BMRB Entry 18257

Title:
E. coli DmsD
Deposition date:
2012-02-11
Original release date:
2012-09-14
Authors:
Charles, Stevens; Mark, Okon; McIntosh, Lawrence
Citation:

Citation: Stevens, Charles; Okon, Mark; McIntosh, Lawrence; Paetzel, Mark. "1H, 13C and 15N resonance assignments and peptide binding site chemical shift perturbation mapping for the Escherichia coli redox enzyme chaperone DmsD."  Biomol. NMR Assignments 7, 193-197 (2013).
PubMed: 22766963

Assembly members:

Assembly members:
DmsD, polymer, 223 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: pET-15b

Data typeCount
13C chemical shifts1203
15N chemical shifts437
1H chemical shifts439
heteronuclear NOE values177
T1 relaxation values177
T2 relaxation values177

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DmsD1

Entities:

Entity 1, DmsD 223 residues - Formula weight is not available

1   METGLYSERHISHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERHISMET
3   THRHISPHESERGLNGLNASPASNPHESER
4   VALALAALAARGVALLEUGLYALALEUPHE
5   TYRTYRALAPROGLUSERALAGLUALAALA
6   PROLEUVALALAVALLEUTHRSERASPGLY
7   TRPGLUTHRGLNTRPPROLEUPROGLUALA
8   SERLEUALAPROLEUVALTHRALAPHEGLN
9   THRGLNCYSGLUGLUTHRHISALAGLNALA
10   TRPGLNARGLEUPHEVALGLYPROTRPALA
11   LEUPROSERPROPROTRPGLYSERVALTRP
12   LEUASPARGGLUSERVALLEUPHEGLYASP
13   SERTHRLEUALALEUARGGLNTRPMETARG
14   GLULYSGLYILEGLNPHEGLUMETLYSGLN
15   ASNGLUPROGLUASPHISPHEGLYSERLEU
16   LEULEUMETALAALATRPLEUALAGLUASN
17   GLYARGGLNTHRGLUCYSGLUGLULEULEU
18   ALATRPHISLEUPHEPROTRPSERTHRARG
19   PHELEUASPVALPHEILEGLULYSALAGLU
20   HISPROPHETYRARGALALEUGLYGLULEU
21   ALAARGLEUTHRLEUALAGLNTRPGLNSER
22   GLNLEULEUILEPROVALALAVALLYSPRO
23   LEUPHEARG

Samples:

sample_1: DmsD, [U-100% 13C; U-100% 15N], 400 uM; H2O 95%; D2O 5%

sample_2: DmsD, [U-100% 13C; U-100% 15N; U-80% 2H], 400 uM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298.15 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 HCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D NHNCACBsample_2isotropicsample_conditions_1
3D NHNCACBCOsample_2isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian Unity 500 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance III 850 MHz

Related Database Links:

UNP P69853
PDB
DBJ BAA15315 BAB35720 BAG77236 BAI25543 BAI30539
EMBL CAP76090 CAQ32067 CAQ98498 CAR02951 CAR07954
GB AAC74663 AAG56578 AAN43196 AAN80442 AAP17084
PIR F85764
REF NP_310324 NP_416108 NP_707489 WP_000148687 WP_000148688
SP P69853 P69854 P69855 Q8CW16
AlphaFold P77270 Q8CW16 P69853 P69854 P69855

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