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 28079

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28079

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: teEIC backbone and I/L/V methyl resonance assignment   PubMed: 32504625

Deposition date: 2020-02-10 Original release date: 2021-07-16

Authors: Dotas, Rochelle; Veditti, Vincenzo

Citation: Dotas, Rochelle; Nguyen, Trang; Stewart, Charles; Ghirlando, Rodolfo; Potoyan, Davit; Venditti, Vincenzo. "Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I"  J. Mol. Biol. 432, 4481-4498 (2020).

Assembly members:
teEIC, polymer, 316 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21A

Entity Sequences (FASTA):
teEIC: MAITLDGHQVEVCANIGTPK DVEGAERNGAEGVGLYRTEF LYMDRNSLPSEEEQFAAYKA VAEACGSQAVIVRTLDIGGD KELPYLDMPKEMNPFLGYRA IRIAMDRKEILRDQLRAILR ASAFGKLRIMFPMIISVEEV RALRKEIEIYKQELRDEGKA FDESIEIGVMVETPAAATIA RHLAKEVDFFSIGTNDLTQY TLAVDRMNEHVKEYYQPFHP SVLNLIKQVIDASHAEGKWT GMCGELAGDERATLLLLGMG LDEFSMSAISIPRIKKIIRN TNFEDAKVLAEQALAQPTTD ELMTLVNKFIEEKTIC

Data sets:
Data typeCount
13C chemical shifts951
15N chemical shifts276
1H chemical shifts540

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1teEIC1

Entities:

Entity 1, teEIC 316 residues - Formula weight is not available

1   METALAILETHRLEUASPGLYHISGLNVAL
2   GLUVALCYSALAASNILEGLYTHRPROLYS
3   ASPVALGLUGLYALAGLUARGASNGLYALA
4   GLUGLYVALGLYLEUTYRARGTHRGLUPHE
5   LEUTYRMETASPARGASNSERLEUPROSER
6   GLUGLUGLUGLNPHEALAALATYRLYSALA
7   VALALAGLUALACYSGLYSERGLNALAVAL
8   ILEVALARGTHRLEUASPILEGLYGLYASP
9   LYSGLULEUPROTYRLEUASPMETPROLYS
10   GLUMETASNPROPHELEUGLYTYRARGALA
11   ILEARGILEALAMETASPARGLYSGLUILE
12   LEUARGASPGLNLEUARGALAILELEUARG
13   ALASERALAPHEGLYLYSLEUARGILEMET
14   PHEPROMETILEILESERVALGLUGLUVAL
15   ARGALALEUARGLYSGLUILEGLUILETYR
16   LYSGLNGLULEUARGASPGLUGLYLYSALA
17   PHEASPGLUSERILEGLUILEGLYVALMET
18   VALGLUTHRPROALAALAALATHRILEALA
19   ARGHISLEUALALYSGLUVALASPPHEPHE
20   SERILEGLYTHRASNASPLEUTHRGLNTYR
21   THRLEUALAVALASPARGMETASNGLUHIS
22   VALLYSGLUTYRTYRGLNPROPHEHISPRO
23   SERVALLEUASNLEUILELYSGLNVALILE
24   ASPALASERHISALAGLUGLYLYSTRPTHR
25   GLYMETCYSGLYGLULEUALAGLYASPGLU
26   ARGALATHRLEULEULEULEUGLYMETGLY
27   LEUASPGLUPHESERMETSERALAILESER
28   ILEPROARGILELYSLYSILEILEARGASN
29   THRASNPHEGLUASPALALYSVALLEUALA
30   GLUGLNALALEUALAGLNPROTHRTHRASP
31   GLULEUMETTHRLEUVALASNLYSPHEILE
32   GLUGLULYSTHRILECYS

Samples:

sample_1: teEIC, [U-13C; U-15N; U-2H], 1 mM; D2O, [U-99% 2H], 10%; DTT 2 mM; sodium chloride 100 mM; TRIS 20 mM; EDTA 1 mM; MgCl2 4 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 273 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 HCACOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian Avance 700 MHz

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