BMRB Entry 25117

Title:
1H, 13C, and 15N Chemical Shift Assignments for SAIL-DsbA
Deposition date:
2014-07-31
Original release date:
2022-05-12
Authors:
Schmidt, Elena; Ikeya, Teppei; Takeda, Mitsuhiro; Loehr, Frank; Buchner, Lena; Ito, Yutaka; Kainosho, Masatsune; Guentert, Peter
Citation:

Citation: Schmidt, Elena; Ikeya, Teppei; Takeda, Mitsuhiro; Loehr, Frank; Buchner, Lena; Ito, Yutaka; Kainosho, Masatsune; Guentert, Peter. "Automated resonance assignment of the 21kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA"  J. Magn. Reson. 249, 88-93 (2014).
PubMed: 25462951

Assembly members:

Assembly members:
DsbA_protein, polymer, 189 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: cell free synthesis   Host organism: Escherichia coli   Vector: na

Data sets:
Data typeCount
13C chemical shifts1495
15N chemical shifts403
1H chemical shifts1923

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DsbA monomer1

Entities:

Entity 1, DsbA monomer 189 residues - Formula weight is not available

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 protein, SAIL, 0.36 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.02 M; pH: 3.7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

CYANA v3.96, Guentert - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

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