BMRB Entry 19046

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19046

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Title:
Sequence-specific backbone 1H, 13C and 15N assignments of the 34 kDa catalytic domain of PTPN5
Deposition date:
2013-02-20
Original release date:
2013-05-30
Authors:
Francis, Dana; Page, Rebecca; Peti, Wolfgang
Citation:

Citation: Francis, Dana; Page, Rebecca; Peti, Wolfgang. "Sequence-specific backbone 1H, 13C and 15N assignments of the 34 kDa catalytic domain of PTPN5 (STEP)."  Biomol. NMR Assignments 8, 185-188 (2014).
PubMed: 23640000

Assembly members:

Assembly members:
PTPN5, polymer, 301 residues, 34834 Da.

Natural source:

Natural source:   Common Name: House mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet28a derivative

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PTPN5: GHMASSPREESAHEYLLSAS RVLRAEELHEKALDPFLLQA EFFEIPMNFVDPKEYDIPGL VRKNRYKTILPNPHSRVRLT SPDPEDPLSSYINANYIRGY SGEEKVYIATQGPIVSTVAD FWRMVWQERTPIIVMITNIE EMNEKCTEYWPEEQVVHDGV EITVQKVIHTEDYRLRLISL RRGTEERTLKHYWFTSWPDQ KTPDRAPPLLHLVREVEEAA QQEGPHCSPIIVHCSAGIGR TGCFIATSICCQQLRREGVV DILKTTCQLRQDRGGMIQTC EQYQFVHHAMSLYEKQLSHQ S

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts212
1H chemical shifts212

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PTPN51

Entities:

Entity 1, PTPN5 301 residues - 34834 Da.

Residues 1-5 represent a non-native affinity tag.

1   GLYHISMETALASERSERPROARGGLUGLU
2   SERALAHISGLUTYRLEULEUSERALASER
3   ARGVALLEUARGALAGLUGLULEUHISGLU
4   LYSALALEUASPPROPHELEULEUGLNALA
5   GLUPHEPHEGLUILEPROMETASNPHEVAL
6   ASPPROLYSGLUTYRASPILEPROGLYLEU
7   VALARGLYSASNARGTYRLYSTHRILELEU
8   PROASNPROHISSERARGVALARGLEUTHR
9   SERPROASPPROGLUASPPROLEUSERSER
10   TYRILEASNALAASNTYRILEARGGLYTYR
11   SERGLYGLUGLULYSVALTYRILEALATHR
12   GLNGLYPROILEVALSERTHRVALALAASP
13   PHETRPARGMETVALTRPGLNGLUARGTHR
14   PROILEILEVALMETILETHRASNILEGLU
15   GLUMETASNGLULYSCYSTHRGLUTYRTRP
16   PROGLUGLUGLNVALVALHISASPGLYVAL
17   GLUILETHRVALGLNLYSVALILEHISTHR
18   GLUASPTYRARGLEUARGLEUILESERLEU
19   ARGARGGLYTHRGLUGLUARGTHRLEULYS
20   HISTYRTRPPHETHRSERTRPPROASPGLN
21   LYSTHRPROASPARGALAPROPROLEULEU
22   HISLEUVALARGGLUVALGLUGLUALAALA
23   GLNGLNGLUGLYPROHISCYSSERPROILE
24   ILEVALHISCYSSERALAGLYILEGLYARG
25   THRGLYCYSPHEILEALATHRSERILECYS
26   CYSGLNGLNLEUARGARGGLUGLYVALVAL
27   ASPILELEULYSTHRTHRCYSGLNLEUARG
28   GLNASPARGGLYGLYMETILEGLNTHRCYS
29   GLUGLNTYRGLNPHEVALHISHISALAMET
30   SERLEUTYRGLULYSGLNLEUSERHISGLN
31   SER

Samples:

sample_1: PTPN5, [U-13C; U-15N; U-2H], 0.4 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_2: PTPN5, [U-15N]-Leu, 0.3 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_3: PTPN5, [U-15N]-Tyr, 0.3 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_4: PTPN5, [U-15N]-Phe, 0.3 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_5: PTPN5, [U-15N]-Glu, 0.3 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_6: PTPN5, [U-15N]-Asp, 0.3 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_7: PTPN5, [U-15N]-Val, 0.3 mM; HEPES 50 mM; sodium chloride 150 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_7isotropicsample_conditions_1

Software:

TOPSPIN v3.0/3.1, 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:

DBJ BAC29993
GB AAA73574 AAB19491 AAH51975 AAH79592 AAH92196
REF NP_001157037 NP_038671 NP_062126 XP_005087780 XP_006229314
SP P35234 P54830
AlphaFold P35234 P54830

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