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 5404

Title: Backbone and Side Chain assignments of Peptide Deformylase complexed with Actinonin   PubMed: 12070337

Deposition date: 2002-06-26 Original release date: 2005-05-20

Authors: Byerly, Doug; McElroy, Craig; Foster, Mark

Citation: Byerly, D.; McElroy, C.; Foster, M.. "Mapping the surface of Escherichia coli peptide deformylase by NMR with organic solvents."  Protein Sci. 11, 1850-1853 (2002).

Assembly members:
Peptide Deformylase, polymer, 147 residues, 16684 Da.
ACTINONIN, non-polymer, 385.498 Da.

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Peptide Deformylase: SVLQVLHIPDERLRKVAKPV EEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVI DVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALV PRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGK LFMDYLS

Data sets:
Data typeCount
13C chemical shifts618
15N chemical shifts149
1H chemical shifts1045

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDF1
2Actinonin2

Entities:

Entity 1, PDF 147 residues - 16684 Da.

1   SERVALLEUGLNVALLEUHISILEPROASP
2   GLUARGLEUARGLYSVALALALYSPROVAL
3   GLUGLUVALASNALAGLUILEGLNARGILE
4   VALASPASPMETPHEGLUTHRMETTYRALA
5   GLUGLUGLYILEGLYLEUALAALATHRGLN
6   VALASPILEHISGLNARGILEILEVALILE
7   ASPVALSERGLUASNARGASPGLUARGLEU
8   VALLEUILEASNPROGLULEULEUGLULYS
9   SERGLYGLUTHRGLYILEGLUGLUGLYCYS
10   LEUSERILEPROGLUGLNARGALALEUVAL
11   PROARGALAGLULYSVALLYSILEARGALA
12   LEUASPARGASPGLYLYSPROPHEGLULEU
13   GLUALAASPGLYLEULEUALAILECYSILE
14   GLNHISGLUMETASPHISLEUVALGLYLYS
15   LEUPHEMETASPTYRLEUSER

Entity 2, Actinonin - C19 H35 N3 O5 - 385.498 Da.

1   BB2

Samples:

sample_1: Peptide Deformylase, [U-95% 13C; U-90% 15N], 0.5 – 1.2 mM; TRIS 20 mM; NaN3 0.02%

cond_1: pH: 7.2; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
15N TOCSY-HSQCsample_1not availablecond_1
15N NOESY-HSQCsample_1not availablecond_1
HNHAsample_1not availablecond_1
HBHA(CBCACO)NHsample_1not availablecond_1
CBCA(CO)NHsample_1not availablecond_1
HNCACBsample_1not availablecond_1
13C NOESY-HSQCsample_1not availablecond_1
HCCH-TOCSYsample_1not availablecond_1
HCCH-COSYsample_1not availablecond_1
HNCOsample_1not availablecond_1
HACAHB-COSYsample_1not availablecond_1
C(CO)NH-TOCSYsample_1not availablecond_1

Software:

NMRPipe -

NMRView -

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 4089 6142
PDB
DBJ BAB37575 BAE78005 BAG79085 BAH66202 BAI27558
EMBL CAA11508 CAA45206 CAA54367 CAA54826 CAD09179
GB AAA58084 AAC76312 AAF76758 AAG58408 AAL22269
PIR AB1010
REF NP_289848 NP_312179 NP_417745 NP_458493 NP_462310
SP A1AGH8 A8A591 A8AQI1 A9MN80 A9N8B1

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