BMRB Entry 34451

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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/BMR34451
MolProbity Validation Chart

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Title:
Solution structure of MacpD, a acyl carrier protein, from Pseudomonas fluorescens involved in Mupirocin biosynthesis.
Deposition date:
2019-11-15
Original release date:
2020-02-13
Authors:
Williams, C.; Crump, M.
Citation:

Citation: Walker, P.; Rowe, M.; Winter, A.; Weir, A.; Akter, N.; Wang, L.; Race, P.; Williams, C.; Song, Z.; Simpson, T.; Willis, C.; Crump, M.. "A Priming Cassette Generates Hydroxylated Acyl Starter Units in Mupirocin and Thiomarinol Biosynthesis."  Acs Chem. Biol. 15, 494-503 (2020).
PubMed: 31977176

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, 14936.705 Da.

Natural source:

Natural source:   Common Name: Pseudomonas fluorescens   Taxonomy ID: 294   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas fluorescens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET151/D-TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHGKPIPNPLLGLDS TENLYFQGIDPFTLNHQVMD QVFDQVEHQIAQVLGAKGGP LVAVEIDSRFSDLGLSSLDL ATLISNLEAVYGTDPFADAV AITSIVTVADLARAYAQQGV PGPSPDPLDAQLRDLRQL

Data sets:
Data typeCount
13C chemical shifts445
15N chemical shifts110
1H chemical shifts746

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 138 residues - 14936.705 Da.

1   METHISHISHISHISHISHISGLYLYSPRO
2   ILEPROASNPROLEULEUGLYLEUASPSER
3   THRGLUASNLEUTYRPHEGLNGLYILEASP
4   PROPHETHRLEUASNHISGLNVALMETASP
5   GLNVALPHEASPGLNVALGLUHISGLNILE
6   ALAGLNVALLEUGLYALALYSGLYGLYPRO
7   LEUVALALAVALGLUILEASPSERARGPHE
8   SERASPLEUGLYLEUSERSERLEUASPLEU
9   ALATHRLEUILESERASNLEUGLUALAVAL
10   TYRGLYTHRASPPROPHEALAASPALAVAL
11   ALAILETHRSERILEVALTHRVALALAASP
12   LEUALAARGALATYRALAGLNGLNGLYVAL
13   PROGLYPROSERPROASPPROLEUASPALA
14   GLNLEUARGASPLEUARGGLNLEU

Samples:

sample_1: MacpD, acyl carrier protein, [U-99% 15N], 1 ± 0.2 mM; sodium azide 0.1 ± 0.1 mM; sodium phosphate 50 ± 0.2 mM

sample_2: MacpD, acyl carrier protein, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium azide 0.1 ± 0.1 mM; sodium phosphate 50 ± 0.2 mM

sample_3: MacpD, acyl carrier protein 1 ± 0.1 mM; sodium phosphate 50 ± 0.2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

TopSpin v3.5, Bruker Biospin - collection

VNMR v4, varian - collection

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - structure calculation

NMR spectrometers:

  • Agilent vnmrs 600 MHz
  • Bruker AVANCE III 700 MHz

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