholas. "PTP1B inhibition suggests a therapeutic strategy for Rett syndrome"  J. Clin. Invest. 125, 3163-3177 (2015).
PubMed: 26214522

Assembly members:

Assembly members:
PTP1B, polymer, 308 residues, Formula weight is not available
CPT-157633, non-polymer, 465.209 Da.

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: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PTP1B: GHMASMEMEKEFEQIDKSGS WAAIYQDIRHEASDFPCRVA KLPKNKNRNRYRDVSPFDHS RIKLHQEDNDYINASLIKME EAQRSYILTQGPLPNTCGHF WEMVWEQKSRGVVMLNRVME KGSLKCAQYWPQKEEKEMIF EDTNLKLTLISEDIKSYYTV RQLELENLTTQETREILHFH YTTWPDFGVPESPASFLNFL FKVRESGSLSPEHGPVVVHC SAGIGRSGTFCLADTCLLLM DKRKDPSSVDIKKVLLEMRK FRMGLIQTADQLRFSYLAVI EGAKFIMGDSSVQDQWKELS HEDLEPHN

Data sets:
Data typeCount
13C chemical shifts244
15N chemical shifts212
1H chemical shifts212

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PTP1B1
2CPT-1576332

Entities:

Entity 1, PTP1B 308 residues - Formula weight is not available

GHMAS are cloning artefacts

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   GLUGLYALALYSPHEILEMETGLYASPSER
30   SERVALGLNASPGLNTRPLYSGLULEUSER
31   HISGLUASPLEUGLUPROHISASN

Entity 2, CPT-157633 - C12H14BrF2N2O6PS - 465.209 Da.

1   CPT-157633

Samples:

sample_1: PTP1B, [U-99% 13C; U-99% 15N; U-95% 2H], 0.2 mM; CPT-157633 0.3 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: ambient atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment

TOPSPIN v3.1.4, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

BMRB 19223 19224
PDB
DBJ BAF83327 BAG11007 BAG38152 BAG61697
EMBL CAH90487 CAN13184
GB AAA60157 AAA60223 AAH15660 AAH18164 AAP35398
REF NP_001106906 NP_001125254 NP_001245122 NP_001265547 NP_002818
SP P18031
AlphaFold P18031

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