BMRB Entry 25706

Name: 1H, 13C, and 15N Chemical Shift Assignments of PKS domains
Published: 2016-03-21

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PDB ID: 2n5d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25706
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments of PKS domains

Deposition date:

2015-07-14

Original release date:

2016-03-21

Authors:

Dorival, Gonathan; Annaval, Thibault; Risser, Fanny; Collin, Sabrina; Roblin, Pierre; Jacob, Christophe; Gruez, Arnaud; Chagot, Benjamin; Weissman, Kira

Citation:

Citation: Dorival, Gonathan; Annaval, Thibault; Risser, Fanny; Collin, Sabrina; Roblin, Pierre; Jacob, Christophe; Gruez, Arnaud; Chagot, Benjamin; Weissman, Kira. "Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase" J. Am. Chem. Soc. 138, 4155-4167 (2016).
PubMed: 26982529

Assembly members:

Assembly members:
entity, polymer, 84 residues, 8455.489 Da.

Natural source:

Natural source: Common Name: high GC Gram+ Taxonomy ID: 1961 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces virginiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pBG102 (pet27 derivative)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPGSYTGAGEPSQADLDALL SAVRDNRLSIEQAVTLLTPR RGGGSGGGSMDAKEILTRFK DGGLDRAAAQALLAGRTPAA APRP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	321
15N chemical shifts	80
1H chemical shifts	518

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 84 residues - 8455.489 Da.

Residues 1-5 represent a non-native affinity tag. Residues 6-41 is from VirA protein. Residues 42-49 is an non-native fusion linker. Residues 50-88 is from VirFG protein.

1

GLY

PRO

GLY

SER

TYR

THR

GLY

ALA

GLY

GLU

2

PRO

SER

GLN

ALA

ASP

LEU

ASP

ALA

LEU

3

SER

ALA

VAL

ARG

ASP

ASN

ARG

LEU

SER

ILE

4

GLU

GLN

ALA

VAL

THR

LEU

THR

PRO

ARG

5

ARG

GLY

SER

GLY

SER

MET

6

ASP

ALA

LYS

GLU

ILE

LEU

THR

ARG

PHE

LYS

7

ASP

GLY

LEU

ASP

ARG

ALA

GLN

8

ALA

LEU

ALA

GLY

ARG

THR

PRO

ALA

9

ALA

PRO

ARG

PRO

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY v3.115, Goddard - chemical shift assignment

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

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS v+, Cornilescu, Delaglio and Bax - structure solution

NMR spectrometers:

Bruker Avance 600 MHz