BMRB Entry 15659

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15659
MolProbity Validation Chart

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Title:
The actinorhodin apo acyl carrier protein from S. coelicolor
Deposition date:
2008-02-15
Original release date:
2008-09-11
Authors:
Crump, Matthew; Evans, Simon; Christopher, Williams
Citation:

Citation: Evans, Simon; Williams, Christopher; Arthur, Christopher; Burston, Steven; Simpson, Thomas; Crosby, John; Crump, Matthew. "An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein"  ChemBioChem 9, 2424-2432 (2008).
PubMed: 18770515

Assembly members:

Assembly members:
act_ACP, polymer, 86 residues, 9239.254 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 1902   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces coelicolor

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
act_ACP: MATLLTTDDLRRALVESAGE TDGTDLSGDFLDLRFEDIGY DSLALMETAARLESRYGVSI PDDVAGRVDTPRELLDLING ALAEAA

Data sets:
Data typeCount
13C chemical shifts362
15N chemical shifts92
1H chemical shifts577

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 86 residues - 9239.254 Da.

This sequence contains a C17S mutation to prevent dimerisation of the ACP under NMR conditions.

1   METALATHRLEULEUTHRTHRASPASPLEU
2   ARGARGALALEUVALGLUSERALAGLYGLU
3   THRASPGLYTHRASPLEUSERGLYASPPHE
4   LEUASPLEUARGPHEGLUASPILEGLYTYR
5   ASPSERLEUALALEUMETGLUTHRALAALA
6   ARGLEUGLUSERARGTYRGLYVALSERILE
7   PROASPASPVALALAGLYARGVALASPTHR
8   PROARGGLULEULEUASPLEUILEASNGLY
9   ALALEUALAGLUALAALA

Samples:

13C_15N_labelled_Sample: act ACP, [U-98% 13C; U-98% 15N], 1-2 ± 0.1 mM; D2O 5%; H2O 95%; potassium phosphate 20 ± 2 mM; sodium azide 1 ± 0.1 mM

ACP_standard_conditions: pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C_15N_labelled_SampleisotropicACP_standard_conditions
3D CBCA(CO)NH13C_15N_labelled_SampleisotropicACP_standard_conditions
3D HNCO13C_15N_labelled_SampleisotropicACP_standard_conditions
3D HNCACB13C_15N_labelled_SampleisotropicACP_standard_conditions
3D HCCH-TOCSY13C_15N_labelled_SampleisotropicACP_standard_conditions
3D HNHA13C_15N_labelled_SampleisotropicACP_standard_conditions
3D 1H-15N NOESY13C_15N_labelled_SampleisotropicACP_standard_conditions
3D 1H-13C NOESY13C_15N_labelled_SampleisotropicACP_standard_conditions

Software:

ARIA v1.2, CCPN, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Linge, O'Donoghue and Nilges - chemical shift assignment, processing, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15658 16196 16197 16199 16200 16201 16202 16203 25284 25287
PDB
EMBL CAA45045 CAC44202
GB AIJ13577 EFD66960 EOY50075 KKD13304
REF NP_629239 WP_003973889
SP Q02054
AlphaFold Q02054

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