BMRB Entry 4425

Title:
Solution structure of apo-biotinyl domain from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance NMR spectroscopy
Deposition date:
1999-09-29
Original release date:
1999-12-23
Authors:
ROBERTS, E.; SHU, N.; HOWARD, M.; BROADHURST, R.; CHAPMAN-SMITH, A.; WALLACE, J.; MORRIS, T.; CRONAN, J.; PERHAM, R.
Citation:

Citation: ROBERTS, E.; SHU, N.; HOWARD, M.; BROADHURST, R.; CHAPMAN-SMITH, A.; WALLACE, J.; MORRIS, T.; CRONAN, J.; PERHAM, R.. "SOLUTION STRUCTURES OF APO- AND HOLO-BIOTINYL DOMAINS FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOP"  Biochemistry 38, 5045-5053 (1999).

Assembly members:

Assembly members:
ACETYL-COA CARBOXYLASE, polymer, 82 residues, Formula weight is not available

Natural source:

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

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

Experimental source:

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

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts557
13C chemical shifts267
15N chemical shifts82

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1acc biotinyl domain1

Entities:

Entity 1, acc biotinyl domain 82 residues - Formula weight is not available

1   ALAALAGLUILESERGLYHISILEVALARG
2   SERPROMETVALGLYTHRPHETYRARGTHR
3   PROSERPROASPALALYSALAPHEILEGLU
4   VALGLYGLNLYSVALASNVALGLYASPTHR
5   LEUCYSILEVALGLUALAMETLYSMETMET
6   ASNGLNILEGLUALAASPLYSSERGLYTHR
7   VALLYSALAILELEUVALGLUSERGLYGLN
8   PROVALGLUPHEASPGLUPROLEUVALVAL
9   ILEGLU

Samples:

sample_1: ACETYL-COA CARBOXYLASE, [U-100% 13C; U-100% 15N], 3.0 mM; sodium phosphate 20 mM

sample_2: ACETYL-COA CARBOXYLASE, [U-100% 15N], 3.0 mM; sodium phosphate 20 mM

sample_3: ACETYL-COA CARBOXYLASE 3.0 mM; sodium phosphate 20 mM

sample_cond_1: pH: 6.8; temperature: 303 K; ionic strength: 20 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
DQF-COSYnot availablenot availablenot available
NOESYnot availablenot availablenot available
15N-1H-HSQCnot availablenot availablenot available
HNHAnot availablenot availablenot available
HNHBnot availablenot availablenot available
15N-NOESY-HMQCnot availablenot availablenot available
15N-TOCSY-HMQCnot availablenot availablenot available
HNCACBnot availablenot availablenot available
13C-NOESY-HSQCnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker AMX 600 MHz

Related Database Links:

BMRB 4426
PDB
DBJ BAB37550 BAE77296 BAG79060 BAI27525 BAI32704
EMBL CAA32933 CAD07894 CAP77706 CAQ33581 CAQ90726
GB AAA23408 AAA23744 AAA23745 AAA58058 AAC76287
PIR AH0912
REF NP_312154 NP_417721 NP_457755 NP_462289 NP_709050
SP P0ABD8 P0ABD9 P0ABE0 P0ABE1
AlphaFold P0ABE0

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