BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 27989

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27989

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Title: Backbone and side-chain chemical shift assignments of the ribosome-inactivating protein trichobakin (TBK) in solution   PubMed: 31734904

Deposition date: 2019-07-30 Original release date: 2019-11-25

Authors: Britikov, Vladimir; Britikova, Elena; Bocharov, Eduard; Urban, Anatoly; Lesovoy, Dmitry; Le, Thi Bich Thao; Phan, Van Chi; Usanov, Sergey; Arseniev, Alexander

Citation: Britikov, Vladimir; Britikova, Elena; Urban, Anatoly; Lesovoy, Dmitry; Le, Thi Bich Thao; Van Phan, Chi; Usanov, Sergey; Arseniev, Alexander; Bocharov, Eduard. "Backbone and side-chain chemical shift assignments for the ribosome-inactivating protein trichobakin (TBK)"  Biomol. NMR Assignments 14, 55-61 (2020).

Assembly members:
trichobakin, polymer, 247 residues, Formula weight is not available

Natural source:   Common Name: Trichosanthes sp. Bac Kan 8-98   Taxonomy ID: 118182   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Trichosanthes sp. Bac Kan 8-98

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
trichobakin: DVSFRLSGATSSSYGVFISN LRKALPYERKLYDIPLLRST LPGSQRYALIHLTNYADETI SVAIDVTNVYVMGYRAGDTS YFFNEASATEAAKYVFKDAK RKVTLPYSGNYERLQIAAGK IRENIPLGLPALDSAITTLF YYNANSAASALMVLIQSTSE AARYKFIEQQIGKRVDKTFL PSLAIISLENSWSALSKQIQ IASTNNGQFETPVVLINAQN QRVTITNVDAGVVTSNIALL PNRNNMA

Data sets:
Data typeCount
13C chemical shifts995
15N chemical shifts247
1H chemical shifts1578

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1trichobakin1

Entities:

Entity 1, trichobakin 247 residues - Formula weight is not available

1   ASPVALSERPHEARGLEUSERGLYALATHR
2   SERSERSERTYRGLYVALPHEILESERASN
3   LEUARGLYSALALEUPROTYRGLUARGLYS
4   LEUTYRASPILEPROLEULEUARGSERTHR
5   LEUPROGLYSERGLNARGTYRALALEUILE
6   HISLEUTHRASNTYRALAASPGLUTHRILE
7   SERVALALAILEASPVALTHRASNVALTYR
8   VALMETGLYTYRARGALAGLYASPTHRSER
9   TYRPHEPHEASNGLUALASERALATHRGLU
10   ALAALALYSTYRVALPHELYSASPALALYS
11   ARGLYSVALTHRLEUPROTYRSERGLYASN
12   TYRGLUARGLEUGLNILEALAALAGLYLYS
13   ILEARGGLUASNILEPROLEUGLYLEUPRO
14   ALALEUASPSERALAILETHRTHRLEUPHE
15   TYRTYRASNALAASNSERALAALASERALA
16   LEUMETVALLEUILEGLNSERTHRSERGLU
17   ALAALAARGTYRLYSPHEILEGLUGLNGLN
18   ILEGLYLYSARGVALASPLYSTHRPHELEU
19   PROSERLEUALAILEILESERLEUGLUASN
20   SERTRPSERALALEUSERLYSGLNILEGLN
21   ILEALASERTHRASNASNGLYGLNPHEGLU
22   THRPROVALVALLEUILEASNALAGLNASN
23   GLNARGVALTHRILETHRASNVALASPALA
24   GLYVALVALTHRSERASNILEALALEULEU
25   PROASNARGASNASNMETALA

Samples:

sample_1: trichobakin, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate buffer 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CcpNmr_Analysis v2.4.2, CCPN - chemical shift assignment, data analysis, peak picking

TOPSPIN v3.2, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP Q9LRE3

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts