BMRB Entry 16327

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16327

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Title:
DsbA wild type oxidized
Deposition date:
2009-05-29
Original release date:
2009-12-18
Authors:
Sperling, Lindsay; Berthold, Deborah; Sasser, Terry; Jeisy-Scott, Vistoria; Rienstra, Chad
Citation:

Citation: Sperling, Lindsay; Berthold, Deborah; Sasser, Terry; Jeisy-Scott, Victoria; Rienstra, Chad. "Assignment Strategies for Large Proteins by Magic-Angle Spinning NMR: The 21-kDa Disulfide-Bond-Forming Enzyme DsbA"  J. Mol. Biol. 399, 268-282 (2010).
PubMed: 20394752

Assembly members:

Assembly members:
DsbA, polymer, 189 residues, 21000 Da.

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: purified from the natural source   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DsbA: AQYEDGKQYTTLEKPVAGAP QVLEFFSFFCPHCYQFEEVL HISDNVKKKLPEGVKMTKYH VNFMGGDLGKDLTQAWAVAM ALGVEDKVTVPLFEGVQKTQ TIRSASDIRDVFINAGIKGE EYDAAWNSFVVKSLVAQQEK AAADVQLRGVPAMFVNGKYQ LNPQGMDTSNMDVFVQQYAD TVKYLSEKK

Data sets:
Data typeCount
13C chemical shifts694
15N chemical shifts172

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DsbA1

Entities:

Entity 1, DsbA 189 residues - 21000 Da.

1   ALAGLNTYRGLUASPGLYLYSGLNTYRTHR
2   THRLEUGLULYSPROVALALAGLYALAPRO
3   GLNVALLEUGLUPHEPHESERPHEPHECYS
4   PROHISCYSTYRGLNPHEGLUGLUVALLEU
5   HISILESERASPASNVALLYSLYSLYSLEU
6   PROGLUGLYVALLYSMETTHRLYSTYRHIS
7   VALASNPHEMETGLYGLYASPLEUGLYLYS
8   ASPLEUTHRGLNALATRPALAVALALAMET
9   ALALEUGLYVALGLUASPLYSVALTHRVAL
10   PROLEUPHEGLUGLYVALGLNLYSTHRGLN
11   THRILEARGSERALASERASPILEARGASP
12   VALPHEILEASNALAGLYILELYSGLYGLU
13   GLUTYRASPALAALATRPASNSERPHEVAL
14   VALLYSSERLEUVALALAGLNGLNGLULYS
15   ALAALAALAASPVALGLNLEUARGGLYVAL
16   PROALAMETPHEVALASNGLYLYSTYRGLN
17   LEUASNPROGLNGLYMETASPTHRSERASN
18   METASPVALPHEVALGLNGLNTYRALAASP
19   THRVALLYSTYRLEUSERGLULYSLYS

Samples:

sample_1: DsbA, [U-13C; U-15N], 15 mg

sample_2: DsbA, [2-13C-glycerol; U-15N], 15 mg

sample_3: DsbA, [1,3-13C-glycerol; U-15N], 15 mg

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13Csample_1solidsample_conditions_1
2D 13C-13Csample_2solidsample_conditions_1
2D 13C-13Csample_3solidsample_conditions_1
2D 15N-(13CA)-13CXsample_1solidsample_conditions_1
2D 15N-(13CO)-13CXsample_1solidsample_conditions_1
3D 15N-13CA-13CXsample_1solidsample_conditions_1
3D 15N-13CO-13CXsample_1solidsample_conditions_1
3D 13CA-15N-(13CO)-13CXsample_1solidsample_conditions_1
4D 13CA-15N-13CO-13CXsample_1solidsample_conditions_1
2D 15N-13CX (TEDOR)sample_2solidsample_conditions_1
3D 15N-13CA-13CXsample_2solidsample_conditions_1
3D 15N-13CO-13CXsample_3solidsample_conditions_1
2D 13CA-13CO (IPAP)sample_1solidsample_conditions_1
2D 13C-13C (COSY)sample_1solidsample_conditions_1
2D 15N-13CX (TEDOR)sample_3solidsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian Infinity Plus 500 MHz

Related Database Links:

BMRB 17710 18396 18543 18544
PDB
DBJ BAB38206 BAE77448 BAG79665 BAI27892 BAI33015
EMBL CAA44868 CAA56736 CAA90910 CAP78318 CAQ34212
GB AAA23715 AAB02995 AAC43519 AAC43520 AAC43521
REF NP_312810 NP_418297 NP_709659 WP_000725331 WP_000725332
SP P0A4L5 P0A4L6 P0AEG4 P0AEG5 P52235
AlphaFold P0A4L5 P0A4L6 P0AEG4 P0AEG5 P52235