BMRB Entry 19223

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19223

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Title:
Sequence specific backbone assignment of the catalytic domain of protein phosphatase 1B (PTP1B) in the ligand-free state
Deposition date:
2013-05-03
Original release date:
2014-09-26
Authors:
Koveal, Dorothy; Miller, Daniel; Page, Rebecca; Peti, Wolfgang
Citation:

Citation: Krishnan, Navasona; Koveal, Dorothy; Miller, Daniel; Xue, Bin; Akshinthala, Sai Dipikaa; Kragelj, Jaka; Jensen, Malene Ringkjobing; Gauss, Carla-Maria; Page, Rebecca; Blackledge, Martin; Muthuswamy, Senthil; Peti, Wolfgang; Tonks, Nicholas. "Targeting the disordered C terminus of PTP1B with an allosteric inhibitor."  Nat. Chem. Biol. 10, 558-566 (2014).
PubMed: 24845231

Assembly members:

Assembly members:
PTP1B, 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: GHMASMEMEKEFEQIDKSGS WAAIYQDIRHEASDFPCRVA KLPKNKNRNRYRDVSPFDHS RIKLHQEDNDYINASLIKME EAQRSYILTQGPLPNTCGHF WEMVWEQKSRGVVMLNRVME KGSLKCAQYWPQKEEKEMIF EDTNLKLTLISEDIKSYYTV RQLELENLTTQETREILHFH YTTWPDFGVPESPASFLNFL FKVRESGSLSPEHGPVVVHC SAGIGRSGTFCLADTCLLLM DKRKDPSSVDIKKVLLEMRK FRMGLIQTADQLRFSYLAVI EGAKFIMGDSSVQDQWKELS HEDLEPHN

Data sets:
Data typeCount
13C chemical shifts512
15N chemical shifts232
1H chemical shifts232

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PTP1B1

Entities:

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

The first five residues (GHMAS) represent non-native residues that remain after cleavage of the N-terminal affinity tag

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

Samples:

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

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

sample_3: PTP1B, [U-15N]-Leu, 0.42 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_4: PTP1B, [U-15N]-Tyr, 1.0 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_5: PTP1B, [U-15N]-Phe, 1.0 mM; HEPES 50 mM; sodium chloride 150 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_6: PTP1B, [U-15N]-Val, 0.6 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_3isotropicsample_conditions_1
2D 1H-15N TROSYsample_4isotropicsample_conditions_1
2D 1H-15N TROSYsample_5isotropicsample_conditions_1
2D 1H-15N TROSYsample_6isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY HNCAsample_2isotropicsample_conditions_1
3D TROSY HNCOCAsample_2isotropicsample_conditions_1
3D TROSY HNCACBsample_2isotropicsample_conditions_1
3D TROSY HNCOCACBsample_2isotropicsample_conditions_1
3D 1H-15N TROSY NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 19224 25375
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