BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26932

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for MTTTm   PubMed: 28284017

Deposition date: 2016-11-03 Original release date: 2017-03-27

Authors: Burban, David; Jennings, Patricia

Citation: Burban, David; Jennings, Patricia. "Backbone assignments for the SPOUT methyltransferase MTT Tm , a knotted protein from Thermotoga maritima"  Biomol. NMR Assign. 11, 151-154 (2017).

Assembly members:
MTTTm, polymer, 162 residues, Formula weight is not available

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermotoga maritima

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

Entity Sequences (FASTA):
MTTTm: SLRVRIAVIGKLDGFIKEGI KHYEKFLRRFCKPEVLEIKR VHRGSIEEIVRKETEDLTNR ILPGSFVMVMDKRGEEVSSE EFADFLKDLEMKGKDITILI GGPYGLNEEIFAKAHRVFSL SKMTFTHGMTVLIVLEQIFR AFKIIHGENYHYEGGSHHHH HH

Data sets:
Data typeCount
13C chemical shifts438
15N chemical shifts145
1H chemical shifts145

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1MTTTm monomer1

Entities:

Entity 1, MTTTm monomer 162 residues - Formula weight is not available

1   SERLEUARGVALARGILEALAVALILEGLY
2   LYSLEUASPGLYPHEILELYSGLUGLYILE
3   LYSHISTYRGLULYSPHELEUARGARGPHE
4   CYSLYSPROGLUVALLEUGLUILELYSARG
5   VALHISARGGLYSERILEGLUGLUILEVAL
6   ARGLYSGLUTHRGLUASPLEUTHRASNARG
7   ILELEUPROGLYSERPHEVALMETVALMET
8   ASPLYSARGGLYGLUGLUVALSERSERGLU
9   GLUPHEALAASPPHELEULYSASPLEUGLU
10   METLYSGLYLYSASPILETHRILELEUILE
11   GLYGLYPROTYRGLYLEUASNGLUGLUILE
12   PHEALALYSALAHISARGVALPHESERLEU
13   SERLYSMETTHRPHETHRHISGLYMETTHR
14   VALLEUILEVALLEUGLUGLNILEPHEARG
15   ALAPHELYSILEILEHISGLYGLUASNTYR
16   HISTYRGLUGLYGLYSERHISHISHISHIS
17   HISHIS

Samples:

sample_1: MTTTm, [U-100% 13C; U-100% 15N], 350 uM; sodium acetate buffer 75 mM

sample_conditions_1: ionic strength: 75 mM; pH: 5.6; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian Avance 800 MHz

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