BMRB Entry 30199

Name: Solution structure of apo ArCP from yersiniabactin synthetase
Published: 2017-05-04

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PDB ID: 5ttb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30199
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 structure of apo ArCP from yersiniabactin synthetase

Deposition date:

2016-11-02

Original release date:

2017-05-04

Authors:

Frueh, D.; Goodrich, A.

Citation:

Citation: Goodrich, Andrew; Meyers, David; Frueh, Dominique. "Molecular impact of covalent modifications on nonribosomal peptide synthetase carrier protein communication" J. Biol. Chem. 292, 10002-10013 (2017).
PubMed: 28455448

Assembly members:

Assembly members:
Siderophore yersiniabactin, polymer, 82 residues, 9771.064 Da.

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 632 Superkingdom: Bacteria Kingdom: not available Genus/species: Yersinia pestis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Siderophore yersiniabactin: GTDNRHAADYQQLRERLIQE LNLTPQQLHEESNLIQAGLD SIRLMRWLHWFRKNGYRLTL RELYAAPTLAAWNQLMLSRS PE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	349
15N chemical shifts	79
1H chemical shifts	512

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 82 residues - 9771.064 Da.

1

GLY

THR

ASP

ASN

ARG

HIS

ALA

ASP

TYR

2

GLN

LEU

ARG

GLU

ARG

LEU

ILE

GLN

GLU

3

LEU

ASN

LEU

THR

PRO

GLN

LEU

HIS

GLU

4

GLU

SER

ASN

LEU

ILE

GLN

ALA

GLY

LEU

ASP

5

SER

ILE

ARG

LEU

MET

ARG

TRP

LEU

HIS

TRP

6

PHE

ARG

LYS

ASN

GLY

TYR

ARG

LEU

THR

LEU

7

ARG

GLU

LEU

TYR

ALA

PRO

THR

LEU

ALA

8

ALA

TRP

ASN

GLN

LEU

MET

LEU

SER

ARG

SER

9

PRO

GLU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CA)CB	sample_2	isotropic	sample_conditions_1
3D H(CCCO)NH	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
2D hbCBcgcdHD	sample_3	isotropic	sample_conditions_2
2D hbCBcgcdceHE	sample_3	isotropic	sample_conditions_2

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

BMRB Entry 30199

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: