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 51022

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51022

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Title: Backbone assignments of truncated form of TagA from Thermoanaerobacter italicus   PubMed: 34864059

Deposition date: 2021-07-21 Original release date: 2021-12-13

Authors: Martinez, Orlando; Mahoney, Brendan; Clubb, Robert

Citation: Martinez, Orlando; Mahoney, Brendan; Goring, Andrew; Yi, Sung-Wook; Tran, Denise; Cascio, Duilio; Phillips, Martin; Muthana, Musleh; Chen, Xi; Jung, Michael; Loo, Joseph; Clubb, Robert. "Insight into the molecular basis of substrate recognition by the wall teichoic acid glycosyltransferase TagA"  J. Biol. Chem. 298, 101464-101464 (2021).

Assembly members:
entity_1, polymer, 195 residues, 21633.08 Da.

Natural source:   Common Name: Thermoanaerobacter italicus   Taxonomy ID: 108150   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermoanaerobacter italicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMAPLe4

Entity Sequences (FASTA):
entity_1: MERLDIFGVPIDRVTMIQAV DILNNFLQENRLHIVATPNA EIVMMAQKDKEYMEILNNTD LNVPDGSGIVFASKVFKKPL PERVAGFDLMLEFIKGISSK GVKIYLLGAAAQVAEQARAN LEKLYPGVKIVGTHHGYFTE EEENKIIEEINNKGAEVLFV ALGAPKQEKWIYKNKDKLKV KIAMGVGGSFDVIAG

Data sets:
Data typeCount
13C chemical shifts323
15N chemical shifts114
1H chemical shifts114

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TiTagA_11
2TiTagA_21

Entities:

Entity 1, TiTagA_1 195 residues - 21633.08 Da.

1   METGLUARGLEUASPILEPHEGLYVALPRO
2   ILEASPARGVALTHRMETILEGLNALAVAL
3   ASPILELEUASNASNPHELEUGLNGLUASN
4   ARGLEUHISILEVALALATHRPROASNALA
5   GLUILEVALMETMETALAGLNLYSASPLYS
6   GLUTYRMETGLUILELEUASNASNTHRASP
7   LEUASNVALPROASPGLYSERGLYILEVAL
8   PHEALASERLYSVALPHELYSLYSPROLEU
9   PROGLUARGVALALAGLYPHEASPLEUMET
10   LEUGLUPHEILELYSGLYILESERSERLYS
11   GLYVALLYSILETYRLEULEUGLYALAALA
12   ALAGLNVALALAGLUGLNALAARGALAASN
13   LEUGLULYSLEUTYRPROGLYVALLYSILE
14   VALGLYTHRHISHISGLYTYRPHETHRGLU
15   GLUGLUGLUASNLYSILEILEGLUGLUILE
16   ASNASNLYSGLYALAGLUVALLEUPHEVAL
17   ALALEUGLYALAPROLYSGLNGLULYSTRP
18   ILETYRLYSASNLYSASPLYSLEULYSVAL
19   LYSILEALAMETGLYVALGLYGLYSERPHE
20   ASPVALILEALAGLY

Samples:

sample_1: TiTagA, [U-99% 13C; U-99% 15N; U-70% 2H], 550 ± 50 uM; sodium phosphate 50 ± 5 mM; sodium chloride 100 ± 5 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5 - collection

NMRPipe v9.9 - processing

CARA v1.9.1.7 - chemical shift assignment

NMRFAM-SPARKY v1.414 - data analysis

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE NEO 800 MHz

Related Database Links:

UNP D3T4E0
PDB
AlphaFold D3T4E0

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