BMRB Entry 50903

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50903

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Title:
TCPTP residues 1-302
Deposition date:
2021-04-20
Original release date:
2021-11-10
Authors:
Singh, Jai; Li, Yang; Peti, Wolfgang; Meng, Tzu-Ching; Page, Rebecca
Citation:

Citation: Singh, Jai Prakash; Li, Yang; Chen, Yi-Yun; Hsu, Shang-Te Danny; Page, Rebecca; Peti, Wolfgang; Meng, Tzu-Ching. "The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1"  Nat. Commun. 13, 94-94 (2022).
PubMed: 35013194

Assembly members:

Assembly members:
entity_1, polymer, 307 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):
entity_1: GHMGSMPTTIEREFEELDTQ RRWQPLYLEIRNESHDYPHR VAKFPENRNRNRYRDVSPYD HSRVKLQNAENDYINASLVD IEEAQRSYILTQGPLPNTCC HFWLMVWQQKTKAVVMLNRI VEKESVKCAQYWPTDDQEML FKETGFSVKLLSEDVKSYYT VHLLQLENINSGETRTISHF HYTTWPDFGVPESPASFLNF LFKVRESGSLNPDHGPAVIH CSAGIGRSGTFSLVDTCLVL MEKGDDINIKQVLLNMRKYR MGLIQTPDQLRFSYMAIIEG AKCIKGDSSIQKRWKELSKE DLSPAFD

Data sets:
Data typeCount
13C chemical shifts602
15N chemical shifts211
1H chemical shifts211

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TCPTP 1-3021

Entities:

Entity 1, TCPTP 1-302 307 residues - Formula weight is not available

The first five residues GHMGS are from cloning vector, TCPTP sequence starts from MPTTI.

1   GLYHISMETGLYSERMETPROTHRTHRILE
2   GLUARGGLUPHEGLUGLULEUASPTHRGLN
3   ARGARGTRPGLNPROLEUTYRLEUGLUILE
4   ARGASNGLUSERHISASPTYRPROHISARG
5   VALALALYSPHEPROGLUASNARGASNARG
6   ASNARGTYRARGASPVALSERPROTYRASP
7   HISSERARGVALLYSLEUGLNASNALAGLU
8   ASNASPTYRILEASNALASERLEUVALASP
9   ILEGLUGLUALAGLNARGSERTYRILELEU
10   THRGLNGLYPROLEUPROASNTHRCYSCYS
11   HISPHETRPLEUMETVALTRPGLNGLNLYS
12   THRLYSALAVALVALMETLEUASNARGILE
13   VALGLULYSGLUSERVALLYSCYSALAGLN
14   TYRTRPPROTHRASPASPGLNGLUMETLEU
15   PHELYSGLUTHRGLYPHESERVALLYSLEU
16   LEUSERGLUASPVALLYSSERTYRTYRTHR
17   VALHISLEULEUGLNLEUGLUASNILEASN
18   SERGLYGLUTHRARGTHRILESERHISPHE
19   HISTYRTHRTHRTRPPROASPPHEGLYVAL
20   PROGLUSERPROALASERPHELEUASNPHE
21   LEUPHELYSVALARGGLUSERGLYSERLEU
22   ASNPROASPHISGLYPROALAVALILEHIS
23   CYSSERALAGLYILEGLYARGSERGLYTHR
24   PHESERLEUVALASPTHRCYSLEUVALLEU
25   METGLULYSGLYASPASPILEASNILELYS
26   GLNVALLEULEUASNMETARGLYSTYRARG
27   METGLYLEUILEGLNTHRPROASPGLNLEU
28   ARGPHESERTYRMETALAILEILEGLUGLY
29   ALALYSCYSILELYSGLYASPSERSERILE
30   GLNLYSARGTRPLYSGLULEUSERLYSGLU
31   ASPLEUSERPROALAPHEASP

Samples:

sample_1: TCPTP residues 1-302, [U-100% 13C; U-100% 15N; U-80% 2H], 450 uM; HEPES 20 mM; sodium chloride 150 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 170 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection, processing

CARA - chemical shift assignment

CcpNMR - data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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