BMRB Entry 15680

Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15680

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Title:
Sequence-specific 1H, 13C and 15N backbone resonance assignments of the 34kDa catalytic domain of human PTPN7
Deposition date:
2008-03-13
Original release date:
2008-06-05
Authors:
Jeeves, Mark; McClelland, Darren; Barr, Alastair; Overduin, Michael
Citation:

Citation: Jeeves, Mark; McClelland, Darren; Barr, Alastair; Overduin, Michael. "Sequence-specific 1H, 13C and 15N backbone resonance assignments of the 34 kDa catalytic domain of human PTPN7"  Biomol. NMR Assignments 2, 101-103 (2008).
PubMed: 19636879

Assembly members:

Assembly members:
PTPN7, polymer, 296 residues, 33737.3 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: pNIC28-Bsa4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PTPN7: SMNTPREVTLHFLRTAGHPL TRWALQRQPPSPKQLEEEFL KIPSNFVSPEDLDIPGHASK DRYKTILPNPQSRVCLGRAQ SQEDGDYINANYIRGYDGKE KVYIATQGPMPNTVSDFWEM VWQEEVSLIVMLTQLREGKE KCVHYWPTEEETYGPFQIRI QDMKECPEYTVRQLTIQYQE ERRSVKHILFSAWPDHQTPE SAGPLLRLVAEVEESPETAA HPGPIVVHCSAGIGRTGCFI ATRIGCQQLKARGEVDILGI VCQLRLDRGGMIQTAEQYQF LHHTLALYAGQLPEEP

Data sets:
Data typeCount
13C chemical shifts763
15N chemical shifts245
1H chemical shifts248

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Phosphatase domain of PTPN71

Entities:

Entity 1, Phosphatase domain of PTPN7 296 residues - 33737.3 Da.

First 2 residues are from the purification tag. PTPN7 specific sequence begins with N65. The full native protein sequence is as follows: mvqahggrsraqpltlslgaamtqpppektpakkhvrlqerrgsnvalmldvrslgavepicsNTPREVTLHFLRTAGHP LTRWALQRQPPSPKQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGK EKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQ EERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILG IVCQLRLDRGGMIQTAEQYQFLHHTLALYAGQLPEEP

1   SERMETASNTHRPROARGGLUVALTHRLEU
2   HISPHELEUARGTHRALAGLYHISPROLEU
3   THRARGTRPALALEUGLNARGGLNPROPRO
4   SERPROLYSGLNLEUGLUGLUGLUPHELEU
5   LYSILEPROSERASNPHEVALSERPROGLU
6   ASPLEUASPILEPROGLYHISALASERLYS
7   ASPARGTYRLYSTHRILELEUPROASNPRO
8   GLNSERARGVALCYSLEUGLYARGALAGLN
9   SERGLNGLUASPGLYASPTYRILEASNALA
10   ASNTYRILEARGGLYTYRASPGLYLYSGLU
11   LYSVALTYRILEALATHRGLNGLYPROMET
12   PROASNTHRVALSERASPPHETRPGLUMET
13   VALTRPGLNGLUGLUVALSERLEUILEVAL
14   METLEUTHRGLNLEUARGGLUGLYLYSGLU
15   LYSCYSVALHISTYRTRPPROTHRGLUGLU
16   GLUTHRTYRGLYPROPHEGLNILEARGILE
17   GLNASPMETLYSGLUCYSPROGLUTYRTHR
18   VALARGGLNLEUTHRILEGLNTYRGLNGLU
19   GLUARGARGSERVALLYSHISILELEUPHE
20   SERALATRPPROASPHISGLNTHRPROGLU
21   SERALAGLYPROLEULEUARGLEUVALALA
22   GLUVALGLUGLUSERPROGLUTHRALAALA
23   HISPROGLYPROILEVALVALHISCYSSER
24   ALAGLYILEGLYARGTHRGLYCYSPHEILE
25   ALATHRARGILEGLYCYSGLNGLNLEULYS
26   ALAARGGLYGLUVALASPILELEUGLYILE
27   VALCYSGLNLEUARGLEUASPARGGLYGLY
28   METILEGLNTHRALAGLUGLNTYRGLNPHE
29   LEUHISHISTHRLEUALALEUTYRALAGLY
30   GLNLEUPROGLUGLUPRO

Samples:

sample_1: sodium chloride 80 mM; HEPES 50 mM; TCEP 0.5 mM; PTPN7, [U-100% 13C; U-100% 15N; 100% 2H], 1 mM

sample_2: PTPN7, [U-100% 13C; U-100% 15N; 50% 2H], 1 mM; sodium chloride 80 mM; HEPES 50 mM; TCEP 0.5 mM

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_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 HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 900 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAA01946 BAG54453 BAG56727 BAG62662 BAG64051
GB AAA59531 AAH01746 AAM69538 AAP88850 AAX32352
REF NP_001186726 NP_002823 NP_542155 XP_001106613 XP_001140385
SP P35236
AlphaFold P35236

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