BMRB Entry 27241

Title:
E.coli GcvH backbone chemical shift assignments
Deposition date:
2017-08-31
Original release date:
2018-01-29
Authors:
Yadav, Usha; Sundd, Monica
Citation:

Citation: Yadav, Usha; Sundd, Monica. "Backbone chemical shift assignments of the glycine cleavage complex H protein of Escherichia coli"  Biomol. NMR Assign. 12, 163-165 (2018).
PubMed: 29335837

Assembly members:

Assembly members:
Glycine_cleavage_complex_H_protein, polymer, 128 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts120
1H chemical shifts120

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Glycine cleavage complex H protein polypeptide1

Entities:

Entity 1, Glycine cleavage complex H protein polypeptide 128 residues - Formula weight is not available

1   SERASNVALPROALAGLULEULYSTYRSER
2   LYSGLUHISGLUTRPLEUARGLYSGLUALA
3   ASPGLYTHRTYRTHRVALGLYILETHRGLU
4   HISALAGLNGLULEULEUGLYASPMETVAL
5   PHEVALASPLEUPROGLUVALGLYALATHR
6   VALSERALAGLYASPASPCYSALAVALALA
7   GLUSERVALLYSALAALASERASPILETYR
8   ALAPROVALSERGLYGLUILEVALALAVAL
9   ASNASPALALEUSERASPSERPROGLULEU
10   VALASNSERGLUPROTYRALAGLYGLYTRP
11   ILEPHELYSILELYSALASERASPGLUSER
12   GLULEUGLUSERLEULEUASPALATHRALA
13   TYRGLUALALEULEUGLUASPGLU

Samples:

sample_1: Glycine cleavage complex H protein, [U-99% 13C; U-99% 15N], 2 mM; Tris HCl buffer 50 mM; soduim chloride 200 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.8; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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