BMRB Entry 31046

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31046
MolProbity Validation Chart

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Title:
The solution structure of abxF in complex with its product (-)-ABX, an enzyme catalyzing the formation of the chiral spiroketal of an anthrabenzoxocinone antibiotic, (-)-ABX
Deposition date:
2022-10-06
Original release date:
2024-04-03
Authors:
Jia, X.; Yan, X.; Qu, X.; Mobli, M.
Citation:

Citation: Jia, X.; Yan, X.; Mobli, M.; Qu, X.. "The solution structure of abxF, an enzyme catalyzing the formation of chiral spiroketal of an antibiotics, (-)-ABX."  .

Assembly members:

Assembly members:
entity_1, polymer, 245 residues, 25191.973 Da.
entity_2, non-polymer, 460.475 Da.

Natural source:

Natural source:   Common Name: Streptomyces sp.   Taxonomy ID: 1931   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces sp.

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMSHDAVRPAPGEPTWVD LLTPDRGAALQFYSALFGWE FSTTSDGTSPYTMCRLRGRE VCSIGDLGENPGPALGGWSS YLSVDDADAAAAAVPELGGA VLLGPIDILAQGRMLLAGDP SGHRVGLWQAKEHTGSGPDD GIGAYTRSELLTGASATDGA FYRGLFGADFATESGTDGGG RRAAIRQVGPAAPSGWYPCF RAQESAVPAAVMLGASVLLR YDCPDGPAVVVSAPGGEVFT LLLTD

Data typeCount
13C chemical shifts942
15N chemical shifts235
1H chemical shifts1507

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 245 residues - 25191.973 Da.

1   GLYSERHISMETSERHISASPALAVALARG
2   PROALAPROGLYGLUPROTHRTRPVALASP
3   LEULEUTHRPROASPARGGLYALAALALEU
4   GLNPHETYRSERALALEUPHEGLYTRPGLU
5   PHESERTHRTHRSERASPGLYTHRSERPRO
6   TYRTHRMETCYSARGLEUARGGLYARGGLU
7   VALCYSSERILEGLYASPLEUGLYGLUASN
8   PROGLYPROALALEUGLYGLYTRPSERSER
9   TYRLEUSERVALASPASPALAASPALAALA
10   ALAALAALAVALPROGLULEUGLYGLYALA
11   VALLEULEUGLYPROILEASPILELEUALA
12   GLNGLYARGMETLEULEUALAGLYASPPRO
13   SERGLYHISARGVALGLYLEUTRPGLNALA
14   LYSGLUHISTHRGLYSERGLYPROASPASP
15   GLYILEGLYALATYRTHRARGSERGLULEU
16   LEUTHRGLYALASERALATHRASPGLYALA
17   PHETYRARGGLYLEUPHEGLYALAASPPHE
18   ALATHRGLUSERGLYTHRASPGLYGLYGLY
19   ARGARGALAALAILEARGGLNVALGLYPRO
20   ALAALAPROSERGLYTRPTYRPROCYSPHE
21   ARGALAGLNGLUSERALAVALPROALAALA
22   VALMETLEUGLYALASERVALLEULEUARG
23   TYRASPCYSPROASPGLYPROALAVALVAL
24   VALSERALAPROGLYGLYGLUVALPHETHR
25   LEULEULEUTHRASP

Entity 2, unit_2 - C27 H24 O7 - 460.475 Da.

1   WOZ

Samples:

sample_1: abxF, [U-100% 13C; U-100% 15N], 1.25 mM; (-)-ABX 1.25 mM; D2O, [U-100% 2H], 5 % v/v; H2O 95 % v/v; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 3 mM; DTT 5 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESY - filteredsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic - filteredsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromatic - filteredsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESY - filteredsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-13C HSQC constant timesample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CcpNmr Analysis vVersion 2.4.2, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE 900 MHz
  • Bruker AVANCE 700 MHz

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