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 15735

Title: truncated AcrA from Campylobacter jejuni for glycosylation studies   PubMed: 19154179

Deposition date: 2008-04-17 Original release date: 2009-01-23

Authors: Slynko, Vadim; Schubert, Mario; Numao, Shin; Kowarik, Michael; Aebi, Markus; Allain, Frederic

Citation: Slynko, Vadim; Schubert, Mario; Numao, Shin; Kowarik, Michael; Aebi, Markus; Allain, Frederic. "NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation"  J. Am. Chem. Soc. 131, 1274-1281 (2009).

Assembly members:
AcrA(61-210DD), polymer, 116 residues, 12748.376 Da.

Natural source:   Common Name: Campylobacter jejuni   Taxonomy ID: 197   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Campylobacter jejuni

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

Entity Sequences (FASTA):
AcrA(61-210DD): DVIIKPQVSGVIVNKLFKAG DKVKKGQTLFIIEQDQASKD FNRSKALFSQSAISQKEYDS SLATLDHTEIKAPFDGTIGD ALVNIGDYVSASTTELVRVT NLNPIYADGSHHHHHH

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts117
1H chemical shifts752

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 116 residues - 12748.376 Da.

The construct consists of residues 61-210 of AcrA of C. jejuni with deletions of res. 97-117 and 146-166 and two mutations: K96Q K131Q.

1   ASPVALILEILELYSPROGLNVALSERGLY
2   VALILEVALASNLYSLEUPHELYSALAGLY
3   ASPLYSVALLYSLYSGLYGLNTHRLEUPHE
4   ILEILEGLUGLNASPGLNALASERLYSASP
5   PHEASNARGSERLYSALALEUPHESERGLN
6   SERALAILESERGLNLYSGLUTYRASPSER
7   SERLEUALATHRLEUASPHISTHRGLUILE
8   LYSALAPROPHEASPGLYTHRILEGLYASP
9   ALALEUVALASNILEGLYASPTYRVALSER
10   ALASERTHRTHRGLULEUVALARGVALTHR
11   ASNLEUASNPROILETYRALAASPGLYSER
12   HISHISHISHISHISHIS

Samples:

sample_1: AcrA(61-210DD), [U-100% 15N], 1 mM; potassium phosphate 50 mM

sample_2: AcrA(61-210DD), [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM

sample_3: AcrA(61-210DD), [U-100% 15N], 1 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.4; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

AMBER v8, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

ATHNOS-CANDID, Herrmann, Guntert, Wuthrich - geometry optimization

SPARKY, Goddard - chemical shift assignment

TOPSPIN v2.0, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 15737
PDB

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