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 25904

Title: Sequence-specific 1H, 13C, and 15N backbone resonance assignment of the monomeric 2-Deoxy-D-ribose-5-phosphate aldolase (DERA) mutant (K58E-Y96W)

Deposition date: 2015-11-20 Original release date: 2017-03-09

Authors: Dick, Markus; Hartmann, Rudolf; Schwarten, Melanie; Willbold, Dieter; Pietruszka, Joerg

Citation: Dick, Markus; Hartmann, Rudolf; Weiergraeber, Oliver; Bisterfeld, Carolin; Classen, Thomas; Schwarten, Melanie; Neudecker, Philipp; Willbold, Dieter; Pietruszka, Joerg. "Mechanism-based inhibition of an aldolase at high concentrations of its natural substrate acetaldehyde: structural insights and protective strategies"  Chem. Sci. 7, 4492-4502 (2016).

Assembly members:
DERA_MON, polymer, 265 residues, 28583.5691 Da.

Natural source:   Common Name: Escherichia coli (strain K12)   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
DERA_MON: MTDLKASSLRALKLMDLTTL NDDDTDEKVIALCHQAKTPV GNTAAICIYPRFIPIARETL KEQGTPEIRIATVTNFPHGN DDIDIALAETRAAIAWGADE VDVVFPYRALMAGNEQVGFD LVKACKEACAAANVLLKVII ETGELKDEALIRKASEISIK AGADFIKTSTGKVAVNATPE SARIMMEVIRDMGVEKTVGF KPAGGVRTAEDAQKYLAIAD ELFGADWADARHYRFGASSL LASLLKALGHGDGKSASSYH HHHHH

Data sets:
Data typeCount
13C chemical shifts507
15N chemical shifts244
1H chemical shifts244

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DERA MON1

Entities:

Entity 1, DERA MON 265 residues - 28583.5691 Da.

1   METTHRASPLEULYSALASERSERLEUARG
2   ALALEULYSLEUMETASPLEUTHRTHRLEU
3   ASNASPASPASPTHRASPGLULYSVALILE
4   ALALEUCYSHISGLNALALYSTHRPROVAL
5   GLYASNTHRALAALAILECYSILETYRPRO
6   ARGPHEILEPROILEALAARGGLUTHRLEU
7   LYSGLUGLNGLYTHRPROGLUILEARGILE
8   ALATHRVALTHRASNPHEPROHISGLYASN
9   ASPASPILEASPILEALALEUALAGLUTHR
10   ARGALAALAILEALATRPGLYALAASPGLU
11   VALASPVALVALPHEPROTYRARGALALEU
12   METALAGLYASNGLUGLNVALGLYPHEASP
13   LEUVALLYSALACYSLYSGLUALACYSALA
14   ALAALAASNVALLEULEULYSVALILEILE
15   GLUTHRGLYGLULEULYSASPGLUALALEU
16   ILEARGLYSALASERGLUILESERILELYS
17   ALAGLYALAASPPHEILELYSTHRSERTHR
18   GLYLYSVALALAVALASNALATHRPROGLU
19   SERALAARGILEMETMETGLUVALILEARG
20   ASPMETGLYVALGLULYSTHRVALGLYPHE
21   LYSPROALAGLYGLYVALARGTHRALAGLU
22   ASPALAGLNLYSTYRLEUALAILEALAASP
23   GLULEUPHEGLYALAASPTRPALAASPALA
24   ARGHISTYRARGPHEGLYALASERSERLEU
25   LEUALASERLEULEULYSALALEUGLYHIS
26   GLYASPGLYLYSSERALASERSERTYRHIS
27   HISHISHISHISHIS

Samples:

Sample_1: DERA_MON, [U-13C; U-15N], 1.0 mM; D2O 5%; H2O 95%

Condition_set_1: ionic strength: 0.020 M; pH: 6.800; pressure: 1.000 atm; temperature: 298.150 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCSample_1isotropicCondition_set_1
3D HNCOSample_1isotropicCondition_set_1
HNcaCO (H[N[ca[CO]]])Sample_1isotropicCondition_set_1
3D HN(CO)CASample_1isotropicCondition_set_1
3D HNCASample_1isotropicCondition_set_1

Software:

CcpNmr_Analysis v2.4, CCPN - Assignment

NMRPipe v8.1, NIH - Processing

VnmrJ v2.3, Agilent Technologies (formerly Varian) - Acquisition

NMR spectrometers:

  • Varian VNMRS 900 MHz

Related Database Links:

UniProt P0A6L0

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