BMRB Entry 34870

Name: Solution NMR structure of the novel adaptor domain TomBN91 from the Tomaymycin non-ribosomal peptide synthetase
Published: 2024-06-20

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PDB ID: 8qsx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34870
MolProbity Validation Chart

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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:

Solution NMR structure of the novel adaptor domain TomBN91 from the Tomaymycin non-ribosomal peptide synthetase

Deposition date:

2023-10-11

Original release date:

2024-06-20

Authors:

Karanth, M.; Kirkpatrick, J.; Carlomagno, T.

Citation:

Citation: Karanth, M.; Kirkpatrick, J.; Krausze, J.; Schmelz, S.; Scrima, A.; Carlomagno, T.. "The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain" Sci. Adv. 10, eadm9404-eadm9404 (2024).
PubMed: 38896613

Assembly members:

Assembly members:
entity_1, polymer, 95 residues, 9985.311 Da.

Natural source:

Natural source: Common Name: Streptomyces regensis Taxonomy ID: 68263 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces regensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPMLMNSPLRTTVLDLARTT LGSADLTAHEPLADRCEHPA LLDDLATTLTAVFAVEITGA DLAAGATVADVAARMDDRRD APRIPELRAGLAPRD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	371
15N chemical shifts	88
1H chemical shifts	620

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 95 residues - 9985.311 Da.

1

GLY

PRO

MET

LEU

MET

ASN

SER

PRO

LEU

ARG

2

THR

VAL

LEU

ASP

LEU

ALA

ARG

THR

3

LEU

GLY

SER

ALA

ASP

LEU

THR

ALA

HIS

GLU

4

PRO

LEU

ALA

ASP

ARG

CYS

GLU

HIS

PRO

ALA

5

LEU

ASP

LEU

ALA

THR

LEU

THR

6

ALA

VAL

PHE

ALA

VAL

GLU

ILE

THR

GLY

ALA

7

ASP

LEU

ALA

GLY

ALA

THR

VAL

ALA

ASP

8

VAL

ALA

ARG

MET

ASP

ARG

ASP

9

ALA

PRO

ARG

ILE

PRO

GLU

LEU

ARG

ALA

GLY

10

LEU

ALA

PRO

ARG

ASP

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D TOCSY-HSQC	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1

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

BMRB Entry 34870

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: