BMRB Entry 34451

Name: Solution structure of MacpD, a acyl carrier protein, from Pseudomonas fluorescens involved in Mupirocin biosynthesis.
Published: 2020-02-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34451

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of MacpD, a acyl carrier protein, from Pseudomonas fluorescens involved in Mupirocin biosynthesis. PubMed: 31977176

Deposition date: 2019-11-15 Original release date: 2020-02-13

Authors: Williams, C.; Crump, M.

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. ., .-. (2020).

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

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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	445
15N chemical shifts	110
1H chemical shifts	746

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 138 residues - 14936.705 Da.

1

MET

HIS

GLY

LYS

PRO

2

ILE

PRO

ASN

PRO

LEU

GLY

LEU

ASP

SER

3

THR

GLU

ASN

LEU

TYR

PHE

GLN

GLY

ILE

ASP

4

PRO

PHE

THR

LEU

ASN

HIS

GLN

VAL

MET

ASP

5

GLN

VAL

PHE

ASP

GLN

VAL

GLU

HIS

GLN

ILE

6

ALA

GLN

VAL

LEU

GLY

ALA

LYS

GLY

PRO

7

LEU

VAL

ALA

VAL

GLU

ILE

ASP

SER

ARG

PHE

8

SER

ASP

LEU

GLY

LEU

SER

LEU

ASP

LEU

9

ALA

THR

LEU

ILE

SER

ASN

LEU

GLU

ALA

VAL

10

TYR

GLY

THR

ASP

PRO

PHE

ALA

ASP

ALA

VAL

11

ALA

ILE

THR

SER

ILE

VAL

THR

VAL

ALA

ASP

12

LEU

ALA

ARG

ALA

TYR

ALA

GLN

GLY

VAL

13

PRO

GLY

PRO

SER

PRO

ASP

PRO

LEU

ASP

ALA

14

GLN

LEU

ARG

ASP

LEU

ARG

GLN

LEU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts