BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18257

Title: E. coli DmsD   PubMed: 22766963

Authors: Charles, Stevens; Mark, Okon; McIntosh, Lawrence

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).

Assembly members:
DmsD, polymer, 223 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
DmsD: MGSHHHHHHSSGLVPRGSHM THFSQQDNFSVAARVLGALF YYAPESAEAAPLVAVLTSDG WETQWPLPEASLAPLVTAFQ TQCEETHAQAWQRLFVGPWA LPSPPWGSVWLDRESVLFGD STLALRQWMREKGIQFEMKQ NEPEDHFGSLLLMAAWLAEN GRQTECEELLAWHLFPWSTR FLDVFIEKAEHPFYRALGEL ARLTLAQWQSQLLIPVAVKP LFR

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