BMRB Entry 34085

Name: Bamb_5917 Acyl-Carrier Protein
Published: 2018-07-26

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PDB ID: 5mti
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34085
MolProbity Validation Chart

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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: Bamb_5917 Acyl-Carrier Protein PubMed: 31548674

Deposition date: 2017-01-09 Original release date: 2018-07-26

Authors: Gallo, A.; Kosol, S.; Griffiths, D.; Masschelein, J.; Alkhalaf, L.; Smith, H.; Valentic, T.; Tsai, S.; Challis, G.; Lewandowski, J.

Citation: Kosol, Simone; Gallo, Angelo; Griffiths, Daniel; Valentic, Timothy; Masschelein, Joleen; Jenner, Matthew; de Los Santos, Emmanuel; Manzi, Lucio; Sydor, Paulina; Rea, Dean; Zhou, Shanshan; Fulop, Vilmos; Oldham, Neil; Tsai, Shiou-Chuan; Challis, Gregory; Lewandowski, Jozef. "Structural basis for chain release from the enacyloxin polyketide synthase" Nat. Chem. 11, 913-923 (2019).

Assembly members:
Phosphopantetheine-binding protein, polymer, 107 residues, 11323.716 Da.

Natural source: Common Name: b-proteobacteria Taxonomy ID: 339670 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia ambifaria

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

Entity Sequences (FASTA):
Phosphopantetheine-binding protein: GIDPFTGAAAGVSAAGIEPD LTAIWQALFALPAVGRHQDF FALGGDSQLGLRMLAQLRER HGVDLPLRCLYEAPTVARLA ETIVRLAAPAPSGDQDDASE YEEGVIR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	396
15N chemical shifts	96
1H chemical shifts	640

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_1 107 residues - 11323.716 Da.

1

GLY

ILE

ASP

PRO

PHE

THR

GLY

ALA

2

GLY

VAL

SER

ALA

GLY

ILE

GLU

PRO

ASP

3

LEU

THR

ALA

ILE

TRP

GLN

ALA

LEU

PHE

ALA

4

LEU

PRO

ALA

VAL

GLY

ARG

HIS

GLN

ASP

PHE

5

PHE

ALA

LEU

GLY

ASP

SER

GLN

LEU

GLY

6

LEU

ARG

MET

LEU

ALA

GLN

LEU

ARG

GLU

ARG

7

HIS

GLY

VAL

ASP

LEU

PRO

LEU

ARG

CYS

LEU

8

TYR

GLU

ALA

PRO

THR

VAL

ALA

ARG

LEU

ALA

9

GLU

THR

ILE

VAL

ARG

LEU

ALA

PRO

ALA

10

PRO

SER

GLY

ASP

GLN

ASP

ALA

SER

GLU

11

TYR

GLU

GLY

VAL

ILE

ARG

Samples:

sample_1: 15N_PCP17, [U-99% 15N], 0.5 mM; D2O 10%; DSS 1%; H2O 90%; potassium phosphate 50 mM; sodium chloride 200 mM

sample_2: 13C,15N_PCP17, [U-13C; U-15N], 0.3 mM; D2O 10%; DSS 1%; H2O 90%; potassium phosphate 50 mM; sodium chloride 200 mM

sample_conditions_1: ionic strength: 250 mM; pH: 6.50; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	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 HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1

Software:

AMBER v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

ATNOS/CANDID vUNIO, Herrmann, Guntert and Wuthrich - peak picking

CARA v3, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v3.5pl6, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker AvanceII 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts